BCR_RAT
ID BCR_RAT Reviewed; 1270 AA.
AC F1LXF1;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Breakpoint cluster region protein {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P11274};
GN Name=Bcr {ECO:0000312|RGD:1307993};
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP INTERACTION WITH DLG4, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=20962234; DOI=10.1523/jneurosci.1711-10.2010;
RA Oh D., Han S., Seo J., Lee J.R., Choi J., Groffen J., Kim K., Cho Y.S.,
RA Choi H.S., Shin H., Woo J., Won H., Park S.K., Kim S.Y., Jo J.,
RA Whitcomb D.J., Cho K., Kim H., Bae Y.C., Heisterkamp N., Choi S.Y., Kim E.;
RT "Regulation of synaptic Rac1 activity, long-term potentiation maintenance,
RT and learning and memory by BCR and ABR Rac GTPase-activating proteins.";
RL J. Neurosci. 30:14134-14144(2010).
RN [3] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Protein with a unique structure having two opposing
CC regulatory activities toward small GTP-binding proteins. The C-terminus
CC is a GTPase-activating protein (GAP) domain which stimulates GTP
CC hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of
CC GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the
CC active GTP-bound form. The central Dbl homology (DH) domain functions
CC as guanine nucleotide exchange factor (GEF) that modulates the GTPases
CC CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1
CC from the GDP-bound to the GTP-bound form. The amino terminus contains
CC an intrinsic kinase activity (By similarity). Functions as an important
CC negative regulator of neuronal RAC1 activity (By similarity). Regulates
CC macrophage functions such as CSF1-directed motility and phagocytosis
CC through the modulation of RAC1 activity. Plays a major role as a RHOA
CC GEF in keratinocytes being involved in focal adhesion formation and
CC keratinocyte differentiation (By similarity).
CC {ECO:0000250|UniProtKB:P11274, ECO:0000250|UniProtKB:Q6PAJ1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P11274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P11274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Homotetramer. Interacts with PDZK1 (By similarity). May
CC interact with CCPG1 (By similarity). Interacts with HCK, FES/FPS, ABL1,
CC PIK3R1 and GRB2 (By similarity). Interacts with SH2D5 (By similarity).
CC Interacts with DLG4 (PubMed:20962234). {ECO:0000250|UniProtKB:P11274,
CC ECO:0000250|UniProtKB:Q6PAJ1, ECO:0000269|PubMed:20962234}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q6PAJ1}. Synapse {ECO:0000269|PubMed:20962234}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, including the cortex,
CC hippocampus, cerebellum, and brainstem, as well as the spinal cord (at
CC protein level). {ECO:0000269|PubMed:20962234}.
CC -!- DEVELOPMENTAL STAGE: Expression is initially high at a late embryonic
CC (E18) stage and maintained at slightly decreased levels throughout
CC postnatal brain development. {ECO:0000269|PubMed:20962234}.
CC -!- DOMAIN: The region involved in binding to ABL1 SH2-domain is rich in
CC serine residues and needs to be Ser/Thr phosphorylated prior to SH2
CC binding. This region is essential for the activation of the ABL1
CC tyrosine kinase and transforming potential of the chimeric BCR-ABL
CC oncogene. {ECO:0000250|UniProtKB:P11274}.
CC -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC {ECO:0000250|UniProtKB:Q6PAJ1}.
CC -!- DOMAIN: The amino terminus contains an intrinsic kinase activity. The
CC central Dbl homology (DH) domain functions as guanine nucleotide
CC exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1.
CC Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to
CC the GTP-bound form. The C-terminus is a Rho-GAP domain which stimulates
CC GTP hydrolysis by RAC1, RAC2 and CDC42. The protein has a unique
CC structure having two opposing regulatory activities toward small GTP-
CC binding proteins. {ECO:0000250|UniProtKB:P11274}.
CC -!- PTM: Autophosphorylated. Phosphorylated by FES/FPS on tyrosine
CC residues, leading to down-regulation of the BCR kinase activity.
CC Phosphorylation by HCK is important for interaction with GRB2.
CC {ECO:0000250|UniProtKB:P11274}.
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; AABR07044649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07044650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1LXF1; -.
DR STRING; 10116.ENSRNOP00000001766; -.
DR jPOST; F1LXF1; -.
DR PaxDb; F1LXF1; -.
DR PeptideAtlas; F1LXF1; -.
DR PRIDE; F1LXF1; -.
DR Ensembl; ENSRNOT00000001766; ENSRNOP00000001766; ENSRNOG00000001304.
DR RGD; 1307993; Bcr.
DR VEuPathDB; HostDB:ENSRNOG00000001304; -.
DR eggNOG; KOG4269; Eukaryota.
DR GeneTree; ENSGT00940000153491; -.
DR HOGENOM; CLU_004164_0_0_1; -.
DR InParanoid; F1LXF1; -.
DR OMA; EKSYNRT; -.
DR TreeFam; TF105082; -.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:F1LXF1; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000001304; Expressed in frontal cortex and 19 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0060216; P:definitive hemopoiesis; ISO:RGD.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:RGD.
