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Integrin alpha-3 (CD49 antigen-like family member C) (FRP-2) (Galactoprotein B3) (GAPB3) (VLA-3 subunit alpha) (CD antigen CD49c) [Cleaved into: Integrin alpha-3 heavy chain; Integrin alpha-3 light chain]

 ITA3_HUMAN              Reviewed;        1051 AA.
P26006; A7E246; B7ZM80; B9EGQ1; D3DTX4; D3DTX5;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
21-SEP-2011, sequence version 5.
10-OCT-2018, entry version 197.
RecName: Full=Integrin alpha-3;
AltName: Full=CD49 antigen-like family member C;
AltName: Full=FRP-2;
AltName: Full=Galactoprotein B3;
Short=GAPB3;
AltName: Full=VLA-3 subunit alpha;
AltName: CD_antigen=CD49c;
Contains:
RecName: Full=Integrin alpha-3 heavy chain;
Contains:
RecName: Full=Integrin alpha-3 light chain;
Flags: Precursor;
Name=ITGA3; Synonyms=MSK18;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=1655803; DOI=10.1083/jcb.115.1.257;
Takada Y., Murphy E., Pil P., Chen C., Ginsberg M.H., Hemler M.E.;
"Molecular cloning and expression of the cDNA for alpha 3 subunit of
human alpha 3 beta 1 (VLA-3), an integrin receptor for fibronectin,
laminin, and collagen.";
J. Cell Biol. 115:257-266(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 33-1051 (ISOFORM 1).
TISSUE=Fibroblast;
PubMed=1714443;
Tsuji T., Hakomori S., Osawa T.;
"Identification of human galactoprotein b3, an oncogenic
transformation-induced membrane glycoprotein, as VLA-3 alpha subunit:
the primary structure of human integrin alpha 3.";
J. Biochem. 109:659-665(1991).
[7]
PROTEIN SEQUENCE OF 33-49.
PubMed=8187758;
Ohta H., Tsurudome M., Matsumura H., Koga Y., Morikawa S., Kawano M.,
Kusugawa S., Komada H., Nishio M., Ito Y.;
"Molecular and biological characterization of fusion regulatory
proteins (FRPs): anti-FRP mAbs induced HIV-mediated cell fusion via an
integrin system.";
EMBO J. 13:2044-2055(1994).
[8]
PROTEIN SEQUENCE OF 33-46.
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).
[9]
PROTEIN SEQUENCE OF 33-40, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
AND INTERACTION WITH FAP.
PubMed=10455171; DOI=10.1074/jbc.274.35.24947;
Mueller S.C., Ghersi G., Akiyama S.K., Sang Q.X., Howard L.,
Pineiro-Sanchez M., Nakahara H., Yeh Y., Chen W.T.;
"A novel protease-docking function of integrin at invadopodia.";
J. Biol. Chem. 274:24947-24952(1999).
[10]
ALTERNATIVE SPLICING, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=9111516;
de Melker A.A., Sterk L.M., Delwel G.O., Fles D.L., Daams H.,
Weening J.J., Sonnenberg A.;
"The A and B variants of the alpha 3 integrin subunit: tissue
distribution and functional characterization.";
Lab. Invest. 76:547-563(1997).
[11]
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).
[12]
PALMITOYLATION AT CYS-1016, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
CYS-1016.
PubMed=15611341; DOI=10.1083/jcb.200404100;
Yang X., Kovalenko O.V., Tang W., Claas C., Stipp C.S., Hemler M.E.;
"Palmitoylation supports assembly and function of integrin-tetraspanin
complexes.";
J. Cell Biol. 167:1231-1240(2004).
[13]
INTERACTION WITH ITGB1; LGALS3 AND CSPG4, AND FUNCTION.
PubMed=15181153; DOI=10.1091/mbc.E04-03-0236;
Fukushi J., Makagiansar I.T., Stallcup W.B.;
"NG2 proteoglycan promotes endothelial cell motility and angiogenesis
via engagement of galectin-3 and alpha3beta1 integrin.";
Mol. Biol. Cell 15:3580-3590(2004).
[14]
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).
[15]
VARIANT ILNEB PRO-628.
PubMed=22512483; DOI=10.1056/NEJMoa1110813;
Has C., Sparta G., Kiritsi D., Weibel L., Moeller A., Vega-Warner V.,
Waters A., He Y., Anikster Y., Esser P., Straub B.K., Hausser I.,
Bockenhauer D., Dekel B., Hildebrandt F., Bruckner-Tuderman L.,
Laube G.F.;
"Integrin alpha3 mutations with kidney, lung, and skin disease.";
N. Engl. J. Med. 366:1508-1514(2012).
[16]
VARIANTS ILNEB ARG-125 AND GLN-274.
