5HT2B_TETFL
ID 5HT2B_TETFL Reviewed; 471 AA.
AC Q8UUG8; Q8UUP7; Q8UUP8; Q8UUP9; Q8UUQ0; Q8UUQ1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Tetraodon fluviatilis (Green pufferfish) (Chelonodon fluviatilis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=47145;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAC85962.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP TISSUE SPECIFICITY.
RC TISSUE=Intestine;
RX PubMed=11744166; DOI=10.1016/s0169-328x(01)00293-5;
RA De Lucchini S., Marracci S., Nardi I.;
RT "The serotonin 5-HT2B receptor from the puffer fish Tetraodon fluviatilis:
RT cDNA cloning, genomic organization and alternatively spliced variants.";
RL Brain Res. Mol. Brain Res. 97:89-93(2001).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for various ergot alkaloid
CC derivatives and psychoactive substances. Ligand binding causes a
CC conformation change that triggers signaling via guanine nucleotide-
CC binding proteins (G proteins) and modulates the activity of down-stream
CC effectors. Beta-arrestin family members inhibit signaling via G
CC proteins and mediate activation of alternative signaling pathways.
CC Signaling activates a phosphatidylinositol-calcium second messenger
CC system that modulates the activity of phosphatidylinositol 3-kinase and
CC down-stream signaling cascades and promotes the release of Ca(2+) ions
CC from intracellular stores. Plays a role in the regulation of dopamine
CC and 5-hydroxytryptamine release, 5-hydroxytryptamine uptake and in the
CC regulation of extracellular dopamine and 5-hydroxytryptamine levels,
CC and thereby affects neural activity (By similarity).
CC {ECO:0000250|UniProtKB:P41595, ECO:0000250|UniProtKB:Q02152}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41595};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P41595}. Synapse,
CC synaptosome {ECO:0000250|UniProtKB:Q02152}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:11744166};
CC IsoId=Q8UUG8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11744166};
CC IsoId=Q8UUG8-2; Sequence=VSP_052051;
CC Name=3 {ECO:0000269|PubMed:11744166};
CC IsoId=Q8UUG8-3; Sequence=VSP_052052, VSP_052053;
CC Name=4 {ECO:0000269|PubMed:11744166};
CC IsoId=Q8UUG8-4; Sequence=VSP_052050;
CC -!- TISSUE SPECIFICITY: Detected in brain, heart and gut.
CC {ECO:0000269|PubMed:11744166}.
CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
CC transmembrane helices. {ECO:0000250|UniProtKB:P41595}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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; AJ315179; CAC86245.1; -; Genomic_DNA.
DR EMBL; AJ315180; CAC86246.1; -; mRNA.
DR EMBL; AJ315181; CAC86247.1; -; mRNA.
DR EMBL; AJ315182; CAC86248.1; -; mRNA.
DR EMBL; AJ315183; CAC86249.1; -; mRNA.
DR EMBL; AJ320211; CAC85962.1; -; mRNA.
DR EMBL; AJ320212; CAC85912.1; -; mRNA.
DR AlphaFoldDB; Q8UUG8; -.
DR SMR; Q8UUG8; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0001587; F:Gq/11-coupled serotonin receptor activity; NAS:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; NAS:UniProtKB.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0048598; P:embryonic morphogenesis; TAS:UniProtKB.
DR GO; GO:0007507; P:heart development; IEA:InterPro.
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; Behavior; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Synapse; Synaptosome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..471
FT /note="5-hydroxytryptamine receptor 2B"
FT /id="PRO_0000239461"
FT TOPO_DOM 1..26
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 27..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 50..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 61..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 84..99
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 100..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 122..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 142..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 163..191
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 192..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 215..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 309..329
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 330..344
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 345..366
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 367..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT MOTIF 122..124
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT MOTIF 187..190
FT /note="[DE]RFG motif; may stabilize a conformation that
FT preferentially activates signaling via beta-arrestin family
FT members"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT MOTIF 360..364
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT MOTIF 469..471
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT BINDING 105
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT BINDING 110
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT BINDING 184
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT SITE 184
FT /note="Hydrophobic barrier that decreases the speed of
FT ligand binding and dissociation"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT LIPID 381
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 334..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 32..471
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11744166"
FT /id="VSP_052050"
FT VAR_SEQ 88..155
FT /note="DSDWPLPEPLCPIWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQHSQYKSR
FT AKVMLKIALVWLISIC -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11744166"
FT /id="VSP_052051"
FT VAR_SEQ 150..177
FT /note="WLISICIAIPIPIKGLRNYPHPNNITFT -> LQSQFQLRGLGTTLILTTSP
FT LPVTIHAC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11744166"
FT /id="VSP_052052"
FT VAR_SEQ 178..471
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11744166"
FT /id="VSP_052053"
FT CONFLICT 5
FT /note="A -> V (in Ref. 1; CAC86249)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="P -> L (in Ref. 1; CAC86249)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="F -> L (in Ref. 1; CAC86247)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="R -> H (in Ref. 1; CAC86247)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="V -> G (in Ref. 1; CAC86247)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="P -> S (in Ref. 1; CAC86247)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="G -> D (in Ref. 1; CAC86247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 53057 MW; 60DC34CA971E18CB CRC64;
MFQAAVGPLQ TNISLPEETP GLELNWAALL IVMVIIPTIG GNILVILAVW LEKKLQNATN
FFLMSLAVAD LLVGLLVMPI ALITILYDSD WPLPEPLCPI WLFLDVLFST ASIMHLCAIS
LDRYIAIKKP IQHSQYKSRA KVMLKIALVW LISICIAIPI PIKGLRNYPH PNNITFTSNH
TCVLKTDTFQ EFIIFGSLVA FFIPLTIMMI IYFLTVRVLR KKVYLLRSKV TQRFSYPIIS
TVFQREQAAN PPQPEQPDST GNSLARIQEK TDTDGMSSPT GDEKSFRRLS TMGKKSMQTL
TNEQRASKVL GIVFLLFVVM WCPFFITNIT SALCGPCDAN IIGRLMEIFS WVGYVSSGIN
PLVYTLFNKT FRQAFTRYIT CNYRNFASKE QGRSFRASTV DRMLTHISPR SSVAENAKLF
TKQEIKNETT DYRSPLGCLQ PSAQTSTGVV LDKILLTHTE NCKQEERVSC V
