ITA7_HUMAN
ID ITA7_HUMAN Reviewed; 1181 AA.
AC Q13683; B4E3U0; C9JMD3; C9JMZ6; O43197; Q86W93; Q9NY89; Q9UET0; Q9UEV2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Integrin alpha-7;
DE Contains:
DE RecName: Full=Integrin alpha-7 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-7 light chain;
DE Contains:
DE RecName: Full=Integrin alpha-7 70 kDa form;
DE Flags: Precursor;
GN Name=ITGA7; ORFNames=UNQ406/PRO768;
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 ALPHA-7X2B AND ALPHA-7X2DB), AND
RP VARIANT HIS-695.
RC TISSUE=Fetal heart, and Osteoblast;
RX PubMed=9473524; DOI=10.1006/bbrc.1998.8092;
RA Leung E., Lim S.P., Berg R., Yang Y., Ni J., Wang S.-X., Krissansen G.W.;
RT "A novel extracellular domain variant of the human integrin alpha 7 subunit
RT generated by alternative intron splicing.";
RL Biochem. Biophys. Res. Commun. 243:317-325(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-7X2B), INVOLVEMENT IN MDCI, AND
RP VARIANT HIS-695.
RX PubMed=9590299; DOI=10.1038/ng0598-94;
RA Hayashi Y.K., Chou F.-L., Engvall E., Ogawa M., Matsuda C., Hirabayashi S.,
RA Yokochi K., Ziober B.L., Kramer R.H., Kaufman S.J., Ozawa E., Goto Y.,
RA Nonaka I., Tsukahara T., Wang J.Z., Hoffman E.P., Arahata K.;
RT "Mutations in the integrin alpha7 gene cause congenital myopathy.";
RL Nat. Genet. 19:94-97(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-7X2B), AND VARIANT HIS-695.
RA Vizirianakis I.S., Ziober B.L., Kramer R.H.;
RT "Cloning of human integrin alpha-7 cDNA.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANT
RP HIS-695.
RC TISSUE=Skeletal muscle;
RX PubMed=10403775; DOI=10.1006/bbrc.1999.0916;
RA Vignier N., Moghadaszadeh B., Gary F., Beckmann J., Mayer U., Guicheney P.;
RT "Structure, genetic localization, and identification of the cardiac and
RT skeletal muscle transcripts of the human integrin alpha7 gene (ITGA7).";
RL Biochem. Biophys. Res. Commun. 260:357-364(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-7X1B), AND VARIANT
RP HIS-695.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT HIS-695.
RC TISSUE=Uterus;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-7X2B), AND VARIANTS
RP VAL-457; MET-506; HIS-586 AND VAL-696.
RC TISSUE=Brain;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1105-1181 (ISOFORMS
RP ALPHA-7X1B/ALPHA-7X2B/ALPHA-7X2DB/ALPHA-7X1X2B/2).
RC TISSUE=Fetal muscle;
RX PubMed=8126096; DOI=10.1242/jcs.106.4.1139;
RA Song W.K., Wang W., Sato H., Bielser D.A., Kaufman S.J.;
RT "Expression of alpha 7 integrin cytoplasmic domains during skeletal muscle
RT development: alternate forms, conformational change, and homologies with
RT serine/threonine kinases and tyrosine phosphatases.";
RL J. Cell Sci. 106:1139-1152(1993).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1105-1181 (ISOFORMS ALPHA-7X1X2B AND
RP ALPHA-7X1X2A).
RC TISSUE=Skeletal muscle;
RX PubMed=9352853; DOI=10.1053/gast.1997.v113.pm9352853;
RA Basora N., Vachon P.H., Herring-Gillam F.E., Perreault N., Beaulieu J.-F.;
RT "Relation between integrin alpha7Bbeta1 expression in human intestinal
RT cells and enterocytic differentiation.";
RL Gastroenterology 113:1510-1521(1997).
RN [11]
RP PROTEIN SEQUENCE OF 34-45.
