5HT2B_HUMAN
ID 5HT2B_HUMAN Reviewed; 481 AA.
AC P41595; B2R9D5; Q53TI1; Q62221; Q6P523;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=5-hydroxytryptamine receptor 2B;
DE Short=5-HT-2B;
DE Short=5-HT2B;
DE AltName: Full=Serotonin receptor 2B;
GN Name=HTR2B;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8143856; DOI=10.1016/0014-5793(94)80590-3;
RA Schmuck K., Ullmer C., Engels P., Luebbert H.;
RT "Cloning and functional characterization of the human 5-HT2B serotonin
RT receptor.";
RL FEBS Lett. 342:85-90(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7926008; DOI=10.1016/0014-5793(94)00968-6;
RA Choi D.S., Birraux G., Launay J.-M., Maroteaux L.;
RT "The human serotonin 5-HT2B receptor: pharmacological link between 5-HT2
RT and 5-HT1D receptors.";
RL FEBS Lett. 352:393-399(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Uterus;
RX PubMed=8078486;
RA Kursar J.D., Nelson D.L., Wainscott D.B., Baez M.;
RT "Molecular cloning, functional expression, and mRNA tissue distribution of
RT the human 5-hydroxytryptamine2B receptor.";
RL Mol. Pharmacol. 46:227-234(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10722792; DOI=10.1006/mcpr.1999.0281;
RA Kim S.J., Veenstra-VanderWeele J., Hanna G.L., Gonen D., Leventhal B.L.,
RA Cook E.H. Jr.;
RT "Mutation screening of human 5-HT(2B) receptor gene in early-onset
RT obsessive-compulsive disorder.";
RL Mol. Cell. Probes 14:47-52(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8882600; DOI=10.1111/j.1476-5381.1996.tb16700.x;
RA Ullmer C., Boddeke H.G., Schmuck K., Lubbert H.;
RT "5-HT2B receptor-mediated calcium release from ryanodine-sensitive
RT intracellular stores in human pulmonary artery endothelial cells.";
RL Br. J. Pharmacol. 117:1081-1088(1996).
RN [11]
RP INTERACTION WITH MPDZ.
RX PubMed=11150294; DOI=10.1074/jbc.m008089200;
RA Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J.,
RA Luebbert H., Ullmer C.;
RT "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with PDZ10
RT of the multi-PDZ domain protein MUPP1.";
RL J. Biol. Chem. 276:12974-12982(2001).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12970106; DOI=10.1038/sj.bjp.0705437;
RA Schaerlinger B., Hickel P., Etienne N., Guesnier L., Maroteaux L.;
RT "Agonist actions of dihydroergotamine at 5-HT2B and 5-HT2C receptors and
RT their possible relevance to antimigraine efficacy.";
RL Br. J. Pharmacol. 140:277-284(2003).
RN [13]
RP REVIEW.
RX PubMed=18476671; DOI=10.1021/cr078224o;
RA Nichols D.E., Nichols C.D.;
RT "Serotonin receptors.";
RL Chem. Rev. 108:1614-1641(2008).
RN [14]
RP FUNCTION.
RX PubMed=18703043; DOI=10.1016/j.ejphar.2008.07.040;
RA Cussac D., Boutet-Robinet E., Ailhaud M.C., Newman-Tancredi A.,
RA Martel J.C., Danty N., Rauly-Lestienne I.;
RT "Agonist-directed trafficking of signalling at serotonin 5-HT2A, 5-HT2B and
RT 5-HT2C-VSV receptors mediated Gq/11 activation and calcium mobilisation in
RT CHO cells.";
RL Eur. J. Pharmacol. 594:32-38(2008).
RN [15]
RP FUNCTION, INVOLVEMENT IN IMPULSIVE BEHAVIOR, TISSUE SPECIFICITY,
RP POLYMORPHISM, AND VARIANTS GLU-45; LEU-173 AND TRP-388.
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).
