ID NRG2_HUMAN Reviewed; 850 AA. AC O14511; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 25-MAY-2022, entry version 183. DE RecName: Full=Pro-neuregulin-2, membrane-bound isoform; DE Short=Pro-NRG2; DE Contains: DE RecName: Full=Neuregulin-2; DE Short=NRG-2; DE AltName: Full=Divergent of neuregulin-1; DE Short=DON-1; DE AltName: Full=Neural- and thymus-derived activator for ERBB kinases; DE Short=NTAK; DE Flags: Precursor; GN Name=NRG2; Synonyms=NTAK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Neuroblastoma; RX PubMed=9348101; DOI=10.1093/oxfordjournals.jbchem.a021806; RA Higashiyama S., Horikawa M., Yamada K., Ichino N., Nakano N., Nakagawa T., RA Miyagawa J., Matsushita N., Nagatsu T., Taniguchi N., Ishiguro H.; RT "A novel brain-derived member of the epidermal growth factor family that RT interacts with ErbB3 and ErbB4."; RL J. Biochem. 122:675-680(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DON-1B AND DON-1R). RC TISSUE=Fetal brain; RX PubMed=9199335; DOI=10.1128/mcb.17.7.4007; RA Busfield S.J., Michnick D.A., Chickering T.W., Revett T.L., Ma J., RA Woolf E.A., Comrack C.A., Dussault B.J., Woolf J., Goodearl A.D.J., RA Gearing D.P.; RT "Characterization of a neuregulin-related gene, Don-1, that is highly RT expressed in restricted regions of the cerebellum and hippocampus."; RL Mol. Cell. Biol. 17:4007-4014(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1; 2; RP 3; 4; 5 AND 6). RC TISSUE=Fetal brain, and Lung; RX PubMed=10369162; DOI=10.1007/s004390050961; RA Ring H.Z., Chang H., Guilbot A., Brice A., LeGuern E., Francke U.; RT "The human neuregulin 2 (NRG2) gene: cloning, mapping and evaluation as a RT candidate for the autosomal recessive form of Charcot-Marie-Tooth disease RT linked to 5q."; RL Hum. Genet. 104:326-332(1999). RN [4] RP INTERACTION WITH ERBB4. RX PubMed=10867024; DOI=10.1074/jbc.c901015199; RA Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C., RA Carraway K.L. III; RT "Ligand discrimination in signaling through an ErbB4 receptor homodimer."; RL J. Biol. Chem. 275:19803-19807(2000). CC -!- FUNCTION: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. CC Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in CC ligand-stimulated tyrosine phosphorylation and activation of the ERBB CC receptors. May also promote the heterodimerization with the EGF CC receptor. CC -!- SUBUNIT: Interacts with ERBB3 and ERBB4. {ECO:0000269|PubMed:10867024}. CC -!- SUBCELLULAR LOCATION: [Pro-neuregulin-2, membrane-bound isoform]: Cell CC membrane {ECO:0000250}; Single-pass type I membrane protein CC {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Neuregulin-2]: Secreted {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Name=1; CC IsoId=O14511-1; Sequence=Displayed; CC Name=2; CC IsoId=O14511-2; Sequence=VSP_003453; CC Name=3; CC IsoId=O14511-3; Sequence=VSP_003455; CC Name=4; CC IsoId=O14511-4; Sequence=VSP_003454; CC Name=5; CC IsoId=O14511-5; Sequence=VSP_003458, VSP_003459; CC Name=6; CC IsoId=O14511-6; Sequence=VSP_003456, VSP_003457; CC Name=DON-1B; CC IsoId=O14511-7; Sequence=VSP_003452, VSP_003455; CC Name=DON-1R; CC IsoId=O14511-8; Sequence=VSP_003451; CC -!