RC TISSUE=Melanoma;
RX PubMed=1839357; DOI=10.1091/mbc.2.10.805;
RA Kramer R.H., Vu M.P., Cheng Y.F., Ramos D.M., Timpl R., Waleh N.;
RT "Laminin-binding integrin alpha 7 beta 1: functional characterization and
RT expression in normal and malignant melanocytes.";
RL Cell Regul. 2:805-817(1991).
RN [12]
RP PROTEIN SEQUENCE OF 34-48.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [13]
RP FUNCTION.
RX PubMed=9307969; DOI=10.1091/mbc.8.9.1723;
RA Ziober B.L., Chen Y.Q., Kramer R.H.;
RT "The laminin-binding activity of the alpha 7 integrin receptor is defined
RT by developmentally regulated splicing in the extracellular domain.";
RL Mol. Biol. Cell 8:1723-1734(1997).
RN [14]
RP FUNCTION.
RX PubMed=10694445; DOI=10.1006/excr.2000.4806;
RA Schoeber S., Mielenz D., Echtermeyer F., Hapke S., Poeschl E.,
RA von der Mark H., Moch H., von der Mark K.;
RT "The role of extracellular and cytoplasmic splice domains of alpha7-
RT integrin in cell adhesion and migration on laminins.";
RL Exp. Cell Res. 255:303-313(2000).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=8626012; DOI=10.1006/dbio.1996.0057;
RA Martin P.T., Kaufman S.J., Kramer R.H., Sanes J.R.;
RT "Synaptic integrins in developing, adult, and mutant muscle: selective
RT association of alpha1, alpha7A, and alpha7B integrins with the
RT neuromuscular junction.";
RL Dev. Biol. 174:125-139(1996).
RN [16]
RP FUNCTION.
RX PubMed=17641293; DOI=10.1165/rcmb.2007-0165oc;
RA Tran T., Ens-Blackie K., Rector E.S., Stelmack G.L., McNeill K.D.,
RA Tarone G., Gerthoffer W.T., Unruh H., Halayko A.J.;
RT "Laminin-binding integrin alpha7 is required for contractile phenotype
RT expression by human airway myocytes.";
RL Am. J. Respir. Cell Mol. Biol. 37:668-680(2007).
RN [17]
RP CLEAVAGE BY UROKINASE.
RX PubMed=18940796; DOI=10.1074/jbc.m804661200;
RA Liu J., Gurpur P.B., Kaufman S.J.;
RT "Genetically determined proteolytic cleavage modulates alpha7beta1 integrin
RT function.";
RL J. Biol. Chem. 283:35668-35678(2008).
RN [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1025.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [19]
RP INTERACTION WITH CIB1.
RX PubMed=22779914; DOI=10.1139/o2012-021;
RA Huang H., Bogstie J.N., Vogel H.J.;
RT "Biophysical and structural studies of the human calcium- and integrin-
RT binding protein family: understanding their functional similarities and
RT differences.";
RL Biochem. Cell Biol. 90:646-656(2012).
CC -!- FUNCTION: Integrin alpha-7/beta-1 is the primary laminin receptor on
CC skeletal myoblasts and adult myofibers. During myogenic
CC differentiation, it may induce changes in the shape and mobility of
CC myoblasts, and facilitate their localization at laminin-rich sites of
CC secondary fiber formation. It is involved in the maintenance of the
CC myofibers cytoarchitecture as well as for their anchorage, viability
CC and functional integrity. Isoform Alpha-7X2B and isoform Alpha-7X1B
CC promote myoblast migration on laminin 1 and laminin 2/4, but isoform
CC Alpha-7X1B is less active on laminin 1 (In vitro). Acts as Schwann cell
CC receptor for laminin-2. Acts as a receptor of COMP and mediates its
CC effect on vascular smooth muscle cells (VSMCs) maturation (By
CC similarity). Required to promote contractile phenotype acquisition in
CC differentiated airway smooth muscle (ASM) cells. {ECO:0000250,
CC ECO:0000269|PubMed:10694445, ECO:0000269|PubMed:17641293,
CC ECO:0000269|PubMed:9307969}.