RN [16]
RP REVIEW.
RX PubMed=20945968; DOI=10.33549/physiolres.931903;
RA Pytliak M., Vargova V., Mechirova V., Felsoci M.;
RT "Serotonin receptors - from molecular biology to clinical applications.";
RL Physiol. Res. 60:15-25(2011).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-132; ASP-135;
RP VAL-136; SER-139; THR-140; VAL-208; LEU-209; LYS-211; PHE-217; MET-218;
RP ALA-225; TRP-337; PHE-340; ASN-344; LEU-347; VAL-348; LEU-362; GLU-363;
RP VAL-366 AND TYR-370.
RX PubMed=23519210; DOI=10.1126/science.1232807;
RA Wang C., Jiang Y., Ma J., Wu H., Wacker D., Katritch V., Han G.W., Liu W.,
RA Huang X.P., Vardy E., McCorvy J.D., Gao X., Zhou X.E., Melcher K.,
RA Zhang C., Bai F., Yang H., Yang L., Jiang H., Roth B.L., Cherezov V.,
RA Stevens R.C., Xu H.E.;
RT "Structural basis for molecular recognition at serotonin receptors.";
RL Science 340:610-614(2013).
RN [18] {ECO:0007744|PDB:4IB4}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 36-248 AND 314-405 IN COMPLEX WITH
RP THE AGONIST ERGOTAMINE, FUNCTION, ROLE IN ARRESTIN-MEDIATED SIGNALING AND
RP CALCIUM RELEASE, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, AND DISULFIDE
RP BONDS.
RX PubMed=23519215; DOI=10.1126/science.1232808;
RA Wacker D., Wang C., Katritch V., Han G.W., Huang X.P., Vardy E.,
RA McCorvy J.D., Jiang Y., Chu M., Siu F.Y., Liu W., Xu H.E., Cherezov V.,
RA Roth B.L., Stevens R.C.;
RT "Structural features for functional selectivity at serotonin receptors.";
RL Science 340:615-619(2013).
RN [19] {ECO:0007744|PDB:4NC3}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 36-248 AND 314-405 IN COMPLEX
RP WITH ERGOTAMINE, FUNCTION, DISULFIDE BONDS, AND TOPOLOGY.
RX PubMed=24357322; DOI=10.1126/science.1244142;
RA Liu W., Wacker D., Gati C., Han G.W., James D., Wang D., Nelson G.,
RA Weierstall U., Katritch V., Barty A., Zatsepin N.A., Li D.,
RA Messerschmidt M., Boutet S., Williams G.J., Koglin J.E., Seibert M.M.,
RA Wang C., Shah S.T., Basu S., Fromme R., Kupitz C., Rendek K.N.,
RA Grotjohann I., Fromme P., Kirian R.A., Beyerlein K.R., White T.A.,
RA Chapman H.N., Caffrey M., Spence J.C., Stevens R.C., Cherezov V.;
RT "Serial femtosecond crystallography of G protein-coupled receptors.";
RL Science 342:1521-1524(2013).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 41-248 AND 314-400 IN COMPLEX
RP WITH LYSERGIC ACID DIETHYLAMIDE, FUNCTION, DISULFIDE BONDS, SUBCELLULAR
RP LOCATION, TOPOLOGY, AND MUTAGENESIS OF LEU-209.
