ID   ITA3_HUMAN              Reviewed;        1051 AA.
AC   P26006; A7E246; B7ZM80; B9EGQ1; D3DTX4; D3DTX5;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 5.
DT   27-MAR-2024, entry version 230.
DE   RecName: Full=Integrin alpha-3;
DE   AltName: Full=CD49 antigen-like family member C;
DE   AltName: Full=FRP-2;
DE   AltName: Full=Galactoprotein B3;
DE            Short=GAPB3;
DE   AltName: Full=VLA-3 subunit alpha;
DE   AltName: CD_antigen=CD49c;
DE   Contains:
DE     RecName: Full=Integrin alpha-3 heavy chain;
DE   Contains:
DE     RecName: Full=Integrin alpha-3 light chain;
DE   Flags: Precursor;
GN   Name=ITGA3; Synonyms=MSK18;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=1655803; DOI=10.1083/jcb.115.1.257;
RA   Takada Y., Murphy E., Pil P., Chen C., Ginsberg M.H., Hemler M.E.;
RT   "Molecular cloning and expression of the cDNA for alpha 3 subunit of human
RT   alpha 3 beta 1 (VLA-3), an integrin receptor for fibronectin, laminin, and
RT   collagen.";
RL   J. Cell Biol. 115:257-266(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 33-1051 (ISOFORM 1).
RC   TISSUE=Fibroblast;
RX   PubMed=1714443; DOI=10.1093/oxfordjournals.jbchem.a123436;
RA   Tsuji T., Hakomori S., Osawa T.;
RT   "Identification of human galactoprotein b3, an oncogenic transformation-
RT   induced membrane glycoprotein, as VLA-3 alpha subunit: the primary
RT   structure of human integrin alpha 3.";
RL   J. Biochem. 109:659-665(1991).
RN   [7]
RP   PROTEIN SEQUENCE OF 33-49.
RX   PubMed=8187758; DOI=10.1002/j.1460-2075.1994.tb06479.x;
RA   Ohta H., Tsurudome M., Matsumura H., Koga Y., Morikawa S., Kawano M.,
RA   Kusugawa S., Komada H., Nishio M., Ito Y.;
RT   "Molecular and biological characterization of fusion regulatory proteins
RT   (FRPs): anti-FRP mAbs induced HIV-mediated cell fusion via an integrin
RT   system.";
RL   EMBO J. 13:2044-2055(1994).
RN   [8]
RP   PROTEIN SEQUENCE OF 33-46.
RX   PubMed=3033641; DOI=10.1073/pnas.84.10.3239;
RA   Takada Y., Strominger J.L., Hemler M.E.;
RT   "The very late antigen family of heterodimers is part of a superfamily of
RT   molecules involved in adhesion and embryogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:3239-3243(1987).
RN   [9]
RP   PROTEIN SEQUENCE OF 33-40, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH FAP.
RX   PubMed=10455171; DOI=10.1074/jbc.274.35.24947;
RA   Mueller S.C., Ghersi G., Akiyama S.K., Sang Q.X., Howard L.,
RA   Pineiro-Sanchez M., Nakahara H., Yeh Y., Chen W.T.;
RT   "A novel protease-docking function of integrin at invadopodia.";
RL   J. Biol. Chem. 274:24947-24952(1999).
RN   [10]
RP   ALTERNATIVE SPLICING, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX   PubMed=9111516;
RA   de Melker A.A., Sterk L.M., Delwel G.O., Fles D.L., Daams H., Weening J.J.,
RA   Sonnenberg A.;
RT   "The A and B variants of the alpha 3 integrin subunit: tissue distribution
RT   and functional characterization.";
RL   Lab. Invest. 76:547-563(1997).
RN   [11]
RP   DISULFIDE BONDS.
RX   PubMed=14596610; DOI=10.1021/bi034726u;
RA   Krokhin O.V., Cheng K., Sousa S.L., Ens W., Standing K.G., Wilkins J.A.;
RT   "Mass spectrometric based mapping of the disulfide bonding patterns of
RT   integrin alpha chains.";
RL   Biochemistry 42:12950-12959(2003).
RN   [12]
RP   PALMITOYLATION AT CYS-1016, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   CYS-1016.