- TISSUE SPECIFICITY: Restricted to the cerebellum in the adult. CC -!- DOMAIN: The cytoplasmic domain may be involved in the regulation of CC trafficking and proteolytic processing. Regulation of the proteolytic CC processing involves initial intracellular domain dimerization (By CC similarity). {ECO:0000250}. CC -!- DOMAIN: ERBB receptor binding is elicited entirely by the EGF-like CC domain. {ECO:0000250}. CC -!- PTM: Proteolytic cleavage close to the plasma membrane on the external CC face leads to the release of the soluble growth factor form. CC {ECO:0000250}. CC -!- PTM: Extensive glycosylation precedes the proteolytic cleavage. CC {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the neuregulin family. {ECO:0000305}. 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; AB005060; BAA23417.1; -; mRNA. DR EMBL; AF119162; AAF28848.1; -; Genomic_DNA. DR EMBL; AF119151; AAF28848.1; JOINED; Genomic_DNA. DR EMBL; AF119152; AAF28848.1; JOINED; Genomic_DNA. DR EMBL; AF119153; AAF28848.1; JOINED; Genomic_DNA. DR EMBL; AF119154; AAF28848.1; JOINED; Genomic_DNA. DR EMBL; AF119155; AAF28848.1; JOINED; Genomic_DNA. DR EMBL; AF119158; AAF28848.1; JOINED; Genomic_DNA. DR EMBL; AF119159; AAF28848.1; JOINED; Genomic_DNA. DR EMBL; AF119160; AAF28848.1; JOINED; Genomic_DNA. DR EMBL; AF119161; AAF28848.1; JOINED; Genomic_DNA. DR EMBL; AF119162; AAF28849.1; -; Genomic_DNA. DR EMBL; AF119151; AAF28849.1; JOINED; Genomic_DNA. DR EMBL; AF119152; AAF28849.1; JOINED; Genomic_DNA. DR EMBL; AF119153; AAF28849.1; JOINED; Genomic_DNA. DR EMBL; AF119154; AAF28849.1; JOINED; Genomic_DNA. DR EMBL; AF119156; AAF28849.1; JOINED; Genomic_DNA. DR EMBL; AF119158; AAF28849.1; JOINED; Genomic_DNA. DR EMBL; AF119159; AAF28849.1; JOINED; Genomic_DNA. DR EMBL; AF119160; AAF28849.1; JOINED; Genomic_DNA. DR EMBL; AF119161; AAF28849.1; JOINED; Genomic_DNA. DR EMBL; AF119162; AAF28850.1; -; Genomic_DNA. DR EMBL; AF119151; AAF28850.1; JOINED; Genomic_DNA. DR EMBL; AF119152; AAF28850.1; JOINED; Genomic_DNA. DR EMBL; AF119153; AAF28850.1; JOINED; Genomic_DNA. DR EMBL; AF119154; AAF28850.1; JOINED; Genomic_DNA. DR EMBL; AF119155; AAF28850.1; JOINED; Genomic_DNA. DR EMBL; AF119157; AAF28850.1; JOINED; Genomic_DNA. DR EMBL; AF119158; AAF28850.1; JOINED; Genomic_DNA. DR EMBL; AF119159; AAF28850.1; JOINED; Genomic_DNA. DR EMBL; AF119160; AAF28850.1; JOINED; Genomic_DNA. DR EMBL; AF119161; AAF28850.1; JOINED; Genomic_DNA. DR EMBL; AF119162; AAF28851.1; -; Genomic_DNA. DR EMBL; AF119151; AAF28851.1; JOINED; Genomic_DNA. DR EMBL; AF119152; AAF28851.1; JOINED; Genomic_DNA. DR EMBL; AF119153; AAF28851.1; JOINED; Genomic_DNA. DR EMBL; AF119154; AAF28851.1; JOINED; Genomic_DNA. DR EMBL; AF119156; AAF28851.1; JOINED; Genomic_DNA. DR EMBL; AF119157; AAF28851.1; JOINED; Genomic_DNA. DR EMBL; AF119158; AAF28851.1; JOINED; Genomic_DNA. DR EMBL; AF119159; AAF28851.1; JOINED; Genomic_DNA. DR EMBL; AF119160; AAF28851.1; JOINED; Genomic_DNA. DR EMBL; AF119161; AAF28851.1; JOINED; Genomic_DNA. DR EMBL; AF119158; AAF28852.1; -; Genomic_DNA. DR