ID ITA7_MOUSE Reviewed; 1179 AA. AC Q61738; O88731; O88732; P70350; Q61737; Q61741; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 24-JAN-2024, entry version 169. DE RecName: Full=Integrin alpha-7; DE Contains: DE RecName: Full=Integrin alpha-7 heavy chain; DE Contains: DE RecName: Full=Integrin alpha-7 light chain; DE Flags: Precursor; GN Name=Itga7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-7X2B), NUCLEOTIDE SEQUENCE RP [GENOMIC DNA] OF 1-70 (ISOFORM ALPHA-7X1X2B), NUCLEOTIDE SEQUENCE [MRNA] OF RP 1031-1179 (ISOFORMS ALPHA-7X1A/ALPHA-7X2A/ALPHA-7X1X2A), AND ALTERNATIVE RP SPLICING. RC STRAIN=BALB/cJ; TISSUE=Heart; RX PubMed=8253814; DOI=10.1016/s0021-9258(19)74380-4; RA Ziober B.L., Vu M.P., Waleh N., Crawford J., Lin C.-S., Kramer R.H.; RT "Alternative extracellular and cytoplasmic domains of the integrin alpha 7 RT subunit are differentially expressed during development."; RL J. Biol. Chem. 268:26773-26783(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA-7X1X2A AND ALPHA-7X1X2B). RC STRAIN=129/Sv; RA Saher G., Echtermeyer F., Beier D.R., Poeschl E., Mayer U.; RT "Genomic organization and chromosomal localization of the mouse integrin RT alpha7 gene."; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70. RC STRAIN=C57BL/6 X CBA; RX PubMed=8798472; DOI=10.1074/jbc.271.37.22915; RA Ziober B.L., Kramer R.H.; RT "Identification and characterization of the cell type-specific and RT developmentally regulated alpha7 integrin gene promoter."; RL J. Biol. Chem. 271:22915-22922(1996). RN [4] RP PROTEIN SEQUENCE OF 34-58. RC TISSUE=Melanoma; RX PubMed=1839357; DOI=10.1091/mbc.2.10.805; RA Kramer R.H., Vu M.P., Cheng Y.F., Ramos D.M., Timpl R., Waleh N.; RT "Laminin-binding integrin alpha 7 beta 1: functional characterization and RT expression in normal and malignant melanocytes."; RL Cell Regul. 2:805-817(1991). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1013-1179 (ISOFORMS RP ALPHA-7X1A/ALPHA-7X2A/ALPHA-7X1X2A). RC STRAIN=C57BL/6 X BALB/c; RX PubMed=8360188; DOI=10.1016/s0021-9258(17)46729-9; RA Collo G., Starr L., Quaranta V.; RT "A new isoform of the laminin receptor integrin alpha 7 beta 1 is RT developmentally regulated in skeletal muscle."; RL J. Biol. Chem. 268:19019-19024(1993). RN [6] RP TISSUE SPECIFICITY. RX PubMed=8626012; DOI=10.1006/dbio.1996.0057; RA Martin P.T., Kaufman S.J., Kramer R.H., Sanes J.R.; RT "Synaptic integrins in developing, adult, and mutant muscle: selective RT association of alpha1, alpha7A, and alpha7B integrins with the RT neuromuscular junction."; RL Dev. Biol. 174:125-139(1996). RN [7] RP FUNCTION. RX PubMed=9354797; DOI=10.1038/ng1197-318; RA Mayer U., Saher G., Fassler R., Bornemann A., Echtermeyer F., RA von der Mark H., Miosge N., Poeschl E., von der Mark K.; RT "Absence of integrin alpha 7 causes a novel form of muscular dystrophy."; RL Nat. Genet. 17:318-323(1997). RN [8] RP ADP-RIBOSYLATION. RX PubMed=7721841; DOI=10.1074/jbc.270.16.9227; RA Zolkiewska A., Moss J.; RT "Processing of ADP-ribosylated integrin alpha 7 in skeletal muscle RT myotubes."; RL J. Biol. Chem. 270:9227-9233(1995). RN [9] RP ABSENCE OF CLEAVAGE BY UROKINASE. RX PubMed=18940796; DOI=10.1074/jbc.m804661200; RA Liu J., Gurpur P.B., Kaufman S.J.; RT "Genetically determined proteolytic cleavage modulates alpha7beta1 integrin RT function."; RL J. Biol. Chem. 283:35668-35678(2008). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1023. RC TISSUE=Myoblast; RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200; RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.; RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome: RT identification, glycosite occupancy, and membrane orientation."; RL Mol. Cell. Proteomics 8:2555-2569(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, and Lung; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Integrin alpha-7/beta-1 is the primary laminin receptor on CC skeletal myoblasts and adult myofibers. During myogenic CC differentiation, it may induce changes in the shape and mobility of CC myoblasts, and facilitate their localization at laminin-rich sites of CC secondary fiber formation. Involved in the maintenance of the myofibers CC cytoarchitecture as well as for their anchorage, viability and CC functional integrity. Mice carrying a ITGA7 null allele are viable and CC fertile, but show progressive muscular dystrophy starting soon after CC birth, but with a distinct variability in different muscle types. CC Required to promote contractile phenotype acquisition in differentiated CC airway smooth muscle (ASM) cells. Acts as a Schwann cell receptor for CC laminin-2. Acts as a receptor of COMP and mediates its effect on CC vascular smooth muscle cells (VSMCs) maturation (By similarity). CC {ECO:0000250, ECO:0000269|PubMed:9354797}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit CC is composed of a heavy and a light chain linked by a disulfide bond. CC Alpha-7 associates with beta-1. Interacts with COMP. Interacts (via C- CC terminus intracellular tail region) with CIB1; the interaction is CC stabilized/increased in a calcium- and magnesium-dependent manner (By CC similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q61738-6; Q8C2K1: Def6; NbExp=3; IntAct=EBI-1786329, EBI-2121188; CC Q61738-6; Q6A028: Swap70; NbExp=2; IntAct=EBI-1786329, EBI-2121215; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Comment=Additional isoforms seem to exist. There is a combination of CC at least four alternatively spliced domains, two extracellular (X1 CC and X2) and two cytoplasmic (A and B). A third potential CC alternatively spliced cytoplasmic domain (C) doesn't appear to be CC expressed. So far detected are isoform alpha-7X1A, isoform alpha-7X1B CC and isoform alpha-7X2B. Experimental confirmation may be lacking for CC some isoforms.; CC Name=Alpha-7X1X2B; CC IsoId=Q61738-1; Sequence=Displayed; CC Name=Alpha-7X1A; CC IsoId=Q61738-2; Sequence=VSP_002732, VSP_002733; CC Name=Alpha-7X1B; CC IsoId=Q61738-3; Sequence=VSP_002732; CC Name=Alpha-7X2A; CC IsoId=Q61738-4; Sequence=VSP_002731, VSP_002733; CC Name=Alpha-7X2B; CC IsoId=Q61738-5; Sequence=VSP_002731; CC Name=Alpha-7X1X2A; CC IsoId=Q61738-6; Sequence=VSP_002733; CC -!- TISSUE SPECIFICITY: Isoforms containing segment X2 are found in adult CC heart, lung and skeletal muscle. Isoforms containing segment X1 are CC expressed in adult heart, lung and in proliferating skeletal myoblasts CC but not in adult skeletal muscle. Isoforms containing segment a are CC exclusively found in skeletal muscle. Isoforms containing segment B are CC widely expressed. In muscle fibers isoforms containing segment A and B CC are expressed at myotendinous and neuromuscular junctions; isoforms CC containing segment C are expressed at neuromuscular junctions and at CC extrasynaptic sites. {ECO:0000269|PubMed:8626012}. CC -!- DEVELOPMENTAL STAGE: Isoforms are developmentally regulated during the CC formation of skeletal muscle. Undifferentiated (replicating) myoblasts CC express isoforms containing segment B only, whereas differentiated CC myoblasts express isoforms containing segments A or B. CC -!- PTM: ADP-ribosylated on at least two sites of the extracellular domain CC in skeletal myotubes (in vitro). CC -!