LAMB2_MOUSE
ID LAMB2_MOUSE Reviewed; 1799 AA.
AC Q61292; Q62182; Q8R0Y0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Laminin subunit beta-2;
DE AltName: Full=Laminin-11 subunit beta;
DE AltName: Full=Laminin-14 subunit beta;
DE AltName: Full=Laminin-15 subunit beta;
DE AltName: Full=Laminin-3 subunit beta;
DE AltName: Full=Laminin-4 subunit beta;
DE AltName: Full=Laminin-7 subunit beta;
DE AltName: Full=Laminin-9 subunit beta;
DE AltName: Full=S-laminin subunit beta;
DE Short=S-LAM beta;
DE Flags: Precursor;
GN Name=Lamb2; Synonyms=Lams;
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 [GENOMIC DNA].
RC STRAIN=129/J;
RX PubMed=8662701; DOI=10.1074/jbc.271.23.13407;
RA Durkin M.E., Gautam M., Loechel S., Sanes J.R., Merlie J.P.,
RA Albrechtsen R., Wewer U.M.;
RT "Structural organization of the human and mouse laminin beta2 chain genes,
RT and alternative splicing at the 5' end of the human transcript.";
RL J. Biol. Chem. 271:13407-13416(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 348-428.
RC TISSUE=Lung;
RX PubMed=8043959; DOI=10.1007/bf00356563;
RA Aberdam D., Galliano M.-F., Mattei M.-G., Ortonne J.-P., Meneguzzi G.;
RT "S-laminin gene (Lams) maps to F1 band of mouse chromosome 9.";
RL Mamm. Genome 5:393-394(1994).
RN [5]
RP FUNCTION.
RC STRAIN=129/J;
RX PubMed=7885444; DOI=10.1038/374258a0;
RA Noakes P.G., Gautam M., Mudd J., Sanes J.R., Merlie J.P.;
RT "Aberrant differentiation of neuromuscular junctions in mice lacking s-
RT laminin/laminin beta 2.";
RL Nature 374:258-262(1995).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components. {ECO:0000269|PubMed:7885444}.
CC -!- FUNCTION: Laminin-3 (S-laminin) regulates the formation of motor nerve
CC terminals. {ECO:0000269|PubMed:7885444}.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end. Beta-2 is a
CC subunit of laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221
CC or S-merosin), laminin-7 (laminin-321 or KS-laminin), laminin-9
CC (laminin-421), laminin-11 (laminin-521), laminin-14 (laminin-423) and
CC laminin-15 (laminin-523).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- TISSUE SPECIFICITY: Neuromuscular synapse and kidney glomerulus.
CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC other laminin chains to form a coiled coil structure.
CC -!- DOMAIN: Domains VI and IV are globular.
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; U43541; AAC53535.1; -; Genomic_DNA.
DR EMBL; U42624; AAC53535.1; JOINED; Genomic_DNA.
DR EMBL; CH466560; EDL21291.1; -; Genomic_DNA.
DR EMBL; CH466560; EDL21292.1; -; Genomic_DNA.
DR EMBL; BC026051; AAH26051.1; -; mRNA.
DR EMBL; X75928; CAA53532.1; -; mRNA.
DR CCDS; CCDS23528.1; -.
DR PIR; I48749; I48749.
DR RefSeq; NP_032509.2; NM_008483.3.
DR RefSeq; XP_006511711.1; XM_006511648.2.
DR AlphaFoldDB; Q61292; -.
DR SMR; Q61292; -.
DR BioGRID; 201102; 9.
DR ComplexPortal; CPX-3010; Laminin-121 complex.
DR ComplexPortal; CPX-3011; Laminin-221 complex.
DR ComplexPortal; CPX-3014; Laminin-321 complex.
DR ComplexPortal; CPX-3017; Laminin-521 complex.
DR ComplexPortal; CPX-3019; Laminin-423 complex.
DR ComplexPortal; CPX-3020; Laminin-522 complex.
DR ComplexPortal; CPX-3021; Laminin-523 complex.
DR ComplexPortal; CPX-3031; Laminin-421 complex.
DR IntAct; Q61292; 1.
DR MINT; Q61292; -.
DR STRING; 10090.ENSMUSP00000069087; -.
DR GlyConnect; 2460; 8 N-Linked glycans (1 site).
DR GlyGen; Q61292; 7 sites, 7 N-linked glycans (1 site).
DR iPTMnet; Q61292; -.
DR PhosphoSitePlus; Q61292; -.
DR MaxQB; Q61292; -.
DR PaxDb; Q61292; -.
DR PeptideAtlas; Q61292; -.
