SH2B1_RAT
ID SH2B1_RAT Reviewed; 756 AA.
AC Q62985; O55072;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=SH2B adapter protein 1;
DE AltName: Full=FceRI gamma-chain-interacting protein SH2-B;
DE AltName: Full=SH2 domain-containing protein 1B;
DE AltName: Full=SH2-B PH domain-containing signaling mediator 1;
GN Name=Sh2b1; Synonyms=Sh2-b, Sh2bpsm1;
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 [MRNA] (ISOFORM 1), AND INTERACTION WITH FCER1G.
RC TISSUE=Mast cell;
RX PubMed=9636306; DOI=10.1038/nbt1295-1474;
RA Osborne M.A., Dalton S., Kochan J.P.;
RT "The yeast tribrid system -- genetic detection of trans-phosphorylated
RT ITAM-SH2-interactions.";
RL Biotechnology (N.Y.) 13:1474-1478(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PHOSPHORYLATION, AND
RP INTERACTION WITH JAK2.
RC TISSUE=Kidney;
RX PubMed=9343427; DOI=10.1128/mcb.17.11.6633;
RA Rui L., Mathews L.S., Hotta K., Gustafson T.A., Carter-Su C.;
RT "Identification of SH2-Bbeta as a substrate of the tyrosine kinase JAK2
RT involved in growth hormone signaling.";
RL Mol. Cell. Biol. 17:6633-6644(1997).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=9742218; DOI=10.1042/bj3350103;
RA Kotani K., Wilden P., Pillay T.S.;
RT "SH2-Balpha is an insulin-receptor adapter protein and substrate that
RT interacts with the activation loop of the insulin-receptor kinase.";
RL Biochem. J. 335:103-109(1998).
RN [4]
RP INTERACTION WITH PDGFRA/B.
RX PubMed=9694882; DOI=10.1074/jbc.273.33.21239;
RA Rui L., Carter-Su C.;
RT "Platelet-derived growth factor (PDGF) stimulates the association of SH2-
RT Bbeta with PDGF receptor and phosphorylation of SH2-Bbeta.";
RL J. Biol. Chem. 273:21239-21245(1998).
RN [5]
RP FUNCTION IN NGF SIGNALING, INTERACTION WITH NTRK1, AND PHOSPHORYLATION.
RX PubMed=9856458; DOI=10.1016/s0896-6273(00)80620-0;
RA Qian X., Riccio A., Zhang Y., Ginty D.D.;
RT "Identification and characterization of novel substrates of Trk receptors
RT in developing neurons.";
RL Neuron 21:1017-1029(1998).
RN [6]
RP FUNCTION IN NGF SIGNALING, PHOSPHORYLATION AT SER-96, AND MUTAGENESIS OF
RP SER-96.
RX PubMed=10473609; DOI=10.1074/jbc.274.37.26485;
RA Rui L., Herrington J., Carter-Su C.;
RT "SH2-B, a membrane-associated adapter, is phosphorylated on multiple
RT serines/threonines in response to nerve growth factor by kinases within the
RT MEK/ERK cascade.";
RL J. Biol. Chem. 274:26485-26492(1999).
RN [7]
RP FUNCTION IN JAK2 ACTIVATION, AND MUTAGENESIS OF ARG-555.
RX PubMed=10377387; DOI=10.1073/pnas.96.13.7172;
RA Rui L., Carter-Su C.;
RT "Identification of SH2-bbeta as a potent cytoplasmic activator of the
RT tyrosine kinase Janus kinase 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7172-7177(1999).
RN [8]
RP FUNCTION, INTERACTION WITH JAK2, AND MUTAGENESIS OF ARG-555.
RX PubMed=10757801; DOI=10.1128/mcb.20.9.3168-3177.2000;
RA Rui L., Gunter D.R., Herrington J., Carter-Su C.;
RT "Differential binding to and regulation of JAK2 by the SH2 domain and N-
RT terminal region of SH2-bbeta.";
RL Mol. Cell. Biol. 20:3168-3177(2000).
RN [9]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH SH2B2.
