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Integrin alpha-5 (CD49 antigen-like family member E) (Fibronectin receptor subunit alpha) (Integrin alpha-F) (VLA-5) (CD antigen CD49e) [Cleaved into: Integrin alpha-5 heavy chain; Integrin alpha-5 light chain]

 ITA5_HUMAN              Reviewed;        1049 AA.
P08648; Q96HA5;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
10-OCT-2002, sequence version 2.
25-OCT-2017, entry version 200.
RecName: Full=Integrin alpha-5;
AltName: Full=CD49 antigen-like family member E;
AltName: Full=Fibronectin receptor subunit alpha;
AltName: Full=Integrin alpha-F;
AltName: Full=VLA-5;
AltName: CD_antigen=CD49e;
Contains:
RecName: Full=Integrin alpha-5 heavy chain;
Contains:
RecName: Full=Integrin alpha-5 light chain;
Flags: Precursor;
Name=ITGA5; Synonyms=FNRA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2958481; DOI=10.1083/jcb.105.3.1183;
Argraves W.S., Suzuki S., Arai H., Thompson K., Pierschbacher M.D.,
Ruoslahti E.;
"Amino acid sequence of the human fibronectin receptor.";
J. Cell Biol. 105:1183-1190(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-73.
PubMed=1834647;
Birkenmeier T.M., McQuillan J.J., Boedeker E.D., Argraves W.S.,
Ruoslahti E., Dean D.C.;
"The alpha 5 beta 1 fibronectin receptor. Characterization of the
alpha 5 gene promoter.";
J. Biol. Chem. 266:20544-20549(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 16-1049.
PubMed=2450560; DOI=10.1021/bi00399a021;
Fitzgerald L.A., Poncz M., Steiner B., Rall S.C., Bennett J.S.,
Phillips D.R.;
"Comparison of cDNA-derived protein sequences of the human fibronectin
and vitronectin receptor alpha-subunits and platelet glycoprotein
IIb.";
Biochemistry 26:8158-8165(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 821-1049.
PubMed=2944883;
Argraves W.S., Pytela R., Suzuki S., Millan J.L., Pierschbacher M.D.,
Ruoslahti E.;
"cDNA sequences from the alpha subunit of the fibronectin receptor
predict a transmembrane domain and a short cytoplasmic peptide.";
J. Biol. Chem. 261:12922-12924(1986).
[6]
PROTEIN SEQUENCE OF 42-55.
PubMed=3033641; DOI=10.1073/pnas.84.10.3239;
Takada Y., Strominger J.L., Hemler M.E.;
"The very late antigen family of heterodimers is part of a superfamily
of molecules involved in adhesion and embryogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 84:3239-3243(1987).
[7]
INTERACTION WITH HIV-1 TAT.
PubMed=10397733;
Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S.,
Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.;
"The Tat protein of human immunodeficiency virus type-1 promotes
vascular cell growth and locomotion by engaging the alpha5beta1 and
alphavbeta3 integrins and by mobilizing sequestered basic fibroblast
growth factor.";
Blood 94:663-672(1999).
[8]
INTERACTION WITH NISCH.
PubMed=11912194; DOI=10.1074/jbc.M111838200;
Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.;
"Insulin receptor substrate 4 associates with the protein IRAS.";
J. Biol. Chem. 277:19439-19447(2002).
[9]
DISULFIDE BONDS.
PubMed=14596610; DOI=10.1021/bi034726u;
Krokhin O.V., Cheng K., Sousa S.L., Ens W., Standing K.G.,
Wilkins J.A.;
"Mass spectrometric based mapping of the disulfide bonding patterns of
integrin alpha chains.";
Biochemistry 42:12950-12959(2003).
[10]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN PARVOVIRUS
B19 CAPSID PROTEIN.
PubMed=12907437; DOI=10.1182/blood-2003-05-1522;
Weigel-Kelley K.A., Yoder M.C., Srivastava A.;
"Alpha5beta1 integrin as a cellular coreceptor for human parvovirus
B19: requirement of functional activation of beta1 integrin for viral
entry.";
Blood 102:3927-3933(2003).
[11]
INTERACTION WITH NOV.
PubMed=12695522; DOI=10.1074/jbc.M302028200;
Lin C.G., Leu S.J., Chen N., Tebeau C.M., Lin S.X., Yeung C.Y.,
Lau L.F.;
"CCN3 (NOV) is a novel angiogenic regulator of the CCN protein
family.";
J. Biol. Chem. 278:24200-24208(2003).
[12]
FUNCTION, AND INTERACTION WITH FBN1.