PubMed=27717396; DOI=10.1186/s13023-016-0514-z;
Colombo E.A., Spaccini L., Volpi L., Negri G., Cittaro D.,
Lazarevic D., Zirpoli S., Farolfi A., Gervasini C., Cubellis M.V.,
Larizza L.;
"Viable phenotype of ILNEB syndrome without nephrotic impairment in
siblings heterozygous for unreported integrin alpha3 mutations.";
Orphanet J. Rare Dis. 11:136-136(2016).
-!- FUNCTION: Integrin alpha-3/beta-1 is a receptor for fibronectin,
laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin
alpha-3/beta-1 provides a docking site for FAP (seprase) at
invadopodia plasma membranes in a collagen-dependent manner and
hence may participate in the adhesion, formation of invadopodia
and matrix degradation processes, promoting cell invasion. Alpha-
3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of
endothelial cells migration. {ECO:0000269|PubMed:10455171,
ECO:0000269|PubMed:15181153}.
-!- 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-3 associates with beta-1. Interacts with
HPS5. Interacts with FAP (seprase); the interaction occurs at the
cell surface of invadopodia membrane in a collagen-dependent
manner. {ECO:0000269|PubMed:10455171,
ECO:0000269|PubMed:15181153}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15611341};
Single-pass type I membrane protein {ECO:0000255}. Cell membrane
{ECO:0000269|PubMed:15611341}; Lipid-anchor
{ECO:0000269|PubMed:15611341}. Cell projection, invadopodium
membrane {ECO:0000269|PubMed:10455171}; Single-pass type I
membrane protein {ECO:0000255}. Cell projection, filopodium
membrane {ECO:0000269|PubMed:10455171}; Single-pass type I
membrane protein {ECO:0000255}. Note=Enriched preferentially at
invadopodia, cell membrane protrusions that correspond to sites of
cell invasion, in a collagen-dependent manner.
{ECO:0000269|PubMed:10455171}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Alpha-3A;
IsoId=P26006-2; Sequence=Displayed;
Name=2; Synonyms=Alpha-3B;
IsoId=P26006-1; Sequence=VSP_002721;
-!- TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 is
expressed in brain and heart. In brain, both isoforms are
exclusively expressed on vascular smooth muscle cells, whereas in
heart isoform 1 is strongly expressed on vascular smooth muscle
cells, isoform 2 is detected only on endothelial vein cells.
{ECO:0000269|PubMed:9111516}.
-!- PTM: Isoform 1, but not isoform 2, is phosphorylated on serine
residues. Phosphorylation increases after phorbol 12-myristate 13-
acetate stimulation. {ECO:0000269|PubMed:9111516}.
-!- DISEASE: Interstitial lung disease, nephrotic syndrome, and
epidermolysis bullosa, congenital (ILNEB) [MIM:614748]: A
multiorgan disorder characterized by congenital nephrotic
syndrome, interstitial lung disease, and epidermolysis bullosa.
The respiratory and renal features predominate, and lung
involvement accounts for the lethal course of the disease.
{ECO:0000269|PubMed:22512483, ECO:0000269|PubMed:27717396}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
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EMBL; M59911; AAA36120.1; -; mRNA.
EMBL; AK289961; BAF82650.1; -; mRNA.
EMBL; AC002401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94645.1; -; Genomic_DNA.
EMBL; CH471109; EAW94646.1; -; Genomic_DNA.
EMBL; CH471109; EAW94647.1; -; Genomic_DNA.
EMBL; CH471109; EAW94648.1; -; Genomic_DNA.
EMBL; BC136636; AAI36637.1; -; mRNA.
EMBL; BC144328; AAI44329.1; -; mRNA.
EMBL; BC150190; AAI50191.1; -; mRNA.
EMBL; D01038; BAA00845.1; -; mRNA.
CCDS; CCDS11558.1; -. [P26006-2]
PIR; A40021; A40021.
RefSeq; NP_002195.1; NM_002204.3. [P26006-2]
UniGene; Hs.265829; -.
UniGene; Hs.660689; -.
ProteinModelPortal; P26006; -.
BioGrid; 109882; 17.
ComplexPortal; CPX-1797; Integrin alpha3-beta1 complex.
CORUM; P26006; -.
DIP; DIP-140N; -.
IntAct; P26006; 7.
MINT; P26006; -.
STRING; 9606.ENSP00000007722; -.
BindingDB; P26006; -.
ChEMBL; CHEMBL3525; -.
GuidetoPHARMACOLOGY; 2442; -.
GlyConnect; 738; -.
iPTMnet; P26006; -.
PhosphoSitePlus; P26006; -.
SwissPalm; P26006; -.
