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Q13683

- ITA7_HUMAN

UniProt

Q13683 - ITA7_HUMAN

Protein

Integrin alpha-7

Gene

ITGA7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. It is involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Isoform Alpha-7X2B and isoform Alpha-7X1B promote myoblast migration on laminin 1 and laminin 2/4, but isoform Alpha-7X1B is less active on laminin 1 (In vitro). Acts as Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation By similarity. Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells.By similarity3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei647 – 6482Cleavage; by urokinase

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi372 – 3809Sequence Analysis
    Calcium bindingi434 – 4429Sequence Analysis
    Calcium bindingi492 – 5009Sequence Analysis

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. blood vessel morphogenesis Source: Ensembl
    2. cell-matrix adhesion Source: ProtInc
    3. cell migration Source: Ensembl
    4. extracellular matrix organization Source: Reactome
    5. integrin-mediated signaling pathway Source: UniProtKB-KW
    6. muscle organ development Source: ProtInc
    7. regulation of cell shape Source: UniProtKB-KW
    8. skeletal muscle tissue development Source: Ensembl

    Keywords - Molecular functioni

    Integrin, Receptor

    Keywords - Biological processi

    Cell adhesion, Cell shape

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_13552. Integrin cell surface interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.
    SignaLinkiQ13683.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Integrin alpha-7
    Cleaved into the following 3 chains:
    Gene namesi
    Name:ITGA7
    ORF Names:UNQ406/PRO768
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6143. ITGA7.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. cytoplasm Source: Ensembl
    3. integrin alpha7-beta1 complex Source: Ensembl
    4. muscle tendon junction Source: Ensembl
    5. neuromuscular junction Source: Ensembl
    6. plasma membrane Source: Reactome
    7. sarcolemma Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Muscular dystrophy congenital due to integrin alpha-7 deficiency (MDCI) [MIM:613204]: A form of congenital muscular dystrophy. Patients present at birth, or within the first few months of life, with hypotonia, muscle weakness and often with joint contractures.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Congenital muscular dystrophy

    Organism-specific databases

    MIMi613204. phenotype.
    Orphaneti2020. Congenital fiber-type disproportion myopathy.
    34520. Congenital muscular dystrophy with integrin alpha-7 deficiency.
    PharmGKBiPA29943.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 33332 PublicationsAdd
    BLAST
    Chaini34 – 11811148Integrin alpha-7PRO_0000016267Add
    BLAST
    Chaini34 – 955922Integrin alpha-7 heavy chainSequence AnalysisPRO_0000016268Add
    BLAST
    Chaini648 – 1181534Integrin alpha-7 70 kDa formPRO_0000398833Add
    BLAST
    Chaini959 – 1181223Integrin alpha-7 light chainSequence AnalysisPRO_0000016269Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi94 ↔ 103By similarity
    Disulfide bondi140 ↔ 163By similarity
    Disulfide bondi184 ↔ 197By similarity
    Disulfide bondi539 ↔ 546By similarity
    Disulfide bondi552 ↔ 615By similarity
    Disulfide bondi681 ↔ 687By similarity
    Disulfide bondi781 ↔ 792By similarity
    Glycosylationi786 – 7861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi939 ↔ 994Interchain (between heavy and light chains)By similarity
    Glycosylationi989 – 9891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1001 ↔ 1006By similarity
    Glycosylationi1025 – 10251N-linked (GlcNAc...)1 Publication
    Glycosylationi1045 – 10451N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    ADP-ribosylated on at least two sites of the extracellular domain in skeletal myotubes.By similarity
    A 70 kDa form is created by proteolytic cleavage. Cleavage is elevated during myogenic differentiation and the cleaved form enhances cell adhesion and spreading on laminin.1 Publication

    Keywords - PTMi

    ADP-ribosylation, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ13683.
    PaxDbiQ13683.
    PRIDEiQ13683.

    PTM databases

    PhosphoSiteiQ13683.

