ID   ACE2_YEAST_z     STANDARD;      PRT;   770 AA.
AC   P21192;
DT   01-MAY-1991 (REL. 18, CREATED)
DT   01-MAY-1991 (REL. 18, LAST SEQUENCE UPDATE)
DT   01-OCT-1993 (REL. 27, LAST ANNOTATION UPDATE)
DE   METALLOTHIONEIN EXPRESSION ACTIVATOR.
GN   ACE2.
OS   SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
OC   EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=DBY939;
RM   91094864
RA   BUTLER G., THIELE D.J.;
RL   MOL. CELL. BIOL. 11:476-485(1991).
CC   -!- FUNCTION: ACE2 PLAYS A ROLE IN REGULATING BASAL-LEVEL EXPRESSION
CC       OF CUP1.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- SIMILARITY: STRONG, TO YEAST TRANSCRIPTIONAL FACTOR SWI5.
DR   EMBL; M55619; SCACE2.
DR   PIR; S12943; TWBYA2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2.
KW   TRANSCRIPTION REGULATION; ACTIVATOR; ZINC-FINGER; DNA-BINDING;
KW   REPEAT; METAL-BINDING; NUCLEAR PROTEIN.
FT   DOMAIN      603    685       ZINC-FINGERS.
FT   ZN_FING     603    627       C2H2-TYPE.
FT   ZN_FING     633    657       C2H2-TYPE.
FT   ZN_FING     662    685       C2H2-TYPE.
SQ   SEQUENCE   770 AA;  86633 MW;  3048776 CN;
     MDNVVDPWYI NPSGFAKDTQ DEEYVQHHDN VNPTIPPPDN YILNNENDDG LDNLLGMDYY        60
     NIDDLLTQEL RDLDIPLVPS PKTGDGSSDK KNIDRTWNLG DENNKVSHYS KKSMSSHKRG       120
     LSGTAIFGFL GHNKTLSISS LQQSILNMSK DPQPMELINE LGNHNTVKNN NDDFDHIREN       180
     DGENSYLSQV LLKQQEELRI ALEKQKEVNE KLEKQLRDNQ IQQEKLRKVL EEQEEVAQKL       240
     VSGATNSNSK PGSPVILKTP AMQNGRMKDN AIIVTTNSAN GGYQFPPPTL ISPRMSNTSI       300
     NGSPSRKYHR QRYPNKSPES NGLNLFSSNS GYLRDSELLS FSPQNYNLNL DGLTYNDHNN       360
     TSDKNNNDKK NSTGDNIFRL FEKTSPGGLS ISPRINGNSL RSPFLVGTDK SRDDRYAAGT       420
     FTPRTQLSPI HKKRESVVST VSTISQLQDD TEPIHMRNTQ NPTLRNANAL ASSSVLPPIP       480
     GSSNNTPIKN SLPQKHVFQH TPVKAPPKNG SNLAPLLNAP DLTDHQLEIK TPIRNNSHCE       540
     VESYPQVPPV THDIHKSPTL HSTSPLPDEI IPRTTPMKIT KKPTTLPPGT IDQYVKELPD       600
     KLFECLYPNC NKVFKRRYNI RSHIQTHLQD RPYSCDFPGC TKAFVRNHDL IRHKISHNAK       660
     KYICPCGKRF NREDALMVHR SRMICTGGKK LEHSINKKLT SPKKSLLDSP HDTSPVKETI       720
     ARDKDGSVLM KMEEQLRDDM RKHGLLDPPP STAAHEQNSN RTLSNETDAL                  770
//


ID   AGIE_RAT_z       STANDARD;      PRT;   916 AA.
AC   Q00900;
DT   01-JUL-1993 (REL. 26, CREATED)
DT   01-JUL-1993 (REL. 26, LAST SEQUENCE UPDATE)
DT   01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE)
DE   DNA-BINDING PROTEIN AGIE-BP1 (ANGIOTENSINOGEN GENE-INDUCIBLE
DE   ENHANCER-BINDING PROTEIN 1) (FRAGMENT).
GN   AGIE-BP1.
OS   RATTUS NORVEGICUS (RAT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=LIVER;
RM   91203912
RA   RON D., BRASIER A.R., HABENER J.F.;
RL   MOL. CELL. BIOL. 11:2887-2895(1991).
CC   -!- FUNCTION: BINDS TO DNA AT THE ACUTE-PHASE RESPONSE ELEMENT OF THE
CC       ANGIOTENSINOGEN GENE AND RELATED NUCLEAR FACTOR KAPPA-B BINDING
CC       SITES THROUGH A ZINC-FINGER MOTIF.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- DOMAIN: CONTAINS TEN REPEATS OF THE MOTIF X-S-P-X-R/K.
DR   EMBL; M65251; RNAGIEBP1.
DR   PIR; A39796; A39796.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2.
KW   ZINC-FINGER; METAL-BINDING; DNA-BINDING; NUCLEAR PROTEIN; REPEAT.
FT   NON_TER       1      1
FT   DOMAIN      269    321       ZINC-FINGERS.
FT   ZN_FING     269    291       C2H2-TYPE.
FT   ZN_FING     297    321       C2H2-TYPE.
FT   DOMAIN      369    396       ASP/GLU-RICH (ACIDIC).
FT   DOMAIN      528    618       REPEAT-RICH REGION.
