|ITA7_HUMAN » Integrin alpha-7 »|
|Hydrophobic Thickness||38.4 ± 1.2 Å|
|Tilt Angle||0 ± 1°|
|Links||UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, Reactome|
|TM Segments||1081-1109 (1081-1112)|
Dilated cardiomyopathy (KEGG)
ECM-receptor interaction (KEGG)
Focal adhesion (KEGG)
Hypertrophic cardiomyopathy (KEGG)
PI3K-Akt signaling pathway (KEGG)
Signal Transduction (Reactome)
|UniProt annotation for ITA7_HUMAN » Integrin alpha-7|
|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. SUBUNIT: 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. 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. DEVELOPMENTAL STAGE: In renewing intestinal epithelium, expression of isoforms containing segment B correlates with the onset of enterocytic differentiation. DISEASE: Muscular dystrophy congenital due to integrin alpha-7 deficiency (MDCI) OMIM: 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. is caused by mutations affecting the gene represented in this entry.|
|UniProt features for ITA7_HUMAN » Integrin alpha-7|
SIGNAL 1 33 |
CHAIN 34 1181 Integrin alpha-7.
CHAIN 34 955 Integrin alpha-7 heavy chain (Potential).
CHAIN 648 1181 Integrin alpha-7 70 kDa form.
CHAIN 959 1181 Integrin alpha-7 light chain (Potential).
REPEAT 35 103 FG-GAP 1.
REPEAT 110 175 FG-GAP 2.
REPEAT 185 238 FG-GAP 3.
REPEAT 292 350 FG-GAP 4.
REPEAT 351 411 FG-GAP 5.
REPEAT 412 467 FG-GAP 6.
REPEAT 471 530 FG-GAP 7.
REPEAT 1157 1160 1.
REPEAT 1165 1168 2.
REPEAT 1173 1176 3.
REGION 1157 1176 3 X 4 AA repeats of D-X-H-P.
MOTIF 1107 1111 GFFKR motif.
SITE 647 648 Cleavage; by urokinase.
DISULFID 94 103 By similarity.
DISULFID 140 163 By similarity.
DISULFID 184 197 By similarity.
DISULFID 539 546 By similarity.
DISULFID 552 615 By similarity.
DISULFID 681 687 By similarity.
DISULFID 781 792 By similarity.
DISULFID 939 994 Interchain (between heavy and light chains) (By similarity).
DISULFID 1001 1006 By similarity.
|Amino Acid Sequence for ITA7_HUMAN » Integrin alpha-7|
|MAGARSRDPW GASGICYLFG SLLVELLFSR AVAFNLDVMG ALRKEGEPGS LFGFSVALHR QLQPRPQSWL LVGAPQALAL PGQQANRTGG LFACPLSLEE TDCYRVDIDQ GADMQKESKE NQWLGVSVRS QGPGGKIVTC AHRYEARQRV DQILETRDMI GRCFVLSQDL AIRDELDGGE WKFCEGRPQG HEQFGFCQQG TAAAFSPDSH YLLFGAPGTY NWKGTARVEL CAQGSADLAH LDDGPYEAGG EKEQDPRLIP VPANSYFGLL FVTNIDSSDP DQLVYKTLDP ADRLPGPAGD LALNSYLGFS IDSGKGLVRA EELSFVAGAP RANHKGAVVI LRKDSASRLV PEVMLSGERL TSGFGYSLAV ADLNSDGWPD LIVGAPYFFE RQEELGGAVY VYLNQGGHWA GISPLRLCGS PDSMFGISLA VLGDLNQDGF PDIAVGAPFD GDGKVFIYHG SSLGVVAKPS QVLEGEAVGI KSFGYSLSGS LDMDGNQYPD LLVGSLADTA VLFRARPILH VSHEVSIAPR SIDLEQPNCA GGHSVCVDLR VCFSYIAVPS SYSPTVALDY VLDADTDRRL RGQVPRVTFL SRNLEEPKHQ ASGTVWLKHQ HDRVCGDAMF QLQENVKDKL RAIVVTLSYS LQTPRLRRQA PGQGLPPVAP ILNAHQPSTQ RAEIHFLKQG CGEDKICQSN LQLVHARFCT RVSDTEFQPL PMDVDGTTAL FALSGQPVIG LELMVTNLPS DPAQPQADGD DAHEAQLLVM LPDSLHYSGV RALDPAEKPL CLSNENASHV ECELGNPMKR GAQVTFYLIL STSGISIETT ELEVELLLAT ISEQELHPVS ARARVFIELP LSIAGMAIPQ QLFFSGVVRG ERAMQSERDV GSKVKYEVTV SNQGQSLRTL GSAFLNIMWP HEIANGKWLL YPMQVELEGG QGPGQKGLCS PRPNILHLDV DSRDRRRREL EPPEQQEPGE RQEPSMSWWP VSSAEKKKNI TLDCARGTAN CVVFSCPLYS FDRAAVLHVW GRLWNSTFLE EYSAVKSLEV IVRANITVKS SIKNLMLRDA STVIPVMVYL DPMAVVAEGV PWWVILLAVL AGLLVLALLV LLLWKMGFFK RAKHPEATVP QYHAVKIPRE DRQQFKEEKT GTILRNNWGS PRREGPDAHP ILAADGHPEL GPDGHPGPGT A|