RX   PubMed=15611341; DOI=10.1083/jcb.200404100;
RA   Yang X., Kovalenko O.V., Tang W., Claas C., Stipp C.S., Hemler M.E.;
RT   "Palmitoylation supports assembly and function of integrin-tetraspanin
RT   complexes.";
RL   J. Cell Biol. 167:1231-1240(2004).
RN   [13]
RP   INTERACTION WITH ITGB1; LGALS3 AND CSPG4, AND FUNCTION.
RX   PubMed=15181153; DOI=10.1091/mbc.e04-03-0236;
RA   Fukushi J., Makagiansar I.T., Stallcup W.B.;
RT   "NG2 proteoglycan promotes endothelial cell motility and angiogenesis via
RT   engagement of galectin-3 and alpha3beta1 integrin.";
RL   Mol. Biol. Cell 15:3580-3590(2004).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RX   PubMed=32487760; DOI=10.1128/mbio.01087-20;
RA   Alqarihi A., Gebremariam T., Gu Y., Swidergall M., Alkhazraji S.,
RA   Soliman S.S.M., Bruno V.M., Edwards J.E. Jr., Filler S.G., Uppuluri P.,
RA   Ibrahim A.S.;
RT   "GRP78 and Integrins Play Different Roles in Host Cell Invasion during
RT   Mucormycosis.";
RL   MBio 11:e01087-e01087(2020).
RN   [16]
RP   VARIANT JEB7 PRO-628.
RX   PubMed=22512483; DOI=10.1056/nejmoa1110813;
RA   Has C., Sparta G., Kiritsi D., Weibel L., Moeller A., Vega-Warner V.,
RA   Waters A., He Y., Anikster Y., Esser P., Straub B.K., Hausser I.,
RA   Bockenhauer D., Dekel B., Hildebrandt F., Bruckner-Tuderman L., Laube G.F.;
RT   "Integrin alpha3 mutations with kidney, lung, and skin disease.";
RL   N. Engl. J. Med. 366:1508-1514(2012).
RN   [17]
RP   VARIANTS JEB7 ARG-125 AND GLN-274.
RX   PubMed=27717396; DOI=10.1186/s13023-016-0514-z;
RA   Colombo E.A., Spaccini L., Volpi L., Negri G., Cittaro D., Lazarevic D.,
RA   Zirpoli S., Farolfi A., Gervasini C., Cubellis M.V., Larizza L.;
RT   "Viable phenotype of ILNEB syndrome without nephrotic impairment in
RT   siblings heterozygous for unreported integrin alpha3 mutations.";
RL   Orphanet J. Rare Dis. 11:136-136(2016).
CC   -!- FUNCTION: Integrin alpha-3/beta-1 is a receptor for fibronectin,
CC       laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-
CC       3/beta-1 provides a docking site for FAP (seprase) at invadopodia
CC       plasma membranes in a collagen-dependent manner and hence may
CC       participate in the adhesion, formation of invadopodia and matrix
CC       degradation processes, promoting cell invasion. Alpha-3/beta-1 may
CC       mediate with LGALS3 the stimulation by CSPG4 of endothelial cells
CC       migration. {ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:15181153}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGA3:ITGB1 may act as a
CC       receptor for R.delemar CotH7 in alveolar epithelial cells, which may be
CC       an early step in pulmonary mucormycosis disease progression.
CC       {ECO:0000269|PubMed:32487760}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC       is composed of a heavy and a light chain linked by a disulfide bond.
CC       Alpha-3 associates with beta-1. Interacts with HPS5. Interacts with FAP
CC       (seprase); the interaction occurs at the cell surface of invadopodia
CC       membrane in a collagen-dependent manner. {ECO:0000269|PubMed:10455171,
CC       ECO:0000269|PubMed:15181153}.