PubMed=12807887; DOI=10.1074/jbc.M303159200;
Bax D.V., Bernard S.E., Lomas A., Morgan A., Humphries J.,
Shuttleworth C.A., Humphries M.J., Kielty C.M.;
"Cell adhesion to fibrillin-1 molecules and microfibrils is mediated
by alpha 5 beta 1 and alpha v beta 3 integrins.";
J. Biol. Chem. 278:34605-34616(2003).
[13]
INTERACTION WITH COMP.
PubMed=16051604; DOI=10.1074/jbc.M504778200;
Chen F.-H., Thomas A.O., Hecht J.T., Goldring M.B., Lawler J.;
"Cartilage oligomeric matrix protein/thrombospondin 5 supports
chondrocyte attachment through interaction with integrins.";
J. Biol. Chem. 280:32655-32661(2005).
[14]
INTERACTION WITH RAB21.
PubMed=16754960; DOI=10.1083/jcb.200509019;
Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M.,
Ivaska J.;
"Small GTPase Rab21 regulates cell adhesion and controls endosomal
traffic of beta1-integrins.";
J. Cell Biol. 173:767-780(2006).
[15]
FUNCTION, INTERACTION WITH FBN1, AND SUBCELLULAR LOCATION.
PubMed=17158881; DOI=10.1074/jbc.M607008200;
Jovanovic J., Takagi J., Choulier L., Abrescia N.G., Stuart D.I.,
van der Merwe P.A., Mardon H.J., Handford P.A.;
"alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative
studies of molecular determinants underlying integrin-rgd affinity and
specificity.";
J. Biol. Chem. 282:6743-6751(2007).
[16]
FUNCTION.
PubMed=18635536; DOI=10.1074/jbc.M804835200;
Saegusa J., Akakura N., Wu C.Y., Hoogland C., Ma Z., Lam K.S.,
Liu F.T., Takada Y.K., Takada Y.;
"Pro-inflammatory secretory phospholipase A2 type IIA binds to
integrins alphavbeta3 and alpha4beta1 and induces proliferation of
monocytic cells in an integrin-dependent manner.";
J. Biol. Chem. 283:26107-26115(2008).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297; ASN-307; ASN-675 AND
ASN-773.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297; ASN-307; ASN-771 AND
ASN-773.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PROTEOLYTIC CLEAVAGE BY PCSK5.
PubMed=22740495; DOI=10.1093/humrep/des203;
Paule S., Aljofan M., Simon C., Rombauts L.J., Nie G.;
"Cleavage of endometrial alpha-integrins into their functional forms
is mediated by proprotein convertase 5/6.";
Hum. Reprod. 27:2766-2774(2012).
[21]
INTERACTION WITH CIB1.
PubMed=24011356; DOI=10.1021/bi400678y;
Freeman T.C. Jr., Black J.L., Bray H.G., Dagliyan O., Wu Y.I.,
Tripathy A., Dokholyan N.V., Leisner T.M., Parise L.V.;
"Identification of novel integrin binding partners for calcium and
integrin binding protein 1 (CIB1): structural and thermodynamic basis
of CIB1 promiscuity.";
Biochemistry 52:7082-7090(2013).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN
METAPNEUMOVIRUS FUSION PROTEIN.
PubMed=24478423; DOI=10.1128/JVI.03491-13;
Wei Y., Zhang Y., Cai H., Mirza A.M., Iorio R.M., Peeples M.E.,
Niewiesk S., Li J.;
"Roles of the putative integrin-binding motif of the human
metapneumovirus fusion (f) protein in cell-cell fusion, viral
infectivity, and pathogenesis.";
J. Virol. 88:4338-4352(2014).
[25]
FUNCTION.
PubMed=25398877; DOI=10.1074/jbc.M114.579946;
Fujita M., Zhu K., Fujita C.K., Zhao M., Lam K.S., Kurth M.J.,
Takada Y.K., Takada Y.;
"Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces
integrin activation through direct binding to a newly identified
binding site (site 2) in integrins alphavbeta3, alpha4beta1, and
alpha5beta1.";
J. Biol. Chem. 290:259-271(2015).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[27]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 42-664 IN COMPLEX WITH
ANTIBODY; ITGB1 AND RGD PEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT
ASN-84; ASN-182; ASN-297; ASN-307; ASN-316 AND ASN-609,
SUBSTRATE-BINDING SITES, CALCIUM-BINDING SITES, AND SUBUNIT.