    Expressioni

    Tissue specificityi

    Isoforms containing segment A are predominantly expressed in skeletal muscle. Isoforms containing segment B are abundantly expressed in skeletal muscle, moderately in cardiac muscle, small intestine, colon, ovary and prostate and weakly in lung and testes. Isoforms containing segment X2D are expressed at low levels in fetal and adult skeletal muscle and in cardiac muscle, but are not detected in myoblasts and myotubes. In muscle fibers isoforms containing segment A and B are expressed at myotendinous and neuromuscular junctions; isoforms containing segment C are expressed at neuromuscular junctions and at extrasynaptic sites. Isoforms containing segments X1 or X2 or, at low levels, X1X2 are expressed in fetal and adult skeletal muscle (myoblasts and myotubes) and cardiac muscle.1 Publication

    Developmental stagei

    In renewing intestinal epithelium, expression of isoforms containing segment B correlates with the onset of enterocytic differentiation.

    Gene expression databases

    ArrayExpressiQ13683.
    BgeeiQ13683.
    CleanExiHS_ITGA7.
    GenevestigatoriQ13683.

    Organism-specific databases

    HPAiHPA008427.

    Interactioni

    Subunit structurei

    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-7 associates with beta-1. Interacts with COMP By similarity. Interacts (via C-terminus intracellular tail region) with CIB1; the interaction is stabilized/increased in a calcium- and magnesium-dependent manner.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi109885. 6 interactions.
    DIPiDIP-5981N.
    IntActiQ13683. 1 interaction.
    MINTiMINT-140160.
    STRINGi9606.ENSP00000257879.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13683.
    SMRiQ13683. Positions 34-680, 1077-1114.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini34 – 10821049ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1104 – 118178CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1083 – 110321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati35 – 10369FG-GAP 1Add
    BLAST
    Repeati110 – 17566FG-GAP 2Add
    BLAST
    Repeati185 – 23854FG-GAP 3Add
    BLAST
    Repeati292 – 35059FG-GAP 4Add
    BLAST
    Repeati351 – 41161FG-GAP 5Add
    BLAST
    Repeati412 – 46756FG-GAP 6Add
    BLAST
    Repeati471 – 53060FG-GAP 7Add
    BLAST
    Repeati1157 – 116041
    Repeati1165 – 116842
    Repeati1173 – 117643

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1157 – 1176203 X 4 AA repeats of D-X-H-PAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1107 – 11115GFFKR motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi953 – 9586Poly-Arg

    Sequence similaritiesi

    Belongs to the integrin alpha chain family.Curated
    Contains 7 FG-GAP repeats.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG26407.
    HOVERGENiHBG108011.
    InParanoidiQ13683.
    KOiK06583.
    OMAiQGPGQKG.
    PhylomeDBiQ13683.
    TreeFamiTF105391.

    Family and domain databases

    InterProiIPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    [Graphical view]
    PfamiPF01839. FG-GAP. 2 hits.
    PF08441. Integrin_alpha2. 1 hit.
    [Graphical view]
    PRINTSiPR01185. INTEGRINA.
    SMARTiSM00191. Int_alpha. 5 hits.
    [Graphical view]
    PROSITEiPS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist. There is a combination of at least five alternatively spliced domains, three extracellular (X1, X2 and D) and two cytoplasmic (A and B). A third potential alternatively spliced cytoplasmic domain (C) does not appear to be expressed.