EMBL; AF119151; AAF28852.1; JOINED; Genomic_DNA. DR EMBL; AF119152; AAF28852.1; JOINED; Genomic_DNA. DR EMBL; AF119153; AAF28852.1; JOINED; Genomic_DNA. DR EMBL; AF119154; AAF28852.1; JOINED; Genomic_DNA. DR EMBL; AF119155; AAF28852.1; JOINED; Genomic_DNA. DR EMBL; AF119156; AAF28852.1; JOINED; Genomic_DNA. DR EMBL; AF119157; AAF28853.1; -; Genomic_DNA. DR EMBL; AF119151; AAF28853.1; JOINED; Genomic_DNA. DR EMBL; AF119152; AAF28853.1; JOINED; Genomic_DNA. DR EMBL; AF119153; AAF28853.1; JOINED; Genomic_DNA. DR EMBL; AF119154; AAF28853.1; JOINED; Genomic_DNA. DR EMBL; AF119155; AAF28853.1; JOINED; Genomic_DNA. DR EMBL; AF119156; AAF28853.1; JOINED; Genomic_DNA. DR CCDS; CCDS4217.1; -. [O14511-1] DR PIR; JC5700; JC5700. DR RefSeq; NP_001171864.1; NM_001184935.1. DR RefSeq; NP_004874.1; NM_004883.2. [O14511-1] DR RefSeq; NP_053584.1; NM_013981.3. [O14511-2] DR RefSeq; NP_053585.1; NM_013982.2. [O14511-3] DR RefSeq; NP_053586.1; NM_013983.2. [O14511-4] DR RefSeq; XP_006714873.1; XM_006714810.3. [O14511-6] DR AlphaFoldDB; O14511; -. DR BioGRID; 114917; 5. DR STRING; 9606.ENSP00000354910; -. DR GlyGen; O14511; 5 sites. DR iPTMnet; O14511; -. DR PhosphoSitePlus; O14511; -. DR BioMuta; NRG2; -. DR EPD; O14511; -. DR MassIVE; O14511; -. DR PaxDb; O14511; -. DR PeptideAtlas; O14511; -. DR PRIDE; O14511; -. DR ProteomicsDB; 48047; -. [O14511-1] DR ProteomicsDB; 48048; -. [O14511-2] DR ProteomicsDB; 48049; -. [O14511-3] DR ProteomicsDB; 48050; -. [O14511-4] DR ProteomicsDB; 48051; -. [O14511-5] DR ProteomicsDB; 48052; -. [O14511-6] DR ProteomicsDB; 48053; -. [O14511-7] DR ProteomicsDB; 48054; -. [O14511-8] DR Antibodypedia; 26820; 200 antibodies from 25 providers. DR DNASU; 9542; -. DR Ensembl; ENST00000289409.8; ENSP00000289409.4; ENSG00000158458.21. [O14511-2] DR Ensembl; ENST00000289422.11; ENSP00000289422.7; ENSG00000158458.21. [O14511-3] DR Ensembl; ENST00000340391.8; ENSP00000342660.3; ENSG00000158458.21. [O14511-8] DR Ensembl; ENST00000358522.7; ENSP00000351323.3; ENSG00000158458.21. [O14511-4] DR Ensembl; ENST00000361474.6; ENSP00000354910.1; ENSG00000158458.21. DR Ensembl; ENST00000378238.5; ENSP00000367483.4; ENSG00000158458.21. [O14511-5] DR GeneID; 9542; -. DR KEGG; hsa:9542; -. DR MANE-Select; ENST00000361474.6; ENSP00000354910.1; NM_004883.3; NP_004874.1. DR UCSC; uc003lev.3; human. [O14511-1] DR CTD; 9542; -. DR DisGeNET; 9542; -. DR GeneCards; NRG2; -. DR HGNC; HGNC:7998; NRG2. DR HPA; ENSG00000158458; Low tissue specificity. DR MIM; 603818; gene. DR neXtProt; NX_O14511; -. DR OpenTargets; ENSG00000158458; -. DR PharmGKB; PA31777; -. DR VEuPathDB; HostDB:ENSG00000158458; -. DR eggNOG; ENOG502QRNM; Eukaryota. DR GeneTree; ENSGT00940000158778; -. DR HOGENOM; CLU_023628_0_0_1; -. DR InParanoid; O14511; -. DR OMA; QMADYMS; -. DR OrthoDB; 313400at2759; -. DR PhylomeDB; O14511; -. DR TreeFam; TF332469; -. DR PathwayCommons; O14511; -. DR Reactome; R-HSA-1227986; Signaling by ERBB2. DR Reactome; R-HSA-1236394; Signaling by ERBB4. DR Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling. DR Reactome; R-HSA-1250342; PI3K events in ERBB4 