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Q13683 (ITA7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin alpha-7
Gene names
Name:ITGA7
ORF Names:UNQ406/PRO768
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1181 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13 Ref.14 Ref.16

Subunit structure

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. Ref.19

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

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. Ref.15

Developmental stage

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

Post-translational modification

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. Ref.17

Involvement in disease

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. Ref.2

Sequence similarities

Belongs to the integrin alpha chain family.

Contains 7 FG-GAP repeats.

Ontologies

Keywords
   Biological processCell adhesion
Cell shape
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCongenital muscular dystrophy
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionIntegrin
Receptor
   PTMADP-ribosylation
Cleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood vessel morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell migration

Inferred from electronic annotation. Source: Ensembl

cell-matrix adhesion

Traceable author statement PubMed 9354797. Source: ProtInc

extracellular matrix organization

Traceable author statement. Source: Reactome

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

muscle organ development

Traceable author statement PubMed 9354797Ref.2. Source: ProtInc

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentalpha7-beta1 integrin complex

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

muscle tendon junction

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

sarcolemma

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

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)

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.
Note: Gene prediction based on similarity to mouse ortholog.
Isoform Alpha-7X1B (identifier: Q13683-3)

The sequence of this isoform differs from the canonical sequence as follows:
     268-307: Missing.
Isoform Alpha-7X2B (identifier: Q13683-7)

The sequence of this isoform differs from the canonical sequence as follows:
     224-267: Missing.
Isoform Alpha-7X2DB (identifier: Q13683-9)

The sequence of this isoform differs from the canonical sequence as follows:
     702-776: Missing.
Isoform Alpha-7X1X2A (identifier: Q13683-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1106-1181: MGFFKRAKHP...PDGHPGPGTA → CGFFHRSSQS...PRPPCPSTMR
Isoform 2 (identifier: Q13683-13)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Ref.11 Ref.12
Chain34 – 11811148Integrin alpha-7
PRO_0000016267
Chain34 – 955922Integrin alpha-7 heavy chain Potential
PRO_0000016268
Chain648 – 1181534Integrin alpha-7 70 kDa form
PRO_0000398833
Chain959 – 1181223Integrin alpha-7 light chain Potential
PRO_0000016269

Regions

Topological domain34 – 10821049Extracellular Potential
Transmembrane1083 – 110321Helical; Potential
Topological domain1104 – 118178Cytoplasmic Potential
Repeat35 – 10369FG-GAP 1
Repeat110 – 17566FG-GAP 2
Repeat185 – 23854FG-GAP 3
Repeat292 – 35059FG-GAP 4
Repeat351 – 41161FG-GAP 5
Repeat412 – 46756FG-GAP 6
Repeat471 – 53060FG-GAP 7
Repeat1157 – 116041
Repeat1165 – 116842
Repeat1173 – 117643
Calcium binding372 – 3809 Potential
Calcium binding434 – 4429 Potential
Calcium binding492 – 5009 Potential
Region1157 – 1176203 X 4 AA repeats of D-X-H-P
Motif1107 – 11115GFFKR motif
Compositional bias953 – 9586Poly-Arg

Sites

Site647 – 6482Cleavage; by urokinase

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation7861N-linked (GlcNAc...) Potential
Glycosylation9891N-linked (GlcNAc...) Potential
Glycosylation10251N-linked (GlcNAc...) Ref.18
Glycosylation10451N-linked (GlcNAc...) Potential
Disulfide bond94 ↔ 103 By similarity
Disulfide bond140 ↔ 163 By similarity
Disulfide bond184 ↔ 197 By similarity
Disulfide bond539 ↔ 546 By similarity
Disulfide bond552 ↔ 615 By similarity
Disulfide bond681 ↔ 687 By similarity
Disulfide bond781 ↔ 792 By similarity
Disulfide bond939 ↔ 994Interchain (between heavy and light chains) By similarity
Disulfide bond1001 ↔ 1006 By similarity

