ID 5HT3B_HUMAN Reviewed; 441 AA. AC O95264; B0YJ23; Q0VJC3; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 177. DE RecName: Full=5-hydroxytryptamine receptor 3B {ECO:0000305|PubMed:10521471}; DE Short=5-HT3-B; DE Short=5-HT3B; DE AltName: Full=Serotonin receptor 3B; DE Flags: Precursor; GN Name=HTR3B {ECO:0000312|HGNC:HGNC:5298}; 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), FUNCTION, TRANSPORTER ACTIVITY, AND RP TISSUE SPECIFICITY. RC TISSUE=Small intestine; RX PubMed=10521471; DOI=10.1074/jbc.274.43.30799; RA Dubin A.E., Huvar R., D'Andrea M.R., Pyati J., Zhu J.Y., Joy K.C., RA Wilson S.J., Galindo J.E., Glass C.A., Luo L., Jackson M.R., RA Lovenberg T.W., Erlander M.G.; RT "The pharmacological and functional characteristics of the serotonin 5- RT HT(3A) receptor are specifically modified by a 5-HT(3B) receptor subunit."; RL J. Biol. Chem. 274:30799-30810(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=9950429; DOI=10.1038/16941; RA Davies P.A., Pistis M., Hanna M.C., Peters J.A., Lambert J.J., Hales T.G., RA Kirkness E.F.; RT "The 5-HT3B subunit is a major determinant of serotonin-receptor RT function."; RL Nature 397:359-363(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT SER-129. RC TISSUE=Brain; RX PubMed=17010535; DOI=10.1016/j.gene.2006.08.002; RA Tzvetkov M.V., Meineke C., Oetjen E., Hirsch-Ernst K., Brockmoller J.; RT "Tissue-specific alternative promoters of the serotonin receptor gene HTR3B RT in human brain and intestine."; RL Gene 386:52-62(2007). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP FUNCTION, DOMAIN, AND REGION. RX PubMed=12867984; DOI=10.1038/nature01788; RA Kelley S.P., Dunlop J.I., Kirkness E.F., Lambert J.J., Peters J.A.; RT "A cytoplasmic region determines single-channel conductance in 5-HT3 RT receptors."; RL Nature 424:321-324(2003). RN [7] RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBUNIT. RX PubMed=17392525; DOI=10.1124/mol.106.032144; RA Niesler B., Walstab J., Combrink S., Moeller D., Kapeller J., Rietdorf J., RA Boenisch H., Goethert M., Rappold G., Bruess M.; RT "Characterization of the novel human serotonin receptor subunits 5-HT3C, 5- RT HT3D, and 5-HT3E."; RL Mol. Pharmacol. 72:8-17(2007). RN [8] RP SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-52; ASN-96; ASN-138; RP ASN-168 AND ASN-203, AND MUTAGENESIS OF ASN-52; ASN-96; ASN-138; ASN-168 RP AND ASN-203. RX PubMed=21138434; DOI=10.1111/j.1471-4159.2010.07129.x; RA Massoura A.N., Dover T.J., Newman A.S., Barnes N.M.; RT "The identification of N-glycosylated residues of the human 5-HT3B receptor RT subunit: importance for cell membrane expression."; RL J. Neurochem. 116:975-983(2011). RN [9] RP VARIANTS SER-129; ARG-156 AND ILE-183. RX PubMed=15389765; DOI=10.1002/ajmg.b.30070; RA Frank B., Niesler B., Noethen M.M., Neidt H., Propping P., Bondy B., RA Rietschel M., Maier W., Albus M., Rappold G.; RT "Investigation of the human serotonin receptor gene HTR3B in bipolar RT affective and schizophrenic patients."; RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 131:1-5(2004). RN [10] RP VARIANTS SER-129; ARG-156 AND ILE-183. RX PubMed=15293096; DOI=10.1007/s10067-004-0927-2; RA Frank B., Niesler B., Bondy B., Spaeth M., Pongratz D.E., Ackenheil M., RA Fischer C., Rappold G.; RT "Mutational analysis of serotonin receptor genes: HTR3A and HTR3B in RT fibromyalgia patients."; RL Clin. Rheumatol. 