CC   -!- INTERACTION:
CC       P26006; P48509: CD151; NbExp=6; IntAct=EBI-2550768, EBI-10210332;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15611341,
CC       ECO:0000269|PubMed:32487760}; Single-pass type I membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15611341}; Lipid-
CC       anchor {ECO:0000269|PubMed:15611341}. Cell projection, invadopodium
CC       membrane {ECO:0000269|PubMed:10455171}; Single-pass type I membrane
CC       protein {ECO:0000255}. Cell projection, filopodium membrane
CC       {ECO:0000269|PubMed:10455171}; Single-pass type I membrane protein
CC       {ECO:0000255}. Note=Enriched preferentially at invadopodia, cell
CC       membrane protrusions that correspond to sites of cell invasion, in a
CC       collagen-dependent manner. {ECO:0000269|PubMed:10455171}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Alpha-3A;
CC         IsoId=P26006-2; Sequence=Displayed;
CC       Name=2; Synonyms=Alpha-3B;
CC         IsoId=P26006-1; Sequence=VSP_002721;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 is
CC       expressed in brain and heart. In brain, both isoforms are exclusively
CC       expressed on vascular smooth muscle cells, whereas in heart isoform 1
CC       is strongly expressed on vascular smooth muscle cells, isoform 2 is
CC       detected only on endothelial vein cells. {ECO:0000269|PubMed:9111516}.
CC   -!- PTM: Isoform 1, but not isoform 2, is phosphorylated on serine
CC       residues. Phosphorylation increases after phorbol 12-myristate 13-
CC       acetate stimulation. {ECO:0000269|PubMed:9111516}.
CC   -!- DISEASE: Epidermolysis bullosa, junctional 7, with interstitial lung
CC       disease and nephrotic syndrome (JEB7) [MIM:614748]: A form of
CC       epidermolysis bullosa, a genodermatosis characterized by recurrent
CC       blistering, fragility of the skin and mucosal epithelia, and erosions
CC       caused by minor mechanical trauma. JEB7 is an autosomal recessive form
CC       associated with congenital nephrotic syndrome and interstitial lung
CC       disease. The respiratory and renal features predominate, and lung
CC       involvement accounts for the lethal course of the disease.
CC       {ECO:0000269|PubMed:22512483, ECO:0000269|PubMed:27717396}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- BIOTECHNOLOGY: Antibodies against integrin alpha-3 ITGA3 protects
CC       epithelial cells from invasion by the fungus R.delemar, a causative
CC       agent of mucormycosis, and could thus potentially be used to treat
CC       mucormycosis disease. {ECO:0000305|PubMed:32487760}.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR   EMBL; M59911; AAA36120.1; -; mRNA.
DR   EMBL; AK289961; BAF82650.1; -; mRNA.
DR   EMBL; AC002401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471109; EAW94645.1; -; Genomic_DNA.
DR   EMBL; CH471109; EAW94646.1; -; Genomic_DNA.
DR   EMBL; CH471109; EAW94647.1; -; Genomic_DNA.
DR   EMBL; CH471109; EAW94648.1; -; Genomic_DNA.
DR   EMBL; BC136636; AAI36637.1; -; mRNA.
DR   EMBL; BC144328; AAI44329.1; -; mRNA.
DR   EMBL; BC150190; AAI50191.1; -; mRNA.
DR   EMBL; D01038; BAA00845.1; -; mRNA.
DR   CCDS; CCDS11558.1; -. [P26006-2]
DR   PIR; A40021; A40021.
DR   RefSeq; NP_002195.1; NM_002204.3. [P26006-2]
DR   AlphaFoldDB; P26006; -.
DR   SMR; P26006; -.
DR   BioGRID; 109882; 82.
DR   ComplexPortal; CPX-1797; Integrin alpha3-beta1 complex.
DR   CORUM; P26006; -.
DR   DIP; DIP-140N; -.
DR   IntAct; P26006; 29.
DR   MINT; P26006; -.
DR   STRING; 9606.ENSP00000315190; -.
DR   BindingDB; P26006; -.
DR   ChEMBL; CHEMBL3525; -.
DR   GuidetoPHARMACOLOGY; 2442; -.
DR   GlyConnect; 738; 3 N-Linked glycans (2 sites).
DR   GlyCosmos; P26006; 14 sites, 5 glycans.
DR   GlyGen; P26006; 18 sites, 5 N-linked glycans (2 sites), 2 O-linked glycans (4 sites).
DR   iPTMnet; P26006; -.
DR   PhosphoSitePlus; P26006; -.
DR   SwissPalm; P26006; -.
DR   BioMuta; ITGA3; -.