PubMed=22451694; DOI=10.1083/jcb.201111077;
Nagae M., Re S., Mihara E., Nogi T., Sugita Y., Takagi J.;
"Crystal structure of alpha5beta1 integrin ectodomain: atomic details
of the fibronectin receptor.";
J. Cell Biol. 197:131-140(2012).
-!- FUNCTION: Integrin alpha-5/beta-1 is a receptor for fibronectin
and fibrinogen. It recognizes the sequence R-G-D in its ligands.
ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct
from the classical ligand-binding site (site 1) and this induces
integrin conformational changes and enhanced ligand binding to
site 1 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a
receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell
adhesion to FBN1 (PubMed:12807887, PubMed:17158881).
{ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:17158881,
ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:25398877}.
-!- FUNCTION: (Microbial infection) Integrin ITGA5:ITGB1 acts as a
receptor for human metapneumovirus (PubMed:12907437). Integrin
ITGA2:ITGB1 acts as a receptor for human parvovirus B19
(PubMed:24478423). In case of HIV-1 infection, the interaction
with extracellular viral Tat protein seems to enhance angiogenesis
in Kaposi's sarcoma lesions (PubMed:10397733).
{ECO:0000269|PubMed:10397733, ECO:0000269|PubMed:12907437,
ECO:0000269|PubMed:24478423}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
subunit is composed of a heavy and a light chain linked by a
disulfide bond. Alpha-5 associates with beta-1. Interacts with
HPS5 and NISCH. Interacts with RAB21 and COMP. Interacts with
CIB1. ITGA5:ITGB1 interacts with NOV. ITGA5:ITGB1 interacts with
FBN1 (PubMed:12807887, PubMed:17158881).
{ECO:0000269|PubMed:11912194, ECO:0000269|PubMed:12695522,
ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:16051604,
ECO:0000269|PubMed:16754960, ECO:0000269|PubMed:17158881,
ECO:0000269|PubMed:22451694, ECO:0000269|PubMed:24011356}.
-!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB1 interacts with
human metapneumovirus fusion protein.
{ECO:0000269|PubMed:12907437}.
-!- SUBUNIT: (Microbial infection) Integrin ITGA2:ITGB1 interacts with
human parvovirus B19 capsid proteins.
{ECO:0000269|PubMed:24478423}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
{ECO:0000269|PubMed:10397733}.
-!- INTERACTION:
P17813:ENG; NbExp=4; IntAct=EBI-1382311, EBI-2834630;
P05556:ITGB1; NbExp=5; IntAct=EBI-1382311, EBI-703066;
O14786:NRP1; NbExp=2; IntAct=EBI-1382311, EBI-1187100;
P97333:Nrp1 (xeno); NbExp=3; IntAct=EBI-1382311, EBI-1555129;
Q9H0F6:SHARPIN; NbExp=4; IntAct=EBI-1382311, EBI-3942966;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Cell junction, focal adhesion
{ECO:0000269|PubMed:17158881}. Cell surface
{ECO:0000269|PubMed:17158881}.
-!- PTM: Proteolytic cleavage by PCSK5 mediates activation of the
precursor. {ECO:0000269|PubMed:22740495}.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
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EMBL; X06256; CAA29601.1; -; mRNA.
EMBL; BC008786; AAH08786.1; -; mRNA.
EMBL; M13918; AAA52467.1; ALT_SEQ; mRNA.
CCDS; CCDS8880.1; -.
PIR; A27079; A27079.
RefSeq; NP_002196.4; NM_002205.4.
UniGene; Hs.505654; -.
PDB; 3VI3; X-ray; 2.90 A; A/C=42-664.
PDB; 3VI4; X-ray; 2.90 A; A/C=42-664.
PDB; 4WJK; X-ray; 1.85 A; A=42-491.
PDB; 4WK0; X-ray; 1.78 A; A=42-491.
PDB; 4WK2; X-ray; 2.50 A; A=42-491.
PDB; 4WK4; X-ray; 2.50 A; A=42-491.
PDBsum; 3VI3; -.
PDBsum; 3VI4; -.
PDBsum; 4WJK; -.
PDBsum; 4WK0; -.
PDBsum; 4WK2; -.
PDBsum; 4WK4; -.
ProteinModelPortal; P08648; -.
SMR; P08648; -.
BioGrid; 109884; 35.
CORUM; P08648; -.
DIP; DIP-40037N; -.
