ITA7_RAT
ID ITA7_RAT Reviewed; 1135 AA.
AC Q63258; Q5HZX9; Q63026; Q63027;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Integrin alpha-7;
DE AltName: Full=H36-alpha7;
DE Contains:
DE RecName: Full=Integrin alpha-7 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-7 light chain;
DE Contains:
DE RecName: Full=Integrin alpha-7 70 kDa form;
DE Flags: Precursor;
GN Name=Itga7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-7X1B).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 34-1135 (ISOFORM ALPHA-7X1B).
RC TISSUE=Skeletal muscle;
RX PubMed=1315319; DOI=10.1083/jcb.117.3.643;
RA Song W.K., Wang W., Foster R.F., Bielser D.A., Kaufman S.J.;
RT "H36-alpha 7 is a novel integrin alpha chain that is developmentally
RT regulated during skeletal myogenesis.";
RL J. Cell Biol. 117:643-657(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 969-1135 (ISOFORMS ALPHA-7X1A AND
RP ALPHA-7X1C).
RC TISSUE=Skeletal muscle;
RX PubMed=8126096; DOI=10.1242/jcs.106.4.1139;
RA Song W.K., Wang W., Sato H., Bielser D.A., Kaufman S.J.;
RT "Expression of alpha 7 integrin cytoplasmic domains during skeletal muscle
RT development: alternate forms, conformational change, and homologies with
RT serine/threonine kinases and tyrosine phosphatases.";
RL J. Cell Sci. 106:1139-1152(1993).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=17598176; DOI=10.1002/glia.20536;
RA Chernousov M.A., Kaufman S.J., Stahl R.C., Rothblum K., Carey D.J.;
RT "Alpha7beta1 integrin is a receptor for laminin-2 on Schwann cells.";
RL Glia 55:1134-1144(2007).
RN [6]
RP CLEAVAGE BY UROKINASE, AND MUTAGENESIS OF ARG-603.
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 [7]
RP FUNCTION, AND INTERACTION WITH COMP.
RX PubMed=20019333; DOI=10.1161/circresaha.109.202762;
RA Wang L., Zheng J., Du Y., Huang Y., Li J., Liu B., Liu C.J., Zhu Y.,
RA Gao Y., Xu Q., Kong W., Wang X.;
RT "Cartilage oligomeric matrix protein maintains the contractile phenotype of
RT vascular smooth muscle cells by interacting with alpha(7)beta(1)
RT integrin.";
RL Circ. Res. 106:514-525(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. Required to promote contractile phenotype
CC acquisition in differentiated airway smooth muscle (ASM) cells (By
CC similarity). Acts as Schwann cell receptor for laminin-2. Acts as a
CC receptor of COMP and mediates its effect on vascular smooth muscle
CC cells (VSMCs) maturation. {ECO:0000250, ECO:0000269|PubMed:17598176,
CC ECO:0000269|PubMed:20019333}.
CC -!- SUBUNIT: Interacts (via C-terminus intracellular tail region) with
CC CIB1; the interaction is stabilized/increased in a calcium- and
CC magnesium-dependent manner (By similarity). Heterodimer of an alpha and
CC a beta subunit. The alpha subunit is composed of a heavy and a light
CC chain linked by a disulfide bond. Alpha-7 associates with beta-1.
CC Interacts with COMP. {ECO:0000250, ECO:0000269|PubMed:20019333}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=Alpha-7X1B;
CC IsoId=Q63258-1; Sequence=Displayed;
CC Name=Alpha-7X1A;
CC IsoId=Q63258-2; Sequence=VSP_002734;
CC Name=Alpha-7X1C;
CC IsoId=Q63258-3; Sequence=VSP_002735;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscle. Expressed
CC in replicating myoblasts. In differentiated muscle fibers localizes
CC between fibers and the surrounding matrix. Isoform Alpha-7X1A and
CC isoform Alpha-7X1B are expressed at myotendinous and neuromuscular
CC junctions; isoform Alpha-7X1C is expressed at neuromuscular junctions
CC and at extrasynaptic sites. {ECO:0000269|PubMed:8626012}.
CC -!- DEVELOPMENTAL STAGE: Isoforms are developmentally regulated during the
CC formation of skeletal muscle. Isoform Alpha-7X1A and isoform Alpha-7X1C
CC are induced upon terminal myogenic differentiation; isoform Alpha-7X1B
CC is present earlier in replicating cells and diminishes upon
CC differentiation.