23:338-344(2004). RN [11] RP VARIANTS SER-129; THR-143 AND ILE-183. RX PubMed=16487942; DOI=10.1016/j.biopsych.2005.11.008; RA Yamada K., Hattori E., Iwayama Y., Ohnishi T., Ohba H., Toyota T., RA Takao H., Minabe Y., Nakatani N., Higuchi T., Detera-Wadleigh S.D., RA Yoshikawa T.; RT "Distinguishable haplotype blocks in the HTR3A and HTR3B region in the RT Japanese reveal evidence of association of HTR3B with female major RT depression."; RL Biol. Psychiatry 60:192-201(2006). RN [12] RP VARIANT ARG-156. RX PubMed=21179162; DOI=10.1038/nature09629; RA Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T., RA Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., Hodgkinson C.A., RA Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., Peltonen L., RA Virkkunen M., Goldman D.; RT "A population-specific HTR2B stop codon predisposes to severe RT impulsivity."; RL Nature 468:1061-1066(2010). CC -!- FUNCTION: Forms serotonin (5-hydroxytryptamine/5-HT3)-activated cation- CC selective channel complexes, which when activated cause fast, CC depolarizing responses in neurons. {ECO:0000269|PubMed:10521471, CC ECO:0000269|PubMed:12867984, ECO:0000269|PubMed:17392525, CC ECO:0000269|PubMed:9950429}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, CC ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:9950429}; CC -!- CATALYTIC ACTIVITY: CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; CC Evidence={ECO:0000269|PubMed:9950429}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, CC ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10521471, CC ECO:0000269|PubMed:17392525, ECO:0000269|PubMed:9950429}; CC -!- SUBUNIT: Forms homopentameric as well as heteropentameric serotonin- CC activated cation-selective channel complexes with HTR3A. The homomeric CC complex is not functional. Heteropentameric complexes display CC properties which resemble that of neuronal serotonin-activated channels CC in vivo. {ECO:0000269|PubMed:17392525, ECO:0000269|PubMed:9950429}. CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane CC {ECO:0000305|PubMed:9950429}; Multi-pass membrane protein CC {ECO:0000269|PubMed:21138434}. Cell membrane CC {ECO:0000269|PubMed:21138434}; Multi-pass membrane protein CC {ECO:0000269|PubMed:21138434}. Note=Presumably retained within the CC endoplasmic reticulum unless complexed with HTR3A. CC {ECO:0000269|PubMed:21138434}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O95264-1; Sequence=Displayed; CC Name=2; CC IsoId=O95264-2; Sequence=VSP_029796; CC -!- TISSUE SPECIFICITY: Expressed in the brain cortex, in the caudate CC nucleus, the hippocampus, the thalamus and the amygdala. Detected in CC the kidney and testis as well as in monocytes of the spleen, small and CC large intestine, uterus, prostate, ovary and placenta. CC {ECO:0000269|PubMed:10521471, ECO:0000269|PubMed:9950429}. CC -!- DOMAIN: The HA-stretch region of HTR3B seems to confer increased CC conductance to HTR3A/HTR3B heteromers compared to that of HTR3A CC homomers. {ECO:0000269|PubMed:12867984}. CC -!- PTM: N-glycosylation required for membrane localization. CC {ECO:0000269|PubMed:21138434}. CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. CC 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily. HTR3B sub- CC subfamily. {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; AF169255; AAF03691.1; -; mRNA. DR EMBL; AF080582; AAD12242.1; -; mRNA. DR EMBL; AM293589; CAL25321.1; -; mRNA. DR EMBL; EF444985; ACA06001.1; -; Genomic_DNA. DR EMBL; AK314268; BAG36930.1; -; mRNA. DR CCDS; CCDS8364.1; -. [O95264-1] DR CCDS; CCDS86249.1; -. [O95264-2] DR RefSeq; NP_006019.1; NM_006028.4. [O95264-1] DR RefSeq; XP_011541365.1; XM_011543063.1. DR AlphaFoldDB; O95264; -. DR SMR; O95264; -. DR BioGRID; 114615; 54. DR ComplexPortal; CPX-271; 5-hydroxytryptamine-3A/B receptor complex. DR IntAct; O95264; 1. DR STRING; 9606.ENSP00000260191; -. DR BindingDB; O95264; -. DR ChEMBL; CHEMBL3895; -. DR DrugBank; DB01239; Chlorprothixene. DR