5HT3B_HUMAN
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 03-AUG-2022, entry version 168.
DE RecName: Full=5-hydroxytryptamine receptor 3B;
DE Short=5-HT3-B;
DE Short=5-HT3B;
DE AltName: Full=Serotonin receptor 3B;
DE Flags: Precursor;
GN Name=HTR3B;
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), AND 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), TISSUE SPECIFICITY, AND SUBUNIT.
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, 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 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, GLYCOSYLATION AT ASN-52; ASN-96; ASN-138; ASN-168 AND
RP ASN-203, AND MUTAGENESIS OF ASN-52; ASN-96; ASN-138; ASN-168 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: This is one of the several different receptors for 5-
CC hydroxytryptamine (serotonin), a biogenic hormone that functions as a
CC neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-
CC gated ion channel, which when activated causes fast, depolarizing
CC responses. It is a cation-specific, but otherwise relatively
CC nonselective, ion channel. {ECO:0000269|PubMed:12867984}.
CC -!- SUBUNIT: Forms a pentaheteromeric complex with HTR3A. Not functional as
CC a homomeric complex. {ECO:0000269|PubMed:17392525,
CC ECO:0000269|PubMed:9950429}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21138434};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21138434}.
CC Note=Presumably retained within the endoplasmic reticulum unless
CC complexed with HTR3A.
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 -!- PTM: N-glycosylation required for membrane localization.
CC {ECO:0000269|PubMed:21138434}.
CC -!- MISCELLANEOUS: The HA-stretch region of HTR3B seems to confer increased
CC conductance to HTR3A/HTR3B heteromers compared to that of HTR3A
CC homomers.
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}.
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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 GlyGen; O95264; 6 sites.
DR iPTMnet; O95264; -.
DR PhosphoSitePlus; O95264; -.
DR BioMuta; HTR3B; -.
DR MassIVE; O95264; -.
DR PaxDb; O95264; -.
DR PeptideAtlas; O95264; -.
DR PRIDE; O95264; -.
DR TopDownProteomics; O95264-1; -. [O95264-1]
DR Antibodypedia; 18362; 180 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 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; FRSYLFM; -.
DR OrthoDB; 611108at2759; -.
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; 11 hits in 1071 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 tissues.
DR ExpressionAtlas; O95264; baseline and differential.
DR Genevisible; O95264; HS.
DR GO; GO:0009986; C:cell surface; IDA:CACAO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:InterPro.
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:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0022850; F:serotonin-gated cation-selective channel activity; IGI:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; IDA:ComplexPortal.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 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 PANTHER; PTHR18945; PTHR18945; 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; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane; Receptor;
KW Reference proteome; Signal; 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:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..286
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..441
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 381..413
FT /note="HA-stretch"
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"
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