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-7 associates with beta-1. Interacts with COMP (By similarity).
CC Interacts (via C-terminus intracellular tail region) with CIB1; the
CC interaction is stabilized/increased in a calcium- and magnesium-
CC dependent manner. {ECO:0000250, ECO:0000269|PubMed:22779914}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist. There is a combination of
CC at least five alternatively spliced domains, three extracellular (X1,
CC X2 and D) and two cytoplasmic (A and B). A third potential
CC alternatively spliced cytoplasmic domain (C) does not appear to be
CC expressed.;
CC Name=Alpha-7X1X2B;
CC IsoId=Q13683-1; Sequence=Displayed;
CC Name=Alpha-7X1B;
CC IsoId=Q13683-3; Sequence=VSP_002728;
CC Name=Alpha-7X2B;
CC IsoId=Q13683-7; Sequence=VSP_002727;
CC Name=Alpha-7X2DB;
CC IsoId=Q13683-9; Sequence=VSP_042364;
CC Name=Alpha-7X1X2A;
CC IsoId=Q13683-10; Sequence=VSP_002730;
CC Name=2;
CC IsoId=Q13683-13; Sequence=VSP_040487, VSP_040488, VSP_002728;
CC -!- TISSUE SPECIFICITY: Isoforms containing segment A are predominantly
CC expressed in skeletal muscle. Isoforms containing segment B are
CC abundantly expressed in skeletal muscle, moderately in cardiac muscle,
CC small intestine, colon, ovary and prostate and weakly in lung and
CC testes. Isoforms containing segment X2D are expressed at low levels in
CC fetal and adult skeletal muscle and in cardiac muscle, but are not
CC detected in myoblasts and myotubes. In muscle fibers isoforms
CC containing segment A and B are expressed at myotendinous and
CC neuromuscular junctions; isoforms containing segment C are expressed at
CC neuromuscular junctions and at extrasynaptic sites. Isoforms containing
CC segments X1 or X2 or, at low levels, X1X2 are expressed in fetal and
CC adult skeletal muscle (myoblasts and myotubes) and cardiac muscle.
CC {ECO:0000269|PubMed:8626012}.
CC -!- DEVELOPMENTAL STAGE: In renewing intestinal epithelium, expression of
CC isoforms containing segment B correlates with the onset of enterocytic
CC differentiation.
CC -!- PTM: ADP-ribosylated on at least two sites of the extracellular domain
CC in skeletal myotubes. {ECO:0000250}.
CC -!- PTM: A 70 kDa form is created by proteolytic cleavage. Cleavage is
CC elevated during myogenic differentiation and the cleaved form enhances
CC cell adhesion and spreading on laminin. {ECO:0000269|PubMed:18940796}.
CC -!- DISEASE: Muscular dystrophy congenital due to integrin alpha-7
CC deficiency (MDCI) [MIM:613204]: A form of congenital muscular
CC dystrophy. Patients present at birth, or within the first few months of
CC life, with hypotonia, muscle weakness and often with joint
CC contractures. {ECO:0000269|PubMed:9590299}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; AF032108; AAC39708.1; -; mRNA.
DR EMBL; AF052050; AAC18968.1; -; mRNA.
DR EMBL; AF072132; AAC80458.1; -; mRNA.
DR EMBL; AJ228836; CAB41534.1; -; Genomic_DNA.
DR EMBL; AJ228837; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228838; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228839; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228840; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228842; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228843; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228844; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228845; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228846; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228847; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228848; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228849; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228850; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228851; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228852; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228853; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228854; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228855; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228856; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228857; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228858; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228859; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228860; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228862; CAB41534.1; JOINED; Genomic_DNA.
DR EMBL; AJ228836; CAB41535.1; -; Genomic_DNA.
DR EMBL; AJ228837; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228838; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228839; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228841; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228842; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228843; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228844; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228845; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228846; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228847; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228848; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228849; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228850; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228851; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228852; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228853; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228854; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228855; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228856; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228857; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228858; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228859; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228860; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AJ228862; CAB41535.1; JOINED; Genomic_DNA.