    Isoform Alpha-7X1X2B (identifier: Q13683-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGARSRDPW GASGICYLFG SLLVELLFSR AVAFNLDVMG ALRKEGEPGS     50
    LFGFSVALHR QLQPRPQSWL LVGAPQALAL PGQQANRTGG LFACPLSLEE 100
    TDCYRVDIDQ GADMQKESKE NQWLGVSVRS QGPGGKIVTC AHRYEARQRV 150
    DQILETRDMI GRCFVLSQDL AIRDELDGGE WKFCEGRPQG HEQFGFCQQG 200
    TAAAFSPDSH YLLFGAPGTY NWKGTARVEL CAQGSADLAH LDDGPYEAGG 250
    EKEQDPRLIP VPANSYFGLL FVTNIDSSDP DQLVYKTLDP ADRLPGPAGD 300
    LALNSYLGFS IDSGKGLVRA EELSFVAGAP RANHKGAVVI LRKDSASRLV 350
    PEVMLSGERL TSGFGYSLAV ADLNSDGWPD LIVGAPYFFE RQEELGGAVY 400
    VYLNQGGHWA GISPLRLCGS PDSMFGISLA VLGDLNQDGF PDIAVGAPFD 450
    GDGKVFIYHG SSLGVVAKPS QVLEGEAVGI KSFGYSLSGS LDMDGNQYPD 500
    LLVGSLADTA VLFRARPILH VSHEVSIAPR SIDLEQPNCA GGHSVCVDLR 550
    VCFSYIAVPS SYSPTVALDY VLDADTDRRL RGQVPRVTFL SRNLEEPKHQ 600
    ASGTVWLKHQ HDRVCGDAMF QLQENVKDKL RAIVVTLSYS LQTPRLRRQA 650
    PGQGLPPVAP ILNAHQPSTQ RAEIHFLKQG CGEDKICQSN LQLVRARFCT 700
    RVSDTEFQPL PMDVDGTTAL FALSGQPVIG LELMVTNLPS DPAQPQADGD 750
    DAHEAQLLVM LPDSLHYSGV RALDPAEKPL CLSNENASHV ECELGNPMKR 800
    GAQVTFYLIL STSGISIETT ELEVELLLAT ISEQELHPVS ARARVFIELP 850
    LSIAGMAIPQ QLFFSGVVRG ERAMQSERDV GSKVKYEVTV SNQGQSLRTL 900
    GSAFLNIMWP HEIANGKWLL YPMQVELEGG QGPGQKGLCS PRPNILHLDV 950
    DSRDRRRREL EPPEQQEPGE RQEPSMSWWP VSSAEKKKNI TLDCARGTAN 1000
    CVVFSCPLYS FDRAAVLHVW GRLWNSTFLE EYSAVKSLEV IVRANITVKS 1050
    SIKNLMLRDA STVIPVMVYL DPMAVVAEGV PWWVILLAVL AGLLVLALLV 1100
    LLLWKMGFFK RAKHPEATVP QYHAVKIPRE DRQQFKEEKT GTILRNNWGS 1150
    PRREGPDAHP ILAADGHPEL GPDGHPGPGT A 1181

    Note: Gene prediction based on similarity to mouse ortholog.

    Length:1,181
    Mass (Da):128,948
    Last modified:October 5, 2010 - v3
    Checksum:i341C0C72CDB8CA57
    GO
    Isoform Alpha-7X1B (identifier: Q13683-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         268-307: Missing.

    Show »
    Length:1,141
    Mass (Da):124,690
    Checksum:i156565867C8DC8FB
    GO
    Isoform Alpha-7X2B (identifier: Q13683-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         224-267: Missing.

    Show »
    Length:1,137
    Mass (Da):124,307
    Checksum:i43AB97240F469166
    GO
    Isoform Alpha-7X2DB (identifier: Q13683-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         702-776: Missing.

    Show »
    Length:1,106
    Mass (Da):121,065
    Checksum:iCF40297895F88BD2
    GO
    Isoform Alpha-7X1X2A (identifier: Q13683-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1106-1181: MGFFKRAKHP...PDGHPGPGTA → CGFFHRSSQS...PRPPCPSTMR

    Show »
    Length:1,162
    Mass (Da):126,631
    Checksum:iFC25805EDFC23D68
    GO
    Isoform 2 (identifier: Q13683-13) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-97: Missing.
         98-138: LEETDCYRVD...RSQGPGGKIV → MAPFATPMVQ...TRRSPFEGKE
         268-307: Missing.

    Show »
    Length:1,044
    Mass (Da):114,545
    Checksum:i84DF3FB44EE2A31D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti873 – 8731A → T in AAC18968. (PubMed:9590299)Curated
    Sequence conflicti1005 – 10051S → I in AAC18968. (PubMed:9590299)Curated
    Sequence conflicti1013 – 10131R → H in AAH50280. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti457 – 4571I → V.1 Publication
    Corresponds to variant rs17857367 [ dbSNP | Ensembl ].
    VAR_067015
    Natural varianti506 – 5061L → M.1 Publication
    Corresponds to variant rs17854599 [ dbSNP | Ensembl ].
    VAR_067016
    Natural varianti586 – 5861R → H.1 Publication
    Corresponds to variant rs17854598 [ dbSNP | Ensembl ].
    VAR_067017
    Natural varianti695 – 6951R → H.6 Publications
    Corresponds to variant rs1800974 [ dbSNP | Ensembl ].
    VAR_014759
    Natural varianti696 – 6961A → V.1 Publication
    Corresponds to variant rs17855684 [ dbSNP | Ensembl ].
    VAR_067018

