VTNC_PIG
ID VTNC_PIG Reviewed; 459 AA.
AC P48819;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Vitronectin;
DE Short=VN;
DE AltName: Full=S-protein;
DE AltName: Full=Serum-spreading factor;
DE Flags: Precursor;
GN Name=VTN;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8982862; DOI=10.1093/oxfordjournals.jbchem.a021512;
RA Yoneda A., Kojima K., Matsumoto I., Yamamoto K., Ogawa H.;
RT "Porcine vitronectin, the most compact form of single-chain vitronectin:
RT the smallest molecular mass among vitronectins was ascribed to deletion and
RT substitution of base pairs, and proteolytic trimming of the peptide.";
RL J. Biochem. 120:954-960(1996).
RN [2]
RP PROTEIN SEQUENCE OF 20-44.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with SERPINE1/PAI1 and C1QBP (By
CC similarity). {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:0000250}.
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; D63145; BAA09630.1; -; mRNA.
DR PIR; JC5139; JC5139.
DR RefSeq; NP_999269.1; NM_214104.1.
DR AlphaFoldDB; P48819; -.
DR SMR; P48819; -.
DR STRING; 9823.ENSSSCP00000025875; -.
DR GlyConnect; 624; 18 N-Linked glycans.
DR PaxDb; P48819; -.
DR PeptideAtlas; P48819; -.
DR PRIDE; P48819; -.
DR Ensembl; ENSSSCT00005057711; ENSSSCP00005035566; ENSSSCG00005036184.
DR Ensembl; ENSSSCT00005057747; ENSSSCP00005035585; ENSSSCG00005036184.
DR Ensembl; ENSSSCT00025081975; ENSSSCP00025035576; ENSSSCG00025059518.
DR Ensembl; ENSSSCT00035086772; ENSSSCP00035036171; ENSSSCG00035064407.
DR Ensembl; ENSSSCT00055001958; ENSSSCP00055001475; ENSSSCG00055001101.
DR Ensembl; ENSSSCT00055001978; ENSSSCP00055001488; ENSSSCG00055001101.
DR Ensembl; ENSSSCT00065106107; ENSSSCP00065047173; ENSSSCG00065076697.
DR Ensembl; ENSSSCT00065106142; ENSSSCP00065047196; ENSSSCG00065076697.
DR GeneID; 397192; -.
DR KEGG; ssc:397192; -.
DR CTD; 7448; -.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; P48819; -.
DR OrthoDB; 419397at2759; -.
DR Reactome; R-SSC-2129379; Molecules associated with elastic fibres.
DR Reactome; R-SSC-216083; Integrin cell surface interactions.
DR Reactome; R-SSC-3000170; Syndecan interactions.
DR Reactome; R-SSC-3000178; ECM proteoglycans.
DR Reactome; R-SSC-977606; Regulation of Complement cascade.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
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:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
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; 1.
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..459
FT /note="Vitronectin"
FT /id="PRO_0000036399"
FT DOMAIN 20..63
FT /note="SMB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT REPEAT 135..179
FT /note="Hemopexin 1"
FT REPEAT 180..227
FT /note="Hemopexin 2"
FT REPEAT 228..285
FT /note="Hemopexin 3"
FT REPEAT 400..453
FT /note="Hemopexin 4"
FT REGION 338..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 64..66
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 348..375
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04004"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04004"
FT MOD_RES 398
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 401
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 44
FT /note="C -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 52572 MW; 630E134B0DC706BE CRC64;
MAPLRPLLML ALLAWVALAD QESCKGRCTD GFIAERKCQC DELCSYYQSC CTDYVAECKP
QVTRGDVFLQ PDDEYRAYDY HEETRHNTSV QEEQRIPVLL AKTEETPVLK PEEEAPPPGP
QTDDLGVPEE ELCSGKPFDA FTNLKNGSVF AFRGLYCYEL DEKAVRPGYP KLIQDVWGIK
GPIDAAFTRI NCQGKTYLFK GSQYWRFDDG VLDPNYPREI SEGFKGIPDD VDAALALPAH
SYSGRERVYF FKGKQYWEYV FQQQPSREEC EGSSPSDVFA HFALMQRDSW EDIFRLLFWS
HSFGGAIEPR VISQDWLGLP EQVDAAMAGQ IYISGSALKP SQPKMTKSAR RSGKRYRSRR
GRGRGRGHSR SQKSHRQSRS TWLPWFSSEE TGPGGYNYDD YKMDWLVPAT CEPIQSVYFF
SGEEYYRVNL RTQRVDTVTP PYPRSIAQYW LGCPVPDQK