DR   DMDM; 347595830; -.
DR   EPD; P26006; -.
DR   jPOST; P26006; -.
DR   MassIVE; P26006; -.
DR   MaxQB; P26006; -.
DR   PaxDb; 9606-ENSP00000007722; -.
DR   PeptideAtlas; P26006; -.
DR   ProteomicsDB; 54305; -. [P26006-2]
DR   ProteomicsDB; 54306; -. [P26006-1]
DR   Pumba; P26006; -.
DR   ABCD; P26006; 39 sequenced antibodies.
DR   Antibodypedia; 18000; 1122 antibodies from 42 providers.
DR   DNASU; 3675; -.
DR   Ensembl; ENST00000007722.11; ENSP00000007722.7; ENSG00000005884.18. [P26006-1]
DR   Ensembl; ENST00000320031.13; ENSP00000315190.8; ENSG00000005884.18. [P26006-2]
DR   GeneID; 3675; -.
DR   KEGG; hsa:3675; -.
DR   MANE-Select; ENST00000320031.13; ENSP00000315190.8; NM_002204.4; NP_002195.1.
DR   UCSC; uc010dbl.4; human. [P26006-2]
DR   AGR; HGNC:6139; -.
DR   CTD; 3675; -.
DR   DisGeNET; 3675; -.
DR   GeneCards; ITGA3; -.
DR   HGNC; HGNC:6139; ITGA3.
DR   HPA; ENSG00000005884; Low tissue specificity.
DR   MalaCards; ITGA3; -.
DR   MIM; 605025; gene.
DR   MIM; 614748; phenotype.
DR   neXtProt; NX_P26006; -.
DR   OpenTargets; ENSG00000005884; -.
DR   Orphanet; 306504; Interstitial lung disease-nephrotic syndrome-epidermolysis bullosa syndrome.
DR   PharmGKB; PA29939; -.
DR   VEuPathDB; HostDB:ENSG00000005884; -.
DR   eggNOG; KOG3637; Eukaryota.
DR   GeneTree; ENSGT00940000157746; -.
DR   HOGENOM; CLU_004111_1_0_1; -.
DR   InParanoid; P26006; -.
DR   OMA; RYNHTGA; -.
DR   OrthoDB; 3816176at2759; -.
DR   TreeFam; TF105391; -.
DR   PathwayCommons; P26006; -.
DR   Reactome; R-HSA-210991; Basigin interactions.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-3000157; Laminin interactions.
DR   Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR   SignaLink; P26006; -.
DR   SIGNOR; P26006; -.
DR   BioGRID-ORCS; 3675; 45 hits in 1157 CRISPR screens.
DR   ChiTaRS; ITGA3; human.
DR   GeneWiki; CD49c; -.
DR   GenomeRNAi; 3675; -.
DR   Pharos; P26006; Tchem.
DR   PRO; PR:P26006; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P26006; Protein.
DR   Bgee; ENSG00000005884; Expressed in metanephric glomerulus and 109 other cell types or tissues.
DR   ExpressionAtlas; P26006; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0060076; C:excitatory synapse; ISS:ARUK-UCL.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:1990812; C:growth cone filopodium; IEA:Ensembl.
DR   GO; GO:0034667; C:integrin alpha3-beta1 complex; IDA:UniProtKB.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0097060; C:synaptic membrane; ISS:ARUK-UCL.
DR   GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR   GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0097062; P:dendritic spine maintenance; ISS:ARUK-UCL.
DR   GO; GO:0035640; P:exploration behavior; ISS:ARUK-UCL.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0050900; P:leukocyte migration; IBA:GO_Central.
DR   GO; GO:0030324; P:lung development; IMP:UniProtKB.
DR   GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
DR   GO; GO:0031345; P:negative regulation of cell projection organization; IEA:Ensembl.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:ARUK-UCL.
DR   GO; GO:0072006; P:nephron development; IMP:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030510; P:regulation of BMP signaling pathway; IMP:UniProtKB.
DR   GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; IMP:UniProtKB.
DR   GO; GO:0097205; P:renal filtration; IMP:UniProtKB.
