ID   ERBB3_MOUSE             Reviewed;        1339 AA.
AC   Q61526; Q3KQR1; Q68J64; Q810U8; Q8K317;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Receptor tyrosine-protein kinase erbB-3;
DE            EC=2.7.10.1;
DE   AltName: Full=Glial growth factor receptor;
DE   AltName: Full=Proto-oncogene-like protein c-ErbB-3;
DE   Flags: Precursor;
GN   Name=Erbb3;
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].
RC   STRAIN=BALB/cJ;
RA   Yamauchi J., Shooter E.M.;
RT   "Involvement of the ErbB3 signaling pathway in Schwann cell migration.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Thyroid;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1061-1154.
RC   TISSUE=Muscle fibroblast;
RX   PubMed=7589796; DOI=10.1006/dbio.1995.0012;
RA   Moscoso L.M., Chu G.C., Gautam M., Noakes P.G., Merlie J.P., Sanes J.R.;
RT   "Synapse-associated expression of an acetylcholine receptor-inducing
RT   protein, ARIA/heregulin, and its putative receptors, ErbB2 and ErbB3, in
RT   developing mammalian muscle.";
RL   Dev. Biol. 172:158-169(1995).
RN   [4]
RP   INTERACTION WITH MYOC.
RX   PubMed=23897819; DOI=10.1074/jbc.m112.446138;
RA   Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C.,
RA   Tomarev S.I.;
RT   "Myocilin mediates myelination in the peripheral nervous system through
RT   ErbB2/3 signaling.";
RL   J. Biol. Chem. 288:26357-26371(2013).
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 and MUC1 (By
CC       similarity). Interacts with MYOC (PubMed:23897819). Found in a ternary
CC       complex with NRG1 and ITGAV:ITGB3 or ITGA6:ITGB4 (By similarity).
CC       {ECO:0000250|UniProtKB:P21860, ECO:0000269|PubMed:23897819,
CC       ECO:0000305}.
CC   -!- INTERACTION:
CC       Q61526; P70424: Erbb2; NbExp=2; IntAct=EBI-931878, EBI-2945468;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: In the muscle, expression localizes to the synaptic
CC       sites of muscle fibers.
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; AY686636; AAT95433.1; -; mRNA.
DR   EMBL; BC029028; AAH29028.1; -; mRNA.
DR   EMBL; BC049279; AAH49279.1; -; mRNA.
DR   EMBL; BC106091; AAI06092.1; -; mRNA.
DR   EMBL; L47240; AAA93533.1; -; mRNA.
DR   CCDS; CCDS24283.1; -.
DR   RefSeq; NP_034283.1; NM_010153.1.
DR   AlphaFoldDB; Q61526; -.
DR   SMR; Q61526; -.
DR   BioGRID; 199497; 26.
DR   IntAct; Q61526; 2.
DR   STRING; 10090.ENSMUSP00000080716; -.
DR   GlyConnect; 2676; 3 N-Linked glycans (1 site).
DR   GlyCosmos; Q61526; 10 sites, 3 glycans.
DR   GlyGen; Q61526; 10 sites, 3 N-linked glycans (1 site).
DR   iPTMnet; Q61526; -.
DR   PhosphoSitePlus; Q61526; -.
DR   MaxQB; Q61526; -.
DR   PaxDb; 10090-ENSMUSP00000080716; -.
DR   PeptideAtlas; Q61526; -.
DR   ProteomicsDB; 275878; -.
DR   ABCD; Q61526; 1 sequenced antibody.
DR   Antibodypedia; 3428; 2987 antibodies from 53 providers.
DR   DNASU; 13867; -.
DR   Ensembl; ENSMUST00000082059.7; ENSMUSP00000080716.7; ENSMUSG00000018166.9.
DR   GeneID; 13867; -.
DR   KEGG; mmu:13867; -.
DR   UCSC; uc007hnm.1; mouse.
DR   AGR; MGI:95411; -.
DR   CTD; 2065; -.
DR   MGI; MGI:95411; Erbb3.
DR   VEuPathDB; HostDB:ENSMUSG00000018166; -.
DR   eggNOG; KOG1025; Eukaryota.
DR   GeneTree; ENSGT00940000156107; -.
DR   HOGENOM; CLU_003384_2_0_1; -.
DR   InParanoid; Q61526; -.
DR   OMA; PDPNQCC; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; Q61526; -.
DR   TreeFam; TF106002; -.
DR   BRENDA; 2.7.10.1; 3474.
DR   Reactome; R-MMU-1227986; Signaling by ERBB2.
DR   Reactome; R-MMU-1236394; Signaling by ERBB4.
DR   Reactome; R-MMU-1250196; SHC1 events in ERBB2 signaling.
DR   Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-MMU-1306955; GRB7 events in ERBB2 signaling.
DR   Reactome; R-MMU-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR   Reactome; R-MMU-1963642; PI3K events in ERBB2 signaling.
DR   Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-MMU-6785631; ERBB2 Regulates Cell Motility.
DR   Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-MMU-8847993; ERBB2 Activates PTK6 Signaling.