SQ   SEQUENCE   916 AA;  101205 MW;  4427664 CN;
     IPAASGPFPP NREILSGSRA PPRRKFSGPS ESRESSDELD IDETSSDMSM SPQSSSLPTG        60
     GSQQEDEGKA RKLPVSMLVH MASGPGGNVA NSTLLFTDVA DFQQILQFPS LRTTTTVSWC       120
     FLNYTKPNFV QQATFKSSVY ASWCISSCNP NPSGLNTKTT LALLRSKQKI TAEIYTLAAM       180
     HRPGTGKLTS SSAWKQFAQM KPDAPFLFGN KLERKLGGNV LKERGKGEIH GDKDLGSKQT       240
     EPIRIKIFEG GYKSNEDYVY VRGRGRGKYI CEECGIRCKK PSMLKKHIRT HTDVRPYVCK       300
     LCNFAFKTKG NLTKHMKSKA HMKKCLELGV SMTSVDETET EEAENMEDLH KTSEKHSMSG       360
     ISTDHQFSDA EESDGEDGDD NDEDDEDDDD FDDQGDLTPK TRSRSTSPQP PRFSSLPVNV       420
     GAVAHGVPSD SSLGHSSLIS YLVTLPSIQV TQLMTPSDSC EDTQMTEYQR LFQSKSTDSE       480
     PDKDRLDIPS SMDEEAMLSS EPSSSPRDFS PSSYRSSPGY DSSPCRDNSP KRYLIPKGDL       540
     SPRRHLSPRR DLSPMRHLSP RKEAALRREM SQGDASPRRH LSPRRPLSPG KDITTRRDLS       600
     PRRERRYMTT IRAPSPRRAL YHNPPLPMGQ YLQTEPIVLG PPNLRRGLPQ VPYFSLYGDQ       660
     EGAYEHHGSS LFPEGPTDYV FSHLPLHSQQ QVRAPIPMVP VGGIQMVHSL PPAISGLHPP       720
     PTLPLPTEGS EEKKGAPGEA LTKDPYTLSR RHEKQAPHVL QSSGLPSSPS SPRLLMKQST       780
     SEDSLNSTER EQEENIQTCT KAIASLRIAT EEAALLGADQ PTWVQESPQK PLESAHISIR       840
     HFSGPEPGQL CTSAAHPDLH DGEKDTFGTS QTAVAHPTFY SKGSVDEKQV DFQSSKELSL       900
     STEEGNEPSS EKNRLH                                                       916
//

ID   BRLA_EMENI_z     STANDARD;      PRT;   432 AA.
AC   P10069;
DT   01-MAR-1989 (REL. 10, CREATED)
DT   01-MAR-1989 (REL. 10, LAST SEQUENCE UPDATE)
DT   01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE)
DE   BRLA PROTEIN.
GN   BRLA.
OS   EMERICELLA NIDULANS (ASPERGILLUS NIDULANS).
OC   EUKARYOTA; FUNGI; ASCOMYCOTINA; PLECTOMYCETES; EUROTIALES.
RN   [1]
RP   SEQUENCE FROM N.A.
RM   88282543
RA   ADAMS T.H., BOYLAN M.T., TIMBERLAKE W.E.;
RL   CELL 54:353-362(1988).
CC   -!- FUNCTION: BRLA MEDIATES THE DEVELOPMENTAL SWITCH FROM THE
CC       INDETERMINATE, APICAL GROWTH PATTERN OF VEGETATIVE CELLS TO THE
CC       BUDDING GROWTH PATTERN OF CONIDIOPHORES. EXPRESSION OF BRLA
CC       LEADS TO ACTIVATION OF ABAA, WETA AND STUA CESSATION OF VEGETATIVE
CC       GROWTH, CELLULAR VACUOLIZATION AND SPORE FORMATION.
CC   -!- FUNCTION: BRLA, ABAA & WETA ARE PIVOTAL REGULATORS OF CONIDIOPHORE
CC       DEVELOPMENT AND CONIDIUM MATURATION. THEY ACT INDIVIDUALLY AND
CC       TOGETHER TO REGULATE THEIR OWN EXPRESSION AND THAT OF NUMEROUS
CC       OTHER SPORULATION-SPECIFIC GENES.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
DR   EMBL; M20631; ANBRLA.
DR   PIR; A28913; A28913.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2.
KW   ZINC-FINGER; METAL-BINDING; DNA-BINDING; DEVELOPMENTAL PROTEIN;
KW   CONIDIATION.
FT   DOMAIN      320    375       ZINC-FINGERS.
FT   ZN_FING     320    344       C2H2-TYPE.
FT   ZN_FING     350    375       C2H2-TYPE.
SQ   SEQUENCE   432 AA;  47932 MW;  963332 CN;
     MRNQSSLSDR LTVEVDCSSL GSNECPSMTS SFSPLESPTP TPTSIYSQGS LESPGWHGAG        60
     SLPNNTYERT PGSASMRSAF RLAGMASTES LGLPYGSMEG QERMPMPDFL SGYDENIEQL       120
     WMPSEAPKSY DHVAQGLAYH QGMHQYPTMA RNTNNNYRHQ AAAYLPESTT NPCLSRSIFH       180
     QPERVPSSMS SSMSMNNMLP WMNLGDSIAP QTIAPSQVGP VTPPPSYTDF PTSLSAFKQH       240
     SPTTPIRSCS LGTGSGADTP LSRLSGGPCE YMDDFQPSPV YRDGFQRPHR VASRKMLRRQ       300
     TSKQNLMLEN LPQVIKQVQF KCKEPGCNGR FKRQEHLKRH MKSHSKEKPH VCWVPGCHRA       360
     FSRSDNLNAH YTKTHSKRGG RNRYVATLDE NSPDYDPEFR GQLTPDGRPI YGSKLDDPIP       420
     GAGDMSLDGW DE                                                           432
//

ID   BTEB_RAT_z       STANDARD;      PRT;   244 AA.
AC   Q01713;
DT   01-APR-1993 (REL. 25, CREATED)
DT   01-APR-1993 (REL. 25, LAST SEQUENCE UPDATE)
DT   01-JUL-1993 (REL. 26, LAST ANNOTATION UPDATE)
DE   TRANSCRIPTION FACTOR BTEB (BASIC TRANSCRIPTION ELEMENT BINDING
DE   PROTEIN).
OS   RATTUS NORVEGICUS (RAT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=LIVER;
RM   93010958
RA   IMATAKA H., SOGAWA K., YASUMOTO K., KIKUCHI Y., SASANO K.,
RA   KOBAYASHI A., HAYAMI M., FUJII-KURIYAMA Y.;
RL   EMBO J. 11:3663-3671(1992).
CC   -!- FUNCTION: TRANSCRIPTION FACTOR THAT BINDS TO GC BOX PROMOTER
CC       ELEMENTS. SELECTIVELY ACTIVATES MRNA SYNTHESIS FROM GENES
CC       CONTAINING TANDEM REPEATS OF GC BOXES BUT REPRESSES GENES WITH
CC       A SINGLE GC BOX.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
DR   EMBL; D12769; RRD12769.
DR   PIR; JS0748; JS0748.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2.
KW   TRANSCRIPTION REGULATION; DNA-BINDING; NUCLEAR PROTEIN; REPEAT;
KW   ZINC-FINGER; METAL-BINDING.
FT   DOMAIN       84    116       ASP/GLU-RICH (ACIDIC).
FT   DOMAIN      143    225       ZINC-FINGERS.
FT   ZN_FING     143    167       C2H2-TYPE.
FT   ZN_FING     173    197       C2H2-TYPE.
FT   ZN_FING     203    225       C2H2-TYPE.
