ITA7_MOUSE
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 03-AUG-2022, entry version 164.
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 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}.
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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 GlyGen; Q61738; 6 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q61738; -.
DR PhosphoSitePlus; Q61738; -.
DR MaxQB; Q61738; -.
DR PaxDb; Q61738; -.
DR PeptideAtlas; Q61738; -.
DR PRIDE; 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 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; IDA: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; 2.130.10.130; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
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 Alpha-
FT 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 Alpha-
FT 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