RX PubMed=28129538; DOI=10.1016/j.cell.2016.12.033;
RA Wacker D., Wang S., McCorvy J.D., Betz R.M., Venkatakrishnan A.J.,
RA Levit A., Lansu K., Schools Z.L., Che T., Nichols D.E., Shoichet B.K.,
RA Dror R.O., Roth B.L.;
RT "Crystal structure of an LSD-bound human serotonin receptor.";
RL Cell 168:377-389(2017).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin) (PubMed:8143856, PubMed:7926008, PubMed:8078486,
CC PubMed:8882600, PubMed:18703043, PubMed:23519210). Also functions as a
CC receptor for various ergot alkaloid derivatives and psychoactive
CC substances (PubMed:8143856, PubMed:7926008, PubMed:8078486,
CC PubMed:12970106, PubMed:18703043, PubMed:23519210, PubMed:23519215,
CC PubMed:24357322, PubMed:28129538). Ligand binding causes a conformation
CC change that triggers signaling via guanine nucleotide-binding proteins
CC (G proteins) and modulates the activity of down-stream effectors
CC (PubMed:8143856, PubMed:8078486, PubMed:8882600, PubMed:23519215,
CC PubMed:28129538). Beta-arrestin family members inhibit signaling via G
CC proteins and mediate activation of alternative signaling pathways
CC (PubMed:23519215, PubMed:28129538). Signaling activates a
CC phosphatidylinositol-calcium second messenger system that modulates the
CC activity of phosphatidylinositol 3-kinase and down-stream signaling
CC cascades and promotes the release of Ca(2+) ions from intracellular
CC stores (PubMed:8143856, PubMed:8078486, PubMed:8882600,
CC PubMed:18703043, PubMed:23519215, PubMed:28129538). Plays a role in the
CC regulation of dopamine and 5-hydroxytryptamine release, 5-
CC hydroxytryptamine uptake and in the regulation of extracellular
CC dopamine and 5-hydroxytryptamine levels, and thereby affects neural
CC activity. May play a role in the perception of pain (By similarity).
CC Plays a role in the regulation of behavior, including impulsive
CC behavior (PubMed:21179162). Required for normal proliferation of
CC embryonic cardiac myocytes and normal heart development. Protects
CC cardiomyocytes against apoptosis. Plays a role in the adaptation of
CC pulmonary arteries to chronic hypoxia. Plays a role in
CC vasoconstriction. Required for normal osteoblast function and
CC proliferation, and for maintaining normal bone density. Required for
CC normal proliferation of the interstitial cells of Cajal in the
CC intestine (By similarity). {ECO:0000250|UniProtKB:P30994,
CC ECO:0000250|UniProtKB:Q02152, ECO:0000269|PubMed:12970106,
CC ECO:0000269|PubMed:18703043, ECO:0000269|PubMed:21179162,
CC ECO:0000269|PubMed:23519210, ECO:0000269|PubMed:23519215,
CC ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538,
CC ECO:0000269|PubMed:7926008, ECO:0000269|PubMed:8078486,
CC ECO:0000269|PubMed:8143856, ECO:0000269|PubMed:8882600}.
CC -!- SUBUNIT: Interacts (via C-terminus) with MPDZ.
CC {ECO:0000269|PubMed:11150294}.
CC -!- INTERACTION:
CC P41595; P28223: HTR2A; NbExp=3; IntAct=EBI-7474947, EBI-6656333;
CC P41595; P28335: HTR2C; NbExp=4; IntAct=EBI-7474947, EBI-994141;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12970106,
CC ECO:0000269|PubMed:23519210, ECO:0000269|PubMed:23519215,
CC ECO:0000269|PubMed:28129538, ECO:0000269|PubMed:7926008,
CC ECO:0000269|PubMed:8078486, ECO:0000269|PubMed:8143856}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:23519215,
CC ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538}. Synapse,
CC synaptosome {ECO:0000250|UniProtKB:Q02152}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in liver, kidney, heart,
CC pulmonary artery, and intestine. Detected at lower levels in blood,
CC placenta and brain, especially in cerebellum, occipital cortex and
CC frontal cortex. {ECO:0000269|PubMed:21179162,
CC ECO:0000269|PubMed:7926008, ECO:0000269|PubMed:8078486,
CC ECO:0000269|PubMed:8143856, ECO:0000269|PubMed:8882600}.
CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
CC transmembrane helices. {ECO:0000269|PubMed:23519215,
CC ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538}.