SQ   SEQUENCE   244 AA;  27155 MW;  313093 CN;
     MSAAAYMDFV AAQCLVSISN RAAVPEHGGA PDAERLRLPE REVTKEHGDP GDTWKDYCTL        60
     VTIAKSLLDL NKYRPIQTPS VCSDSLESPD EDIGSDSDVT TESGSSPSHS PEERQDSGSA       120
     PSPLSLLHSG VASKGKHASE KRHKCPYSGC GKVYGKSSHL KAHYRVHTGE RPFPCTWPDC       180
     LKKFSRSDEL TRHYRTHTGE KQFRCPLCEK RFMRSDHLTK HARRHTDFHP SMIKRSKKAL       240
     ASPL                                                                    244
//

ID   CF23_DROME_z     STANDARD;      PRT;   514 AA.
AC   Q01522;
DT   01-OCT-1993 (REL. 27, CREATED)
DT   01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE)
DT   01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE)
DE   CHORION TRANSCRIPTION FACTOR CF2, ISOFORM III.
GN   CF2.
OS   DROSOPHILA MELANOGASTER (FRUIT FLY).
OC   EUKARYOTA; METAZOA; ARTHROPODA; INSECTA; DIPTERA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=OREGON-R;
RM   93030711
RA   HSU T., GOGOS J.A., KIRSH S.A., KAFATOS F.C.;
RL   SCIENCE 257:1946-1950(1992).
CC   -!- FUNCTION: TRANSCRIPTIONAL REGULATOR. THE EXACT FUNCTION OF THIS
CC       ISOFORM IS NOT YET KNOWN.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- TISSUE SPECIFICITY: TESTIS.
CC   -!- ALTERNATIVE PRODUCTS: THREE DISTINCT ISOFORMS ARE PRODUCED FROM
CC       THE SAME GENE BY ALTERNATIVE SPLICING.
DR   EMBL; M97196; DMBPIS.
DR   FLYBASE; 00286; CF2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2.
KW   NUCLEAR PROTEIN; DNA-BINDING; ZINC-FINGER; TRANS-ACTING FACTOR;
KW   TRANSCRIPTION REGULATION; ALTERNATIVE SPLICING; REPEAT.
FT   ZN_FING      76     97       C2H2-TYPE.
FT   ZN_FING     127    138       C2H2-TYPE.
FT   ZN_FING     366    388       C2H2-TYPE.
SQ   SEQUENCE   514 AA;  56270 MW;  1232604 CN;
     MIKSTTNPQE QRLPRPEDQS PAPPPPPPSS ATTSTAAPAT PTHQVATVIA NMDTLKTAFL        60
     PNLSMDPNVH VSPHYCPMCH QQFERPQHVA DHMQLCHGIT LNAQGAIATL DGGHPQAQQH       120
     PKLSHPCFNC DEKFGNAVDL DEHHRLAHQT PAFLSRCLMC SIYGIHSATQ QPNEYKCTQC       180
     GSICTTAMLA AGQQGFMEQQ EAAVTPDDQL PAMAPRDMRL TPEEQHHQQQ LQAEHHHQQQ       240
     HQQQQQQQQQ QQESLEQQQR EMQEQAQQQQ VHHHQQDQDL AGDQVALKVP PLTVKLNKNA       300
     NGGAIVSHPQ VIIKEEPLSL SDSGDVVNSV PVYAIQANPG VPAPASSGVL VGTQTVPADL       360
     AHKIRHKCPD CPKTFKTPGT LAMHRKIHTG EAEREAVPLR LLREVLQREG LSDQAHTDAH       420
     RREAVHLSVL RQALHAAQRP HCAHDQAASA LGKAGRWPPV TRSCPSRSSS SYSSSKSFWS       480
     WCAAAVVRRH GYRSQEAICG GCGIGLGRTA AETG                                   514
//

ID   CID_DROME_z      STANDARD;      PRT;  1377 AA.
AC   P19538;
DT   01-NOV-1990 (REL. 16, CREATED)
DT   01-NOV-1990 (REL. 16, LAST SEQUENCE UPDATE)
DT   01-AUG-1992 (REL. 23, LAST ANNOTATION UPDATE)
DE   CUBITUS INTERRUPTUS DOMINANT PROTEIN.
GN   CI-D.
OS   DROSOPHILA MELANOGASTER (FRUIT FLY).
OC   EUKARYOTA; METAZOA; ARTHROPODA; INSECTA; DIPTERA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=OREGON-R;
RM   90346286
RA   ORENIC T.V., SLUSARSKI D.C., KROLL K.L., HOLMGREN R.A.;
RL   GENES DEV. 4:1053-1067(1990).
CC   -!- FUNCTION: INVOLVED IN SEGMENT POLARITY.
CC   -!- DEVELOPMENTAL STAGE: EXPRESSED UNIFORMLY THROUGHOUT THE BLASTODERM
CC       STAGE AND GASTRULATION AND DOES NOT RESOLVE INTO SEGMENTALLY
CC       REPEATING STRIPES UNTIL THE END OF THE SHORT PHASE OF GERM-BAND
CC       EXTENSION.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR.
CC   -!- SIMILARITY: TO THE GLI-RELATED GROUP OF C2H2-TYPE ZINC-FINGERS
CC       PROTEINS.
DR   EMBL; X54360; DMCID.
DR   PIR; A35817; A35817.
DR   PIR; S12769; S12769.
DR   FLYBASE; 04859; CI.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2.
KW   DEVELOPMENTAL PROTEIN; SEGMENTATION POLARITY PROTEIN; ZINC-FINGER;
KW   METAL-BINDING; DNA-BINDING; REPEAT; NUCLEAR PROTEIN.
FT   DOMAIN      451    603       ZINC-FINGERS.
FT   ZN_FING     451    476       C2H2-TYPE.
FT   ZN_FING     484    511       C2H2-TYPE.
FT   ZN_FING     517    541       C2H2-TYPE.
FT   ZN_FING     547    572       C2H2-TYPE.
FT   ZN_FING     578    603       C2H2-TYPE.