- PTM: No proteolytic cleavage to produce the 70 kDa form is seen due to CC the presence of a Gly instead of an arginine residue at position 647. CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L23423; AAA16600.1; -; mRNA. DR EMBL; Y12380; CAA73023.1; -; Genomic_DNA. DR EMBL; Y12383; CAA73023.1; JOINED; Genomic_DNA. DR EMBL; Y12384; CAA73023.1; JOINED; Genomic_DNA. DR EMBL; Y12385; CAA73023.1; JOINED; Genomic_DNA. DR EMBL; Y12386; CAA73023.1; JOINED; Genomic_DNA. DR EMBL; Y12387; CAA73023.1; JOINED; Genomic_DNA. DR EMBL; Y12388; CAA73023.1; JOINED; Genomic_DNA. DR EMBL; Y12389; CAA73023.1; JOINED; Genomic_DNA. DR EMBL; Y12390; CAA73023.1; JOINED; Genomic_DNA. DR EMBL; Y12382; CAA73023.1; JOINED; Genomic_DNA. DR EMBL; L23422; AAA16599.1; -; Genomic_DNA. DR EMBL; Y12380; CAA73024.1; -; Genomic_DNA. DR EMBL; Y12383; CAA73024.1; JOINED; Genomic_DNA. DR EMBL; Y12384; CAA73024.1; JOINED; Genomic_DNA. DR EMBL; Y12385; CAA73024.1; JOINED; Genomic_DNA. DR EMBL; Y12386; CAA73024.1; JOINED; Genomic_DNA. DR EMBL; Y12387; CAA73024.1; JOINED; Genomic_DNA. DR EMBL; Y12388; CAA73024.1; JOINED; Genomic_DNA. DR EMBL; Y12389; CAA73024.1; JOINED; Genomic_DNA. DR EMBL; Y12390; CAA73024.1; JOINED; Genomic_DNA. DR EMBL; Y12381; CAA73024.1; JOINED; Genomic_DNA. DR EMBL; Y12382; CAA73024.1; JOINED; Genomic_DNA. DR EMBL; U60419; AAC52772.1; -; Genomic_DNA. DR EMBL; L23421; AAA16598.1; -; mRNA. DR EMBL; L16544; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; I61186; I61186. DR PIR; I61187; I61187. DR AlphaFoldDB; Q61738; -. DR SMR; Q61738; -. DR ComplexPortal; CPX-3121; Integrin alpha7-beta1 complex. DR CORUM; Q61738; -. DR IntAct; Q61738; 4. DR STRING; 10090.ENSMUSP00000096712; -. DR GlyConnect; 2400; 4 N-Linked glycans (2 sites). DR GlyCosmos; Q61738; 6 sites, 4 glycans. DR GlyGen; Q61738; 6 sites, 4 N-linked glycans (2 sites). DR iPTMnet; Q61738; -. DR PhosphoSitePlus; Q61738; -. DR MaxQB; Q61738; -. DR PaxDb; 10090-ENSMUSP00000096712; -. DR PeptideAtlas; Q61738; -. DR ProteomicsDB; 268884; -. [Q61738-1] DR ProteomicsDB; 268885; -. [Q61738-2] DR ProteomicsDB; 268886; -. [Q61738-3] DR ProteomicsDB; 268887; -. [Q61738-4] DR ProteomicsDB; 268888; -. [Q61738-5] DR ProteomicsDB; 268889; -. [Q61738-6] DR AGR; MGI:102700; -. DR MGI; MGI:102700; Itga7. DR eggNOG; KOG3637; Eukaryota. DR InParanoid; Q61738; -. DR PhylomeDB; Q61738; -. DR Reactome; R-MMU-3000157; Laminin interactions. DR Reactome; R-MMU-3000178; ECM proteoglycans. DR PRO; PR:Q61738; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q61738; Protein. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0034677; C:integrin alpha7-beta1 complex; IDA:MGI. DR GO; GO:0008305; C:integrin complex; ISO:MGI. DR GO; GO:0005927; C:muscle tendon junction; IDA:MGI. DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI. DR GO; GO:0042383; C:sarcolemma; IDA:MGI. DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI. DR GO; GO:0005178; F:integrin binding; ISO:MGI. DR GO; GO:0043236; F:laminin binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI. DR GO; GO:0007155; P:cell adhesion; IMP:MGI. DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central. DR GO; GO:0016477; P:cell migration; IMP:MGI. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central. DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI. DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI. DR GO; GO:0050900; P:leukocyte migration; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1. DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1. DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1. DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1. DR Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1. DR InterPro; IPR013517; FG-GAP. DR InterPro; IPR013519; Int_alpha_beta-p. DR InterPro; IPR000413; Integrin_alpha. DR InterPro; IPR018184; Integrin_alpha_C_CS. DR InterPro; IPR013649; Integrin_alpha_Ig-like_1. DR InterPro; IPR048285; Integrin_alpha_Ig-like_2. DR InterPro; IPR048286; Integrin_alpha_Ig-like_3. DR InterPro; IPR028994; Integrin_alpha_N. DR InterPro; IPR032695; Integrin_dom_sf. DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1. DR PANTHER; PTHR23220:SF90; INTEGRIN ALPHA-7; 1. DR Pfam; PF01839; FG-GAP; 2. DR Pfam; PF08441; Integrin_A_Ig_1; 1. DR Pfam; PF20805; Integrin_A_Ig_2; 1. DR Pfam; PF20806; Integrin_A_Ig_3; 1. DR PRINTS; PR01185; INTEGRINA. DR SMART; SM00191; Int_alpha; 5. DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1. DR SUPFAM; SSF69179; Integrin domains; 3. DR PROSITE; PS51470; FG_GAP; 7. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. PE 1: Evidence at protein level; KW ADP-ribosylation; Alternative splicing; Calcium; Cell adhesion; Cell shape; KW Cleavage on pair of basic residues; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Integrin; Membrane; Metal-binding; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..33 FT /evidence="ECO:0000269|PubMed:1839357" FT CHAIN 34..1179 FT /note="Integrin alpha-7" FT /id="PRO_0000016270" FT CHAIN 34..955 FT /note="Integrin alpha-7 heavy chain" FT /evidence="ECO:0000255" FT /id="PRO_0000016271" FT CHAIN 959..1179 FT /note="Integrin alpha-7 light chain" FT /evidence="ECO:0000255" FT /id="PRO_0000016272" FT TOPO_DOM 34..1076 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1077..1102 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1103..1179 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 38..103 FT /note="FG-GAP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 110..175 FT /note="FG-GAP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 185..238 FT /note="FG-GAP 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 292..349 FT /note="FG-GAP 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 350..411 FT /note="FG-GAP 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 412..467 FT /note="FG-GAP 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 471..530 FT /note="FG-GAP 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 1155..1158 FT /note="1" FT REPEAT 1163..1166 FT /note="2" FT REPEAT 1171..1174 FT /note="3" FT REGION 952..978 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1134..1153 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1155..1174 FT /note="3 X 4 AA repeats of D-X-H-P" FT MOTIF 1105..1109 FT /note="GFFKR motif" FT COMPBIAS 952..966 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1138..1152 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 372 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 374 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 376 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 380 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 434 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 436 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 438 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 442 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 492 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 494 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 496 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 498 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 500 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT CARBOHYD 86 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 784 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 988 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1023 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19656770" FT CARBOHYD 1043 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 94..103 FT /evidence="ECO:0000250" FT DISULFID 140..163 FT /evidence="ECO:0000250" FT DISULFID 184..197 FT /evidence="ECO:0000250" FT DISULFID 539..546 FT /evidence="ECO:0000250" FT DISULFID 552..615 FT /evidence="ECO:0000250" FT DISULFID 681..687 FT /evidence="ECO:0000250" FT DISULFID 781..792 FT /evidence="ECO:0000250" FT DISULFID 939..993 FT /note="Interchain (between heavy and light chains)" FT /evidence="ECO:0000250" FT DISULFID 999..1004 FT /evidence="ECO:0000250" FT VAR_SEQ 224..267 FT /note="Missing (in isoform Alpha-7X2A and isoform FT Alpha-7X2B)" FT /evidence="ECO:0000303|PubMed:8253814" FT /id="VSP_002731" FT VAR_SEQ 268..307 FT /note="Missing (in isoform Alpha-7X1A and isoform FT Alpha-7X1B)" FT /evidence="ECO:0000305" FT /id="VSP_002732" FT VAR_SEQ 1104..1179 FT /note="LGFFKRAKHPEATVPQYHAVKIPREDRQQFKEEKTGTIQRSNWGNSQWEGSD FT AHPILAADWHPELGPDGHPVPATA -> CGFFRRNSPSSSFPTNYHRAHLAVQPSAMEA FT GGPGTVGWDSSSGRSTPRPPCPSTTQ (in isoform Alpha-7X1A, isoform FT Alpha-7X2A and isoform Alpha-7X1X2A)" FT /evidence="ECO:0000305" FT /id="VSP_002733" FT CONFLICT 133 FT /note="A -> P (in Ref. 2; CAA73023/CAA73024)" FT /evidence="ECO:0000305" FT CONFLICT 347 FT /note="T -> Q (in Ref. 1; AAA16599)" FT /evidence="ECO:0000305" FT CONFLICT 347 FT /note="T -> S (in Ref. 2; CAA73023/CAA73024)" FT /evidence="ECO:0000305" FT CONFLICT 647 FT /note="G -> R (in Ref. 1; AAA16600)" FT /evidence="ECO:0000305" FT CONFLICT 879..880 FT /note="EL -> DV (in Ref. 2; CAA73023/CAA73024)" FT /evidence="ECO:0000305" FT CONFLICT 882 FT /note="R -> S (in Ref. 2; CAA73023/CAA73024)" FT /evidence="ECO:0000305" FT CONFLICT 904 FT /note="N -> F (in Ref. 2; CAA73023/CAA73024)" FT /evidence="ECO:0000305" FT CONFLICT 989 FT /note="M -> V (in Ref. 2; CAA73023/CAA73024)" FT /evidence="ECO:0000305" FT CONFLICT 994..995 FT /note="PR -> AQG (in Ref. 2; CAA73023/CAA73024)" FT /evidence="ECO:0000305" FT CONFLICT 1031..1034 FT /note="MAVK -> LLIN (in Ref. 1; AAA16598)" FT /evidence="ECO:0000305" FT CONFLICT 1086 FT /note="G -> A (in Ref. 2; CAA73023/CAA73024)" FT /evidence="ECO:0000305" FT CONFLICT Q61738-2:1046 FT /note="G -> A (in Ref. 5; L16544)" FT /evidence="ECO:0000305" FT CONFLICT Q61738-2:1119..1120 FT /note="TQ -> T (in Ref. 1; AAA16598)" FT /evidence="ECO:0000305" FT CONFLICT Q61738-4:1042 FT /note="G -> A (in Ref. 5; L16544)" FT /evidence="ECO:0000305" FT CONFLICT Q61738-4:1115..1116 FT /note="TQ -> T (in Ref. 1; AAA16598)" FT /evidence="ECO:0000305" FT CONFLICT Q61738-6:1086 FT /note="G -> A (in Ref. 5; L16544)" FT /evidence="ECO:0000305" FT CONFLICT Q61738-6:1159..1160 FT /note="TQ -> T (in Ref. 1; AAA16598)" FT /evidence="ECO:0000305" SQ SEQUENCE 1179 AA; 129329 MW; 3C26D5BABF2E463D CRC64; MARIPRCDFL RPPGIYYLIT SLLAGLFLPP AIAFNLDVMG AIRKEGEPGS LFGFSVALHR QLQPRPQSWL LVGAPQALAL PGQQANRTGG LFACPLSLEE TDCYRVDIDR GANVQKESKE NQWLGVSVRS QGAGGKIVTC AHRYESRQRV DQALETRDVI GRCFVLSQDL AIRDELDGGE WKFCEGRPQG HEQFGFCQQG TAATFSPDSH YLVFGAPGTY NWKGTARVEL CAQGSPDLAH LDDGPYEAGG EKEQDPRLIP VPANSYLGLL FVTNIDSSDP DQLVYKTLDP ADRLTGPAGD LTLNSYLGFS IDSGKGLMRS EELSFVAGAP RANHKGAVVI LRKDSATRLI PEVVLSGERL TSGFGYSLAV TDLNNDGWAD LIVGAPYFFE RQEELGGAVY VYMNQGGHWA DISPLRICGS PDSMFGISLA VLGDLNQDGF PDIAVGAPFD GDGKVFIYHG SSLGVVVKPS QVLEGEAVGI KSFGYSLSGG LDVDGNHYPD LLVGSLADTA ALFRARPVLH VSQEIFIDPR AIDLEQPNCA DGRLVCVDIK ICFSYVAVPS SYSPSVALDY MLDGDTDRRL RGQVPRVTFL SRGLDDLRHQ SSGTVWLKHQ HDRVCGDTVF QLQENVKDKL RAIVVTLSYG LRTPPLGRQA PGQELPTVAP ILNAHQPSTQ RTEIHFLKQG CGQDKICQSN LQLERYQFCS RISDTEFQAL PMDLDGRTAL FALSGQPFIG LELTVTNLPS DPSRPQADGD DAHEAQLLVT LPASLRYSGV RALDSVEKPL CLSNDSASHV ECELGNPMKR GAQVTFYLIL STSGITIETT ELEVKLLLAT ISEQELDPVS VRAHVFIELP LSISGVATPQ QLFFSGEVKG ESAMRSEREL GRKVKYEVTV SNQGQSLNTL GSANLNIMWP HEIANGKWLL YPMRVELEGG QGPGKRGICS PRPNILQLDV DSRDRRRREL GQPEPQEPPE KVEPSTSWWP VSSAEKRNMT LDCPRTAKCV VFSCPLYSFD RAAVLHVWGR LWNSTFLEEY MAVKSLEVIV RANITVKSSI KNLLLRDAST VIPVMVYLDP MAVVVEGVPW WVILLGVLAG LLVLALLVLL LWKLGFFKRA KHPEATVPQY HAVKIPREDR QQFKEEKTGT IQRSNWGNSQ WEGSDAHPIL AADWHPELGP DGHPVPATA //