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9797Missing in isoform 2. 1 PublicationVSP_040487Add
    BLAST
    Alternative sequencei98 – 13841LEETD…GGKIV → MAPFATPMVQALTTTRIQRQ AEGFQCWRECGTRRSPFEGK E in isoform 2. 1 PublicationVSP_040488Add
    BLAST
    Alternative sequencei224 – 26744Missing in isoform Alpha-7X2B. 4 PublicationsVSP_002727Add
    BLAST
    Alternative sequencei268 – 30740Missing in isoform Alpha-7X1B and isoform 2. 2 PublicationsVSP_002728Add
    BLAST
    Alternative sequencei702 – 77675Missing in isoform Alpha-7X2DB. 1 PublicationVSP_042364Add
    BLAST
    Alternative sequencei1106 – 118176MGFFK…GPGTA → CGFFHRSSQSSSFPTNYHRA CLAVQPSAMEVGGPGTVGWD SSNGRSTPRPPCPSTMR in isoform Alpha-7X1X2A. 1 PublicationVSP_002730Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF032108 mRNA. Translation: AAC39708.1.
    AF052050 mRNA. Translation: AAC18968.1.
    AF072132 mRNA. Translation: AAC80458.1.
    AJ228836
    , AJ228837, AJ228838, AJ228839, AJ228840, AJ228842, AJ228843, AJ228844, AJ228845, AJ228846, AJ228847, AJ228848, AJ228849, AJ228850, AJ228851, AJ228852, AJ228853, AJ228854, AJ228855, AJ228856, AJ228857, AJ228858, AJ228859, AJ228860, AJ228862 Genomic DNA. Translation: CAB41534.1.
    AJ228836
    , AJ228837, AJ228838, AJ228839, AJ228841, AJ228842, AJ228843, AJ228844, AJ228845, AJ228846, AJ228847, AJ228848, AJ228849, AJ228850, AJ228851, AJ228852, AJ228853, AJ228854, AJ228855, AJ228856, AJ228857, AJ228858, AJ228859, AJ228860, AJ228862 Genomic DNA. Translation: CAB41535.1.
    AY358882 mRNA. Translation: AAQ89241.1.
    AK304864 mRNA. Translation: BAG65602.1.
    AC009779 Genomic DNA. No translation available.
    BC050280 mRNA. Translation: AAH50280.1.
    X74295 mRNA. Translation: CAA52348.1.
    AF034833 mRNA. Translation: AAB87696.1.
    CCDSiCCDS44914.1. [Q13683-13]
    CCDS55832.1. [Q13683-3]
    CCDS8888.1. [Q13683-7]
    PIRiJC5950.
    RefSeqiNP_001138468.1. NM_001144996.1. [Q13683-3]
    NP_001138469.1. NM_001144997.1. [Q13683-13]
    NP_002197.2. NM_002206.2. [Q13683-7]
    XP_005268896.1. XM_005268839.1. [Q13683-1]
    XP_005268898.1. XM_005268841.1. [Q13683-10]
    UniGeneiHs.524484.

    Genome annotation databases

    EnsembliENST00000257879; ENSP00000257879; ENSG00000135424. [Q13683-7]
    ENST00000452168; ENSP00000393844; ENSG00000135424. [Q13683-13]
    ENST00000553804; ENSP00000452120; ENSG00000135424. [Q13683-3]
    ENST00000555728; ENSP00000452387; ENSG00000135424. [Q13683-1]
    GeneIDi3679.
    KEGGihsa:3679.
    UCSCiuc001shg.3. human. [Q13683-7]
    uc001shh.3. human. [Q13683-3]
    uc010sps.2. human. [Q13683-13]