SQ   SEQUENCE   1377 AA;  150881 MW;  9823820 CN;
     MDAYALPTYF PLAYSELQFL ASRRAAAVAA AATVLPGSPC INQHHPTDVS SSVTVPSIIP        60
     TGGTSDSIKT SIQPQICNEN TLLGNAGHQH NHQPQHVHNI NVTGQPHDFH PAYRIPGYME       120
     QLYSLQRTNS ASSFHDPYVN CASAFHLAGL GLGSADFLGS RGLSSLGELH NAAVAAAAAG       180
     SLASTDFHFS VDGNRRLGSP RPPGGSIRAS ISRKRALSSS PYSDSFDINS MIRFSPNSLA       240
     TIMNGSRGSS AASGSYGHIS ATALNPMSHV HSTRLQQIQA HLLRASAGLL NPMTPQQVAA       300
     SGFSIGHMPT SASLRVNDVH PNLSDSHIQI TTSPTVTKDV SQVPAAAFSL KNLDDAREKK       360
     GPFKDVVPEQ PSSTSGGVAQ VEADSASSQL SDRCYNNVVN NITGIPGDVK VNSRLDEYIN       420
     CGSISIPSNE YDCANADTTD IKDEPGDFIE TNCHWRRCRI EFITQDELVK HINNDHIQTN       480
     KKAFVCRWED CTRGEKPFKA QYMLVVHMRR HTGEKPHKCT FEGCFKAYSR LENLKTHLRS       540
     HTGEKPYTCE YPGCSKAFSN ASDRAKHQNR THSNEKPYIC KAPGCTKRYT DPSSLRKHVK       600
     TVHGAEFYAN KKHKGLPLND ANSRLQQNNS RHNLQEHNID SSPCSEDSHL GKMLGTSSPS       660
     IKSESDISSS NHHLVNGVRA SDSLLTYSPD DLAENLNLDD GWNCDDDVDV ADLPIVLRAM       720
     VNIGNGNASA STIGGSVLAR QRFRGRLQTK GINSSTIMLC NIPESNRTFG ISELNQRITE       780
     LKMEPGTDAE IKIPKLPNTT IGGISEDPLQ NQTSFRNTVS NKQGTVSGSI QGQFRRDSQN       840
     STASTYYGSM QSRRSSQSSQ VSSIPTMRPN PSCNSTASFY DPISPGCSRR SSQMSNGANC       900
     NSFTSTSGLP VLNKESNKSL NACINKPNIG VQGVGIYNSS LPPPPSSHLI ATNLKRLQRK       960
     DSEYHNFSSG RFSVPSYMHS LHIKNNKPVG ENEFDKAIAS NARRQTDPVP NINLDPLTNI      1020
     SRFSTTPHSF DINVGKTNNI ASLINKDNLR KDLFTVSIKA DMAMTSDQHP NERINLDEVE      1080
     ELILPDEMLQ YLNLVKDDTN HLEKEHQAVP VGSNVSETIA SNHYREQSNI YYTNKQILTP      1140
     PSNVDIQPNT TFTVQDKFAM TAVGGSFSQR ELSTLAVPNE HGHAKCESFH HQSQKYMNTD      1200
     IGSKQQSALP SAHQRQTEKS NYNQIIDSSM TSLPELNVDS IYPRNETENI FKVHGDHDNE      1260
     IQCGIISQSQ MSPSTNLNND GQFSTVNMQP ITTSKLFPPE PQKIVCDTQA SNTSVMHLDT      1320
     YQRTLEYVQS CQNWMETNNT STNQIQSLPG MPVNNTLFPD VSSSTHPYHG TNMVINV         1377
//

ID   PC1_HUMAN      STANDARD;      PRT;   873 AA.
AC   P22413;
DT   01-AUG-1991 (REL. 19, CREATED)
DT   01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE)
DT   01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE)
DE   PLASMA-CELL MEMBRANE GLYCOPROTEIN PC-1 (ALKALINE PHOSPHODIESTERASE I
DE   (EC 3.1.4.1) / NUCLEOTIDE PYROPHOSPHATASE (EC 3.6.1.9)).
GN   PC1.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RM   91009202
RA   BUCKLEY M.F., LOVELAND K.A., MCKINSTRY W.J., GARSON O.M., GODING J.W.;
RL   J. BIOL. CHEM. 265:17506-17511(1990).
CC   -!- FUNCTION: MAY HAVE A ROLE IN THE REGULATION OF N-GLYCOSYLATION.
CC   -!- CATALYTIC ACTIVITY: HYDROLYTICALLY REMOVES 5'-NUCLEOTIDES
CC       SUCCESSIVELY FROM THE 3'-HYDROXY TERMINI OF 3'-HYDROXY-TERMINATED
CC       OLIGO-NUCLEOTIDES.
CC   -!- CATALYTIC ACTIVITY: A DINUCLEOTIDE + H(2)O = 2 MONONUCLEOTIDE.
CC   -!- SUBUNIT: HOMODIMER, DISULFIDE-LINKED.
CC   -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN.
CC   -!- TISSUE SPECIFICITY: EXPRESSED IN PLASMA CELLS AND ALSO IN A NUMBER
CC       OF NON-LYMPHOID TISSUES, INCLUDING THE DISTAL CONVOLUTED TUBULE
CC       OF THE KIDNEY, CHONDROCYTES, AND EPIDIDYMIS.
CC   -!- SIMILARITY: CONTAINS TWO TANDEM COPIES OF A SOMATOMEDIN-B TYPE
CC       DOMAIN.
DR   EMBL; M57736; HSPC1Q1.
DR   PIR; A39216; A39216.
DR   MIM; 173335; 11TH EDITION.
DR   PROSITE; PS00524; SOMATOMEDIN_B.
KW   GLYCOPROTEIN; TRANSMEMBRANE; DUPLICATION; SIGNAL-ANCHOR; HYDROLASE.
FT   DOMAIN        1     24       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM     25     45       SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN).
FT   DOMAIN       46    873       EXTRACELLULAR (POTENTIAL).
FT   DOMAIN       52     92       SOMATOMEDIN-B LIKE.
FT   DOMAIN       93    136       SOMATOMEDIN-B LIKE.
FT   CARBOHYD    127    127       POTENTIAL.
FT   CARBOHYD    233    233       POTENTIAL.
FT   CARBOHYD    289    289       POTENTIAL.
FT   CARBOHYD    425    425       POTENTIAL.
FT   CARBOHYD    533    533       POTENTIAL.
FT   CARBOHYD    591    591       POTENTIAL.
FT   CARBOHYD    648    648       POTENTIAL.
FT   CARBOHYD    679    679       POTENTIAL.
FT   CARBOHYD    696    696       POTENTIAL.