RX PubMed=11238898; DOI=10.1128/mcb.21.5.1613-1620.2001;
RA Qian X., Ginty D.D.;
RT "SH2-B and APS are multimeric adapters that augment TrkA signaling.";
RL Mol. Cell. Biol. 21:1613-1620(2001).
RN [10]
RP INTERACTION WITH JAK1; JAK2 AND JAK3, AND PHOSPHORYLATION.
RX PubMed=11751854; DOI=10.1074/jbc.m109165200;
RA O'Brien K.B., O'Shea J.J., Carter-Su C.;
RT "SH2-B family members differentially regulate JAK family tyrosine
RT kinases.";
RL J. Biol. Chem. 277:8673-8681(2002).
RN [11]
RP FUNCTION IN ACTIN REORGANIZATION, AND INTERACTION WITH RAC1.
RX PubMed=11786545; DOI=10.1074/jbc.m111138200;
RA Diakonova M., Gunter D.R., Herrington J., Carter-Su C.;
RT "SH2-Bbeta is a Rac-binding protein that regulates cell motility.";
RL J. Biol. Chem. 277:10669-10677(2002).
RN [12]
RP INTERACTION WITH FGFR3.
RX PubMed=11827956; DOI=10.1074/jbc.m102777200;
RA Kong M., Wang C.S., Donoghue D.J.;
RT "Interaction of fibroblast growth factor receptor 3 and the adapter protein
RT SH2-B. A role in STAT5 activation.";
RL J. Biol. Chem. 277:15962-15970(2002).
RN [13]
RP PHOSPHORYLATION AT TYR-439 AND TYR-494, AND MUTAGENESIS OF TYR-439 AND
RP TYR-494.
RX PubMed=12551917; DOI=10.1074/jbc.m210765200;
RA O'Brien K.B., Argetsinger L.S., Diakonova M., Carter-Su C.;
RT "YXXL motifs in SH2-Bbeta are phosphorylated by JAK2, JAK1, and platelet-
RT derived growth factor receptor and are required for membrane ruffling.";
RL J. Biol. Chem. 278:11970-11978(2003).
RN [14]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-231 AND LEU-233.
RX PubMed=15082760; DOI=10.1128/mcb.24.9.3633-3647.2004;
RA Chen L., Carter-Su C.;
RT "Adapter protein SH2-B beta undergoes nucleocytoplasmic shuttling:
RT implications for nerve growth factor induction of neuronal
RT differentiation.";
RL Mol. Cell. Biol. 24:3633-3647(2004).
RN [15]
RP FUNCTION IN GDNF SIGNALING, AND INTERACTION WITH RET.
RX PubMed=16569669; DOI=10.1242/jcs.02845;
RA Zhang Y., Zhu W., Wang Y.G., Liu X.J., Jiao L., Liu X., Zhang Z.H.,
RA Lu C.L., He C.;
RT "Interaction of SH2-Bbeta with RET is involved in signaling of GDNF-induced
RT neurite outgrowth.";
RL J. Cell Sci. 119:1666-1676(2006).
RN [16]
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: Adapter protein for several members of the tyrosine kinase
CC receptor family. Involved in multiple signaling pathways mediated by
CC Janus kinase (JAK) and receptor tyrosine kinases, including the
CC receptors of insulin (INS), insulin-like growth factor I (IGF1), nerve
CC growth factor (NGF), brain-derived neurotrophic factor (BDNF), glial
CC cell line-derived neurotrophic factor (GDNF), platelet-derived growth
CC factor (PDGF) and fibroblast growth factors (FGFs). In growth hormone
CC (GH) signaling, autophosphorylated ('Tyr-813') JAK2 recruits SH2B1,
CC which in turn is phosphorylated by JAK2 on tyrosine residues. These
CC phosphotyrosines form potential binding sites for other signaling
CC proteins. GH also promotes serine/threonine phosphorylation of SH2B1
CC and these phosphorylated residues may serve to recruit other proteins
CC to the GHR-JAK2-SH2B1 complexes, such as RAC1. In leptin (LEP)
CC signaling, binds to and potentiates the activation of JAK2 by globally
CC enhancing downstream pathways. In response to leptin, binds
CC simultaneously to both, JAK2 and IRS1 or IRS2, thus mediating formation
CC of a complex of JAK2, SH2B1 and IRS1 or IRS2. Mediates tyrosine
CC phosphorylation of IRS1 and IRS2, resulting in activation of the PI 3-
CC kinase pathway. Acts as positive regulator of NGF-mediated activation
CC of the Akt/Forkhead pathway; prolongs NGF-induced phosphorylation of
CC AKT1 on 'Ser-473' and AKT1 enzymatic activity. Enhances the kinase
CC activity of the cytokine receptor-associated tyrosine kinase JAK2 and
CC of other receptor tyrosine kinases, such as FGFR3 and NTRK1. For JAK2,
CC the mechanism seems to involve dimerization of both, SH2B1 and JAK2.