ELM; P08648; -.
IntAct; P08648; 20.
MINT; MINT-5005934; -.
STRING; 9606.ENSP00000293379; -.
BindingDB; P08648; -.
ChEMBL; CHEMBL3955; -.
iPTMnet; P08648; -.
PhosphoSitePlus; P08648; -.
SwissPalm; P08648; -.
UniCarbKB; P08648; -.
BioMuta; ITGA5; -.
DMDM; 23831237; -.
EPD; P08648; -.
MaxQB; P08648; -.
PaxDb; P08648; -.
PeptideAtlas; P08648; -.
PRIDE; P08648; -.
TopDownProteomics; P08648; -.
DNASU; 3678; -.
Ensembl; ENST00000293379; ENSP00000293379; ENSG00000161638.
GeneID; 3678; -.
KEGG; hsa:3678; -.
UCSC; uc001sga.4; human.
CTD; 3678; -.
DisGeNET; 3678; -.
EuPathDB; HostDB:ENSG00000161638.10; -.
GeneCards; ITGA5; -.
HGNC; HGNC:6141; ITGA5.
HPA; CAB009008; -.
HPA; HPA002642; -.
MIM; 135620; gene.
neXtProt; NX_P08648; -.
OpenTargets; ENSG00000161638; -.
PharmGKB; PA29941; -.
eggNOG; KOG3637; Eukaryota.
eggNOG; ENOG410XPVZ; LUCA.
GeneTree; ENSGT00760000118782; -.
HOGENOM; HOG000231603; -.
HOVERGEN; HBG006186; -.
InParanoid; P08648; -.
KO; K06484; -.
OMA; PAMFNPE; -.
OrthoDB; EOG091G05Z4; -.
PhylomeDB; P08648; -.
TreeFam; TF105391; -.
Reactome; R-HSA-1566948; Elastic fibre formation.
Reactome; R-HSA-1566977; Fibronectin matrix formation.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-445144; Signal transduction by L1.
SignaLink; P08648; -.
SIGNOR; P08648; -.
ChiTaRS; ITGA5; human.
GeneWiki; ITGA5; -.
GenomeRNAi; 3678; -.
PRO; PR:P08648; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000161638; -.
CleanEx; HS_ITGA5; -.
ExpressionAtlas; P08648; baseline and differential.
Genevisible; P08648; HS.
GO; GO:0071062; C:alphav-beta3 integrin-vitronectin complex; TAS:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0008305; C:integrin complex; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0001726; C:ruffle; TAS:HGNC.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; TAS:BHF-UCL.
GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; TAS:BHF-UCL.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0001525; P:angiogenesis; TAS:BHF-UCL.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
GO; GO:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
GO; GO:0035987; P:endodermal cell differentiation; IMP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IMP:BHF-UCL.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; TAS:BHF-UCL.
GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEP:BHF-UCL.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR032695; Integrin_dom.
Pfam; PF01839; FG-GAP; 2.
Pfam; PF08441; Integrin_alpha2; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SUPFAM; SSF69179; SSF69179; 3.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cell adhesion; Cell junction;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Integrin;
Membrane; Metal-binding; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 41 {ECO:0000269|PubMed:3033641}.
CHAIN 42 1049 Integrin alpha-5.
/FTId=PRO_0000016249.
CHAIN 42 894 Integrin alpha-5 heavy chain.
/FTId=PRO_0000016250.
CHAIN 895 1049 Integrin alpha-5 light chain.
/FTId=PRO_0000016251.
TOPO_DOM 42 995 Extracellular. {ECO:0000255}.
TRANSMEM 996 1021 Helical. {ECO:0000255}.
TOPO_DOM 1022 1049 Cytoplasmic. {ECO:0000255}.
REPEAT 43 108 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 128 188 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 192 245 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 259 311 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 312 377 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 378 437 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 441 504 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 280 288
CA_BIND 334 342
CA_BIND 401 409
CA_BIND 465 473
REGION 1021 1028 Interaction with HPS5.
MOTIF 1024 1028 GFFKR motif.
METAL 280 280 Calcium 1.
METAL 282 282 Calcium 1.
METAL 284 284 Calcium 1.
METAL 286 286 Calcium 1; via carbonyl oxygen.
METAL 288 288 Calcium 1.
METAL 334 334 Calcium 2.
METAL 336 336 Calcium 2.
METAL 338 338 Calcium 2.
METAL 340 340 Calcium 2; via carbonyl oxygen.