CC -!- POLYMORPHISM: A variation at a single nucleotide base, which results in
CC an erroneous stop codon and affects Gln-20, triggers non-sense mediated
CC RNA decay, such that no HTR2B-receptor protein is expressed. It is
CC associated with impulsive behavior and co-segregates with disorders
CC characterized by impulsivity. However, the presence of this variant is
CC not in itself sufficient to cause impulsive behavior: male sex,
CC testosterone level, alcohol and stress exposure are other factors
CC playing important roles. {ECO:0000269|PubMed:21179162}.
CC -!- MISCELLANEOUS: Binds lysergic acid diethylamine (LSD) in the
CC orthosteric pocket, but is not the principal LSD receptor in the brain.
CC Bound LSD dissociates extremely slowly, with a residence time of about
CC 46 minutes at 37 degrees Celsius. {ECO:0000269|PubMed:28129538}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On the spur of a whim
CC - Issue 127 of March 2011;
CC URL="https://web.expasy.org/spotlight/back_issues/127";
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DR EMBL; X77307; CAA54513.1; -; mRNA.
DR EMBL; Z36748; CAA85319.1; -; mRNA.
DR EMBL; AF156160; AAD39259.1; -; Genomic_DNA.
DR EMBL; AF156158; AAD39259.1; JOINED; Genomic_DNA.
DR EMBL; AF156159; AAD39259.1; JOINED; Genomic_DNA.
DR EMBL; AY136751; AAN01277.1; -; mRNA.
DR EMBL; AC009407; AAX93128.1; -; Genomic_DNA.
DR EMBL; AK313741; BAG36482.1; -; mRNA.
DR EMBL; CH471063; EAW70949.1; -; Genomic_DNA.
DR EMBL; BC063123; AAH63123.1; -; mRNA.
DR CCDS; CCDS2483.1; -.
DR PIR; S43687; S43687.
DR PIR; S49442; S49442.
DR RefSeq; NP_000858.3; NM_000867.4.
DR RefSeq; NP_001307687.1; NM_001320758.1.
DR PDB; 4IB4; X-ray; 2.70 A; A=36-248, A=314-405.
DR PDB; 4NC3; X-ray; 2.80 A; A=36-248, A=314-405.
DR PDB; 5TUD; X-ray; 3.00 A; A/D=36-248, A/D=314-405.
DR PDB; 5TVN; X-ray; 2.90 A; A=41-248, A=313-400.
DR PDB; 6DRX; X-ray; 3.10 A; A=36-248, A=314-404.
DR PDB; 6DRY; X-ray; 2.92 A; A=36-248, A=313-404.
DR PDB; 6DRZ; X-ray; 3.10 A; A=36-248, A=313-404.
DR PDB; 6DS0; X-ray; 3.19 A; A=36-248, A=314-404.
DR PDBsum; 4IB4; -.
DR PDBsum; 4NC3; -.
DR PDBsum; 5TUD; -.
DR PDBsum; 5TVN; -.
DR PDBsum; 6DRX; -.
DR PDBsum; 6DRY; -.
DR PDBsum; 6DRZ; -.
DR PDBsum; 6DS0; -.
DR AlphaFoldDB; P41595; -.
DR SMR; P41595; -.
DR BioGRID; 109589; 27.
DR IntAct; P41595; 28.
DR MINT; P41595; -.
DR STRING; 9606.ENSP00000258400; -.
DR BindingDB; P41595; -.
DR ChEMBL; CHEMBL1833; -.
DR DrugBank; DB00543; Amoxapine.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB06216; Asenapine.
DR DrugBank; DB01200; Bromocriptine.
DR DrugBank; DB00248; Cabergoline.
DR DrugBank; DB06016; Cariprazine.
DR DrugBank; DB00477; Chlorpromazine.
DR DrugBank; DB01239; Chlorprothixene.
DR DrugBank; DB01242; Clomipramine.
DR DrugBank; DB00924; Cyclobenzaprine.