DR   GO; GO:0034698; P:response to gonadotropin; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR   GO; GO:0043588; P:skin development; IMP:UniProtKB.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
DR   Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR   Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR   Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR   Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR   InterPro; IPR048286; Integrin_alpha_Ig-like_3.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF89; INTEGRIN ALPHA-3; 1.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF08441; Integrin_A_Ig_1; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 1.
DR   Pfam; PF20806; Integrin_A_Ig_3; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF69179; Integrin domains; 3.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW   Cell projection; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disease variant; Disulfide bond;
KW   Epidermolysis bullosa; Glycoprotein; Integrin; Lipoprotein; Membrane;
KW   Metal-binding; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000269|PubMed:10455171,
FT                   ECO:0000269|PubMed:3033641, ECO:0000269|PubMed:8187758"
FT   CHAIN           33..1051
FT                   /note="Integrin alpha-3"
FT                   /id="PRO_0000016238"
FT   CHAIN           33..872
FT                   /note="Integrin alpha-3 heavy chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016239"
FT   CHAIN           876..1051
FT                   /note="Integrin alpha-3 light chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016240"
FT   TOPO_DOM        33..991
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        992..1014
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1015..1051
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          38..103
FT                   /note="FG-GAP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          110..171
FT                   /note="FG-GAP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          185..235
FT                   /note="FG-GAP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          236..292
FT                   /note="FG-GAP 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          293..354
FT                   /note="FG-GAP 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          356..411
FT                   /note="FG-GAP 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          415..477
FT                   /note="FG-GAP 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REGION          855..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1015..1021
FT                   /note="Interaction with HPS5"
FT   MOTIF           1017..1021
FT                   /note="GFFKR motif"
FT   BINDING         315
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         317
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         319
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         323
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         378
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         380
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         382
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         386
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         439
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         441
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         443
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         445
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         447
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   LIPID           1016
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:15611341"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        573
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        605
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        656
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        697
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        841
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        857
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        926
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        935
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        969
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..103
FT                   /evidence="ECO:0000269|PubMed:14596610"
FT   DISULFID        140..162
FT                   /evidence="ECO:0000269|PubMed:14596610"
FT   DISULFID        185..197
FT                   /evidence="ECO:0000269|PubMed:14596610"
FT   DISULFID        485..490
FT                   /evidence="ECO:0000250"
FT   DISULFID        496..550
FT                   /evidence="ECO:0000250"
FT   DISULFID        615..621
FT                   /evidence="ECO:0000269|PubMed:14596610"
FT   DISULFID        694..702
FT                   /evidence="ECO:0000269|PubMed:14596610"
FT   DISULFID        846..904
FT                   /note="Interchain (between heavy and light chains)"
FT                   /evidence="ECO:0000269|PubMed:14596610"
FT   DISULFID        911..916
FT                   /evidence="ECO:0000269|PubMed:14596610"
FT   VAR_SEQ         1017..1051
FT                   /note="GFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY -> DFFKRTRYYQIMP
FT                   KYHAVRIREEERYPPPGSTLPTKKHWVTSWQTRDQYY (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1655803"
FT                   /id="VSP_002721"
FT   VARIANT         125
FT                   /note="G -> R (in JEB7)"
FT                   /evidence="ECO:0000269|PubMed:27717396"
FT                   /id="VAR_077512"
FT   VARIANT         268
FT                   /note="I -> F (in dbSNP:rs2230390)"
FT                   /id="VAR_055967"
FT   VARIANT         274
FT                   /note="R -> Q (in JEB7; dbSNP:rs745505565)"
FT                   /evidence="ECO:0000269|PubMed:27717396"
FT                   /id="VAR_077513"
FT   VARIANT         628
FT                   /note="R -> P (in JEB7; dbSNP:rs140781106)"
FT                   /evidence="ECO:0000269|PubMed:22512483"
FT                   /id="VAR_068808"
FT   VARIANT         719
FT                   /note="A -> T (in dbSNP:rs2230392)"
FT                   /id="VAR_055968"
FT   VARIANT         840
FT                   /note="G -> S (in dbSNP:rs2301626)"
FT                   /id="VAR_055969"
FT   MUTAGEN         1016
FT                   /note="C->S: Abolishes palmitoylation."
FT                   /evidence="ECO:0000269|PubMed:15611341"
SQ   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
//