METAL 342 342 Calcium 2.
METAL 401 401 Calcium 3.
METAL 403 403 Calcium 3.
METAL 405 405 Calcium 3.
METAL 407 407 Calcium 3; via carbonyl oxygen.
METAL 409 409 Calcium 3.
METAL 465 465 Calcium 4.
METAL 467 467 Calcium 4.
METAL 469 469 Calcium 4.
METAL 471 471 Calcium 4; via carbonyl oxygen.
METAL 473 473 Calcium 4.
BINDING 262 262 Arg of R-G-D substrate.
BINDING 269 269 Arg of R-G-D substrate.
MOD_RES 127 127 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22451694}.
CARBOHYD 182 182 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22451694}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:22451694}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:22451694}.
CARBOHYD 316 316 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22451694}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 530 530 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 593 593 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 609 609 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22451694}.
CARBOHYD 675 675 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 712 712 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 724 724 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 771 771 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 773 773 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 868 868 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 99 108
DISULFID 156 176
DISULFID 192 205
DISULFID 513 522
DISULFID 528 584
DISULFID 645 651
DISULFID 718 731
DISULFID 869 921 Interchain (between heavy and light
chains).
DISULFID 911 916
VARIANT 585 585 R -> I (in dbSNP:rs12318746).
/FTId=VAR_049631.
CONFLICT 26 26 L -> V (in Ref. 1 and 3). {ECO:0000305}.
CONFLICT 33 33 L -> V (in Ref. 1 and 3). {ECO:0000305}.
STRAND 50 53 {ECO:0000244|PDB:4WK0}.
TURN 56 61 {ECO:0000244|PDB:4WK0}.
STRAND 62 67 {ECO:0000244|PDB:4WK0}.
STRAND 69 71 {ECO:0000244|PDB:4WK0}.
STRAND 75 80 {ECO:0000244|PDB:4WK0}.
STRAND 95 101 {ECO:0000244|PDB:4WK0}.
STRAND 102 104 {ECO:0000244|PDB:4WJK}.
STRAND 109 111 {ECO:0000244|PDB:4WK2}.
HELIX 122 124 {ECO:0000244|PDB:4WK0}.
STRAND 125 130 {ECO:0000244|PDB:4WK0}.
STRAND 133 136 {ECO:0000244|PDB:4WK0}.
STRAND 144 149 {ECO:0000244|PDB:4WK0}.
STRAND 152 157 {ECO:0000244|PDB:4WK0}.
STRAND 165 167 {ECO:0000244|PDB:4WK0}.
STRAND 175 180 {ECO:0000244|PDB:4WK0}.
TURN 181 184 {ECO:0000244|PDB:4WK0}.
STRAND 185 189 {ECO:0000244|PDB:4WK0}.
STRAND 193 196 {ECO:0000244|PDB:4WK0}.
TURN 198 204 {ECO:0000244|PDB:4WK0}.
STRAND 209 213 {ECO:0000244|PDB:4WK0}.
STRAND 219 223 {ECO:0000244|PDB:4WK0}.
HELIX 226 229 {ECO:0000244|PDB:4WK0}.
STRAND 231 236 {ECO:0000244|PDB:4WK0}.
HELIX 238 243 {ECO:0000244|PDB:4WK0}.
STRAND 249 251 {ECO:0000244|PDB:4WK4}.
HELIX 265 267 {ECO:0000244|PDB:4WK0}.
STRAND 274 279 {ECO:0000244|PDB:4WK0}.
STRAND 282 286 {ECO:0000244|PDB:4WK0}.
STRAND 288 293 {ECO:0000244|PDB:4WK0}.
TURN 294 300 {ECO:0000244|PDB:4WK0}.
STRAND 302 306 {ECO:0000244|PDB:4WK0}.
TURN 308 310 {ECO:0000244|PDB:4WK0}.
STRAND 313 318 {ECO:0000244|PDB:4WK0}.
STRAND 328 333 {ECO:0000244|PDB:4WK0}.
STRAND 335 339 {ECO:0000244|PDB:4WK0}.
STRAND 342 347 {ECO:0000244|PDB:4WK0}.
STRAND 351 353 {ECO:0000244|PDB:4WK0}.
STRAND 359 361 {ECO:0000244|PDB:4WK0}.
STRAND 364 368 {ECO:0000244|PDB:4WK0}.
STRAND 380 384 {ECO:0000244|PDB:4WK0}.
HELIX 392 394 {ECO:0000244|PDB:3VI3}.