DR   Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling.
DR   BioGRID-ORCS; 13867; 2 hits in 80 CRISPR screens.
DR   ChiTaRS; Erbb3; mouse.
DR   PRO; PR:Q61526; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q61526; Protein.
DR   Bgee; ENSMUSG00000018166; Expressed in small intestine Peyer's patch and 266 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0038143; C:ERBB3:ERBB2 complex; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043125; F:ErbB-3 class receptor binding; ISO:MGI.
DR   GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0038132; F:neuregulin binding; ISS:UniProtKB.
DR   GO; GO:0038131; F:neuregulin receptor activity; IMP:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0030296; F:protein tyrosine kinase activator activity; ISO:MGI.
DR   GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0021545; P:cranial nerve development; IMP:MGI.
DR   GO; GO:0003197; P:endocardial cushion development; IMP:MGI.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:MGI.
DR   GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; IDA:MGI.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR   GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI.
DR   GO; GO:0042552; P:myelination; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR   GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR   GO; GO:0051048; P:negative regulation of secretion; ISO:MGI.
DR   GO; GO:0009968; P:negative regulation of signal transduction; ISO:MGI.
DR   GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR   GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:MGI.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IGI:MGI.
DR   GO; GO:0055025; P:positive regulation of cardiac muscle tissue development; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0014044; P:Schwann cell development; IMP:MGI.
DR   GO; GO:0014037; P:Schwann cell differentiation; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; ISO:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:MGI.
DR   CDD; cd00064; FU; 3.
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.
DR   Genevisible; Q61526; MM.
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_0000042231"
FT   TOPO_DOM        20..641
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        642..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          1028..1052
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1077..1156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1181..1212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1086..1100
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   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:0000250|UniProtKB:P21860"
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        1067
FT                   /note="A -> V (in Ref. 3; AAA93533)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1339 AA;  147613 MW;  59D56FD9C9536FBE CRC64;
     MSAIGTLQVL GFLLSLARGS EMGNSQAVCP GTLNGLSVTG DADNQYQTLY KLYEKCEVVM
     GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSVLPLP NLRVVRGTQV YDGKFAIFVM
     LNYNTNSSHA LRQLRFTQLT EILLGGVYIE KNDKLCHMDT IDWRDIVRVP DAEIVVKNNG
     GNCPPCHEVC KGRCWGPGPE DCQILTKTIC APQCNGRCFG PNPNQCCHDE CAGGCSGPQD
     TDCFACRHFN DSGACVPRCP APLVYNKLTF QLEPNPHIKY QYGGVCVASC PHNFVVDQTF
     CVRACPADKM EVDKNGLKMC EPCRGLCPKA CEGTGSGSRY QTVDSSNIDG FVNCTKILGN
     LDFLITGLNG DPWHKIPALD PEKLNVFRTV REITGYLNIQ SWPPHMHNFS VFSNLTTIGG
     RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS AGRVYISANQ QLCYHHSLNW TRLLRGPAEE
     RLDIKYNRPL GECVAEGKVC DPLCSSGGCW GPGPGQCLSC RNYSREGVCV THCNVLQGEP
     REFVHEAHCF SCHPECQPME GTSTCNGSGS DACARCAHFR DGPHCVNSCP HGILGAKGPI
     YKYPDAQNEC RPCHENCTQG CKGPELQDCL GQAEVLMSKP HLVIAVTVGL TVIFLILGGS
     FLYWRGRRIQ NKRAMRRYLE RGESIEPLDP SEKANKVLAR IFKETELRKL KVLGSGVFGT
     VHKGIWIPEG ESIKIPVCIK VIEDKSGRQS FQAVTDHMLA VGSLDHAHIV RLLGLCPGSS
     LQLVTQYLPL GSLLDHVRQH RETLGPQLLL NWGVQIAKGM YYLEEHSMVH RDLALRNVML
     KSPSQVQVAD FGVADLLPPD DKQLLHSEAK TPIKWMALES IHFGKYTHQS DVWSYGVTVW
     ELMTFGAEPY AGLRLAEIPD LLEKGERLAQ PQICTIDVYM VMVKCWMIDE NIRPTFKELA
     NEFTRMARDP PRYLVIKRAS GPGIPPAAEP SALSTKELQD AELEPDLDLD LDVEVEEEGL
     ATTLGSALSL PTGTLTRPRG SQSLLSPSSG YMPMNQSNLG EACLDSAVLG GREQFSRPIS
     LHPIPRGRQT SESSEGHVTG SEAELQERVS MCRSRSRSRS PRPRGDSAYH SQRHSLLTPV
     TPLSPPGLEE EDGNGYVMPD THLRGTSSSR EGTLSSVGLS SVLGTEEEDE DEEYEYMNRK
     RRGSPARPPR PGSLEELGYE YMDVGSDLSA SLGSTQSCPL HPMAIVPSAG TTPDEDYEYM
     NRRRGAGGSG GDYAAMGACP AAEQGYEEMR AFQGPGHQAP HVRYARLKTL RSLEATDSAF
     DNPDYWHSRL FPKANAQRI
//