SQ   SEQUENCE   873 AA;  99929 MW;  4095996 CN;
>P1;PC1_HUMAN
    Length: 873
MDVGEEPLEK AARARTAKDP NTYKVLSLVL SVCVLTTILG CIFGLKPSCA KEVKSCKGRC
FERTFGNCRC DAACVELGNC CLDYQETCIE PEHIWTCNKF RCGEKRLTRS LCACSDDCKD
KGDCCINYSS VCQGEKSWVE EPCESINEPQ CPAGFETPPT LLFSLDGFRA EYLHTWGGLL
PVISKLKKCG TYTKNMRPVY PTKTFPNHYS IVTGLYPESH GIIDNKMYDP KMNASFSLKS
KEKFNPEWYK GEPIWVTAKY QGLKSGTFFW PGSDVEINGI FPDIYKMYNG SVPFEERILA
VLQWLQLPKD ERPHFYTLYL EEPDSSGHSY GPVSSEVIKA LQRVDGMVGM LMDGLKELNL
HRCLNLILIS DHGMEQGSCK KYIYLNKYLG DVKNIKVIYG PAARLRPSDV PDKYYSFNYE
GIARNLSCRE PNQHFKPYLK HFLPKRLHFA KSDRIEPLTF YLDPQWQLAL NPSERKYCGS
GFHGSDNVFS NMQALFVGYG PGFKHGIEAD TFENIEVYNL MCDLLNLTPA PNNGTHGSLN
HLLKNPVYTP KHPKEVHPLV QCPFTRNPRD NLGCSCNPSI LPIEDFQTQF NLTVAEEKII
KHETLPYGRP RVLQKENTIC LLSQHQFMSG YSQDILMPLW TSYTVDRNDS FSTEDFSNCL
YQDFRIPLSP VHKCSFYKNN TKVSYGFLSP PQLNKNSSGI YSEALLTTNI VPMYQSFQVI
WRYFHDTLLR KYAEERNGVN VVSGPVFDFD YDGRCDSLEN LRQKRRVIRN QEILIPTHFF
IVLTSCKDTS QTPLHCENLD TLAFILPHRT DNSESCVHGK HDSSWVEELL MLHRARITDV
EHITGLSFYQ QRKEPVSDIL KLKTHLPTFS QED
//
ID   PC1_MOUSE      STANDARD;      PRT;   871 AA.
AC   P06802;
DT   01-JAN-1988 (REL. 06, CREATED)
DT   01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE)
DT   01-FEB-1994 (REL. 28, LAST ANNOTATION UPDATE)
DE   PLASMA-CELL MEMBRANE GLYCOPROTEIN PC-1 (ALKALINE PHOSPHODIESTERASE I
DE   (EC 3.1.4.1) / NUCLEOTIDE PYROPHOSPHATASE (EC 3.6.1.9)) (LY-41).
OS   MUS MUSCULUS (MOUSE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RM   87165906
RA   VAN DRIEL I.R., GODING J.W.;
RL   J. BIOL. CHEM. 262:4882-4887(1987).
RN   [2]
RP   PARTIAL SEQUENCE.
RM   85056299
RA   STEARNE P.A., VAN DRIEL I.R., GREGO B., SIMPSON R.J., GODING J.W.;
RL   J. IMMUNOL. 134:443-448(1985).
RN   [3]
RP   FUNCTION, AND SEQUENCE FROM N.A.
RM   91271356
RA   REBBE N.F., TONG B.D., FINLEY E.M., HICKMAN S.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 88:5192-5196(1991).
CC   -!- FUNCTION: MAY HAVE A ROLE IN THE REGULATION OF N-GLYCOSYLATION.
CC   -!- CATALYTIC ACTIVITY: HYDROLYTICALLY REMOVES 5'-NUCLEOTIDES
CC       SUCCESSIVELY FROM THE 3'-HYDROXY TERMINI OF 3'-HYDROXY-TERMINATED
CC       OLIGO-NUCLEOTIDES.
CC   -!- CATALYTIC ACTIVITY: A DINUCLEOTIDE + H(2)O = 2 MONONUCLEOTIDE.
CC   -!- SUBUNIT: HOMODIMER, DISULFIDE-LINKED.
CC   -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN.
CC   -!- TISSUE SPECIFICITY: SELECTIVELY EXPRESSED ON THE SURFACE OF
CC       ANTIBODY-SECRETING CELLS.
CC   -!- SIMILARITY: CONTAINS TWO TANDEM COPIES OF A SOMATOMEDIN-B TYPE
CC       DOMAIN.
DR   EMBL; J02700; MMPC1B.
DR   PIR; A27410; A27410.
DR   PROSITE; PS00524; SOMATOMEDIN_B.
KW   GLYCOPROTEIN; TRANSMEMBRANE; DUPLICATION; SIGNAL-ANCHOR; HYDROLASE.
FT   MOD_RES      ?1     ?1       BLOCKED.
FT   DOMAIN        1     24       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM     25     45       SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN).
FT   DOMAIN       46    871       EXTRACELLULAR (POTENTIAL).
FT   DOMAIN       52     92       SOMATOMEDIN-B LIKE.
FT   DOMAIN       93    136       SOMATOMEDIN-B LIKE.
FT   CARBOHYD    127    127       POTENTIAL.
FT   CARBOHYD    233    233       POTENTIAL.
FT   CARBOHYD    289    289       POTENTIAL.
FT   CARBOHYD    425    425       POTENTIAL.
FT   CARBOHYD    533    533       POTENTIAL.
FT   CARBOHYD    590    590       POTENTIAL.
SQ   SEQUENCE   871 AA;  99487 MW;  4094440 CN;
>P1;PC1_MOUSE
    Length: 871
MDLGEEPLEK ADGARPAKDP NTYKVLSLVL SVCVLTTILG CIFGLKPSCA KEVKSCKGRC
FERTFSNCRC DAACVSLGNC CLDFQETCVE PTHIWTCNKF RCGEKRLSRF VCSCADDCKT
HNDCCINYSS VCQDKKSWVE ETCESIDTPE CPAEFESPPT LLFSLDGFRA EYLHTWGGLL
PVISKLKNCG TYTKNMRPMY PTKTFPNHYS IVTGLYPESH GIIDNKMYDP KMNASFSLKS
KEKFNPLWYK GQPIWVTANH QEVKSGTYFW PGSDVEIDGI LPDIYKVYNG SVPFEERILA
VLEWLQLPSH ERPHFYTLYL EEPDSSGHSH GPVSSEVIKA LQKVDRLVGM LMDGLKDLGL
DKCLNLILIS DHGMEQGSCK KYVYLNKYLG DVNNVKVVYG PAARLRPTDV PETYYSFNYE
ALAKNLSCRE PNQHFRPYLK PFLPKRLHFA KSDRIEPLTF YLDPQWQLAL NPSERKYCGS
GFHGSDNLFS NMQALFIGYG PAFKHGAEVD SFENIEVYNL MCDLLGLIPA PNNGSHGSLN
HLLKKPIYNP SHPKEEGFLS QCPIKSTSND LGCTCDPWIV PIKDFEKQLN LTTEDDDIYH
MTVPYGGPRI LLKQHHVCLL QQQQFLTGYS LDLLMPLWAS YTFLRNDQFS RDDFSNCMYQ
DLRIPLSPVH KCSYYKSNSK LSYGFLTPPR LNRVSNHIYS EALLTSNIVP MYQSFQVIWH
YLHDTLLQRY AHERNGINVV SGPVFDFDYD GRYDSLEILK QNSRVIRSQE ILIPTHFFIV
LTSCKQLSET PLECSALESS AYILPHRPDN IESCTHGKRE SSWVEELLTL HRARVTDVEL
ITGLSFYQDR QESVSELLRL KTHLPIFSQE D
//

ID   PP11_HUMAN     STANDARD;      PRT;   369 AA.
