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   24-JAN-2024, entry version 146.
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   GlyCosmos; P22458; 3 sites, No reported glycans.
DR   iPTMnet; P22458; -.
DR   PaxDb; 9986-ENSOCUP00000024132; -.
DR   GeneID; 100009128; -.
DR   KEGG; ocu:100009128; -.
DR   CTD; 7448; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   InParanoid; P22458; -.
DR   OrthoDB; 5310951at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; 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; 4.10.410.20; -; 1.
DR   Gene3D; 2.110.10.10; Hemopexin-like domain; 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   PANTHER; PTHR22917; HEMOPEXIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22917:SF3; VITRONECTIN; 1.
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; Hemopexin-like domain; 1.
DR   SUPFAM; SSF90188; Somatomedin B domain; 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
//