ITA3_MOUSE
ID ITA3_MOUSE Reviewed; 1053 AA.
AC Q62470; Q08441; Q08442; Q5SWA8; Q5SWB9; Q6P6I1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Integrin alpha-3;
DE AltName: Full=CD49 antigen-like family member C;
DE AltName: Full=Galactoprotein B3;
DE Short=GAPB3;
DE AltName: Full=VLA-3 subunit alpha;
DE AltName: CD_antigen=CD49c;
DE Contains:
DE RecName: Full=Integrin alpha-3 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-3 light chain;
DE Flags: Precursor;
GN Name=Itga3;
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 1).
RC STRAIN=BALB/cJ;
RX PubMed=7759572; DOI=10.1002/jcb.240570221;
RA Takeuchi K., Hirano K., Tuji T., Osawa T., Irimura T.;
RT "cDNA cloning of mouse VLA-3 alpha subunit.";
RL J. Cell. Biochem. 57:371-377(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryonic brain, and Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 913-1053 (ISOFORM 1), PARTIAL NUCLEOTIDE
RP SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=1946438; DOI=10.1073/pnas.88.22.10183;
RA Tamura R.N., Cooper H.M., Collo G., Quaranta V.;
RT "Cell type-specific integrin variants with alternative alpha chain
RT cytoplasmic domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10183-10187(1991).
RN [5]
RP INTERACTION WITH ITGB1; LGALS3 AND CSPG4.
RX PubMed=15181153; DOI=10.1091/mbc.e04-03-0236;
RA Fukushi J., Makagiansar I.T., Stallcup W.B.;
RT "NG2 proteoglycan promotes endothelial cell motility and angiogenesis via
RT engagement of galectin-3 and alpha3beta1 integrin.";
RL Mol. Biol. Cell 15:3580-3590(2004).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-574; ASN-606; ASN-657;
RP ASN-928 AND ASN-937.
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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-512; ASN-574; ASN-657;
RP ASN-937 AND ASN-971.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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-3/beta-1 is a receptor for fibronectin,
CC laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-
CC 3/beta-1 provides a docking site for FAP (seprase) at invadopodia
CC plasma membranes in a collagen-dependent manner and hence may
CC participate in the adhesion, formation of invadopodia and matrix
CC degradation processes, promoting cell invasion. Alpha-3/beta-1 may
CC mediate with LGALS3 the stimulation by CSPG4 of endothelial cells
CC migration. {ECO:0000250|UniProtKB:P26006}.
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-3 associates with beta-1. Interacts with HPS5. Interacts with FAP
CC (seprase); the interaction occurs at the cell surface of invadopodia
CC membrane in a collagen-dependent manner.
CC {ECO:0000250|UniProtKB:P26006}.
CC -!- INTERACTION:
CC Q62470; O35566: Cd151; NbExp=2; IntAct=EBI-8398907, EBI-8369654;
CC Q62470; P28828: Ptprm; NbExp=3; IntAct=EBI-8398907, EBI-8539266;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell
CC projection, invadopodium membrane {ECO:0000250|UniProtKB:P26006};
CC Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC filopodium membrane {ECO:0000250|UniProtKB:P26006}; Single-pass type I
CC membrane protein {ECO:0000255}. Note=Enriched preferentially at
CC invadopodia, cell membrane protrusions that correspond to sites of cell
CC invasion, in a collagen-dependent manner.
CC {ECO:0000250|UniProtKB:P26006}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Alpha-3A;
CC IsoId=Q62470-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha-3B;
CC IsoId=Q62470-2; Sequence=VSP_002722;
CC Name=3;
CC IsoId=Q62470-3; Sequence=VSP_041797;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in heart and
CC brain. Only isoform 1 is detected in lung.
CC {ECO:0000269|PubMed:1946438}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; D13867; BAA02980.1; -; mRNA.
DR EMBL; AL606480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053031; AAH53031.1; -; mRNA.
DR EMBL; BC062205; AAH62205.1; -; mRNA.
DR EMBL; S66292; AAB20356.2; -; mRNA.
DR EMBL; S66294; AAB20357.2; -; mRNA.
DR CCDS; CCDS25271.1; -. [Q62470-1]
DR CCDS; CCDS83877.1; -. [Q62470-3]
DR CCDS; CCDS83878.1; -. [Q62470-2]
DR PIR; B41543; B41543.