DrugBank; DB11273; Dihydroergocornine. DR DrugBank; DB13345; Dihydroergocristine. DR DrugBank; DB00988; Dopamine. DR DrugBank; DB01049; Ergoloid mesylate. DR DrugBank; DB00898; Ethanol. DR DrugBank; DB12141; Gilteritinib. DR DrugBank; DB00715; Paroxetine. DR DrugBank; DB08839; Serotonin. DR DrugBank; DB09304; Setiptiline. DR DrugBank; DB13025; Tiapride. DR DrugBank; DB00246; Ziprasidone. DR DrugCentral; O95264; -. DR GuidetoPHARMACOLOGY; 374; -. DR TCDB; 1.A.9.2.5; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family. DR GlyCosmos; O95264; 6 sites, No reported glycans. DR GlyGen; O95264; 6 sites. DR iPTMnet; O95264; -. DR PhosphoSitePlus; O95264; -. DR BioMuta; HTR3B; -. DR MassIVE; O95264; -. DR PaxDb; 9606-ENSP00000260191; -. DR PeptideAtlas; O95264; -. DR TopDownProteomics; O95264-1; -. [O95264-1] DR Antibodypedia; 18362; 220 antibodies from 30 providers. DR DNASU; 9177; -. DR Ensembl; ENST00000260191.8; ENSP00000260191.2; ENSG00000149305.8. [O95264-1] DR Ensembl; ENST00000537778.5; ENSP00000443118.1; ENSG00000149305.8. [O95264-2] DR GeneID; 9177; -. DR KEGG; hsa:9177; -. DR MANE-Select; ENST00000260191.8; ENSP00000260191.2; NM_006028.5; NP_006019.1. DR UCSC; uc001pok.4; human. [O95264-1] DR AGR; HGNC:5298; -. DR CTD; 9177; -. DR DisGeNET; 9177; -. DR GeneCards; HTR3B; -. DR HGNC; HGNC:5298; HTR3B. DR HPA; ENSG00000149305; Tissue enhanced (brain). DR MIM; 604654; gene. DR neXtProt; NX_O95264; -. DR OpenTargets; ENSG00000149305; -. DR PharmGKB; PA29556; -. DR VEuPathDB; HostDB:ENSG00000149305; -. DR eggNOG; KOG3645; Eukaryota. DR GeneTree; ENSGT00940000158478; -. DR HOGENOM; CLU_018074_5_0_1; -. DR InParanoid; O95264; -. DR OMA; NMANEVP; -. DR OrthoDB; 5489962at2759; -. DR PhylomeDB; O95264; -. DR TreeFam; TF315605; -. DR PathwayCommons; O95264; -. DR Reactome; R-HSA-112314; Neurotransmitter receptors and postsynaptic signal transmission. DR SignaLink; O95264; -. DR SIGNOR; O95264; -. DR BioGRID-ORCS; 9177; 14 hits in 1151 CRISPR screens. DR GeneWiki; HTR3B; -. DR GenomeRNAi; 9177; -. DR Pharos; O95264; Tchem. DR PRO; PR:O95264; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; O95264; Protein. DR Bgee; ENSG00000149305; Expressed in prefrontal cortex and 45 other cell types or tissues. DR ExpressionAtlas; O95264; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:CACAO. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:1904602; C:serotonin-activated cation-selective channel complex; IGI:GO_Central. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IBA:GO_Central. DR GO; GO:0022850; F:serotonin-gated monoatomic cation channel activity; IDA:UniProtKB. DR GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:ComplexPortal. DR GO; GO:0007210; P:serotonin receptor signaling pathway; IDA:ComplexPortal. DR CDD; cd19012; LGIC_ECD_5-HT3B; 1. DR CDD; cd19063; LGIC_TM_5-HT3; 1. DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1. DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1. DR InterPro; IPR008132; 5HT3_rcpt. DR InterPro; IPR008134; 5HT3_rcpt_B. DR InterPro; IPR006202; Neur_chan_lig-bd. DR InterPro; IPR036734; Neur_chan_lig-bd_sf. DR InterPro; IPR006201; Neur_channel. DR InterPro; IPR036719; Neuro-gated_channel_TM_sf. DR InterPro; IPR038050; Neuro_actylchol_rec. DR InterPro; IPR006029; Neurotrans-gated_channel_TM. DR NCBIfam; TIGR00860; LIC; 1. DR PANTHER; PTHR18945:SF53; 5-HYDROXYTRYPTAMINE RECEPTOR 3B; 1. DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR01710; 5HT3BRECEPTR. DR PRINTS; PR01708; 5HT3RECEPTOR. DR PRINTS; PR00252; NRIONCHANNEL. DR SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1. DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1. DR