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Q13683

- ITA7_HUMAN

UniProt

Q13683 - ITA7_HUMAN

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Protein

Integrin alpha-7

Gene
ITGA7, UNQ406/PRO768
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.3 Publications

Sites

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

Regions

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

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 10821049Extracellular Reviewed predictionAdd
BLAST
Transmembranei1083 – 110321Helical; Reviewed predictionAdd
BLAST
Topological domaini1104 – 118178Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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 chain Reviewed predictionPRO_0000016268Add
BLAST
Chaini648 – 1181534Integrin alpha-7 70 kDa formPRO_0000398833Add
BLAST
Chaini959 – 1181223Integrin alpha-7 light chain Reviewed predictionPRO_0000016269Add
BLAST

Amino acid modifications

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

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.1 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.

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

Contains 7 FG-GAP repeats.

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

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. VSP_040487Add
BLAST
Alternative sequencei98 – 13841LEETD…GGKIV → MAPFATPMVQALTTTRIQRQ AEGFQCWRECGTRRSPFEGK E in isoform 2. VSP_040488Add
BLAST
Alternative sequencei224 – 26744Missing in isoform Alpha-7X2B. VSP_002727Add
BLAST
Alternative sequencei268 – 30740Missing in isoform Alpha-7X1B and isoform 2. VSP_002728Add
BLAST
Alternative sequencei702 – 77675Missing in isoform Alpha-7X2DB. VSP_042364Add
BLAST
Alternative sequencei1106 – 118176MGFFK…GPGTA → CGFFHRSSQSSSFPTNYHRA CLAVQPSAMEVGGPGTVGWD SSNGRSTPRPPCPSTMR in isoform Alpha-7X1X2A. VSP_002730Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti873 – 8731A → T in AAC18968. 1 Publication
Sequence conflicti1005 – 10051S → I in AAC18968. 1 Publication
Sequence conflicti1013 – 10131R → H in AAH50280. 1 Publication

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]
ENST00000257880; ENSP00000257880; ENSG00000135424. [Q13683-10]
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 ]
ENST00000257880 ; ENSP00000257880 ; ENSG00000135424 . [Q13683-10 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 149 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

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