ID   ERBB3_RAT               Reviewed;        1339 AA.
AC   Q62799; Q62955;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 3.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Receptor tyrosine-protein kinase erbB-3;
DE            EC=2.7.10.1;
DE   AltName: Full=Proto-oncogene-like protein c-ErbB-3;
DE   Flags: Precursor;
GN   Name=Erbb3;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8522190; DOI=10.1016/0378-1119(95)00436-a;
RA   Hellyer N.J., Kim H.-H., Greaves C.H., Sierke S.L., Koland J.G.;
RT   "Cloning of the rat ErbB3 cDNA and characterization of the recombinant
RT   protein.";
RL   Gene 165:279-284(1995).
RN   [2]
RP   SEQUENCE REVISION TO 85; 513 AND 565.
RA   Hellyer N.J., Koland J.G.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 922-1097.
RC   STRAIN=Sprague-Dawley; TISSUE=Sciatic nerve;
RX   PubMed=9030624; DOI=10.1523/jneurosci.17-05-01642.1997;
RA   Carroll S.L., Miller M.L., Frohnert P.W., Kim S.S., Corbett J.A.;
RT   "Expression of neuregulins and their putative receptors, ErbB2 and ErbB3,
RT   is induced during Wallerian degeneration.";
RL   J. Neurosci. 17:1642-1659(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, AND IDENTIFICATION BY
RP   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: Tyrosine-protein kinase that plays an essential role as cell
CC       surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is
CC       activated by it; ligand-binding increases phosphorylation on tyrosine
CC       residues and promotes its association with the p85 subunit of
CC       phosphatidylinositol 3-kinase. May also be activated by CSPG5. Involved
CC       in the regulation of myeloid cell differentiation.
CC       {ECO:0000250|UniProtKB:P21860}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBUNIT: Monomer and homodimer. Heterodimer with each of the other ERBB
CC       receptors (Potential). Interacts with CSPG5, PA2G4, GRB7, MYOC and
CC       MUC1. Found in a ternary complex with NRG1 and ITGAV:ITGB3 or
CC       ITGA6:ITGB4 (By similarity). {ECO:0000250|UniProtKB:P21860,
CC       ECO:0000250|UniProtKB:Q61526, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- DOMAIN: The cytoplasmic part of the receptor may interact with the SH2
CC       or SH3 domains of many signal-transducing proteins.
CC   -!- PTM: Autophosphorylated. Ligand-binding increases phosphorylation on
CC       tyrosine residues and promotes its association with the p85 subunit of
CC       phosphatidylinositol 3-kinase. {ECO:0000250|UniProtKB:P21860}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; U29339; AAC28498.2; -; mRNA.
DR   EMBL; U52530; AAC53050.1; -; mRNA.
DR   PIR; JC4387; JC4387.
DR   RefSeq; NP_058914.2; NM_017218.3.
DR   AlphaFoldDB; Q62799; -.
DR   SMR; Q62799; -.
DR   BioGRID; 248136; 7.
DR   DIP; DIP-41029N; -.
DR   ELM; Q62799; -.
DR   IntAct; Q62799; 1.
DR   STRING; 10116.ENSRNOP00000006796; -.
DR   GlyCosmos; Q62799; 10 sites, No reported glycans.
DR   GlyGen; Q62799; 10 sites.
DR   iPTMnet; Q62799; -.
DR   PhosphoSitePlus; Q62799; -.
DR   PaxDb; 10116-ENSRNOP00000006796; -.
DR   ABCD; Q62799; 1 sequenced antibody.
DR   DNASU; 29496; -.
DR   GeneID; 29496; -.
DR   KEGG; rno:29496; -.
DR   UCSC; RGD:69323; rat.
DR   AGR; RGD:69323; -.
DR   CTD; 2065; -.
DR   RGD; 69323; Erbb3.
DR   eggNOG; KOG1025; Eukaryota.
DR   InParanoid; Q62799; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; Q62799; -.
DR   BRENDA; 2.7.10.1; 5301.
DR   Reactome; R-RNO-1227986; Signaling by ERBB2.
DR   Reactome; R-RNO-1236394; Signaling by ERBB4.
DR   Reactome; R-RNO-1250196; SHC1 events in ERBB2 signaling.
DR   Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-RNO-1306955; GRB7 events in ERBB2 signaling.
DR   Reactome; R-RNO-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR   Reactome; R-RNO-1963642; PI3K events in ERBB2 signaling.
DR   Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-RNO-6785631; ERBB2 Regulates Cell Motility.
DR   Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-RNO-8847993; ERBB2 Activates PTK6 Signaling.
DR   Reactome; R-RNO-8863795; Downregulation of ERBB2 signaling.
DR   PRO; PR:Q62799; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR   GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR   GO; GO:0038143; C:ERBB3:ERBB2 complex; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR   GO; GO:0043235; C:receptor complex; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043125; F:ErbB-3 class receptor binding; ISO:RGD.
DR   GO; GO:0019838; F:growth factor binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0038132; F:neuregulin binding; IMP:RGD.
DR   GO; GO:0038131; F:neuregulin receptor activity; IMP:RGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR   GO; GO:0030296; F:protein tyrosine kinase activator activity; ISO:RGD.
DR   GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:RGD.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:RGD.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0007409; P:axonogenesis; IEP:RGD.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR   GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR   GO; GO:0021545; P:cranial nerve development; ISO:RGD.
DR   GO; GO:0003197; P:endocardial cushion development; ISO:RGD.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:RGD.