UniCarbKB; P26006; -.
BioMuta; ITGA3; -.
DMDM; 347595830; -.
EPD; P26006; -.
PaxDb; P26006; -.
PeptideAtlas; P26006; -.
PRIDE; P26006; -.
ProteomicsDB; 54305; -.
ProteomicsDB; 54306; -. [P26006-1]
Ensembl; ENST00000007722; ENSP00000007722; ENSG00000005884. [P26006-1]
Ensembl; ENST00000320031; ENSP00000315190; ENSG00000005884. [P26006-2]
GeneID; 3675; -.
KEGG; hsa:3675; -.
UCSC; uc010dbl.4; human. [P26006-2]
CTD; 3675; -.
DisGeNET; 3675; -.
EuPathDB; HostDB:ENSG00000005884.17; -.
GeneCards; ITGA3; -.
HGNC; HGNC:6139; ITGA3.
HPA; CAB018594; -.
HPA; HPA008572; -.
MalaCards; ITGA3; -.
MIM; 605025; gene.
MIM; 614748; phenotype.
neXtProt; NX_P26006; -.
OpenTargets; ENSG00000005884; -.
Orphanet; 306504; Congenital nephrotic syndrome-interstitial lung disease-epidermolysis bullosa syndrome.
PharmGKB; PA29939; -.
eggNOG; ENOG410IPB6; Eukaryota.
eggNOG; ENOG410ZZD8; LUCA.
GeneTree; ENSGT00760000118782; -.
HOGENOM; HOG000015786; -.
HOVERGEN; HBG108011; -.
InParanoid; P26006; -.
KO; K06482; -.
OMA; YNQSAGN; -.
OrthoDB; EOG091G012D; -.
TreeFam; TF105391; -.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000157; Laminin interactions.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
SIGNOR; P26006; -.
ChiTaRS; ITGA3; human.
GeneWiki; CD49c; -.
GenomeRNAi; 3675; -.
PMAP-CutDB; P26006; -.
PRO; PR:P26006; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000005884; Expressed in 99 organ(s), highest expression level in adult mammalian kidney.
CleanEx; HS_ITGA3; -.
ExpressionAtlas; P26006; baseline and differential.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:1990812; C:growth cone filopodium; IEA:Ensembl.
GO; GO:0034667; C:integrin alpha3-beta1 complex; IDA:UniProtKB.
GO; GO:0008305; C:integrin complex; TAS:ProtInc.
GO; GO:0071438; C:invadopodium membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
GO; GO:0005518; F:collagen binding; IEA:Ensembl.
GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0043236; F:laminin binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
GO; GO:0097062; P:dendritic spine maintenance; IEA:Ensembl.
GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0030324; P:lung development; IMP:UniProtKB.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
GO; GO:0031345; P:negative regulation of cell projection organization; IEA:Ensembl.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
GO; GO:0072006; P:nephron development; IMP:UniProtKB.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0030510; P:regulation of BMP signaling pathway; IMP:UniProtKB.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
GO; GO:0030111; P:regulation of Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0097205; P:renal filtration; IMP:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0034698; P:response to gonadotropin; IEA:Ensembl.
GO; GO:0043588; P:skin development; IMP:UniProtKB.
Gene3D; 2.130.10.130; -; 1.
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; IPR028994; Integrin_alpha_N.
InterPro; IPR032695; Integrin_dom_sf.
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;
Alternative splicing; Calcium; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Epidermolysis bullosa; Glycoprotein; Integrin;
Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 32 {ECO:0000269|PubMed:10455171,
ECO:0000269|PubMed:3033641,
ECO:0000269|PubMed:8187758}.
CHAIN 33 1051 Integrin alpha-3.
/FTId=PRO_0000016238.
CHAIN 33 872 Integrin alpha-3 heavy chain.
{ECO:0000255}.
/FTId=PRO_0000016239.
CHAIN 876 1051 Integrin alpha-3 light chain.
{ECO:0000255}.
/FTId=PRO_0000016240.
TOPO_DOM 33 991 Extracellular. {ECO:0000255}.
TRANSMEM 992 1014 Helical. {ECO:0000255}.
TOPO_DOM 1015 1051 Cytoplasmic. {ECO:0000255}.
REPEAT 38 103 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 110 171 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 185 235 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 236 292 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 293 354 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 356 411 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 415 477 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 315 323 {ECO:0000255}.
CA_BIND 378 386 {ECO:0000255}.
CA_BIND 439 447 {ECO:0000255}.
REGION 1015 1021 Interaction with HPS5.
MOTIF 1017 1021 GFFKR motif.
LIPID 1016 1016 S-palmitoyl cysteine.