CC Enhances RET phosphorylation and kinase activity. Isoforms seem to be
CC differentially involved in IGF-I and PDGF-induced mitogenesis (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:10377387,
CC ECO:0000269|PubMed:10473609, ECO:0000269|PubMed:10757801,
CC ECO:0000269|PubMed:11238898, ECO:0000269|PubMed:11786545,
CC ECO:0000269|PubMed:16569669, ECO:0000269|PubMed:9343427,
CC ECO:0000269|PubMed:9856458}.
CC -!- SUBUNIT: Self-associates. Homopentamer. Forms a heteromultimeric
CC complex with SH2B2. Interacts with SH2B2. Isoform 1 interacts via its
CC SH2 domain with JAK2. Isoform 2 interacts via its SH2 domain and its N-
CC terminus with JAK2; the SH2 domain is required for the major
CC interaction with JAK2 phosphorylated on tyrosine residues; the N-
CC terminus provides a low-affinity binding to JAK2 independent of JAK2
CC phosphorylation. Isoform 1 interacts via its SH2 domain with INSR; the
CC interaction requires receptor activation. Isoform 1 interacts with
CC IGF1R; the interaction requires receptor activation. Isoform 2
CC interacts via its SH2 domain with FGFR3. Isoform 2 interacts with RET;
CC the interaction requires RET kinase activity. Isoform 2 interacts with
CC RAC1. Isoform 2 interacts with PDGFRA and/or PDGFRB; the interaction
CC requires receptor activation. Interacts with ISR1 and ISR2. Probably
CC part of a complex consisting of INSR, ISR1 and SH2B1. Probably part of
CC a ternary complex consisting of SH2B1, JAK2 and ISR1 or ISR2 (By
CC similarity). May interact with FCER1G. Interacts (via SH2 domain) with
CC NTRK1 (phosphorylated). {ECO:0000250, ECO:0000269|PubMed:10757801,
CC ECO:0000269|PubMed:11238898, ECO:0000269|PubMed:11751854,
CC ECO:0000269|PubMed:11786545, ECO:0000269|PubMed:11827956,
CC ECO:0000269|PubMed:16569669, ECO:0000269|PubMed:9343427,
CC ECO:0000269|PubMed:9636306, ECO:0000269|PubMed:9694882,
CC ECO:0000269|PubMed:9856458}.
CC -!- INTERACTION:
CC Q62985; P07949: RET; Xeno; NbExp=3; IntAct=EBI-7395583, EBI-2480756;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15082760}. Membrane
CC {ECO:0000305|PubMed:15082760}. Nucleus {ECO:0000269|PubMed:15082760}.
CC Note=Shuttles between the nucleus and the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62985-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62985-2; Sequence=VSP_032045;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Expressed in
CC epididymal adipose tissue, liver and skeletal muscle.
CC {ECO:0000269|PubMed:9742218}.
CC -!- PTM: Phosphorylated on tyrosine residues in response to treatment with
CC growth hormone (GH), IFN-gamma (IFNG), BDNF, PDGF and FGF.