DR PRIDE; Q61292; -.
DR ProteomicsDB; 263696; -.
DR Antibodypedia; 995; 390 antibodies from 30 providers.
DR DNASU; 16779; -.
DR Ensembl; ENSMUST00000065014; ENSMUSP00000069087; ENSMUSG00000052911.
DR GeneID; 16779; -.
DR KEGG; mmu:16779; -.
DR UCSC; uc009rpr.2; mouse.
DR CTD; 3913; -.
DR MGI; MGI:99916; Lamb2.
DR VEuPathDB; HostDB:ENSMUSG00000052911; -.
DR eggNOG; KOG0994; Eukaryota.
DR GeneTree; ENSGT00940000156060; -.
DR HOGENOM; CLU_001560_1_0_1; -.
DR InParanoid; Q61292; -.
DR OMA; CFNNWDI; -.
DR OrthoDB; 65841at2759; -.
DR PhylomeDB; Q61292; -.
DR TreeFam; TF312903; -.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 16779; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Lamb2; mouse.
DR PRO; PR:Q61292; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q61292; protein.
DR Bgee; ENSMUSG00000052911; Expressed in humerus cartilage element and 250 other tissues.
DR ExpressionAtlas; Q61292; baseline and differential.
DR Genevisible; Q61292; MM.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043256; C:laminin complex; IDA:MGI.
DR GO; GO:0005608; C:laminin-3 complex; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; IC:ComplexPortal.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IPI:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0014002; P:astrocyte development; IGI:MGI.
DR GO; GO:0048677; P:axon extension involved in regeneration; IMP:MGI.
DR GO; GO:0007411; P:axon guidance; IGI:MGI.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; IGI:MGI.
DR GO; GO:0072274; P:metanephric glomerular basement membrane development; IMP:MGI.
DR GO; GO:0072249; P:metanephric podocyte development; IMP:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IC:ComplexPortal.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IC:ComplexPortal.
DR GO; GO:0110011; P:regulation of basement membrane organization; IC:ComplexPortal.
DR GO; GO:0060041; P:retina development in camera-type eye; IGI:MGI.
DR GO; GO:0014044; P:Schwann cell development; IDA:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IGI:MGI.
DR CDD; cd00055; EGF_Lam; 13.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 10.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01248; EGF_LAM_1; 12.
DR PROSITE; PS50027; EGF_LAM_2; 13.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Cell adhesion; Coiled coil; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1799
FT /note="Laminin subunit beta-2"
FT /id="PRO_0000017069"
FT DOMAIN 46..285
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 286..349
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 350..412
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 413..472
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 473..524
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 525..555
FT /note="Laminin EGF-like 5; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 564..778
FT /note="Laminin IV type B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00462"
FT DOMAIN 784..831
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 832..877
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 878..927
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 928..986
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 987..1038
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1039..1095
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1096..1143
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1144..1190
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1191..1410
FT /note="Domain II"
FT REGION 1339..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1443
FT /note="Domain alpha"
FT REGION 1444..1799
FT /note="Domain I"
FT REGION 1679..1701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1257..1304
FT /evidence="ECO:0000255"
FT COILED 1473..1527
FT /evidence="ECO:0000255"
FT COILED 1577..1791
FT /evidence="ECO:0000255"
FT COMPBIAS 1344..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55268"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1086
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 286..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 288..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 315..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 327..347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 350..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 352..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 380..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 392..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 413..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 415..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 443..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 455..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 473..487
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 475..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 496..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 508..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 525..537
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 527..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 546..555
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 784..796
