Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P22458

- VTNC_RABIT

UniProt

P22458 - VTNC_RABIT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 475456VitronectinPRO_0000036400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 40Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi24 ↔ 28Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi28 ↔ 58Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi38 ↔ 51Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi38 ↔ 40Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi44 ↔ 50PROSITE-ProRule annotation
Disulfide bondi51 ↔ 58Alternate; alternatePROSITE-ProRule annotation
Modified residuei69 – 691PhosphothreonineBy similarity
Modified residuei75 – 751SulfotyrosineSequence Analysis
Modified residuei78 – 781SulfotyrosineSequence Analysis
Modified residuei80 – 801SulfotyrosineSequence Analysis
Glycosylationi87 – 871N-linked (GlcNAc...)1 Publication
Glycosylationi169 – 1691N-linked (GlcNAc...)1 Publication
Glycosylationi242 – 2421N-linked (GlcNAc...)1 Publication
Modified residuei279 – 2791SulfotyrosineSequence Analysis
Modified residuei282 – 2821SulfotyrosineSequence Analysis
Modified residuei312 – 3121PhosphoserineBy similarity
Modified residuei394 – 3941PhosphoserineBy 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.By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000024132.

Structurei

3D structure databases

ProteinModelPortaliP22458.
SMRiP22458. Positions 20-70.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 39227Glycosaminoglycan binding regionAdd
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.Curated
Contains 1 SMB (somatomedin-B) domain.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG245064.
HOGENOMiHOG000133161.
HOVERGENiHBG002902.
InParanoidiP22458.

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

        10         20         30         40         50
MAPLRPIFTL ALLLWVVLAD QESCKDRCTE GFNANRKCQC DELCSYYQSC
60 70 80 90 100
CADYAAECKP QVTRGDVFTM PEDEYGPYDY IEQTKDNASV HAQPESPTVG
110 120 130 140 150
QEPTLSPDLQ TEGGAEPTHE VPLEPEMETL RPEGEDLQAG TTELGTSASP
160 170 180 190 200
AEEELCSGKP FDAFTDLKNG SLFAFRGQYC YELDETAVRP GYPKLIQDVW
210 220 230 240 250
GIEGPIDAAF TRINCQGKTY LFKGSQYWRF EDGILDPDYP RNISEGFSGI
260 270 280 290 300
PDNVDAAFAL PAHSYSGRER VYFFKGDKYW EYQFQQQPSQ EECEGSSLSA
310 320 330 340 350
VFEHFAMLHR DSWEDIFKLL FWGRPSGGAR QPQFISRDWH GVPGKVDAAM
360 370 380 390 400
AGRIYISGLT PSPSAKKQKS RRRSRKRYRS RYGRGRSQNS RRLSRSISRL
410 420 430 440 450
WFSSEEVSLG PYNYEDYETS WLKPATSEPI QSVYFFSGDK YYRVNLRTQR
460 470
VDTVNPPYPR SIAQYWLGCP APGGQ
Length:475
Mass (Da):53,943
Last modified:August 1, 1991 - v1
Checksum:iD5D1F31B8C2FA12D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261D → G AA sequence (PubMed:1372829)Curated
Sequence conflicti34 – 352AN → SD AA sequence (PubMed:1372829)Curated
Sequence conflicti44 – 441C → P AA sequence (PubMed:1372829)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi 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.
InParanoidi P22458.

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: October 29, 2014
This is version 111 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