DR DrugBank; DB00434; Cyproheptadine.
DR DrugBank; DB11273; Dihydroergocornine.
DR DrugBank; DB13345; Dihydroergocristine.
DR DrugBank; DB00320; Dihydroergotamine.
DR DrugBank; DB01142; Doxepin.
DR DrugBank; DB05492; Epicept NP-1.
DR DrugBank; DB01049; Ergoloid mesylate.
DR DrugBank; DB00696; Ergotamine.
DR DrugBank; DB06678; Esmirtazapine.
DR DrugBank; DB00574; Fenfluramine.
DR DrugBank; DB12141; Gilteritinib.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB00589; Lisuride.
DR DrugBank; DB04829; Lysergic acid diethylamide.
DR DrugBank; DB00353; Methylergometrine.
DR DrugBank; DB00247; Methysergide.
DR DrugBank; DB06148; Mianserin.
DR DrugBank; DB01454; Midomafetamine.
DR DrugBank; DB00805; Minaprine.
DR DrugBank; DB08804; Nandrolone decanoate.
DR DrugBank; DB06229; Ocaperidone.
DR DrugBank; DB05461; OPC-28326.
DR DrugBank; DB00715; Paroxetine.
DR DrugBank; DB01186; Pergolide.
DR DrugBank; DB09286; Pipamperone.
DR DrugBank; DB06153; Pizotifen.
DR DrugBank; DB05607; PRX-08066.
DR DrugBank; DB09304; Setiptiline.
DR DrugBank; DB01079; Tegaserod.
DR DrugBank; DB13025; Tiapride.
DR DrugBank; DB00508; Triflupromazine.
DR DrugBank; DB01392; Yohimbine.
DR DrugBank; DB00315; Zolmitriptan.
DR DrugCentral; P41595; -.
DR GuidetoPHARMACOLOGY; 7; -.
DR TCDB; 9.A.14.3.7; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P41595; 1 site.
DR iPTMnet; P41595; -.
DR PhosphoSitePlus; P41595; -.
DR BioMuta; HTR2B; -.
DR DMDM; 1168220; -.
DR MassIVE; P41595; -.
DR PaxDb; P41595; -.
DR PRIDE; P41595; -.
DR ABCD; P41595; 1 sequenced antibody.
DR Antibodypedia; 2921; 402 antibodies from 33 providers.
DR DNASU; 3357; -.
DR Ensembl; ENST00000258400.4; ENSP00000258400.3; ENSG00000135914.6.
DR GeneID; 3357; -.
DR KEGG; hsa:3357; -.
DR MANE-Select; ENST00000258400.4; ENSP00000258400.3; NM_000867.5; NP_000858.3.
DR UCSC; uc002vro.4; human.
DR CTD; 3357; -.
DR DisGeNET; 3357; -.
DR GeneCards; HTR2B; -.
DR HGNC; HGNC:5294; HTR2B.
DR HPA; ENSG00000135914; Tissue enhanced (adrenal gland, cervix, endometrium, smooth muscle).
DR MIM; 601122; gene.
DR neXtProt; NX_P41595; -.
DR OpenTargets; ENSG00000135914; -.
DR PharmGKB; PA29554; -.
DR VEuPathDB; HostDB:ENSG00000135914; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244937; -.
DR HOGENOM; CLU_009579_11_3_1; -.
DR InParanoid; P41595; -.
DR OMA; TYFLTIQ; -.
DR OrthoDB; 962038at2759; -.
DR PhylomeDB; P41595; -.
DR TreeFam; TF316350; -.
DR PathwayCommons; P41595; -.
DR Reactome; R-HSA-390666; Serotonin receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P41595; -.
DR SIGNOR; P41595; -.
DR BioGRID-ORCS; 3357; 15 hits in 1073 CRISPR screens.
DR GeneWiki; 5-HT2B_receptor; -.
DR GenomeRNAi; 3357; -.