STRAND 396 400 {ECO:0000244|PDB:4WK0}.
STRAND 405 407 {ECO:0000244|PDB:4WK0}.
STRAND 409 414 {ECO:0000244|PDB:4WK0}.
STRAND 424 428 {ECO:0000244|PDB:4WK0}.
STRAND 440 443 {ECO:0000244|PDB:4WK0}.
STRAND 458 464 {ECO:0000244|PDB:4WK0}.
STRAND 466 471 {ECO:0000244|PDB:4WK0}.
STRAND 473 478 {ECO:0000244|PDB:4WK0}.
HELIX 479 481 {ECO:0000244|PDB:4WK0}.
STRAND 483 487 {ECO:0000244|PDB:4WK0}.
STRAND 492 503 {ECO:0000244|PDB:3VI3}.
STRAND 513 520 {ECO:0000244|PDB:3VI3}.
STRAND 522 532 {ECO:0000244|PDB:3VI3}.
STRAND 534 536 {ECO:0000244|PDB:3VI3}.
STRAND 538 548 {ECO:0000244|PDB:3VI3}.
TURN 549 555 {ECO:0000244|PDB:3VI3}.
STRAND 560 562 {ECO:0000244|PDB:3VI3}.
TURN 563 565 {ECO:0000244|PDB:3VI3}.
STRAND 566 577 {ECO:0000244|PDB:3VI3}.
STRAND 583 591 {ECO:0000244|PDB:3VI3}.
STRAND 604 612 {ECO:0000244|PDB:3VI3}.
STRAND 614 616 {ECO:0000244|PDB:3VI3}.
STRAND 620 622 {ECO:0000244|PDB:3VI3}.
STRAND 634 641 {ECO:0000244|PDB:3VI3}.
SEQUENCE 1049 AA; 114536 MW; 6B4D558D4F739CBA CRC64;
MGSRTPESPL HAVQLRWGPR RRPPLLPLLL LLLPPPPRVG GFNLDAEAPA VLSGPPGSFF
GFSVEFYRPG TDGVSVLVGA PKANTSQPGV LQGGAVYLCP WGASPTQCTP IEFDSKGSRL
LESSLSSSEG EEPVEYKSLQ WFGATVRAHG SSILACAPLY SWRTEKEPLS DPVGTCYLST
DNFTRILEYA PCRSDFSWAA GQGYCQGGFS AEFTKTGRVV LGGPGSYFWQ GQILSATQEQ
IAESYYPEYL INLVQGQLQT RQASSIYDDS YLGYSVAVGE FSGDDTEDFV AGVPKGNLTY
GYVTILNGSD IRSLYNFSGE QMASYFGYAV AATDVNGDGL DDLLVGAPLL MDRTPDGRPQ
EVGRVYVYLQ HPAGIEPTPT LTLTGHDEFG RFGSSLTPLG DLDQDGYNDV AIGAPFGGET
QQGVVFVFPG GPGGLGSKPS QVLQPLWAAS HTPDFFGSAL RGGRDLDGNG YPDLIVGSFG
VDKAVVYRGR PIVSASASLT IFPAMFNPEE RSCSLEGNPV ACINLSFCLN ASGKHVADSI
GFTVELQLDW QKQKGGVRRA LFLASRQATL TQTLLIQNGA REDCREMKIY LRNESEFRDK
LSPIHIALNF SLDPQAPVDS HGLRPALHYQ SKSRIEDKAQ ILLDCGEDNI CVPDLQLEVF
GEQNHVYLGD KNALNLTFHA QNVGEGGAYE AELRVTAPPE AEYSGLVRHP GNFSSLSCDY
FAVNQSRLLV CDLGNPMKAG ASLWGGLRFT VPHLRDTKKT IQFDFQILSK NLNNSQSDVV
SFRLSVEAQA QVTLNGVSKP EAVLFPVSDW HPRDQPQKEE DLGPAVHHVY ELINQGPSSI
SQGVLELSCP QALEGQQLLY VTRVTGLNCT TNHPINPKGL ELDPEGSLHH QQKREAPSRS
SASSGPQILK CPEAECFRLR CELGPLHQQE SQSLQLHFRV WAKTFLQREH QPFSLQCEAV
YKALKMPYRI LPRQLPQKER QVATAVQWTK AEGSYGVPLW IIILAILFGL LLLGLLIYIL
YKLGFFKRSL PYGTAMEKAQ LKPPATSDA


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