DR EMBL; AY358882; AAQ89241.1; -; mRNA.
DR EMBL; AK304864; BAG65602.1; -; mRNA.
DR EMBL; AC009779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050280; AAH50280.1; -; mRNA.
DR EMBL; X74295; CAA52348.1; -; mRNA.
DR EMBL; AF034833; AAB87696.1; -; mRNA.
DR CCDS; CCDS44914.1; -. [Q13683-13]
DR CCDS; CCDS55832.1; -. [Q13683-3]
DR CCDS; CCDS8888.1; -. [Q13683-7]
DR PIR; JC5950; JC5950.
DR RefSeq; NP_001138468.1; NM_001144996.1. [Q13683-3]
DR RefSeq; NP_001138469.1; NM_001144997.1. [Q13683-13]
DR RefSeq; NP_002197.2; NM_002206.2. [Q13683-7]
DR RefSeq; XP_005268896.1; XM_005268839.1. [Q13683-1]
DR RefSeq; XP_005268898.1; XM_005268841.1. [Q13683-10]
DR AlphaFoldDB; Q13683; -.
DR SMR; Q13683; -.
DR BioGRID; 109885; 118.
DR ComplexPortal; CPX-1804; Integrin alpha7-beta1 complex.
DR CORUM; Q13683; -.
DR DIP; DIP-5981N; -.
DR IntAct; Q13683; 25.
DR MINT; Q13683; -.
DR STRING; 9606.ENSP00000452120; -.
DR TCDB; 8.A.54.1.5; the integrin (integrin) family.
DR GlyGen; Q13683; 5 sites.
DR iPTMnet; Q13683; -.
DR PhosphoSitePlus; Q13683; -.
DR BioMuta; ITGA7; -.
DR DMDM; 308153592; -.
DR EPD; Q13683; -.
DR jPOST; Q13683; -.
DR MassIVE; Q13683; -.
DR MaxQB; Q13683; -.
DR PaxDb; Q13683; -.
DR PeptideAtlas; Q13683; -.
DR PRIDE; Q13683; -.
DR ProteomicsDB; 59654; -. [Q13683-1]
DR ProteomicsDB; 59655; -. [Q13683-10]
DR ProteomicsDB; 59656; -. [Q13683-13]
DR ProteomicsDB; 59657; -. [Q13683-3]
DR ProteomicsDB; 59658; -. [Q13683-7]
DR ProteomicsDB; 59659; -. [Q13683-9]
DR Antibodypedia; 1495; 277 antibodies from 30 providers.
DR DNASU; 3679; -.
DR Ensembl; ENST00000257879.11; ENSP00000257879.7; ENSG00000135424.19. [Q13683-7]
DR Ensembl; ENST00000452168.6; ENSP00000393844.2; ENSG00000135424.19. [Q13683-13]
DR Ensembl; ENST00000553804.6; ENSP00000452120.1; ENSG00000135424.19. [Q13683-3]
DR Ensembl; ENST00000555728.5; ENSP00000452387.1; ENSG00000135424.19. [Q13683-1]
DR GeneID; 3679; -.
DR KEGG; hsa:3679; -.
DR MANE-Select; ENST00000257879.11; ENSP00000257879.7; NM_002206.3; NP_002197.2. [Q13683-7]
DR UCSC; uc001shg.4; human. [Q13683-1]
DR CTD; 3679; -.
DR DisGeNET; 3679; -.
DR GeneCards; ITGA7; -.
DR HGNC; HGNC:6143; ITGA7.
DR HPA; ENSG00000135424; Tissue enhanced (skeletal).
DR MalaCards; ITGA7; -.
DR MIM; 600536; gene.
DR MIM; 613204; phenotype.
DR neXtProt; NX_Q13683; -.
DR OpenTargets; ENSG00000135424; -.
DR Orphanet; 2020; Congenital fiber-type disproportion myopathy.
DR Orphanet; 34520; Congenital muscular dystrophy with integrin alpha-7 deficiency.