DR Pharos; P41595; Tclin.
DR PRO; PR:P41595; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P41595; protein.
DR Bgee; ENSG00000135914; Expressed in decidua and 110 other tissues.
DR Genevisible; P41595; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0098666; C:G protein-coupled serotonin receptor complex; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IMP:UniProtKB.
DR GO; GO:0001587; F:Gq/11-coupled serotonin receptor activity; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IDA:UniProtKB.
DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:UniProtKB.
DR GO; GO:0003300; P:cardiac muscle hypertrophy; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
DR GO; GO:0071502; P:cellular response to temperature stimulus; ISS:UniProtKB.
DR GO; GO:0019934; P:cGMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0098664; P:G protein-coupled serotonin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR GO; GO:0014827; P:intestine smooth muscle contraction; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0014033; P:neural crest cell differentiation; ISS:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; ISS:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IMP:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:UniProtKB.
DR GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0070528; P:protein kinase C signaling; IMP:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0050795; P:regulation of behavior; IMP:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0042310; P:vasoconstriction; IMP:UniProtKB.
DR InterPro; IPR000482; 5HT2B_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF31; PTHR24247:SF31; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00651; 5HT2BRECEPTR.
DR PRINTS; PR01101; 5HTRECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Behavior; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Synapse; Synaptosome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..481
FT /note="5-hydroxytryptamine receptor 2B"
FT /id="PRO_0000068953"
FT TOPO_DOM 1..56
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TRANSMEM 57..79
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TOPO_DOM 80..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TRANSMEM 91..113
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TOPO_DOM 114..129
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TRANSMEM 130..151
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TOPO_DOM 152..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TRANSMEM 172..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TOPO_DOM 193..216
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TRANSMEM 217..239
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TOPO_DOM 240..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TRANSMEM 325..345
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TOPO_DOM 346..360
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TRANSMEM 361..382
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT TOPO_DOM 383..481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538"
FT MOTIF 152..154
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000305|PubMed:23519215,
FT ECO:0000305|PubMed:28129538"
FT MOTIF 212..215
FT /note="[DE]RFG motif; may stabilize a conformation that
FT preferentially activates signaling via beta-arrestin family
FT members"
FT /evidence="ECO:0000305|PubMed:23519215,
FT ECO:0000305|PubMed:28129538"
FT MOTIF 376..380
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000305|PubMed:23519215,
FT ECO:0000305|PubMed:28129538"
FT MOTIF 479..481
FT /note="PDZ-binding"
FT /evidence="ECO:0000269|PubMed:11150294"
FT BINDING 135
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0007744|PDB:4IB4, ECO:0007744|PDB:4NC3"
FT BINDING 140
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0007744|PDB:4IB4, ECO:0007744|PDB:4NC3"
FT BINDING 209
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:23519215,
FT ECO:0007744|PDB:4IB4, ECO:0007744|PDB:4NC3"
FT SITE 209
FT /note="Hydrophobic barrier that decreases the speed of
FT ligand binding and dissociation"
FT /evidence="ECO:0000269|PubMed:28129538"
FT LIPID 397
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 128..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322,
FT ECO:0000269|PubMed:28129538, ECO:0007744|PDB:4IB4,
FT ECO:0007744|PDB:4NC3, ECO:0007744|PDB:5TVN"
FT DISULFID 350..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322,
FT ECO:0000269|PubMed:28129538, ECO:0007744|PDB:4IB4,
FT ECO:0007744|PDB:4NC3, ECO:0007744|PDB:5TVN"
FT VARIANT 45
FT /note="Q -> E (in dbSNP:rs78484969)"
FT /evidence="ECO:0000269|PubMed:21179162"
FT /id="VAR_064574"
FT VARIANT 173
FT /note="F -> L (in dbSNP:rs77570025)"
FT /evidence="ECO:0000269|PubMed:21179162"
FT /id="VAR_064575"
FT VARIANT 388
FT /note="R -> W (in dbSNP:rs77982984)"
FT /evidence="ECO:0000269|PubMed:21179162"
FT /id="VAR_064576"
FT VARIANT 421
FT /note="M -> V (in dbSNP:rs6736017)"
FT /id="VAR_055907"
FT MUTAGEN 132
FT /note="L->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 135
FT /note="D->A: Abolishes agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 136
FT /note="V->A: Slightly decreases agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 139
FT /note="S->A: Slightly decreases agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 140
FT /note="T->A: Slightly decreases agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 208
FT /note="V->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 209
FT /note="L->A: No effect on agonist binding. Strongly
FT increases dissociation of bound lysergic acid diethylamine,
FT without affecting binding affinity. Reduces signaling via
FT arrestins, but has no effect on signaling via the
FT phosphatidylinositol-calcium second messenger system."