CC Phosphorylated on tyrosine residues by JAK2 and JAK1. Phosphorylated on
CC multiple serine and threonine residues in response to treatment with
CC NGF. Phosphorylated on serine residues. {ECO:0000269|PubMed:10473609,
CC ECO:0000269|PubMed:11751854, ECO:0000269|PubMed:12551917,
CC ECO:0000269|PubMed:9343427, ECO:0000269|PubMed:9856458}.
CC -!- SIMILARITY: Belongs to the SH2B adapter family. {ECO:0000305}.
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DR EMBL; U57391; AAC52601.1; -; mRNA.
DR EMBL; AF047577; AAC04575.1; -; mRNA.
DR RefSeq; NP_001041645.1; NM_001048180.1.
DR RefSeq; NP_604451.2; NM_134456.3. [Q62985-1]
DR RefSeq; XP_006230415.1; XM_006230353.3. [Q62985-1]
DR RefSeq; XP_006230416.1; XM_006230354.3. [Q62985-1]
DR AlphaFoldDB; Q62985; -.
DR SMR; Q62985; -.
DR BioGRID; 250140; 5.
DR IntAct; Q62985; 37.
DR MINT; Q62985; -.
DR STRING; 10116.ENSRNOP00000066048; -.
DR iPTMnet; Q62985; -.
DR PhosphoSitePlus; Q62985; -.
DR PaxDb; Q62985; -.
DR PRIDE; Q62985; -.
DR GeneID; 89817; -.
DR KEGG; rno:89817; -.
DR CTD; 25970; -.
DR RGD; 620132; Sh2b1.
DR VEuPathDB; HostDB:ENSRNOG00000049181; -.
DR eggNOG; ENOG502QT43; Eukaryota.
DR InParanoid; Q62985; -.
DR OMA; GILQWRS; -.
DR OrthoDB; 556279at2759; -.
DR PhylomeDB; Q62985; -.
DR Reactome; R-RNO-1170546; Prolactin receptor signaling.
DR Reactome; R-RNO-982772; Growth hormone receptor signaling.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q62985; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000049181; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; Q62985; baseline and differential.
DR Genevisible; Q62985; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:RGD.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:RGD.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:RGD.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; ISO:RGD.
DR CDD; cd10346; SH2_SH2B_family; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR015012; Phe_ZIP.
DR InterPro; IPR036290; Phe_ZIP_sf.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR030523; SH2B.
DR InterPro; IPR030521; SH2B1.
DR InterPro; IPR035057; SH2B1_SH2.
DR PANTHER; PTHR10872; PTHR10872; 1.
DR PANTHER; PTHR10872:SF3; PTHR10872:SF3; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF08916; Phe_ZIP; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00233; PH; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF109805; SSF109805; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Membrane; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; SH2 domain.
FT CHAIN 1..756
FT /note="SH2B adapter protein 1"
FT /id="PRO_0000323611"
FT DOMAIN 247..376
FT /note="PH"
FT DOMAIN 527..625
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..555
FT /note="Interaction with JAK2 (low-affinity binding;
FT independent of JAK2 phosphorylation)"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 24..85
FT /note="Required for self-association"
FT /evidence="ECO:0000250"
FT REGION 85..196
FT /note="Interaction with RAC1"
FT /evidence="ECO:0000269|PubMed:11786545"
FT REGION 100..243
FT /note="Required for NGF signaling"
FT REGION 124..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..233
FT /note="Required for nuclear localization"
FT REGION 262..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZM2"
FT MOD_RES 96
FT /note="Phosphoserine; by MAPK1 or MAPK3; in vitro"
FT /evidence="ECO:0000269|PubMed:10473609"
FT MOD_RES 270
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF2"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZM2"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZM2"
FT MOD_RES 439
FT /note="Phosphotyrosine; by JAK1, JAK2 and PDGFR"
FT /evidence="ECO:0000269|PubMed:12551917"
FT MOD_RES 494
FT /note="Phosphotyrosine; by JAK1, JAK2"
FT /evidence="ECO:0000269|PubMed:12551917"
FT VAR_SEQ 632..756
FT /note="ERSTSRDPTQPSEPPPWTDPPHPGAEEASGAPEVAAATAAAAKERQEKEKAG
FT GGGVQEELVPMAELVPMAELEEAIAPGTEAQGGAGSSGDLEVSLMVQLQQLPLGGNGEE
FT GGHPRAINNQYSFV -> GREQAGSHAGVCEGDRCYPDASSTFLPFGASDCVTEHFP
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9343427"
FT /id="VSP_032045"
FT MUTAGEN 96
FT /note="S->A: Reduces in vitro phosphorylation by MAPK1
FT and/or MAPK3."