AC   P21128;
DT   01-FEB-1991 (REL. 17, CREATED)
DT   01-FEB-1991 (REL. 17, LAST SEQUENCE UPDATE)
DT   01-AUG-1991 (REL. 19, LAST ANNOTATION UPDATE)
DE   PLACENTAL PROTEIN 11 PRECURSOR (PP11) (EC 3.4.21.-).
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 19-29.
RC   TISSUE=PLACENTA;
RM   90274869
RA   GRUNDMANN U., ROEMISCH J., SIEBOLD B., BOHN H., AMANN E.;
RL   DNA CELL BIOL. 9:243-250(1990).
RN   [2]
RP   SOMATOMEDIN-B TYPE DOMAIN.
RM   91248172
RA   JENNE D.;
RL   BIOCHEM. BIOPHYS. RES. COMMUN. 176:1000-1006(1991).
CC   -!- FUNCTION: PROBABLE SERINE PROTEASE.
CC   -!- PLACENTAL PROTEIN 11 IS A PLACENTAL-SPECIFIC PROTEIN BUT IS
CC       ALSO ASSOCIATED WITH VARIOUS MALIGNANT NEOPLASMS.
CC   -!- SIMILARITY: CONTAINS ONE SOMATOMEDIN-B TYPE DOMAIN.
DR   EMBL; M36109; HSPP11AA.
DR   PIR; A34614; A34614.
DR   PROSITE; PS00524; SOMATOMEDIN_B.
KW   HYDROLASE; SERINE PROTEASE; SIGNAL.
FT   SIGNAL        1     18
FT   CHAIN        19    369       PLACENTAL PROTEIN 11.
FT   DOMAIN       45     89       SOMATOMEDIN-B LIKE.
SQ   SEQUENCE   369 AA;  42121 MW;  740291 CN;
>P1;PP11_HUMAN
    Length: 369
MRACISLVLA VLCGLAWAED HKESEPLPQL EEETEEALAS NLYSAPTSCQ GRCYEAFDKH
HQCHCNARCQ EFGNCCKDFE SLCSDHEVSH SSDAITKEEI QSISEKIYRA DTNKAQKEDI
VLNSQNCISP SETRNQVDRC PKPLFTYVNE KLFSKPTYAA FINLLNNYQR ATGHGEHFSA
QELAEQDAFL REIMKTAVMK ELYSFLHHQN RYGSEQEFVD DLKNMWFGLY SRGNEEGDSS
GFEHVFSGEV KKGKVTGFHN WIRFYLEEKE GLVDYYSHIY DGPWDSYPDV LAMQFNWDGY
YKEVGSAFIG SSPEFEFALY SLCFIARPGK VCQLSLGGYP LAVRTYTWDK STYGNGKKYI
ATAYIVSST
//

ID   VTNC_HUMAN     STANDARD;      PRT;   478 AA.
AC   P04004; P01141;
DT   23-OCT-1986 (REL. 02, CREATED)
DT   23-OCT-1986 (REL. 02, LAST SEQUENCE UPDATE)
DT   01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE)
DE   VITRONECTIN PRECURSOR (SERUM SPREADING FACTOR) (S-PROTEIN) (CONTAINS:
DE   SOMATOMEDIN B).
GN   VTN.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RM   86030229
RA   SUZUKI S., OLDBERG A., HAYMAN E.G., PIERSCHBACHER M.D., RUOSLAHTI E.;
RL   EMBO J. 4:2519-2524(1985).
RN   [2]
RP   REVISIONS.
RA   SUZUKI S., OLDBERG A., HAYMAN E.G., PIERSCHBACHER M.D., RUOSLAHTI E.;
RL   SUBMITTED (JUN-1986) TO THE PIR DATA BANK.
RN   [3]
RP   SEQUENCE FROM N.A.
RM   86135941
RA   JENNE D., STANLEY K.K.;
RL   EMBO J. 4:3153-3157(1985).
RN   [4]
RP   SEQUENCE FROM N.A.
RM   88107592
RA   JENNE D., STANLEY K.K.;
RL   BIOCHEMISTRY 26:6735-6742(1987).
RN   [5]
RP   SEQUENCE OF 20-63.
RM   78127267
RA   FRYKLUND L., SIEVERTSSON H.;
RL   FEBS LETT. 87:55-60(1978).
RN   [6]
RP   SEQUENCE OF 399-413.
RC   TISSUE=PLASMA;
RA   HOCHSTRASSER D.F., FRUTIGER S., PAQUET N., BAIROCH A., RAVIER F.,
RA   PASQUALI C., SANCHEZ J.-C., TISSOT J.-D., BJELLQVIST B., VARGAS R.,
RA   APPEL R.D., HUGHES G.J.;
RL   SUBMITTED (JUN-1992) TO THE SWISS-PROT DATA BANK.
RN   [7]
RP   SULFATATION.
RM   90060125
RA   JENNE D., HILLE A., STANLEY K.K., HUTTNER W.B.;
RL   EUR. J. BIOCHEM. 185:391-395(1989).
RN   [8]
RP   PHOSPHORYLATION.
RM   90353578
RA   CHAIN D., KORC-GRODZICKI B., KREIZMAN T., SHALTIEL S.;
RL   FEBS LETT. 269:221-225(1990).
CC   -!- FUNCTION: VITRONECTIN IS A CELL ADHESION AND SPREADING FACTOR
CC       FOUND IN SERUM AND TISSUES. VITRONECTIN INTERACT WITH
CC       GLYCOSAMYNOGLYCANS AND PROTEOGLYCANS. IS RECOGNIZED BY CERTAIN
CC       MEMBERS OF THE INTEGRIN FAMILY AND SERVES AS A CELL-TO-SUBSTRATE
CC       ADHESION MOLECULE. INHIBITOR OF THE MEMBRANE-DAMAGING EFFECT OF
CC       THE TERMINAL CYTOLYTIC COMPLEMENT PATHWAY.