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 786..803
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 805..814
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 817..829
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 832..844
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 834..851
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 853..862
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 865..875
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 878..887
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 880..894
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 897..906
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 909..925
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 928..944
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 930..955
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 957..966
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 969..984
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 987..1001
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 989..1008
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1011..1020
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1023..1036
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1039..1059
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1041..1066
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1068..1077
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1080..1093
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1096..1108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1098..1115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1117..1126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1129..1141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1144..1156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1146..1163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1165..1174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1177..1188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1191
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1194
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1798
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="R -> P (in Ref. 1; AAC53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="G -> V (in Ref. 1; AAC53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="F -> V (in Ref. 1; AAC53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 956
FT /note="Q -> H (in Ref. 1; AAC53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 959
FT /note="E -> A (in Ref. 1; AAC53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 973
FT /note="H -> P (in Ref. 1; AAC53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 1306
FT /note="L -> F (in Ref. 1; AAC53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 1449
FT /note="T -> P (in Ref. 1; AAC53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 1460
FT /note="T -> S (in Ref. 1; AAC53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 1487
FT /note="E -> A (in Ref. 1; AAC53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 1627
FT /note="W -> R (in Ref. 1; AAC53535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1799 AA; 196579 MW; 37CA24B9CDA0791F CRC64;
MEWASGEPGR GRQGQPLPWE LRLGLLLSVL AATLAQAPSL DVPGCSRGSC YPATGDLLVG
RADRLTASST CGLHSPQPYC IVSHLQDEKK CFLCDSRRPF SARDNPNSHR IQNVVTSFAP
QRRTAWWQSE NGVPMVTIQL DLEAEFHFTH LIMTFKTFRP AAMLVERSAD FGRTWHVYRY
FSYDCGADFP GIPLAPPRRW DDVVCESRYS EIEPSTEGEV IYRVLDPAIP IPDPYSSRIQ
NLLKITNLRV NLTRLHTLGD NLLDPRREIR EKYYYALYEL VIRGNCFCYG HASQCAPAPG
APAHAEGMVH GACICKHNTR GLNCEQCQDF YQDLPWHPAE DGHTHACRKC ECNGHTHSCH
FDMAVYLASG NVSGGVCDGC QHNTAGRHCE FCRPFFYRDP TKDMRDPAVC RPCDCDPMGS
QDGGRCDSHD DPVLGLVSGQ CRCKEHVVGT RCQQCRDGFF GLSASDPRGC QRCQCNSRGT
VPGSSPCDSS SGTCFCKRLV TGHGCDRCLP GHWGLSHDLL GCRPCDCDVG GALDPQCDEA
TGQCRCRQHM IGRRCEQVQP GYFRPFLDHL TWEAEAAQGQ GLEVVERLVT NRETPSWTGP
GFVRLREGQE VEFLVTSLPR AMDYDLLLRW EPQVPEQWAE LELMVQRPGP VSAHSPCGHV
LPKDDRIQGM LHPNTRFLVF PRPVCLEPGI SYKLKLKLIG TGGRAQPETS YSGLLIDSLV
LQPHVLVLEM FSGGDAAALE RRTTFERYRC HEEGLMPSKA PLSETCAPLL ISVSALIYNG
ALPCQCDPQG SLSSECSPHG GQCRCKPGVV GRRCDVCATG YYGFGPAGCQ ACQCSPDGAL
SALCEGTSGQ CPCRPGAFGL RCDHCQRGQW GFPNCRPCVC NGRADECDTH TGACLGCRDY
TGGEHCERCI AGFHGDPRLP YGGQCRPCPC PEGPGSQRHF ATSCHRDGYS QQIVCQCREG
YTGLRCEACA PGHFGDPSKP GGRCQLCECS GNIDPMDPDA CDPHTGQCLR CLHNTEGPHC
GYCKPGFHGQ AARQSCHRCT CNLLGTDPRR CPSTDLCHCD PSTGQCPCLP HVQGLNCDHC
APNFWNFTSG RGCQPCACHP SRARGPTCNE FTGQCHCHAG FGGRTCSECQ ELYWGDPGLQ
CRACDCDPRG IDKPQCHRST GHCSCRPGVS GVRCDQCARG FSGVFPACHP CHACFGDWDR
VVQDLAARTR RLEQWAQELQ QTGVLGAFES SFLNMQGKLG MVQAIMSARN ASAASTAKLV
EATEGLRHEI GKTTERLTQL EAELTAVQDE NFNANHALSG LERDGLALNL TLRQLDQHLE
ILKHSNFLGA YDSIRHAHSQ STEAERRANA STFAVPSPVS NSADTRRRTE VLMGAQKENF
NRQHLANQQA LGRLSAHAHT LSLTGINELV CGAPGDAPCA TSPCGGAGCR DEDGQPRCGG
LGCSGAAATA DLALGRARHT QAELQRALVE GGGILSRVSE TRRQAEEAQQ RAQAALDKAN
ASRGQVEQAN QELRELIQNV KDFLSQEGAD PDSIEMVATR VLDISIPASP EQIQRLASEI
AERVRSLADV DTILAHTMGD VRRAEQLLQD AHRARSRAEG ERQKAETVQA ALEEAQRAQG
AAQGAIWGAV VDTQNTEQTL QRVQERMAGA EKSLNSAGER ARQLDALLEA LKLKRAGNSL
AASTAEETAG SAQSRAREAE KQLREQVGDQ YQTVRALAER KAEGVLAAQA RAEQLRDEAR
DLLQAAQDKL QRLQELEGTY EENERALEGK AAQLDGLEAR MRSVLQAINL QVQIYNTCQ