Genevisible; O95264; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein; KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane; KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse; KW Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..441 FT /note="5-hydroxytryptamine receptor 3B" FT /id="PRO_0000312289" FT TOPO_DOM 22..238 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:21138434" FT TRANSMEM 239..259 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 260..268 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:21138434" FT TRANSMEM 269..286 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 287..303 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:21138434" FT TRANSMEM 304..324 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 325..414 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:21138434" FT TRANSMEM 415..435 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 436..441 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:21138434" FT REGION 381..413 FT /note="HA-stretch; determines single-channel conductance in FT 5-HT3 receptors" FT /evidence="ECO:0000269|PubMed:12867984" FT CARBOHYD 52 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21138434" FT CARBOHYD 96 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21138434" FT CARBOHYD 138 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21138434" FT CARBOHYD 168 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21138434" FT CARBOHYD 203 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21138434" FT CARBOHYD 287 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 155..169 FT /evidence="ECO:0000250|UniProtKB:P23979" FT VAR_SEQ 1..17 FT /note="MLSSVMAPLWACILVAA -> MIVYFP (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17010535" FT /id="VSP_029796" FT VARIANT 129 FT /note="Y -> S (in dbSNP:rs1176744)" FT /evidence="ECO:0000269|PubMed:15293096, FT ECO:0000269|PubMed:15389765, ECO:0000269|PubMed:16487942, FT ECO:0000269|PubMed:17010535" FT /id="VAR_037472" FT VARIANT 143 FT /note="I -> T (in dbSNP:rs34550504)" FT /evidence="ECO:0000269|PubMed:16487942" FT /id="VAR_037473" FT VARIANT 156 FT /note="S -> R (in dbSNP:rs72466469)" FT /evidence="ECO:0000269|PubMed:15293096, FT ECO:0000269|PubMed:15389765, ECO:0000269|PubMed:21179162" FT /id="VAR_037474" FT VARIANT 183 FT /note="V -> I (in dbSNP:rs17116138)" FT /evidence="ECO:0000269|PubMed:15293096, FT ECO:0000269|PubMed:15389765, ECO:0000269|PubMed:16487942" FT /id="VAR_037475" FT MUTAGEN 52 FT /note="N->S: Reduced molecular weight. Very little FT expression in the cell membrane." FT /evidence="ECO:0000269|PubMed:21138434" FT MUTAGEN 96 FT /note="N->S: Reduced molecular weight. Very little FT expression in the cell membrane." FT /evidence="ECO:0000269|PubMed:21138434" FT MUTAGEN 138 FT /note="N->S: Reduced molecular weight. Very little FT expression in the cell membrane." FT /evidence="ECO:0000269|PubMed:21138434" FT MUTAGEN 168 FT /note="N->S: Reduced molecular weight and cell membrane FT expression." FT /evidence="ECO:0000269|PubMed:21138434" FT MUTAGEN 203 FT /note="N->S: Reduced molecular weight. Very little FT expression in the cell membrane." FT /evidence="ECO:0000269|PubMed:21138434" SQ SEQUENCE 441 AA; 50292 MW; 2ED59E4E11400648 CRC64; MLSSVMAPLW ACILVAAGIL ATDTHHPQDS ALYHLSKQLL QKYHKEVRPV YNWTKATTVY LDLFVHAILD VDAENQILKT SVWYQEVWND EFLSWNSSMF DEIREISLPL SAIWAPDIII NEFVDIERYP DLPYVYVNSS GTIENYKPIQ VVSACSLETY AFPFDVQNCS LTFKSILHTV EDVDLAFLRS PEDIQHDKKA FLNDSEWELL SVSSTYSILQ SSAGGFAQIQ FNVVMRRHPL VYVVSLLIPS IFLMLVDLGS FYLPPNCRAR IVFKTSVLVG YTVFRVNMSN QVPRSVGSTP LIGHFFTICM AFLVLSLAKS IVLVKFLHDE QRGGQEQPFL CLRGDTDADR PRVEPRAQRA VVTESSLYGE HLAQPGTLKE VWSQLQSISN YLQTQDQTDQ QEAEWLVLLS RFDRLLFQSY LFMLGIYTIT LCSLWALWGG V //