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P22458

- VTNC_RABIT

UniProt

P22458 - VTNC_RABIT

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Protein
Vitronectin
Gene
VTN
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. polysaccharide binding Source: InterPro
  3. scavenger receptor activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. immune response Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Vitronectin
Short name:
VN
Alternative name(s):
Glycoprotein 66
S-protein
Serum-spreading factor
Gene namesi
Name:VTN
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 Publication
Add
BLAST
Chaini20 – 475456Vitronectin
PRO_0000036400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 40Alternate; alternate By similarity
Disulfide bondi24 ↔ 28Alternate; alternate By similarity
Disulfide bondi28 ↔ 58Alternate; alternate By similarity
Disulfide bondi38 ↔ 51Alternate; alternate By similarity
Disulfide bondi38 ↔ 40Alternate; alternate By similarity
Disulfide bondi44 ↔ 50 By similarity
Disulfide bondi51 ↔ 58Alternate; alternate By similarity
Modified residuei69 – 691Phosphothreonine By similarity
Modified residuei75 – 751Sulfotyrosine Reviewed prediction
Modified residuei78 – 781Sulfotyrosine Reviewed prediction
Modified residuei80 – 801Sulfotyrosine Reviewed prediction
Glycosylationi87 – 871N-linked (GlcNAc...) Inferred
Glycosylationi169 – 1691N-linked (GlcNAc...) Inferred
Glycosylationi242 – 2421N-linked (GlcNAc...) Inferred
Modified residuei279 – 2791Sulfotyrosine Reviewed prediction
Modified residuei282 – 2821Sulfotyrosine Reviewed prediction
Modified residuei312 – 3121Phosphoserine By similarity
Modified residuei394 – 3941Phosphoserine By similarity

Post-translational modificationi

Sulfated on 2 tyrosine residues By similarity.
N- and O-glycosylated.1 Publication
It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Expressioni

Tissue specificityi

Plasma.

Interactioni

Subunit structurei

Interacts with SERPINE1/PAI1 and C1QBP By similarity. Monomer.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000024132.

Structurei

3D structure databases

ProteinModelPortaliP22458.
SMRiP22458. Positions 20-70.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 6344SMB
Add
BLAST
Repeati158 – 20245Hemopexin 1
Add
BLAST
Repeati203 – 25048Hemopexin 2
Add
BLAST
Repeati251 – 30555Hemopexin 3
Add
BLAST
Repeati419 – 46951Hemopexin 4
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 39227Glycosaminoglycan binding region
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi64 – 663Cell attachment site

Domaini

The SMB domain mediates interaction with SERPINE1/PAI1 By similarity.

Sequence similaritiesi

Contains 4 hemopexin repeats.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG245064.
HOGENOMiHOG000133161.
HOVERGENiHBG002902.

Family and domain databases

Gene3Di2.110.10.10. 3 hits.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF01033. Somatomedin_B. 1 hit.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00120. HX. 4 hits.
SM00201. SO. 1 hit.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 3 hits.
PROSITEiPS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22458-1 [UniParc]FASTAAdd to Basket

« Hide

MAPLRPIFTL ALLLWVVLAD QESCKDRCTE GFNANRKCQC DELCSYYQSC    50
CADYAAECKP QVTRGDVFTM PEDEYGPYDY IEQTKDNASV HAQPESPTVG 100
QEPTLSPDLQ TEGGAEPTHE VPLEPEMETL RPEGEDLQAG TTELGTSASP 150
AEEELCSGKP FDAFTDLKNG SLFAFRGQYC YELDETAVRP GYPKLIQDVW 200
GIEGPIDAAF TRINCQGKTY LFKGSQYWRF EDGILDPDYP RNISEGFSGI 250
PDNVDAAFAL PAHSYSGRER VYFFKGDKYW EYQFQQQPSQ EECEGSSLSA 300
VFEHFAMLHR DSWEDIFKLL FWGRPSGGAR QPQFISRDWH GVPGKVDAAM 350
AGRIYISGLT PSPSAKKQKS RRRSRKRYRS RYGRGRSQNS RRLSRSISRL 400
WFSSEEVSLG PYNYEDYETS WLKPATSEPI QSVYFFSGDK YYRVNLRTQR 450
VDTVNPPYPR SIAQYWLGCP APGGQ 475
Length:475
Mass (Da):53,943
Last modified:August 1, 1991 - v1
Checksum:iD5D1F31B8C2FA12D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261D → G AA sequence 1 Publication
Sequence conflicti34 – 352AN → SD AA sequence 1 Publication
Sequence conflicti44 – 441C → P AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55442 mRNA. Translation: AAA31258.1.
PIRiA38340.
RefSeqiNP_001075761.1. NM_001082292.1.
UniGeneiOcu.1882.

Genome annotation databases

GeneIDi100009128.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55442 mRNA. Translation: AAA31258.1 .
PIRi A38340.
RefSeqi NP_001075761.1. NM_001082292.1.
UniGenei Ocu.1882.

3D structure databases

ProteinModelPortali P22458.
SMRi P22458. Positions 20-70.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000024132.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009128.

Organism-specific databases

CTDi 7448.

Phylogenomic databases

eggNOGi NOG245064.
HOGENOMi HOG000133161.
HOVERGENi HBG002902.

Family and domain databases

Gene3Di 2.110.10.10. 3 hits.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view ]
Pfami PF00045. Hemopexin. 4 hits.
PF01033. Somatomedin_B. 1 hit.
[Graphical view ]
PRINTSi PR00022. SOMATOMEDINB.
SMARTi SM00120. HX. 4 hits.
SM00201. SO. 1 hit.
[Graphical view ]
SUPFAMi SSF50923. SSF50923. 3 hits.
PROSITEi PS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Monoclonal antibody EMR1a/212D recognizing site of deposition of extracellular lipid in atherosclerosis. Isolation and characterization of a cDNA clone for the antigen."
    Sato R., Komine Y., Imanaka T., Takano T.
    J. Biol. Chem. 265:21232-21236(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Vitronectin diversity in evolution but uniformity in ligand binding and size of the core polypeptide."
    Nakashima N., Miyazaki K., Ishikawa M., Yatohgo T., Ogawa H., Uchibori H., Matsumoto I., Seno N., Hayashi M.
    Biochim. Biophys. Acta 1120:1-10(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-44, GLYCOSYLATION.

Entry informationi

Entry nameiVTNC_RABIT
AccessioniPrimary (citable) accession number: P22458
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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