DR GO; GO:0048872; P:homeostasis of number of cells; ISO:RGD.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; ISO:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:1905517; P:macrophage migration; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0060313; P:negative regulation of blood vessel remodeling; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0002692; P:negative regulation of cellular extravasation; ISO:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:1905522; P:negative regulation of macrophage migration; IEA:Ensembl.
DR GO; GO:0043314; P:negative regulation of neutrophil degranulation; ISO:RGD.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0060268; P:negative regulation of respiratory burst; ISO:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0043312; P:neutrophil degranulation; IEA:Ensembl.
DR GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; ISO:RGD.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; ISO:RGD.
DR GO; GO:0043114; P:regulation of vascular permeability; ISO:RGD.
DR GO; GO:0003014; P:renal system process; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:RGD.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 4.10.280.30; -; 1.
DR InterPro; IPR037769; Abr/Bcr.
DR InterPro; IPR015123; Bcr-Abl_oncoprot_oligo.
DR InterPro; IPR036481; Bcr-Abl_oncoprot_oligo_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23182; PTHR23182; 1.
DR Pfam; PF09036; Bcr-Abl_Oligo; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF69036; SSF69036; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Coiled coil; GTPase activation;
KW Guanine-nucleotide releasing factor; Kinase; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..1270
FT /note="Breakpoint cluster region protein"
FT /id="PRO_0000447439"
FT DOMAIN 497..690
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 707..865
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 892..1019
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1053..1247
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 67..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..55
FT /evidence="ECO:0000255"
FT COMPBIAS 201..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAJ1"
FT MOD_RES 247
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAJ1"
FT MOD_RES 387
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAJ1"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 473
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAJ1"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 553
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 640
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 643
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 692
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
SQ SEQUENCE 1270 AA; 143034 MW; EFDB458FC779D13C CRC64;
MVDSVGFAEA WRAQFPDSEP PRMELRSVGD IEQELERCKA SIRRLEQEVN QERFRMIYLQ
TLLAKEKKSY DRQRWGFRRA AQPPDGAAEP RASAPRLPPA PADGADPAPV EESEARPDGE
GSPSKGRPAT ARRPAAAAPA DRDDRGPPTS VAALRSNFEK IRKGPAQPGS ADAEKPFYVN
VEFHHERGLV KVNDKEVSDR ISSLGSQAMQ MERKKSQQSA GQGLGEAPRP HYRGRSSESS
CGLDGDYEDA ELNPRFLKDN LINANGGNRP PWPPLEYQPY QSIYVGGMMV EGEGKSPLLR
SQSTSEQEKR LTWPRRSYSP RSFEDSGGGY TPDCSSNENL TSSEEDFSSG QSSRVSPSPT
TYRMFRDKSR SPSQNSQQSF DSSSPPTPQC QKRHRQCQVV VSEATIVGVR KTGQIWPSDG
DSTFQGEADS SFGTPPGYGC AADQAEEQRR HQDGLPYIDD SPSSSPHLSS KGRGSPASGA
LEPTKASELD LEKGLEMRKW VLSGILASEE TYLSHLEALL LPMKPLKAAA TTSQPVLTSQ
QIETIFFKVP ELYEIHKEFY DGLFPRVQQW SHQQRVGDLF QKLASQLGVY RAFVDNYGVA
METAEKCCQA NAQFAEISEN LRARSNKDVK DSTTKNSLET LLYKPVDRVT RSTLVLHDLL
KHTPSSHPDH SLLQDALRIS QNFLSSINEE ITPRRQSMTV KKGEHRQLLK DSFMVELVEG
ARKLRHIFLF TDLLLCTKLK KQSGGKTQQY DCKWYIPLTD LSFQMVDELE ALPNIPLVPD
EELDALKIKI SQIKSDIQRE KRANKGSKVM ERLRKKLSEQ ESLLLLMSPS MAFRVHSRNG
KSYTFLISSD YERAEWRESI REQQKKCFKS FSLTSVELQM LTNSCVKLQT VHHIPLTINK
EDDESPGLYG FLHAIVHSAT GFKQSSNLYC TLEVDSFGYF VNKAKTRVYR DTTEPNWNEE
FEIELEGSQT LRILCYEKCY NKMKMAKEDG ESADKLMGKG QVQLDPQTLQ DRDWQRTVID
MNGIEVKLSV KFTSREFSLK RMPSRKQTGV FGVKIAVVTK RERSKVPYIV RQCVEEIERR
GMEEVGIYRV SGVATDIQAL KAAFDVNNKD VSVMMSEMDV NAIAGTLKLY FRELPEPLFT
DEFYPNFAEG IALSDPVAKE SCMLNLLLSL PEANLLTFLF LLDHLKRVAE KETVNKMSLH
NLATVFGPTL LRPSEKESKL PANPSQPITM TDSWSLEVMS QVQVLLYFLQ LEAIPAPDSK
RQSILFSTEV