{ECO:0000269|PubMed:15611341}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 500 500 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 511 511 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 573 573 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 605 605 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 656 656 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 697 697 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 841 841 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 857 857 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 926 926 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 935 935 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 969 969 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 94 103 {ECO:0000269|PubMed:14596610}.
DISULFID 140 162 {ECO:0000269|PubMed:14596610}.
DISULFID 185 197 {ECO:0000269|PubMed:14596610}.
DISULFID 485 490 {ECO:0000250}.
DISULFID 496 550 {ECO:0000250}.
DISULFID 615 621 {ECO:0000269|PubMed:14596610}.
DISULFID 694 702 {ECO:0000269|PubMed:14596610}.
DISULFID 846 904 Interchain (between heavy and light
chains). {ECO:0000269|PubMed:14596610}.
DISULFID 911 916 {ECO:0000269|PubMed:14596610}.
VAR_SEQ 1017 1051 GFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY -> DF
FKRTRYYQIMPKYHAVRIREEERYPPPGSTLPTKKHWVTSW
QTRDQYY (in isoform 2).
{ECO:0000303|PubMed:1655803}.
/FTId=VSP_002721.
VARIANT 125 125 G -> R (in ILNEB).
{ECO:0000269|PubMed:27717396}.
/FTId=VAR_077512.
VARIANT 268 268 I -> F (in dbSNP:rs2230390).
/FTId=VAR_055967.
VARIANT 274 274 R -> Q (in ILNEB; dbSNP:rs745505565).
{ECO:0000269|PubMed:27717396}.
/FTId=VAR_077513.
VARIANT 628 628 R -> P (in ILNEB; dbSNP:rs140781106).
{ECO:0000269|PubMed:22512483}.
/FTId=VAR_068808.
VARIANT 719 719 A -> T (in dbSNP:rs2230392).
/FTId=VAR_055968.
VARIANT 840 840 G -> S (in dbSNP:rs2301626).
/FTId=VAR_055969.
MUTAGEN 1016 1016 C->S: Abolishes palmitoylation.
{ECO:0000269|PubMed:15611341}.
SEQUENCE 1051 AA; 116612 MW; EEAFA7778EF17B21 CRC64;
MGPGPSRAPR APRLMLCALA LMVAAGGCVV SAFNLDTRFL VVKEAGNPGS LFGYSVALHR
QTERQQRYLL LAGAPRELAV PDGYTNRTGA VYLCPLTAHK DDCERMNITV KNDPGHHIIE
DMWLGVTVAS QGPAGRVLVC AHRYTQVLWS GSEDQRRMVG KCYVRGNDLE LDSSDDWQTY
HNEMCNSNTD YLETGMCQLG TSGGFTQNTV YFGAPGAYNW KGNSYMIQRK EWDLSEYSYK
DPEDQGNLYI GYTMQVGSFI LHPKNITIVT GAPRHRHMGA VFLLSQEAGG DLRRRQVLEG
SQVGAYFGSA IALADLNNDG WQDLLVGAPY YFERKEEVGG AIYVFMNQAG TSFPAHPSLL
LHGPSGSAFG LSVASIGDIN QDGFQDIAVG APFEGLGKVY IYHSSSKGLL RQPQQVIHGE
KLGLPGLATF GYSLSGQMDV DENFYPDLLV GSLSDHIVLL RARPVINIVH KTLVPRPAVL
DPALCTATSC VQVELCFAYN QSAGNPNYRR NITLAYTLEA DRDRRPPRLR FAGSESAVFH
GFFSMPEMRC QKLELLLMDN LRDKLRPIII SMNYSLPLRM PDRPRLGLRS LDAYPILNQA
QALENHTEVQ FQKECGPDNK CESNLQMRAA FVSEQQQKLS RLQYSRDVRK LLLSINVTNT
RTSERSGEDA HEALLTLVVP PALLLSSVRP PGACQANETI FCELGNPFKR NQRMELLIAF
EVIGVTLHTR DLQVQLQLST SSHQDNLWPM ILTLLVDYTL QTSLSMVNHR LQSFFGGTVM
GESGMKTVED VGSPLKYEFQ VGPMGEGLVG LGTLVLGLEW PYEVSNGKWL LYPTEITVHG
NGSWPCRPPG DLINPLNLTL SDPGDRPSSP QRRRRQLDPG GGQGPPPVTL AAAKKAKSET
VLTCATGRAH CVWLECPIPD APVVTNVTVK ARVWNSTFIE DYRDFDRVRV NGWATLFLRT
SIPTINMENK TTWFSVDIDS ELVEELPAEI ELWLVLVAVG AGLLLLGLII LLLWKCGFFK
RARTRALYEA KRQKAEMKSQ PSETERLTDD Y


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