DR PIR; I55534; I55534.
DR RefSeq; NP_001293000.1; NM_001306071.1. [Q62470-3]
DR RefSeq; NP_001293091.1; NM_001306162.1. [Q62470-2]
DR RefSeq; NP_038593.1; NM_013565.3. [Q62470-1]
DR RefSeq; XP_006532373.1; XM_006532310.3. [Q62470-2]
DR RefSeq; XP_006532374.1; XM_006532311.3. [Q62470-1]
DR AlphaFoldDB; Q62470; -.
DR SMR; Q62470; -.
DR BioGRID; 200816; 6.
DR ComplexPortal; CPX-3117; Integrin alpha3-beta1 complex.
DR CORUM; Q62470; -.
DR IntAct; Q62470; 6.
DR STRING; 10090.ENSMUSP00000001548; -.
DR GlyConnect; 2423; 6 N-Linked glycans (5 sites). [Q62470-2]
DR GlyGen; Q62470; 13 sites, 6 N-linked glycans (5 sites).
DR iPTMnet; Q62470; -.
DR PhosphoSitePlus; Q62470; -.
DR SwissPalm; Q62470; -.
DR EPD; Q62470; -.
DR jPOST; Q62470; -.
DR MaxQB; Q62470; -.
DR PaxDb; Q62470; -.
DR PeptideAtlas; Q62470; -.
DR PRIDE; Q62470; -.
DR ProteomicsDB; 301682; -. [Q62470-1]
DR ProteomicsDB; 301683; -. [Q62470-2]
DR ProteomicsDB; 301684; -. [Q62470-3]
DR Antibodypedia; 18000; 1064 antibodies from 42 providers.
DR DNASU; 16400; -.
DR Ensembl; ENSMUST00000001548; ENSMUSP00000001548; ENSMUSG00000001507. [Q62470-1]
DR Ensembl; ENSMUST00000107739; ENSMUSP00000103368; ENSMUSG00000001507. [Q62470-3]
DR Ensembl; ENSMUST00000120375; ENSMUSP00000113556; ENSMUSG00000001507. [Q62470-2]
DR GeneID; 16400; -.
DR KEGG; mmu:16400; -.
DR UCSC; uc007kzv.1; mouse. [Q62470-3]
DR UCSC; uc007kzw.1; mouse. [Q62470-1]
DR UCSC; uc007kzx.1; mouse. [Q62470-2]
DR CTD; 3675; -.
DR MGI; MGI:96602; Itga3.
DR VEuPathDB; HostDB:ENSMUSG00000001507; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000157746; -.
DR HOGENOM; CLU_004111_1_0_1; -.
DR InParanoid; Q62470; -.
DR OMA; RYNHTGA; -.
DR OrthoDB; 743479at2759; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR BioGRID-ORCS; 16400; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Itga3; mouse.
DR PRO; PR:Q62470; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q62470; protein.
DR Bgee; ENSMUSG00000001507; Expressed in undifferentiated genital tubercle and 296 other tissues.
DR ExpressionAtlas; Q62470; baseline and differential.
DR Genevisible; Q62470; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0060076; C:excitatory synapse; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0031527; C:filopodium membrane; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:1990812; C:growth cone filopodium; ISO:MGI.
DR GO; GO:0034667; C:integrin alpha3-beta1 complex; ISO:MGI.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0097060; C:synaptic membrane; IDA:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0043236; F:laminin binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
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:0097062; P:dendritic spine maintenance; IMP:MGI.
DR GO; GO:0035640; P:exploration behavior; IGI:MGI.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0050900; P:leukocyte migration; IBA:GO_Central.
DR GO; GO:0030324; P:lung development; ISO:MGI.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0031345; P:negative regulation of cell projection organization; ISO:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IGI:MGI.
DR GO; GO:0072006; P:nephron development; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; ISO:MGI.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:0097205; P:renal filtration; ISO:MGI.
DR GO; GO:0034698; P:response to gonadotropin; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IGI:MGI.
DR GO; GO:0043588; P:skin development; ISO:MGI.