CC   -!- FUNCTION: SOMATOMEDIN B IS A GROWTH HORMONE-DEPENDENT SERUM FACTOR
CC       WITH PROTEASE-INHIBITING ACTIVITY.
CC   -!- SUBUNIT: EXISTS IN TWO FORMS: A SINGLE CHAIN 75 KD FORM (V75) AND
CC       A CLIPPED FORM COMPOSED OF TWO CHAINS (65 KD AND 10 KD) (V65+10)
CC       WHICH ARE HELD TOGETHER BY A DISULFIDE BOND.
CC   -!- TISSUE SPECIFICITY: PLASMA.
CC   -!- SUBCELLULAR LOCATION: EXTRACELLULAR.
CC   -!- SIMILARITY: CONTAINS TWO HEMOPEXIN-LIKE DOMAINS.
CC   -!- SIMILARITY: CONTAINS ONE SOMATOMEDIN-B TYPE DOMAIN.
DR   EMBL; X03168; HSSPROT.
DR   EMBL; X05006; HSSPRO.
DR   PIR; A29744; SGHU1V.
DR   SWISS-2DPAGE; P04004; HUMAN.
DR   MIM; 193190; 11TH EDITION.
DR   PROSITE; PS00024; HEMOPEXIN.
DR   PROSITE; PS00524; SOMATOMEDIN_B.
KW   HEPARIN-BINDING; CELL ADHESION; GLYCOPROTEIN; SULFATATION; SIGNAL;
KW   PHOSPHORYLATION.
FT   SIGNAL        1     19
FT   CHAIN        20    478       VITRONECTIN (V75).
FT   CHAIN        20    398       V65 SUBUNIT.
FT   SITE        398    399       CLEAVAGE.
FT   CHAIN       399    478       V10 SUBUNIT.
FT   PEPTIDE      20     63       SOMATOMEDIN B.
FT   DOMAIN      150    287       HEMOPEXIN-LIKE 1.
FT   DOMAIN      288    478       HEMOPEXIN-LIKE 2.
FT   SITE         64     66       CELL ATTACHMENT SITE.
FT   CARBOHYD     86     86
FT   CARBOHYD    169    169
FT   CARBOHYD    242    242
FT   MOD_RES      75     75       SULFATATION.
FT   MOD_RES      78     78       SULFATATION.
FT   DISULFID    293    430
FT   BINDING     362    395       HEPARIN.
FT   MOD_RES     397    397       PHOSPHORYLATION (BY CAPK).
FT   CONFLICT     50     50       C -> N (IN REF. 5).
FT   CONFLICT    225    225       S -> N (IN REF. 3).
FT   CONFLICT    366    366       A -> T (IN REF. 3).
FT   CONFLICT    400    400       T -> M (IN REF. 3).
SQ   SEQUENCE   478 AA;  54305 MW;  1140198 CN;
>P1;VTNC_HUMAN
    Length: 478
MAPLRPLLIL ALLAWVALAD QESCKGRCTE GFNVDKKCQC DELCSYYQSC CTDYTAECKP
QVTRGDVFTM PEDEYTVYDD GEEKNNATVH EQVGGPSLTS DLQAQSKGNP EQTPVLKPEE
EAPAPEVGAS KPEGIDSRPE TLHPGRPQPP AEEELCSGKP FDAFTDLKNG SLFAFRGQYC
YELDEKAVRP GYPKLIRDVW GIEGPIDAAF TRINCQGKTY LFKGSQYWRF EDGVLDPDYP
RNISDGFDGI PDNVDAALAL PAHSYSGRER VYFFKGKQYW EYQFQHQPSQ EECEGSSLSA
VFEHFAMMQR DSWEDIFELL FWGRTSAGTR QPQFISRDWH GVPGQVDAAM AGRIYISGMA
PRPSLAKKQR FRHRNRKGYR SQRGHSRGRN QNSRRPSRAT WLSLFSSEES NLGANNYDDY
RMDWLVPATC EPIQSVFFFS GDKYYRVNLR TRRVDTVDPP YPRSIAQYWL GCPAPGHL
//

ID   VTNC_MOUSE     STANDARD;      PRT;   476 AA.
AC   P29788;
DT   01-APR-1993 (REL. 25, CREATED)
DT   01-APR-1993 (REL. 25, LAST SEQUENCE UPDATE)
DT   01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE)
DE   VITRONECTIN PRECURSOR (SERUM SPREADING FACTOR) (S-PROTEIN) (CONTAINS:
DE   SOMATOMEDIN B).
OS   MUS MUSCULUS (MOUSE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=BALB/C; TISSUE=LIVER;
RA   EHRLICH H.J., RICHTER B., VON DER AHE D., PREISSNER K.T.;
RL   SUBMITTED (NOV-1991) TO EMBL/GENBANK/DDBJ DATA BANKS.
CC   -!- FUNCTION: VITRONECTIN IS A CELL ADHESION AND SPREADING FACTOR
CC       FOUND IN SERUM AND TISSUES. VITRONECTIN INTERACT WITH
CC       GLYCOSAMYNOGLYCANS AND PROTEOGLYCANS. IS RECOGNIZED BY CERTAIN
CC       MEMBERS OF THE INTEGRIN FAMILY AND SERVES AS A CELL-TO-SUBSTRATE
CC       ADHESION MOLECULE. INHIBITOR OF THE MEMBRANE-DAMAGING EFFECT OF
CC       THE TERMINAL CYTOLYTIC COMPLEMENT PATHWAY.
CC   -!- FUNCTION: SOMATOMEDIN B IS A GROWTH HORMONE-DEPENDENT SERUM FACTOR
CC       WITH PROTEASE-INHIBITING ACTIVITY.
CC   -!- TISSUE SPECIFICITY: PLASMA.
CC   -!- SUBCELLULAR LOCATION: EXTRACELLULAR.
CC   -!- SIMILARITY: CONTAINS TWO HEMOPEXIN-LIKE DOMAINS.
CC   -!- SIMILARITY: CONTAINS ONE SOMATOMEDIN-B TYPE DOMAIN.
DR   EMBL; X63003; MMVITN.
DR   PIR; S19894; SGMSV.
DR   PROSITE; PS00024; HEMOPEXIN.
DR   PROSITE; PS00524; SOMATOMEDIN_B.
KW   HEPARIN-BINDING; CELL ADHESION; GLYCOPROTEIN; SULFATATION; SIGNAL;
KW   PHOSPHORYLATION.