DR PharmGKB; PA29943; -.
DR VEuPathDB; HostDB:ENSG00000135424; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000159891; -.
DR InParanoid; Q13683; -.
DR OMA; NEGPWRV; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; Q13683; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; Q13683; -.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR SignaLink; Q13683; -.
DR SIGNOR; Q13683; -.
DR BioGRID-ORCS; 3679; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; ITGA7; human.
DR GeneWiki; ITGA7; -.
DR GenomeRNAi; 3679; -.
DR Pharos; Q13683; Tbio.
DR PRO; PR:Q13683; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q13683; protein.
DR Bgee; ENSG00000135424; Expressed in apex of heart and 183 other tissues.
DR ExpressionAtlas; Q13683; baseline and differential.
DR Genevisible; Q13683; HS.
DR GO; GO:0009986; C:cell surface; IC:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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: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:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
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:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR Gene3D; 2.130.10.130; -; 1.
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 InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Alternative splicing; Calcium; Cell adhesion; Cell shape;
KW Cleavage on pair of basic residues; Congenital muscular dystrophy;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Integrin;
KW Membrane; Metal-binding; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:1839357"
FT CHAIN 34..1181
FT /note="Integrin alpha-7"
FT /id="PRO_0000016267"
FT CHAIN 34..955
FT /note="Integrin alpha-7 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016268"
FT CHAIN 648..1181
FT /note="Integrin alpha-7 70 kDa form"
FT /id="PRO_0000398833"
FT CHAIN 959..1181
FT /note="Integrin alpha-7 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016269"
FT TOPO_DOM 34..1082
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1083..1103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1104..1181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 35..103
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 110..175
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 185..238
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 292..349
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 350..411
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 412..467
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 471..530
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 1157..1160
FT /note="1"
FT REPEAT 1165..1168
FT /note="2"
FT REPEAT 1173..1176
FT /note="3"
FT REGION 950..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1176
FT /note="3 X 4 AA repeats of D-X-H-P"
FT MOTIF 1107..1111
FT /note="GFFKR motif"
FT COMPBIAS 950..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 374
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 376
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 436
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 494
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT SITE 647..648
FT /note="Cleavage; by urokinase"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 786
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1025
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1045
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..103
FT /evidence="ECO:0000250"
FT DISULFID 140..163
FT /evidence="ECO:0000250"
FT DISULFID 184..197
FT /evidence="ECO:0000250"