FT /evidence="ECO:0000269|PubMed:23519210,
FT ECO:0000269|PubMed:28129538"
FT MUTAGEN 211
FT /note="K->A: Impairs protein folding and stability.
FT Strongly reduced cell surface expression."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 217
FT /note="F->A: Slightly decreases agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 218
FT /note="M->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 225
FT /note="A->S: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 337
FT /note="W->A: Slightly decreases agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 340
FT /note="F->A: Slightly decreases agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 344
FT /note="N->A: Slightly decreases agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 347
FT /note="L->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 348
FT /note="V->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 362
FT /note="L->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 363
FT /note="E->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 366
FT /note="V->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 370
FT /note="Y->A: Slightly decreases agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT CONFLICT 452
FT /note="T -> P (in Ref. 2; CAA85319)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="Q -> R (in Ref. 9; AAH63123)"
FT /evidence="ECO:0000305"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:6DRZ"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:4IB4"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:4IB4"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4IB4"
FT HELIX 88..106
FT /evidence="ECO:0007829|PDB:4IB4"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:4IB4"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:4IB4"
FT HELIX 127..158
FT /evidence="ECO:0007829|PDB:4IB4"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6DRX"
FT HELIX 165..187
FT /evidence="ECO:0007829|PDB:4IB4"
FT HELIX 189..193
FT /evidence="ECO:0007829|PDB:4IB4"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:5TUD"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5TUD"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:4IB4"
FT HELIX 227..248
FT /evidence="ECO:0007829|PDB:4IB4"
FT HELIX 314..349
FT /evidence="ECO:0007829|PDB:4IB4"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:4IB4"
FT HELIX 355..381
FT /evidence="ECO:0007829|PDB:4IB4"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:4IB4"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:4IB4"
SQ SEQUENCE 481 AA; 54298 MW; CDA4447ECDBA3B46 CRC64;
MALSYRVSEL QSTIPEHILQ STFVHVISSN WSGLQTESIP EEMKQIVEEQ GNKLHWAALL
ILMVIIPTIG GNTLVILAVS LEKKLQYATN YFLMSLAVAD LLVGLFVMPI ALLTIMFEAM
WPLPLVLCPA WLFLDVLFST ASIMHLCAIS VDRYIAIKKP IQANQYNSRA TAFIKITVVW
LISIGIAIPV PIKGIETDVD NPNNITCVLT KERFGDFMLF GSLAAFFTPL AIMIVTYFLT
IHALQKKAYL VKNKPPQRLT WLTVSTVFQR DETPCSSPEK VAMLDGSRKD KALPNSGDET
LMRRTSTIGK KSVQTISNEQ RASKVLGIVF FLFLLMWCPF FITNITLVLC DSCNQTTLQM
LLEIFVWIGY VSSGVNPLVY TLFNKTFRDA FGRYITCNYR ATKSVKTLRK RSSKIYFRNP
MAENSKFFKK HGIRNGINPA MYQSPMRLRS STIQSSSIIL LDTLLLTENE GDKTEEQVSY
V