FT   SIGNAL        1     19       BY SIMILARITY.
FT   CHAIN        20    476       VITRONECTIN.
FT   DOMAIN       20     63       SOMATOMEDIN-B LIKE.
FT   DOMAIN      150    285       HEMOPEXIN-LIKE 1.
FT   DOMAIN      286    476       HEMOPEXIN-LIKE 2.
FT   SITE         64     66       CELL ATTACHMENT SITE.
FT   MOD_RES      75     75       SULFATATION (BY SIMILARITY).
FT   MOD_RES      78     78       SULFATATION (BY SIMILARITY).
FT   CARBOHYD     86     86       POTENTIAL.
FT   CARBOHYD    168    168       POTENTIAL.
FT   CARBOHYD    241    241       POTENTIAL.
FT   DISULFID    291    430       BY SIMILARITY.
FT   BINDING     365    398       HEPARIN (BY SIMILARITY).
FT   MOD_RES     397    397       PHOSPHORYLATION (BY CAPK)
FT                                (BY SIMILARITY).
SQ   SEQUENCE   476 AA;  54690 MW;  1180023 CN;
>P1;VTNC_MOUSE
    Length: 476
MAPLRPFFIL ALVAWVSLAD QESCKGRCTQ GFMASKKCQC DELCTYYQSC CADYMEQCKP
QVTRGDVFTM PEDDYWSYDY VEEPKNNTNT GVQPENTSPP GDLNPRTDGT LKPTAFLDPE
EQPSTPAPKV EQQEEILRPD TTDQGTPEFP EEELCSGKPF DAFTDLKNGS LFAFRGQYCY
ELDETAVRPG YPKLIQDVWG IEGPIDAAFT RINCQGKTYL FKGSQYWRFE DGVLDPGYPR
NISEGFSGIP DNVDAFALPA HRYSGRERVY FFKGKQYWEY EFQQQPSQEE CEGSSLSAVF
EHFALLQRDS WENIFELLFW GRSSDGAREP QFISRNWHGV PGKVDAAMAG RIYVTGSLSH
SAQAKKQKSK RRSRKRYRSR RGRGHRRSQS SNSRRSSRSI WFSLFSSEES GLGTYNNYDY
DMDWLVPATC EPIQVYFFSG DKYYRVNLRT RRVDSVNPPY PRSIAQYWLG CPTSEK
//

ID   VTNC_RABIT     STANDARD;      PRT;   475 AA.
AC   P22458;
DT   01-AUG-1991 (REL. 19, CREATED)
DT   01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE)
DT   01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE)
DE   VITRONECTIN PRECURSOR (SERUM SPREADING FACTOR) (S-PROTEIN)
DE   (GLYCOPROTEIN 66).
OS   ORYCTOLAGUS CUNICULUS (RABBIT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; LAGOMORPHA.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 1-24.
RM   91065939
RA   SATO R., KOMINE Y., IMANAKA T., TAKANO T.;
RL   J. BIOL. CHEM. 265:21232-21236(1990).
CC   -!- FUNCTION: VITRONECTIN IS A CELL ADHESION AND SPREADING FACTOR
CC       FOUND IN SERUM AND TISSUES. VITRONECTIN INTERACT WITH
CC       GLYCOSAMYNOGLYCANS AND PROTEOGLYCANS. IS RECOGNIZED BY CERTAIN
CC       MEMBERS OF THE INTEGRIN FAMILY AND SERVES AS A CELL-TO-SUBSTRATE
CC       ADHESION MOLECULE. INHIBITOR OF THE MEMBRANE-DAMAGING EFFECT OF
CC       THE TERMINAL CYTOLYTIC COMPLEMENT PATHWAY.
CC   -!- TISSUE SPECIFICITY: PLASMA.
CC   -!- SUBCELLULAR LOCATION: EXTRACELLULAR.
CC   -!- SUBUNIT: MONOMER.
CC   -!- SIMILARITY: CONTAINS TWO HEMOPEXIN-LIKE DOMAINS.
CC   -!- SIMILARITY: CONTAINS ONE SOMATOMEDIN-B TYPE DOMAIN.
DR   EMBL; M55442; OCGP66.
DR   PIR; A38340; A38340.
DR   PROSITE; PS00024; HEMOPEXIN.
DR   PROSITE; PS00524; SOMATOMEDIN_B.
KW   HEPARIN-BINDING; CELL ADHESION; GLYCOPROTEIN; SULFATATION; SIGNAL.
FT   SIGNAL        1     19
FT   CHAIN        20    475       VITRONECTIN.
FT   DOMAIN       20     63       SOMATOMEDIN-B LIKE.
FT   DOMAIN      150    287       HEMOPEXIN-LIKE 1.
FT   DOMAIN      288    475       HEMOPEXIN-LIKE 2.
FT   DOMAIN      366    392       GLYCOSAMINOGLYCAN BINDING REGION.
FT   SITE         64     66       CELL ATTACHMENT SITE.
FT   MOD_RES      75     75       SULFATATION (BY SIMILARITY).
FT   MOD_RES      78     78       SULFATATION (BY SIMILARITY).
FT   CARBOHYD     87     87       PROBABLE.
FT   CARBOHYD    169    169       PROBABLE.
FT   CARBOHYD    242    242       PROBABLE.
SQ   SEQUENCE   475 AA;  53943 MW;  1180132 CN;
>P1;VTNC_RABIT
    Length: 475
MAPLRPIFTL ALLLWVVLAD QESCKDRCTE GFNANRKCQC DELCSYYQSC CADYAAECKP
QVTRGDVFTM PEDEYGPYDY IEQTKDNASV HAQPESPTVG QEPTLSPDLQ TEGGAEPTHE
VPLEPEMETL RPEGEDLQAG TTELGTSASP AEEELCSGKP FDAFTDLKNG SLFAFRGQYC
YELDETAVRP GYPKLIQDVW GIEGPIDAAF TRINCQGKTY LFKGSQYWRF EDGILDPDYP
RNISEGFSGI PDNVDAAFAL PAHSYSGRER VYFFKGDKYW EYQFQQQPSQ EECEGSSLSA
VFEHFAMLHR DSWEDIFKLL FWGRPSGGAR QPQFISRDWH GVPGKVDAAM AGRIYISGLT
PSPSAKKQKS RRRSRKRYRS RYGRGRSQNS RRLSRSISRL WFSSEEVSLG PYNYEDYETS
WLKPATSEPI QSVYFFSGDK YYRVNLRTQR VDTVNPPYPR SIAQYWLGCP APGGQ
//