signaling. DR Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling. DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4. DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling. DR Reactome; R-HSA-1306955; GRB7 events in ERBB2 signaling. DR Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling. DR Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling. DR Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling. DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer. DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade. DR Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility. DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-HSA-8847993; ERBB2 Activates PTK6 Signaling. DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling. DR Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants. DR Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants. DR SignaLink; O14511; -. DR SIGNOR; O14511; -. DR BioGRID-ORCS; 9542; 19 hits in 1066 CRISPR screens. DR ChiTaRS; NRG2; human. DR GeneWiki; NRG2; -. DR GenomeRNAi; 9542; -. DR Pharos; O14511; Tbio. DR PRO; PR:O14511; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; O14511; protein. DR Bgee; ENSG00000158458; Expressed in cerebellar vermis and 181 other tissues. DR ExpressionAtlas; O14511; baseline and differential. DR Genevisible; O14511; HS. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW. DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central. DR GO; GO:0048513; P:animal organ development; IBA:GO_Central. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0007399; P:nervous system development; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR040180; Neuregulin. DR InterPro; IPR002154; Neuregulin_C. DR PANTHER; PTHR11100; PTHR11100; 1. DR Pfam; PF07679; I-set; 1. DR Pfam; PF02158; Neuregulin; 1. DR SMART; SM00409; IG; 1. DR SMART; SM00408; IGc2; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Disulfide bond; EGF-like domain; KW Glycoprotein; Growth factor; Immunoglobulin domain; Membrane; KW Reference proteome; Secreted; Transmembrane; Transmembrane helix. FT PROPEP 1..111 FT /evidence="ECO:0000250" FT /id="PRO_0000019472" FT CHAIN 112..850 FT /note="Pro-neuregulin-2, membrane-bound isoform" FT /id="PRO_0000019473" FT CHAIN 112..404 FT /note="Neuregulin-2" FT /id="PRO_0000019474" FT TOPO_DOM 112..405 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 406..426 FT /note="Helical; Note=Internal signal sequence" FT /evidence="ECO:0000255" FT TOPO_DOM 427..850 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 237..332 FT /note="Ig-like C2-type" FT DOMAIN 341..382 FT /note="EGF-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REGION 1..96 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 492..535 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 566..585 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 647..681 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 700..788 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 801..850 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 19..59 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 492..516 