VTNC_RABIT
ID VTNC_RABIT Reviewed; 475 AA.
AC P22458;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Vitronectin;
DE Short=VN;
DE AltName: Full=Glycoprotein 66;
DE AltName: Full=S-protein;
DE AltName: Full=Serum-spreading factor;
DE Flags: Precursor;
GN Name=VTN;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1701177; DOI=10.1016/s0021-9258(17)45350-6;
RA Sato R., Komine Y., Imanaka T., Takano T.;
RT "Monoclonal antibody EMR1a/212D recognizing site of deposition of
RT extracellular lipid in atherosclerosis. Isolation and characterization of a
RT cDNA clone for the antigen.";
RL J. Biol. Chem. 265:21232-21236(1990).
RN [2]
RP PROTEIN SEQUENCE OF 20-44, AND GLYCOSYLATION.
RX PubMed=1372829; DOI=10.1016/0167-4838(92)90417-c;
RA Nakashima N., Miyazaki K., Ishikawa M., Yatohgo T., Ogawa H., Uchibori H.,
RA Matsumoto I., Seno N., Hayashi M.;
RT "Vitronectin diversity in evolution but uniformity in ligand binding and
RT size of the core polypeptide.";
RL Biochim. Biophys. Acta 1120:1-10(1992).
CC -!- FUNCTION: Vitronectin is a cell adhesion and spreading factor found in
CC serum and tissues. Vitronectin interact with glycosaminoglycans and
CC proteoglycans. Is recognized by certain members of the integrin family
CC and serves as a cell-to-substrate adhesion molecule. Inhibitor of the
CC membrane-damaging effect of the terminal cytolytic complement pathway.
CC -!- SUBUNIT: Interacts with SERPINE1/PAI1 and C1QBP (By similarity).
CC Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- DOMAIN: The SMB domain mediates interaction with SERPINE1/PAI1.
CC {ECO:0000250}.
CC -!- PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:P04004}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:1372829}.
CC -!- PTM: It has been suggested that the active SMB domain may be permitted
CC considerable disulfide bond heterogeneity or variability, thus two
CC alternate disulfide patterns based on 3D structures are described with
CC 1 disulfide bond conserved in both.
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DR EMBL; M55442; AAA31258.1; -; mRNA.
DR PIR; A38340; A38340.
DR RefSeq; NP_001075761.1; NM_001082292.1.
DR AlphaFoldDB; P22458; -.
DR SMR; P22458; -.
DR CORUM; P22458; -.
DR STRING; 9986.ENSOCUP00000024132; -.
DR iPTMnet; P22458; -.
DR PRIDE; P22458; -.
DR GeneID; 100009128; -.
DR KEGG; ocu:100009128; -.
DR CTD; 7448; -.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; P22458; -.
DR OrthoDB; 419397at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR CDD; cd00094; HX; 1.
DR Gene3D; 2.110.10.10; -; 2.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR018486; Hemopexin_CS.
DR InterPro; IPR020436; SMB_chordata.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF01033; Somatomedin_B; 1.
DR PRINTS; PR00022; SOMATOMEDINB.
DR SMART; SM00120; HX; 4.
DR SMART; SM00201; SO; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR SUPFAM; SSF90188; SSF90188; 1.
DR PROSITE; PS00024; HEMOPEXIN; 2.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00524; SMB_1; 1.
DR PROSITE; PS50958; SMB_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Heparin-binding; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal; Sulfation.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1372829"
FT CHAIN 20..475
FT /note="Vitronectin"
FT /id="PRO_0000036400"
FT DOMAIN 20..63
FT /note="SMB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT REPEAT 158..202
FT /note="Hemopexin 1"
FT REPEAT 203..250
FT /note="Hemopexin 2"
FT REPEAT 251..305
FT /note="Hemopexin 3"
FT REPEAT 419..469
FT /note="Hemopexin 4"
FT REGION 87..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..392
FT /note="Glycosaminoglycan binding region"
FT MOTIF 64..66
FT /note="Cell attachment site"
FT COMPBIAS 87..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..388
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04004"
FT MOD_RES 75
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 78
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 80
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 279
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 282
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04004"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04004"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:1372829"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:1372829"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:1372829"
FT DISULFID 24..40
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 24..28
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 28..58
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 38..51
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 38..40
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 44..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 51..58
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT CONFLICT 26
FT /note="D -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 34..35
FT /note="AN -> SD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="C -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 53943 MW; D5D1F31B8C2FA12D CRC64;
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