FT /evidence="ECO:0000269|PubMed:10473609"
FT MUTAGEN 231
FT /note="L->A: Abolishes nuclear localization; when
FT associated with A-233."
FT /evidence="ECO:0000269|PubMed:15082760"
FT MUTAGEN 233
FT /note="L->A: Abolishes nuclear localization; when
FT associated with A-231."
FT /evidence="ECO:0000269|PubMed:15082760"
FT MUTAGEN 439
FT /note="Y->F: Fails to enhance GH-induced membrane ruffling;
FT when associated with F-494."
FT /evidence="ECO:0000269|PubMed:12551917"
FT MUTAGEN 439
FT /note="Y->F: Reduces phosphorylation by JAK1, JAK2 and
FT PDGFRA."
FT /evidence="ECO:0000269|PubMed:12551917"
FT MUTAGEN 494
FT /note="Y->F: Fails to enhance GH-induced membrane ruffling;
FT when associated with F-439."
FT /evidence="ECO:0000269|PubMed:12551917"
FT MUTAGEN 494
FT /note="Y->F: Reduces phosphorylation by JAK1 and JAK2."
FT /evidence="ECO:0000269|PubMed:12551917"
FT MUTAGEN 555
FT /note="R->E: Reduces interaction with JAK2 and abolishes
FT JAK2 kinase activity; reduces GH-stimulated cell motility;
FT abolishes interaction with PDGFRA."
FT /evidence="ECO:0000269|PubMed:10377387,
FT ECO:0000269|PubMed:10757801"
FT CONFLICT 211
FT /note="R -> K (in Ref. 2; AAC04575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 79637 MW; D4FCF3086CF3DFE0 CRC64;
MNGAPSPEDG VFPSPPALPP PPPPSWQEFC ESHARAAALD LARRFRLYLA SHPQYAEPGA
EAAFSGRFAE LFLQHFEAEV ARASGSLSPP VLAPLSPGVE IPPSHDLSLE SCRVGGPLAV
LGPSRSSEDL AGPLPSSVSS STTSSKPKLK KRFSLRSVGR SVRGSVRGIL QWRGAVESPS
QAGPLETTSG PPVLGGNSNS NSSGGAGTVG RALANDGTSP GERWTHRFER LRLSRGGGTL
RDGAGVIQRE ELLSFMGAEE AAPDPAGVGR GGGAAGLTSG GGGQPQWQKC RLLLRSEGEG
GGGSRLEFFV PPKASRPRLS IPCSTITDVR TATALEMPDR ENTFVVKVEG PSEYILETTD
ALHVKAWVSD IQECLSPGPC PAISPRPMTL PLAPGTSFLT KDNTESLELP CLNHSESLPS
QDLLLGPSES NDRLSQGAYG GLSDRPSASF SPSSASIAAS HFDSMELLPP ELPPRIPIEE
GPPAGTVHPL STPYPPLDTP EAATGSFLFQ GEAEGGEGDQ PLSGYPWFHG MLSRLKAAQL
VLEGGTSSHG VFLVRQSETR RGEYVLTFNF QGKAKHLRLS LNEEGQCRVQ HLWFQSIFDM
LEHFRVHPIP LESGGSSDVV LVSYVPSQRQ QERSTSRDPT QPSEPPPWTD PPHPGAEEAS
GAPEVAAATA AAAKERQEKE KAGGGGVQEE LVPMAELVPM AELEEAIAPG TEAQGGAGSS
GDLEVSLMVQ LQQLPLGGNG EEGGHPRAIN NQYSFV