CC -!- PTM: ADP-ribosylated on at least two sites of the extracellular domain
CC in skeletal myotubes. {ECO:0000250}.
CC -!- PTM: A 70 kDa form is created by proteolytic cleavage. Cleavage is
CC elevated during myogenic differentiation and the cleaved form enhances
CC cell adhesion and spreading on laminin. {ECO:0000269|PubMed:18940796}.
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; BC088846; AAH88846.1; -; mRNA.
DR EMBL; X65036; CAA46170.1; -; mRNA.
DR EMBL; X74293; CAA52346.1; -; mRNA.
DR EMBL; X74294; CAA52347.1; -; mRNA.
DR PIR; S38783; S38783.
DR PIR; S40148; S40148.
DR PIR; S40149; S40149.
DR RefSeq; NP_110469.1; NM_030842.1. [Q63258-1]
DR AlphaFoldDB; Q63258; -.
DR SMR; Q63258; -.
DR BioGRID; 249497; 2.
DR CORUM; Q63258; -.
DR IntAct; Q63258; 1.
DR STRING; 10116.ENSRNOP00000058370; -.
DR GlyGen; Q63258; 5 sites.
DR iPTMnet; Q63258; -.
DR PhosphoSitePlus; Q63258; -.
DR PaxDb; Q63258; -.
DR PRIDE; Q63258; -.
DR GeneID; 81008; -.
DR KEGG; rno:81008; -.
DR UCSC; RGD:71022; rat. [Q63258-1]
DR CTD; 3679; -.
DR RGD; 71022; Itga7.
DR VEuPathDB; HostDB:ENSRNOG00000007905; -.
DR eggNOG; KOG3637; Eukaryota.
DR HOGENOM; CLU_004111_1_0_1; -.
DR InParanoid; Q63258; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; Q63258; -.
DR Reactome; R-RNO-3000157; Laminin interactions.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR PRO; PR:Q63258; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007905; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; Q63258; baseline and differential.
DR Genevisible; Q63258; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0034677; C:integrin alpha7-beta1 complex; ISO:RGD.
DR GO; GO:0008305; C:integrin complex; IDA:RGD.
DR GO; GO:0005927; C:muscle tendon junction; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:RGD.
DR GO; GO:0005178; F:integrin binding; IPI:RGD.
DR GO; GO:0043236; F:laminin binding; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IDA:RGD.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
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:0035987; P:endodermal cell differentiation; ISO:RGD.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:RGD.
DR GO; GO:0050900; P:leukocyte migration; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
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; Disulfide bond; Glycoprotein; Integrin;
KW Membrane; Metal-binding; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000250"
FT CHAIN 34..1135
FT /note="Integrin alpha-7"
FT /id="PRO_0000293124"
FT CHAIN 34..910
FT /note="Integrin alpha-7 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016273"
FT CHAIN 604..1135
FT /note="Integrin alpha-7 70 kDa form"
FT /id="PRO_0000398834"
FT CHAIN 914..1135
FT /note="Integrin alpha-7 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016274"
FT TOPO_DOM 34..1036
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1037..1057
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1058..1135
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..165
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 248..305
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 306..367
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 368..423
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 427..486
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 1111..1114
FT /note="1"
FT REPEAT 1119..1122
FT /note="2"
FT REPEAT 1127..1130
FT /note="3"
FT REGION 905..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1130
FT /note="3 X 4 AA repeats of D-X-H-P"
FT MOTIF 1061..1065
FT /note="GFFKR motif"
FT COMPBIAS 905..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 448
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT SITE 603..604
FT /note="Cleavage; by urokinase"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 943
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 979
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 999
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 495..502
FT /evidence="ECO:0000250"
FT DISULFID 508..571
FT /evidence="ECO:0000250"
FT DISULFID 637..643
FT /evidence="ECO:0000250"
FT DISULFID 736..747
FT /evidence="ECO:0000250"
FT DISULFID 894..948
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 955..960
FT /evidence="ECO:0000250"
FT VAR_SEQ 1060..1135
FT /note="LGFFKRAKHPEATVPQYHAVKILREDRQQFKEEKTGTIQRSNWGNSQWEGSD
FT AHPILAADWHPELGPDGHPVSVTA -> CGFFRRNSPSSSFPANYHRAHLAVQPSAMEA
FT GGPGTVGWDSSSGRSTLRPLYPSTTQ (in isoform Alpha-7X1A)"
FT /evidence="ECO:0000303|PubMed:8126096"
FT /id="VSP_002734"
FT VAR_SEQ 1065..1135
FT /note="RAKHPEATVPQYHAVKILREDRQQFKEEKTGTIQRSNWGNSQWEGSDAHPIL
FT AADWHPELGPDGHPVSVTA -> CAVPAQRILSIY (in isoform Alpha-
FT 7X1C)"
FT /evidence="ECO:0000303|PubMed:8126096"
FT /id="VSP_002735"
FT MUTAGEN 603
FT /note="R->G: Abolishes cleavage by urokinase."