    Polymorphism databases

    DMDMi308153592.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF032108 mRNA. Translation: AAC39708.1 .
    AF052050 mRNA. Translation: AAC18968.1 .
    AF072132 mRNA. Translation: AAC80458.1 .
    AJ228836
    , AJ228837 , AJ228838 , AJ228839 , AJ228840 , AJ228842 , AJ228843 , AJ228844 , AJ228845 , AJ228846 , AJ228847 , AJ228848 , AJ228849 , AJ228850 , AJ228851 , AJ228852 , AJ228853 , AJ228854 , AJ228855 , AJ228856 , AJ228857 , AJ228858 , AJ228859 , AJ228860 , AJ228862 Genomic DNA. Translation: CAB41534.1 .
    AJ228836
    , AJ228837 , AJ228838 , AJ228839 , AJ228841 , AJ228842 , AJ228843 , AJ228844 , AJ228845 , AJ228846 , AJ228847 , AJ228848 , AJ228849 , AJ228850 , AJ228851 , AJ228852 , AJ228853 , AJ228854 , AJ228855 , AJ228856 , AJ228857 , AJ228858 , AJ228859 , AJ228860 , AJ228862 Genomic DNA. Translation: CAB41535.1 .
    AY358882 mRNA. Translation: AAQ89241.1 .
    AK304864 mRNA. Translation: BAG65602.1 .
    AC009779 Genomic DNA. No translation available.
    BC050280 mRNA. Translation: AAH50280.1 .
    X74295 mRNA. Translation: CAA52348.1 .
    AF034833 mRNA. Translation: AAB87696.1 .
    CCDSi CCDS44914.1. [Q13683-13 ]
    CCDS55832.1. [Q13683-3 ]
    CCDS8888.1. [Q13683-7 ]
    PIRi JC5950.
    RefSeqi NP_001138468.1. NM_001144996.1. [Q13683-3 ]
    NP_001138469.1. NM_001144997.1. [Q13683-13 ]
    NP_002197.2. NM_002206.2. [Q13683-7 ]
    XP_005268896.1. XM_005268839.1. [Q13683-1 ]
    XP_005268898.1. XM_005268841.1. [Q13683-10 ]
    UniGenei Hs.524484.

    3D structure databases

    ProteinModelPortali Q13683.
    SMRi Q13683. Positions 34-680, 1077-1114.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109885. 6 interactions.
    DIPi DIP-5981N.
    IntActi Q13683. 1 interaction.
    MINTi MINT-140160.
    STRINGi 9606.ENSP00000257879.

    PTM databases

    PhosphoSitei Q13683.

    Polymorphism databases

    DMDMi 308153592.

    Proteomic databases

    MaxQBi Q13683.
    PaxDbi Q13683.
    PRIDEi Q13683.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257879 ; ENSP00000257879 ; ENSG00000135424 . [Q13683-7 ]
    ENST00000452168 ; ENSP00000393844 ; ENSG00000135424 . [Q13683-13 ]
    ENST00000553804 ; ENSP00000452120 ; ENSG00000135424 . [Q13683-3 ]
    ENST00000555728 ; ENSP00000452387 ; ENSG00000135424 . [Q13683-1 ]
    GeneIDi 3679.
    KEGGi hsa:3679.
    UCSCi uc001shg.3. human. [Q13683-7 ]
    uc001shh.3. human. [Q13683-3 ]
    uc010sps.2. human. [Q13683-13 ]

    Organism-specific databases

    CTDi 3679.
    GeneCardsi GC12M056078.
    GeneReviewsi ITGA7.
    H-InvDB HIX0010702.
    HIX0201958.
    HGNCi HGNC:6143. ITGA7.
    HPAi HPA008427.
    MIMi 600536. gene.
    613204. phenotype.
    neXtProti NX_Q13683.
    Orphaneti 2020. Congenital fiber-type disproportion myopathy.
    34520. Congenital muscular dystrophy with integrin alpha-7 deficiency.
    PharmGKBi PA29943.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG26407.
    HOVERGENi HBG108011.
    InParanoidi Q13683.
    KOi K06583.
    OMAi QGPGQKG.
    PhylomeDBi Q13683.
    TreeFami TF105391.

    Enzyme and pathway databases

    Reactomei REACT_13552. Integrin cell surface interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.
    SignaLinki Q13683.

    Miscellaneous databases

    GeneWikii ITGA7.
    GenomeRNAii 3679.
    NextBioi 14399.
    PROi Q13683.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13683.
    Bgeei Q13683.
    CleanExi HS_ITGA7.
    Genevestigatori Q13683.

    Family and domain databases

    InterProi IPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    [Graphical view ]
    Pfami PF01839. FG-GAP. 2 hits.
    PF08441. Integrin_alpha2. 1 hit.
    [Graphical view ]
    PRINTSi PR01185. INTEGRINA.
    SMARTi SM00191. Int_alpha. 5 hits.
    [Graphical view ]
    PROSITEi PS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel extracellular domain variant of the human integrin alpha 7 subunit generated by alternative intron splicing."
      Leung E., Lim S.P., Berg R., Yang Y., Ni J., Wang S.-X., Krissansen G.W.
      Biochem. Biophys. Res. Commun. 243:317-325(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-7X2B AND ALPHA-7X2DB), VARIANT HIS-695.
      Tissue: Fetal heart and Osteoblast.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-7X2B), INVOLVEMENT IN MDCI, VARIANT HIS-695.
    3. "Cloning of human integrin alpha-7 cDNA."
      Vizirianakis I.S., Ziober B.L., Kramer R.H.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-7X2B), VARIANT HIS-695.
    4. "Structure, genetic localization, and identification of the cardiac and skeletal muscle transcripts of the human integrin alpha7 gene (ITGA7)."
      Vignier N., Moghadaszadeh B., Gary F., Beckmann J., Mayer U., Guicheney P.
      Biochem. Biophys. Res. Commun. 260:357-364(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANT HIS-695.
      Tissue: Skeletal muscle.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-7X1B), VARIANT HIS-695.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT HIS-695.
      Tissue: Uterus.
    7. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-7X2B), VARIANTS VAL-457; MET-506; HIS-586 AND VAL-696.
      Tissue: Brain.
    9. "Expression of alpha 7 integrin cytoplasmic domains during skeletal muscle development: alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases."
      Song W.K., Wang W., Sato H., Bielser D.A., Kaufman S.J.
      J. Cell Sci. 106:1139-1152(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1105-1181 (ISOFORMS ALPHA-7X1B/ALPHA-7X2B/ALPHA-7X2DB/ALPHA-7X1X2B/2).
      Tissue: Fetal muscle.
    10. "Relation between integrin alpha7Bbeta1 expression in human intestinal cells and enterocytic differentiation."
      Basora N., Vachon P.H., Herring-Gillam F.E., Perreault N., Beaulieu J.-F.
      Gastroenterology 113:1510-1521(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1105-1181 (ISOFORMS ALPHA-7X1X2B AND ALPHA-7X1X2A).
      Tissue: Skeletal muscle.
    11. "Laminin-binding integrin alpha 7 beta 1: functional characterization and expression in normal and malignant melanocytes."
      Kramer R.H., Vu M.P., Cheng Y.F., Ramos D.M., Timpl R., Waleh N.
      Cell Regul. 2:805-817(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-45.
      Tissue: Melanoma.
    12. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-48.
    13. "The laminin-binding activity of the alpha 7 integrin receptor is defined by developmentally regulated splicing in the extracellular domain."
      Ziober B.L., Chen Y.Q., Kramer R.H.
      Mol. Biol. Cell 8:1723-1734(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "The role of extracellular and cytoplasmic splice domains of alpha7-integrin in cell adhesion and migration on laminins."
      Schoeber S., Mielenz D., Echtermeyer F., Hapke S., Poeschl E., von der Mark H., Moch H., von der Mark K.
      Exp. Cell Res. 255:303-313(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Synaptic integrins in developing, adult, and mutant muscle: selective association of alpha1, alpha7A, and alpha7B integrins with the neuromuscular junction."
      Martin P.T., Kaufman S.J., Kramer R.H., Sanes J.R.
      Dev. Biol. 174:125-139(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    16. "Laminin-binding integrin alpha7 is required for contractile phenotype expression by human airway myocytes."
      Tran T., Ens-Blackie K., Rector E.S., Stelmack G.L., McNeill K.D., Tarone G., Gerthoffer W.T., Unruh H., Halayko A.J.
      Am. J. Respir. Cell Mol. Biol. 37:668-680(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Genetically determined proteolytic cleavage modulates alpha7beta1 integrin function."
      Liu J., Gurpur P.B., Kaufman S.J.
      J. Biol. Chem. 283:35668-35678(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY UROKINASE.
    18. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1025.
      Tissue: Liver.
    19. "Biophysical and structural studies of the human calcium- and integrin-binding protein family: understanding their functional similarities and differences."
      Huang H., Bogstie J.N., Vogel H.J.
      Biochem. Cell Biol. 90:646-656(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIB1.

    Entry informationi

    Entry nameiITA7_HUMAN
    AccessioniPrimary (citable) accession number: Q13683
    Secondary accession number(s): B4E3U0
    , C9JMD3, C9JMZ6, O43197, Q86W93, Q9NY89, Q9UET0, Q9UEV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 150 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3