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 649..665 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 760..774 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 821..835 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 52 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 53 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 147 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 278 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 346 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 257..311 FT /evidence="ECO:0000250" FT DISULFID 345..359 FT /evidence="ECO:0000250" FT DISULFID 353..370 FT /evidence="ECO:0000250" FT DISULFID 372..381 FT /evidence="ECO:0000250" FT VAR_SEQ 1..241 FT /note="Missing (in isoform DON-1B)" FT /evidence="ECO:0000303|PubMed:9199335" FT /id="VSP_003452" FT VAR_SEQ 1..233 FT /note="MRQVCCSALPPPPLEKGRCSSYSDSSSSSSERSSSSSSSSSESGSSSRSSSN FT NSSISRPAAPPEPRPQQQPQPRSPAARRAAARSRAAAAGGMRRDPAPGFSMLLFGVSLA FT CYSPSLKSVQDQAYKAPVVVEGKVQGLVPAGGSSSNSTREPPASGRVALVKVLDKWPLR FT SGGLQREQVISVGSCVPLERNQRYIFFLEPTEQPLVFKTAFAPLDTNGKNLKKEVGKIL FT CTDC -> MSESRRRGRGRGKKHPEGRKREREPDPGEK (in isoform DON-1R)" FT /evidence="ECO:0000303|PubMed:9199335" FT /id="VSP_003451" FT VAR_SEQ 374..397 FT /note="NGFFGQRCLEKLPLRLYMPDPKQK -> VGYTGDRCQQFAMVNFSKHLGFEL FT KE (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_003454" FT VAR_SEQ 374..396 FT /note="NGFFGQRCLEKLPLRLYMPDPKQ -> VGYTGDRCQQFAMVNFS (in FT isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_003453" FT VAR_SEQ 397..426 FT /note="KAEELYQKRVLTITGICVALLVVGIVCVVA -> SVLWDTPGTGVSSSQWST FT SPKPRSCTRRGS (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_003458" FT VAR_SEQ 397..422 FT /note="KAEELYQKRVLTITGICVALLVVGIV -> SVLWDTPGTGVSSSQWSTSPST FT LDLN (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_003456" FT VAR_SEQ 397 FT /note="K -> KHLGFELKE (in isoform 3 and isoform DON-1B)" FT /evidence="ECO:0000303|PubMed:9199335" FT /id="VSP_003455" FT VAR_SEQ 423..850 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_003457" FT VAR_SEQ 427..850 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_003459" SQ SEQUENCE 850 AA; 91679 MW; 7124C089435FD2F4 CRC64; MRQVCCSALP PPPLEKGRCS SYSDSSSSSS ERSSSSSSSS SESGSSSRSS SNNSSISRPA APPEPRPQQQ PQPRSPAARR AAARSRAAAA GGMRRDPAPG FSMLLFGVSL ACYSPSLKSV QDQAYKAPVV VEGKVQGLVP AGGSSSNSTR EPPASGRVAL VKVLDKWPLR SGGLQREQVI SVGSCVPLER NQRYIFFLEP TEQPLVFKTA FAPLDTNGKN LKKEVGKILC TDCATRPKLK KMKSQTGQVG EKQSLKCEAA AGNPQPSYRW FKDGKELNRS RDIRIKYGNG RKNSRLQFNK VKVEDAGEYV CEAENILGKD TVRGRLYVNS VSTTLSSWSG HARKCNETAK SYCVNGGVCY YIEGINQLSC KCPNGFFGQR CLEKLPLRLY MPDPKQKAEE LYQKRVLTIT GICVALLVVG IVCVVAYCKT KKQRKQMHNH LRQNMCPAHQ NRSLANGPSH PRLDPEEIQM ADYISKNVPA TDHVIRRETE TTFSGSHSCS PSHHCSTATP TSSHRHESHT WSLERSESLT SDSQSGIMLS SVGTSKCNSP ACVEARARRA AAYNLEERRR ATAPPYHDSV DSLRDSPHSE RYVSALTTPA RLSPVDFHYS LATQVPTFEI TSPNSAHAVS LPPAAPISYR LAEQQPLLRH PAPPGPGPGP GPGPGPGADM QRSYDSYYYP AAGPGPRRGT CALGGSLGSL PASPFRIPED DEYETTQECA PPPPPRPRAR GASRRTSAGP RRWRRSRLNG LAAQRARAAR DSLSLSSGSG GGSASASDDD ADDADGALAA ESTPFLGLRG AHDALRSDSP PLCPAADSRT YYSLDSHSTR ASSRHSRGPP PRAKQDSAPL //