FT DISULFID 539..546
FT /evidence="ECO:0000250"
FT DISULFID 552..615
FT /evidence="ECO:0000250"
FT DISULFID 681..687
FT /evidence="ECO:0000250"
FT DISULFID 781..792
FT /evidence="ECO:0000250"
FT DISULFID 939..994
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 1001..1006
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040487"
FT VAR_SEQ 98..138
FT /note="LEETDCYRVDIDQGADMQKESKENQWLGVSVRSQGPGGKIV -> MAPFATP
FT MVQALTTTRIQRQAEGFQCWRECGTRRSPFEGKE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040488"
FT VAR_SEQ 224..267
FT /note="Missing (in isoform Alpha-7X2B)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9473524, ECO:0000303|PubMed:9590299,
FT ECO:0000303|Ref.3"
FT /id="VSP_002727"
FT VAR_SEQ 268..307
FT /note="Missing (in isoform Alpha-7X1B and isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_002728"
FT VAR_SEQ 702..776
FT /note="Missing (in isoform Alpha-7X2DB)"
FT /evidence="ECO:0000303|PubMed:9473524"
FT /id="VSP_042364"
FT VAR_SEQ 1106..1181
FT /note="MGFFKRAKHPEATVPQYHAVKIPREDRQQFKEEKTGTILRNNWGSPRREGPD
FT AHPILAADGHPELGPDGHPGPGTA -> CGFFHRSSQSSSFPTNYHRACLAVQPSAMEV
FT GGPGTVGWDSSNGRSTPRPPCPSTMR (in isoform Alpha-7X1X2A)"
FT /evidence="ECO:0000303|PubMed:9352853"
FT /id="VSP_002730"
FT VARIANT 457
FT /note="I -> V (in dbSNP:rs17857367)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_067015"
FT VARIANT 506
FT /note="L -> M (in dbSNP:rs17854599)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_067016"
FT VARIANT 586
FT /note="R -> H (in dbSNP:rs17854598)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_067017"
FT VARIANT 695
FT /note="R -> H (in dbSNP:rs1800974)"
FT /evidence="ECO:0000269|PubMed:10403775,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9473524, ECO:0000269|PubMed:9590299,
FT ECO:0000269|Ref.3"
FT /id="VAR_014759"
FT VARIANT 696
FT /note="A -> V (in dbSNP:rs17855684)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_067018"
FT CONFLICT 873
FT /note="A -> T (in Ref. 2; AAC18968)"
FT /evidence="ECO:0000305"
FT CONFLICT 1005
FT /note="S -> I (in Ref. 2; AAC18968)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013
FT /note="R -> H (in Ref. 8; AAH50280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1181 AA; 128948 MW; 341C0C72CDB8CA57 CRC64;
MAGARSRDPW GASGICYLFG SLLVELLFSR AVAFNLDVMG ALRKEGEPGS LFGFSVALHR
QLQPRPQSWL LVGAPQALAL PGQQANRTGG LFACPLSLEE TDCYRVDIDQ GADMQKESKE
NQWLGVSVRS QGPGGKIVTC AHRYEARQRV DQILETRDMI GRCFVLSQDL AIRDELDGGE
WKFCEGRPQG HEQFGFCQQG TAAAFSPDSH YLLFGAPGTY NWKGTARVEL CAQGSADLAH
LDDGPYEAGG EKEQDPRLIP VPANSYFGLL FVTNIDSSDP DQLVYKTLDP ADRLPGPAGD
LALNSYLGFS IDSGKGLVRA EELSFVAGAP RANHKGAVVI LRKDSASRLV PEVMLSGERL
TSGFGYSLAV ADLNSDGWPD LIVGAPYFFE RQEELGGAVY VYLNQGGHWA GISPLRLCGS
PDSMFGISLA VLGDLNQDGF PDIAVGAPFD GDGKVFIYHG SSLGVVAKPS QVLEGEAVGI
KSFGYSLSGS LDMDGNQYPD LLVGSLADTA VLFRARPILH VSHEVSIAPR SIDLEQPNCA
GGHSVCVDLR VCFSYIAVPS SYSPTVALDY VLDADTDRRL RGQVPRVTFL SRNLEEPKHQ
ASGTVWLKHQ HDRVCGDAMF QLQENVKDKL RAIVVTLSYS LQTPRLRRQA PGQGLPPVAP
ILNAHQPSTQ RAEIHFLKQG CGEDKICQSN LQLVRARFCT RVSDTEFQPL PMDVDGTTAL
FALSGQPVIG LELMVTNLPS DPAQPQADGD DAHEAQLLVM LPDSLHYSGV RALDPAEKPL
CLSNENASHV ECELGNPMKR GAQVTFYLIL STSGISIETT ELEVELLLAT ISEQELHPVS
ARARVFIELP LSIAGMAIPQ QLFFSGVVRG ERAMQSERDV GSKVKYEVTV SNQGQSLRTL
GSAFLNIMWP HEIANGKWLL YPMQVELEGG QGPGQKGLCS PRPNILHLDV DSRDRRRREL
EPPEQQEPGE RQEPSMSWWP VSSAEKKKNI TLDCARGTAN CVVFSCPLYS FDRAAVLHVW
GRLWNSTFLE EYSAVKSLEV IVRANITVKS SIKNLMLRDA STVIPVMVYL DPMAVVAEGV
PWWVILLAVL AGLLVLALLV LLLWKMGFFK RAKHPEATVP QYHAVKIPRE DRQQFKEEKT
GTILRNNWGS PRREGPDAHP ILAADGHPEL GPDGHPGPGT A