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 Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Integrin; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000250"
FT CHAIN 33..1053
FT /note="Integrin alpha-3"
FT /id="PRO_0000016241"
FT CHAIN 33..874
FT /note="Integrin alpha-3 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016242"
FT CHAIN 878..1053
FT /note="Integrin alpha-3 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016243"
FT TOPO_DOM 33..993
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 994..1021
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1022..1053
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..171
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 185..235
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 236..293
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 294..355
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 357..412
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 416..478
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 865..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1018
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 859
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 928
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 971
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 94..103
FT /evidence="ECO:0000250"
FT DISULFID 140..162
FT /evidence="ECO:0000250"
FT DISULFID 185..197
FT /evidence="ECO:0000250"
FT DISULFID 486..491
FT /evidence="ECO:0000250"
FT DISULFID 497..551
FT /evidence="ECO:0000250"
FT DISULFID 616..622
FT /evidence="ECO:0000250"
FT DISULFID 695..704
FT /evidence="ECO:0000250"
FT DISULFID 848..906
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 913..918
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..69
FT /note="MGPGPCRVPRAPGWLLRALALMVAACGRVAFAFNLDTRFLVVKEAVNPGSLF
FT GYSVALHRQTERQQRYL -> MSYLQTLVWSPCSESVDLQADWREACKARLTHPPSFSS
FT (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_041797"
FT VAR_SEQ 1019..1053
FT /note="GFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY -> DFFKPTRYYRIMP
FT KYHAVRIREEDRYPPPGSTLPTKKHWVTSWQIRDRYY (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002722"
FT CONFLICT 975
FT /note="W -> C (in Ref. 4; AAB20356/AAB20357)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="D -> N (in Ref. 4; AAB20356/AAB20357)"
FT /evidence="ECO:0000305"
FT CONFLICT 1002
FT /note="G -> S (in Ref. 4; AAB20356/AAB20357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1053 AA; 116745 MW; 6A5E8FBDBA86D6E5 CRC64;
MGPGPCRVPR APGWLLRALA LMVAACGRVA FAFNLDTRFL VVKEAVNPGS LFGYSVALHR
QTERQQRYLL LAGAPRDLAV GDDYTNRTGA VYLCPLTAHK DDCERMDISE KSDPDHHIIE
DMWLGVTVAS QGPAGRVLVC AHRYTKVLWS GLEDQRRMVG KCYVRGNDLQ LDPGDDWQTY
HNEMCNSNTD YLQTGMCQLG TSGGFTQNTV YFGAPGAYNW KGNSYMIQRK DWDLSEYSYR
GSEEQGNLYI GYTVQVGNAI LHPTDIITVV TGAPRHQHMG AVFLLKQESG GDLQRKQVLK
GTQVGAYFGS AIALADLNND GWQDLLVGAP YYFERKEEVG GAVYVFMNQA GASFPDQPSL
LLHGPSRSAF GISIASIGDI NQDGFQDIAV GAPFEGLGKV YIYHSSSGGL LRQPQQIIHG
EKLGLPGLAT FGYSLSGKMD VDENLYPDLL VGSLSDHIVL LRARPVINIL HRTLVARPAV
LDPALCTATS CVQVELCFAY NQSAGNPNYR RNITLAYTLE ADRDRRPPRL RFARSQSSVF
HGFFSMPETH CQTLELLLMD NVRDKLRPIV IAMNYSLPLR MPDRLKLGLR SLDAYPVLNQ
AQAMENHTEV HFQKECGPDN KCDSNLQMRA AFLSEQLQPL SRLQYSRDTK KLFLSINVTN
SPSSQRAGED AHEALLTLEV PSALLLSSVR PSGTCQANNE TILCELGNPF KRNQRMELLI
AFEVIGVTLH TRDLPVLLQL STSSHQDNLQ PVLLTLQVDY TLQASLSLMN HRLQSFFGGT
VMGEAAMKTA EDVGSPLKYE FQVSPVGDGL AALGTLVLGL EWPYEVTNGK WLLYPTEITI
HSNGSWPCQP SGNLVNPLNL TLSDPGVTPL SPQRRRRQLD PGGDQSSPPV TLAAAKKAKS
ETVLTCSNGR ARCVWLECPL PDTSNITNVT VKARVWNSTF IEDYKDFDRV RVDGWATLFL
RTSIPTINME NKTTWFSVDI DSELVEELPA EIELWLVLVA VGAGLLLLGL IILLLWKCGF
FKRARTRALY EAKRQKAEMK SQPSETERLT DDY
