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 11-NOV-2015, entry version 170. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT human alpha 3 beta 1 (VLA-3), an integrin receptor for fibronectin, RT laminin, and 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA 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 RT the 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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; RA Tsuji T., Hakomori S., Osawa T.; RT "Identification of human galactoprotein b3, an oncogenic RT transformation-induced membrane glycoprotein, as VLA-3 alpha subunit: RT the primary structure of human integrin alpha 3."; RL J. Biochem. 109:659-665(1991). RN [7] RP PROTEIN SEQUENCE OF 33-49. RX PubMed=8187758; 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 RT proteins (FRPs): anti-FRP mAbs induced HIV-mediated cell fusion via an RT integrin 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 RT of 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, RP AND 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., RA Weening J.J., Sonnenberg A.; RT "The A and B variants of the alpha 3 integrin subunit: tissue RT distribution 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., RA 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 RT via 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., RA Buerckstuemmer T., 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 VARIANT ILNEB 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., RA Laube G.F.; RT "Integrin alpha3 mutations with kidney, lung, and skin disease."; RL N. Engl. J. Med. 366:1508-1514(2012). CC -!- FUNCTION: Integrin alpha-3/beta-1 is a receptor for fibronectin, CC laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin CC alpha-3/beta-1 provides a docking site for FAP (seprase) at CC invadopodia plasma membranes in a collagen-dependent manner and CC hence may participate in the adhesion, formation of invadopodia CC and matrix degradation processes, promoting cell invasion. Alpha- CC 3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of CC endothelial cells migration. {ECO:0000269|PubMed:10455171, CC ECO:0000269|PubMed:15181153}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha CC subunit is composed of a heavy and a light chain linked by a CC disulfide bond. Alpha-3 associates with beta-1. Interacts with CC HPS5. Interacts with FAP (seprase); the interaction occurs at the CC cell surface of invadopodia membrane in a collagen-dependent CC manner. {ECO:0000269|PubMed:10455171, CC ECO:0000269|PubMed:15181153}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15611341}; CC Single-pass type I membrane protein {ECO:0000255}. Cell membrane CC {ECO:0000269|PubMed:15611341}; Lipid-anchor CC {ECO:0000269|PubMed:15611341}. Cell projection, invadopodium CC membrane {ECO:0000269|PubMed:10455171}; Single-pass type I CC membrane protein {ECO:0000255}. Cell projection, filopodium CC membrane {ECO:0000269|PubMed:10455171}; Single-pass type I CC membrane protein {ECO:0000255}. Note=Enriched preferentially at CC invadopodia, cell membrane protrusions that correspond to sites of CC cell invasion, in a collagen-dependent manner. CC {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 CC exclusively expressed on vascular smooth muscle cells, whereas in CC heart isoform 1 is strongly expressed on vascular smooth muscle CC cells, isoform 2 is detected only on endothelial vein cells. CC {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: Interstitial lung disease, nephrotic syndrome, and CC epidermolysis bullosa, congenital (ILNEB) [MIM:614748]: A CC multiorgan disorder characterized by congenital nephrotic CC syndrome, interstitial lung disease, and epidermolysis bullosa. CC The respiratory and renal features predominate, and lung CC involvement accounts for the lethal course of the disease. CC {ECO:0000269|PubMed:22512483}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the integrin alpha chain family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 7 FG-GAP repeats. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; CCDS11557.1; -. [P26006-1] DR CCDS; CCDS11558.1; -. [P26006-2] DR PIR; A40021; A40021. DR RefSeq; NP_002195.1; NM_002204.2. [P26006-2] DR RefSeq; NP_005492.1; NM_005501.2. [P26006-1] DR UniGene; Hs.265829; -. DR ProteinModelPortal; P26006; -. DR SMR; P26006; 33-862. DR BioGrid; 109882; 16. DR DIP; DIP-140N; -. DR IntAct; P26006; 3. DR MINT; MINT-140288; -. DR STRING; 9606.ENSP00000007722; -. DR ChEMBL; CHEMBL3525; -. DR PhosphoSite; P26006; -. DR BioMuta; ITGA3; -. DR DMDM; 347595830; -. DR MaxQB; P26006; -. DR PaxDb; P26006; -. DR PRIDE; P26006; -. DR Ensembl; ENST00000007722; ENSP00000007722; ENSG00000005884. [P26006-1] DR Ensembl; ENST00000320031; ENSP00000315190; ENSG00000005884. [P26006-2] DR GeneID; 3675; -. DR KEGG; hsa:3675; -. DR UCSC; uc010dbl.3; human. [P26006-2] DR UCSC; uc010dbm.3; human. [P26006-1] DR CTD; 3675; -. DR GeneCards; ITGA3; -. DR HGNC; HGNC:6139; ITGA3. DR HPA; CAB018594; -. DR HPA; HPA008572; -. DR MIM; 605025; gene. DR MIM; 614748; phenotype. DR neXtProt; NX_P26006; -. DR Orphanet; 306504; Congenital nephrotic syndrome-interstitial lung disease-epidermolysis bullosa syndrome. DR PharmGKB; PA29939; -. DR eggNOG; ENOG410IPB6; Eukaryota. DR eggNOG; ENOG410ZZD8; LUCA. DR GeneTree; ENSGT00760000118782; -. DR HOGENOM; HOG000015786; -. DR HOVERGEN; HBG108011; -. DR InParanoid; P26006; -. DR KO; K06482; -. DR OMA; YIGYTMQ; -. DR OrthoDB; EOG7K3TK7; -. DR TreeFam; TF105391; -. DR Reactome; R-HSA-210991; Basigin interactions. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-3000157; Laminin interactions. DR ChiTaRS; ITGA3; human. DR GeneWiki; CD49c; -. DR GenomeRNAi; 3675; -. DR NextBio; 14385; -. DR PMAP-CutDB; P26006; -. DR PRO; PR:P26006; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; P26006; -. DR CleanEx; HS_ITGA3; -. 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; IEA:Ensembl. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB. DR GO; GO:0030426; C:growth cone; IEA:Ensembl. DR GO; GO:0034667; C:integrin alpha3-beta1 complex; IDA:UniProtKB. DR GO; GO:0008305; C:integrin complex; TAS:ProtInc. DR GO; GO:0071438; C:invadopodium membrane; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:0097060; C:synaptic membrane; IEA:Ensembl. DR GO; GO:0001948; F:glycoprotein binding; IPI:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0002020; F:protease binding; IPI:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc. DR GO; GO:0097062; P:dendritic spine maintenance; IEA:Ensembl. DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. 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; IEA:Ensembl. 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:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IDA:UniProtKB. 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: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:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0034698; P:response to gonadotropin; IEA:Ensembl. DR GO; GO:0043588; P:skin development; IMP:UniProtKB. DR InterPro; IPR013517; FG-GAP. DR InterPro; IPR013519; Int_alpha_beta-p. DR InterPro; IPR000413; Integrin_alpha. DR InterPro; IPR013649; Integrin_alpha-2. DR InterPro; IPR018184; Integrin_alpha_C_CS. DR Pfam; PF01839; FG-GAP; 2. DR Pfam; PF08441; Integrin_alpha2; 1. DR PRINTS; PR01185; INTEGRINA. DR SMART; SM00191; Int_alpha; 5. 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; KW Cell membrane; Cell projection; Cleavage on pair of basic residues; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Epidermolysis bullosa; Glycoprotein; Integrin; Lipoprotein; Membrane; KW Metal-binding; Palmitate; Phosphoprotein; Polymorphism; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 32 {ECO:0000269|PubMed:10455171, FT ECO:0000269|PubMed:3033641, FT ECO:0000269|PubMed:8187758}. FT CHAIN 33 1051 Integrin alpha-3. FT /FTId=PRO_0000016238. FT CHAIN 33 872 Integrin alpha-3 heavy chain. FT {ECO:0000255}. FT /FTId=PRO_0000016239. FT CHAIN 876 1051 Integrin alpha-3 light chain. FT {ECO:0000255}. FT /FTId=PRO_0000016240. FT TOPO_DOM 33 991 Extracellular. {ECO:0000255}. FT TRANSMEM 992 1014 Helical. {ECO:0000255}. FT TOPO_DOM 1015 1051 Cytoplasmic. {ECO:0000255}. FT REPEAT 38 103 FG-GAP 1. FT REPEAT 110 171 FG-GAP 2. FT REPEAT 185 236 FG-GAP 3. FT REPEAT 237 293 FG-GAP 4. FT REPEAT 294 354 FG-GAP 5. FT REPEAT 356 411 FG-GAP 6. FT REPEAT 415 477 FG-GAP 7. FT CA_BIND 315 323 {ECO:0000255}. FT CA_BIND 378 386 {ECO:0000255}. FT CA_BIND 439 447 {ECO:0000255}. FT REGION 1015 1021 Interaction with HPS5. FT MOTIF 1017 1021 GFFKR motif. FT LIPID 1016 1016 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:15611341}. FT CARBOHYD 86 86 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 107 107 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 265 265 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 500 500 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 511 511 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 573 573 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 605 605 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 656 656 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 697 697 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 841 841 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 857 857 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 926 926 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 935 935 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 969 969 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 94 103 {ECO:0000269|PubMed:14596610}. FT DISULFID 140 162 {ECO:0000269|PubMed:14596610}. FT DISULFID 185 197 {ECO:0000269|PubMed:14596610}. FT DISULFID 485 490 {ECO:0000250}. FT DISULFID 496 550 {ECO:0000250}. FT DISULFID 615 621 {ECO:0000269|PubMed:14596610}. FT DISULFID 694 702 {ECO:0000269|PubMed:14596610}. FT DISULFID 846 904 Interchain (between heavy and light FT chains). {ECO:0000269|PubMed:14596610}. FT DISULFID 911 916 {ECO:0000269|PubMed:14596610}. FT VAR_SEQ 1017 1051 GFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY -> DF FT FKRTRYYQIMPKYHAVRIREEERYPPPGSTLPTKKHWVTSW FT QTRDQYY (in isoform 2). FT {ECO:0000303|PubMed:1655803}. FT /FTId=VSP_002721. FT VARIANT 268 268 I -> F (in dbSNP:rs2230390). FT /FTId=VAR_055967. FT VARIANT 628 628 R -> P (in ILNEB). FT {ECO:0000269|PubMed:22512483}. FT /FTId=VAR_068808. FT VARIANT 719 719 A -> T (in dbSNP:rs2230392). FT /FTId=VAR_055968. FT VARIANT 840 840 G -> S (in dbSNP:rs2301626). FT /FTId=VAR_055969. FT MUTAGEN 1016 1016 C->S: Abolishes palmitoylation. FT {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 //