DR   GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; ISO:RGD.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR   GO; GO:0060056; P:mammary gland involution; IEP:RGD.
DR   GO; GO:0097049; P:motor neuron apoptotic process; ISO:RGD.
DR   GO; GO:0042552; P:myelination; ISO:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; ISO:RGD.
DR   GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; ISO:RGD.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR   GO; GO:0051048; P:negative regulation of secretion; ISO:RGD.
DR   GO; GO:0009968; P:negative regulation of signal transduction; ISO:RGD.
DR   GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR   GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR   GO; GO:0007422; P:peripheral nervous system development; ISO:RGD.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:RGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:RGD.
DR   GO; GO:0055025; P:positive regulation of cardiac muscle tissue development; ISO:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0046326; P:positive regulation of glucose import; IMP:RGD.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0014044; P:Schwann cell development; ISO:RGD.
DR   GO; GO:0014037; P:Schwann cell differentiation; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; ISO:RGD.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
DR   GO; GO:0043586; P:tongue development; IEP:RGD.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:RGD.
DR   CDD; cd00064; FU; 4.
DR   CDD; cd12095; TM_ErbB3; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR032778; GF_recep_IV.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-dom_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR   PANTHER; PTHR24416:SF88; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-3; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 5.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Signal;
KW   Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1339
FT                   /note="Receptor tyrosine-protein kinase erbB-3"
FT                   /id="PRO_0000016673"
FT   TOPO_DOM        20..643
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        644..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        663..1339
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          707..964
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1023..1052
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1078..1215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1052
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1108..1129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1166..1182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        832
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         713..721
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         740
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         786..788
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         832..837
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         684
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         980
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        616
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        186..194
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        190..202
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        210..218
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        214..226
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        227..235
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        231..243
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        246..255
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        259..286
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        290..301
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        305..320
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        323..327
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        500..509
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        504..517
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        520..529
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        533..549
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        552..565
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        556..573
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        576..585
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        589..610
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        613..621
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   DISULFID        617..629
FT                   /evidence="ECO:0000250|UniProtKB:P21860"
FT   CONFLICT        1028
FT                   /note="L -> P (in Ref. 3; AAC53050)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1339 AA;  147546 MW;  0AA5F2402BBFDF1E CRC64;
     MRATGTLQVL CFLLSLARGS EMGNSQAVCP GTLNGLSVTG DADNQYQTLY KLYEKCEVVM
     GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSVLPLP NLRVVRGTQV YDGKFAIFVM
     LNYNTNSSHA LRQLKFTQLT EILSGGVYIE KNDKLCHMDT IDWRDIVRVR GAEIVVKNNG
     ANCPPCHEVC KGRCWGPGPD DCQILTKTIC APQCNGRCFG PNPNQCCHDE CAGGCSGPQD
     TDCFACRRFN DSGACVPRCP EPLVYNKLTF QLEPNPHTKY QYGGVCVASC PHNFVVDQTF
     CVRACPPDKM EVDKHGLKMC EPCGGLCPKA CEGTGSGSRY QTVDSSNIDG FVNCTKILGN
     LDFLITGLNV DPWHKIPALD PEKLNVFRTV REITGYLNIQ SWPPHMHNFS VFSNLTTIGG
     RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS AGRVYISANQ QLCYHHSLNW TRLLRGPSEE
     RLDIKYDRPL GECLAEGKVC DPLCSSGGCW GPGPGQCLSC RNYSREGVCV THCNFLQGEP
     REFVHEAQCF SCHPECLPME GTSTCNGSGS DACARCAHFR DGPHCVNSCP HGILGAKGPI
     YKYPDAQNEC RPCHENCTQG CNGPELQDCL GQAEVLMSKP HLVIAVTVGL AVILMILGGS
     FLYWRGRRIQ NKRAMRRYLE RGESIEPLDP SEKANKVLAR IFKETELRKL KVLGSGVFGT
     VHKGIWIPEG ESIKIPVCIK VIEDKSGRQS FQAVTDHMLA VGSLDHAHIV RLLGLCPGSS
     LQLVTQYLPL GSLLDHVKQH RETLGPQLLL NWGVQIAKGM YYLEEHSMVH RDLALRNVML
     KSPSQVQVAD FGVADLLPPD DKQLLHSEAK TPIKWMALES IHFGKYTHQS DVWSYGVTVW
     ELMTFGAEPY AGLRLAEIPD LLEKGERLAQ PQICTIDVYM VMVKCWMIDE NIRPTFKELA
     NEFTRMARDP PRYLVIKRAS GPGTPPAAEP SVLTTKELQE AELEPELDLD LDLEAEEEGL
     ATSLGSALSL PTGTLTRPRG SQSLLSPSSG YMPMNQSSLG EACLDSAVLG GREQFSRPIS
     LHPIPRGRPA SESSEGHVTG SEAELQEKVS VCRSRSRSRS PRPRGDSAYH SQRHSLLTPV
     TPLSPPGLEE EDGNGYVMPD THLRGASSSR EGTLSSVGLS SVLGTEEEDE DEEYEYMNRK
     RRGSPPRPPR PGSLEELGYE YMDVGSDLSA SLGSTQSCPL HPMAIVPSAG TTPDEDYEYM
     NRRRGAGGAG GDYAAMGACP AAEQGYEEMR AFQGPGHHAP HVRYARLKTL RSLEATDSAF
     DNPDYWHSRL FPKANAQRT
//