Natural variations

Alternative sequence1 – 9797Missing in isoform 2.
VSP_040487
Alternative sequence98 – 13841LEETD…GGKIV → MAPFATPMVQALTTTRIQRQ AEGFQCWRECGTRRSPFEGK E in isoform 2.
VSP_040488
Alternative sequence224 – 26744Missing in isoform Alpha-7X2B.
VSP_002727
Alternative sequence268 – 30740Missing in isoform Alpha-7X1B and isoform 2.
VSP_002728
Alternative sequence702 – 77675Missing in isoform Alpha-7X2DB.
VSP_042364
Alternative sequence1106 – 118176MGFFK…GPGTA → CGFFHRSSQSSSFPTNYHRA CLAVQPSAMEVGGPGTVGWD SSNGRSTPRPPCPSTMR in isoform Alpha-7X1X2A.
VSP_002730
Natural variant4571I → V. Ref.8
Corresponds to variant rs17857367 [ dbSNP | Ensembl ].
VAR_067015
Natural variant5061L → M. Ref.8
Corresponds to variant rs17854599 [ dbSNP | Ensembl ].
VAR_067016
Natural variant5861R → H. Ref.8
Corresponds to variant rs17854598 [ dbSNP | Ensembl ].
VAR_067017
Natural variant6951R → H. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6
Corresponds to variant rs1800974 [ dbSNP | Ensembl ].
VAR_014759
Natural variant6961A → V. Ref.8
Corresponds to variant rs17855684 [ dbSNP | Ensembl ].
VAR_067018

Experimental info

Sequence conflict8731A → T in AAC18968. Ref.2
Sequence conflict10051S → I in AAC18968. Ref.2
Sequence conflict10131R → H in AAH50280. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha-7X1X2B [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: 341C0C72CDB8CA57

FASTA1,181128,948
        10         20         30         40         50         60 
MAGARSRDPW GASGICYLFG SLLVELLFSR AVAFNLDVMG ALRKEGEPGS LFGFSVALHR 

        70         80         90        100        110        120 
QLQPRPQSWL LVGAPQALAL PGQQANRTGG LFACPLSLEE TDCYRVDIDQ GADMQKESKE 

       130        140        150        160        170        180 
NQWLGVSVRS QGPGGKIVTC AHRYEARQRV DQILETRDMI GRCFVLSQDL AIRDELDGGE 

       190        200        210        220        230        240 
WKFCEGRPQG HEQFGFCQQG TAAAFSPDSH YLLFGAPGTY NWKGTARVEL CAQGSADLAH 

       250        260        270        280        290        300 
LDDGPYEAGG EKEQDPRLIP VPANSYFGLL FVTNIDSSDP DQLVYKTLDP ADRLPGPAGD 

       310        320        330        340        350        360 
LALNSYLGFS IDSGKGLVRA EELSFVAGAP RANHKGAVVI LRKDSASRLV PEVMLSGERL 

       370        380        390        400        410        420 
TSGFGYSLAV ADLNSDGWPD LIVGAPYFFE RQEELGGAVY VYLNQGGHWA GISPLRLCGS 

       430        440        450        460        470        480 
PDSMFGISLA VLGDLNQDGF PDIAVGAPFD GDGKVFIYHG SSLGVVAKPS QVLEGEAVGI 

       490        500        510        520        530        540 
KSFGYSLSGS LDMDGNQYPD LLVGSLADTA VLFRARPILH VSHEVSIAPR SIDLEQPNCA 

       550        560        570        580        590        600 
GGHSVCVDLR VCFSYIAVPS SYSPTVALDY VLDADTDRRL RGQVPRVTFL SRNLEEPKHQ 

       610        620        630        640        650        660 
ASGTVWLKHQ HDRVCGDAMF QLQENVKDKL RAIVVTLSYS LQTPRLRRQA PGQGLPPVAP 

       670        680        690        700        710        720 
ILNAHQPSTQ RAEIHFLKQG CGEDKICQSN LQLVRARFCT RVSDTEFQPL PMDVDGTTAL 

       730        740        750        760        770        780 
FALSGQPVIG LELMVTNLPS DPAQPQADGD DAHEAQLLVM LPDSLHYSGV RALDPAEKPL 

       790        800        810        820        830        840 
CLSNENASHV ECELGNPMKR GAQVTFYLIL STSGISIETT ELEVELLLAT ISEQELHPVS 

       850        860        870        880        890        900 
ARARVFIELP LSIAGMAIPQ QLFFSGVVRG ERAMQSERDV GSKVKYEVTV SNQGQSLRTL 

       910        920        930        940        950        960 
GSAFLNIMWP HEIANGKWLL YPMQVELEGG QGPGQKGLCS PRPNILHLDV DSRDRRRREL 

       970        980        990       1000       1010       1020 
EPPEQQEPGE RQEPSMSWWP VSSAEKKKNI TLDCARGTAN CVVFSCPLYS FDRAAVLHVW 

      1030       1040       1050       1060       1070       1080 
GRLWNSTFLE EYSAVKSLEV IVRANITVKS SIKNLMLRDA STVIPVMVYL DPMAVVAEGV 

      1090       1100       1110       1120       1130       1140 
PWWVILLAVL AGLLVLALLV LLLWKMGFFK RAKHPEATVP QYHAVKIPRE DRQQFKEEKT 

      1150       1160       1170       1180 
GTILRNNWGS PRREGPDAHP ILAADGHPEL GPDGHPGPGT A 

« Hide

Isoform Alpha-7X1B [UniParc].