FT /evidence="ECO:0000269|PubMed:18940796"
FT CONFLICT 79..95
FT /note="ALPGQQANRTGGLFACP -> DSYPDSRQIAHGRPLCLS (in Ref. 2;
FT CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..133
FT /note="SQGA -> PRES (in Ref. 2; CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="R -> E (in Ref. 2; CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..232
FT /note="LLFVTNID -> TARVELCAQG (in Ref. 2; CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 236..259
FT /note="PDQLVYKTLDPADRLTGPAGDLTL -> LAQVDDGPYEAGGEKDQDPRPSPV
FT PA (in Ref. 2; CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="D -> H (in Ref. 2; CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 575..582
FT /note="VFQLQENV -> CVPAAGKR (in Ref. 2; CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="P -> G (in Ref. 2; CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="A -> V (in Ref. 2; CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 678..679
FT /note="LS -> HG (in Ref. 2; CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 833..835
FT /note="RDV -> WDE (in Ref. 2; CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 949..950
FT /note="AQ -> P (in Ref. 2; CAA46170)"
FT /evidence="ECO:0000305"
FT CONFLICT 996
FT /note="V -> G (in Ref. 3; CAA52346/CAA52347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1135 AA; 124194 MW; EEBA7063537A4AF1 CRC64;
MARIPRCDFL GLPGICYLLS FLLAGLLLPR ASAFNLDVMG AIRKEGEPGS LFGFSVALHR
QLQPRPQSWL LVGAPQALAL PGQQANRTGG LFACPLSLEE TDCYRVDIDR GANVQKESKE
NQWLGVSVRS QGAGGKVVTC AHRYESRQRV DQVLETRDVI GRCFVLSQDL AIRDELDGGE
WKFCEGRPQG HEQFGFCQQG TAATFSPDSH YLIFGAPGTY NWKGLLFVTN IDSSDPDQLV
YKTLDPADRL TGPAGDLTLN SYLGFSIDSG KGLMRSEELS FVAGAPRANH KGAVVILRKD
SASRLIPEVV LSGERLTSGF GYSLAVTDLN SDGWADLIVG APYFFERQEE LGGAVYVYMN
QGGHWADISP LRLCGSPDSM FGISLAVLGD LNQDGFPDIA VGAPFDGDGK VFIYHGSSLG
VVTKPSQVLE GEAVGIKSFG YSLSGGLDVD GNHYPDLLVG SLADTAALFR ARPVLHVSQE
IFIDPRAIDL EQPNCADGRL VCVHVKVCFS YVAVPSSYSP IVVLDYVLDG DTDRRLRGQA
PRVTFPGRGP DDLKHQSSGT VSLKHQHDRV CGDTVFQLQE NVKDKLRAIV VTLSYGLQTP
RLRRQAPDQG LPLVAPILNA HQPSTQRTEI HFLKQGCGDD KICQSNLQLA QAQFCSRISD
TEFQALPMDL DGTALFALSG QPFIGLELTV TNLPSDPARP QADGDDAHEA QLLATLPASL
RYSGVRTLDS VEKPLCLSNE NASHVECELG NPMKRGTQVT FYLILSTSGI TIETTELKVE
LLLATISEQD LHPVSVRAHV FIELPLSISG VATPQQLFFS GKVKGESAMR SERDVGSKVK
YEVTVSNQGQ SLNTLGSAFL NIMWPHEIAN GKWLLYPMRV ELEGGQGPEK KGICSPRPNI
LHLDVDSRDR RRRELGQPEP QEPPEKVEPS TSWWPVSSAE KRNVTLDCAQ GTAKCVVFSC
PLYSFDRAAV LHVWGRLWNS TFLEEYMSVK SLEVIVRANI TVKSSIKNLL LRDASTVIPV
MVYLDPVAVV AEGVPWWVIL LAVLAGLLVL ALLVLLLWKL GFFKRAKHPE ATVPQYHAVK
ILREDRQQFK EEKTGTIQRS NWGNSQWEGS DAHPILAADW HPELGPDGHP VSVTA