Checksum: 156565867C8DC8FB
Show »

FASTA1,141124,690
Isoform Alpha-7X2B [UniParc].

Checksum: 43AB97240F469166
Show »

FASTA1,137124,307
Isoform Alpha-7X2DB [UniParc].

Checksum: CF40297895F88BD2
Show »

FASTA1,106121,065
Isoform Alpha-7X1X2A [UniParc].

Checksum: FC25805EDFC23D68
Show »

FASTA1,162126,631
Isoform 2 [UniParc].

Checksum: 84DF3FB44EE2A31D
Show »

FASTA1,044114,545

References

« Hide 'large scale' references
[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]"Mutations in the integrin alpha7 gene cause congenital myopathy."
Hayashi Y.K., Chou F.-L., Engvall E., Ogawa M., Matsuda C., Hirabayashi S., Yokochi K., Ziober B.L., Kramer R.H., Kaufman S.J., Ozawa E., Goto Y., Nonaka I., Tsukahara T., Wang J.Z., Hoffman E.P., Arahata K.
Nat. Genet. 19:94-97(1998) [PubMed] [Europe PMC] [Abstract]
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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF032108 mRNA. Translation: AAC39708.1.
AF052050 mRNA. Translation: AAC18968.1.
AF072132 mRNA. Translation: AAC80458.1.
AJ228836 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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.
PIRJC5950.
RefSeqNP_001138468.1. NM_001144996.1.
NP_001138469.1. NM_001144997.1.
NP_002197.2. NM_002206.2.
XP_005268896.1. XM_005268839.1.
XP_005268898.1. XM_005268841.1.
UniGeneHs.524484.

3D structure databases

ProteinModelPortalQ13683.
SMRQ13683. Positions 34-680, 824-857, 1076-1116.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109885. 6 interactions.
DIPDIP-5981N.
IntActQ13683. 1 interaction.
MINTMINT-140160.
STRING9606.ENSP00000257879.

PTM databases

PhosphoSiteQ13683.

Polymorphism databases

DMDM308153592.

Proteomic databases

PaxDbQ13683.
PRIDEQ13683.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257879; ENSP00000257879; ENSG00000135424. [Q13683-7]
ENST00000257880; ENSP00000257880; ENSG00000135424. [Q13683-10]
ENST00000452168; ENSP00000393844; ENSG00000135424. [Q13683-13]
ENST00000553804; ENSP00000452120; ENSG00000135424. [Q13683-3]
ENST00000555728; ENSP00000452387; ENSG00000135424. [Q13683-1]
GeneID3679.
KEGGhsa:3679.
UCSCuc001shg.3. human. [Q13683-7]
uc001shh.3. human. [Q13683-3]
uc010sps.2. human. [Q13683-13]

Organism-specific databases

CTD3679.
GeneCardsGC12M056078.
H-InvDBHIX0010702.
HIX0201958.
HGNCHGNC:6143. ITGA7.
HPAHPA008427.
MIM600536. gene.
613204. phenotype.
neXtProtNX_Q13683.
Orphanet2020. Congenital fiber-type disproportion myopathy.
34520. Congenital muscular dystrophy with integrin alpha-7 deficiency.
PharmGKBPA29943.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26407.
HOVERGENHBG108011.
InParanoidQ13683.
KOK06583.
OMAQGPGQKG.
PhylomeDBQ13683.
TreeFamTF105391.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
SignaLinkQ13683.

Gene expression databases

ArrayExpressQ13683.
BgeeQ13683.
CleanExHS_ITGA7.
GenevestigatorQ13683.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]
PfamPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSPR01185. INTEGRINA.
SMARTSM00191. Int_alpha. 5 hits.
[Graphical view]
PROSITEPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiITGA7.
GenomeRNAi3679.
NextBio14399.
PROQ13683.
SOURCESearch...

Entry information

Entry nameITA7_HUMAN
AccessionPrimary (citable) accession number: Q13683
Secondary accession number(s): B4E3U0 expand/collapse secondary AC list , C9JMD3, C9JMZ6, O43197, Q86W93, Q9NY89, Q9UET0, Q9UEV2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM