5HT2A_PIG
ID 5HT2A_PIG Reviewed; 470 AA.
AC P50129; Q29004;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=5-hydroxytryptamine receptor 2A;
DE Short=5-HT-2;
DE Short=5-HT-2A;
DE Short=5-HT2A;
DE AltName: Full=Serotonin receptor 2A;
GN Name=HTR2A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7794950; DOI=10.1016/0005-2736(95)00073-c;
RA Johnson M.P., Baez M., Kursar J.D., Nelson D.L.;
RT "Species differences in 5-HT2A receptors: cloned pig and rhesus monkey 5-
RT HT2A receptors reveal conserved transmembrane homology to the human rather
RT than rat sequence.";
RL Biochim. Biophys. Acta 1236:201-206(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 146-213.
RC TISSUE=Pulmonary artery;
RX PubMed=7656980; DOI=10.1016/0014-5793(95)00828-w;
RA Ullmer C., Schmuck K., Kalkman H.O., Luebbert H.;
RT "Expression of serotonin receptor mRNAs in blood vessels.";
RL FEBS Lett. 370:215-221(1995).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for various drugs and
CC psychoactive substances, including mescaline, psilocybin, 1-(2,5-
CC dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid
CC diethylamide (LSD). Ligand binding causes a conformation change that
CC triggers signaling via guanine nucleotide-binding proteins (G proteins)
CC and modulates the activity of down-stream effectors. Beta-arrestin
CC family members inhibit signaling via G proteins and mediate activation
CC of alternative signaling pathways. Signaling activates phospholipase C
CC and a phosphatidylinositol-calcium second messenger system that
CC modulates the activity of phosphatidylinositol 3-kinase and promotes
CC the release of Ca(2+) ions from intracellular stores. Affects neural
CC activity, perception, cognition and mood. Plays a role in the
CC regulation of behavior, including responses to anxiogenic situations
CC and psychoactive substances. Plays a role in intestinal smooth muscle
CC contraction, and may play a role in arterial vasoconstriction (By
CC similarity). {ECO:0000250|UniProtKB:P28223}.
CC -!- SUBUNIT: Interacts (via C-terminus) with MPDZ and PATJ. May interact
CC (via C-terminus) with MPP3, PRDX6, DLG4, DLG1, CASK, APBA1 and MAGI2.
CC Interacts with GRM2 and DRD2; this may affect signaling.
CC {ECO:0000250|UniProtKB:P28223}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14842};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P14842}. Cell
CC projection, axon {ECO:0000250|UniProtKB:P14842}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:P14842}. Membrane, caveola
CC {ECO:0000250|UniProtKB:P14842}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P35363}. Presynapse
CC {ECO:0000250|UniProtKB:P14842}.
CC -!- DOMAIN: The PDZ domain-binding motif is involved in the interaction
CC with PATJ, CASK, APBA1, DLG1 and DLG4. {ECO:0000250|UniProtKB:P28223}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; S78208; AAB34690.1; -; mRNA.
DR EMBL; Z48152; CAA88169.1; -; mRNA.
DR PIR; S66489; S66489.
DR RefSeq; NP_999382.1; NM_214217.1.
DR AlphaFoldDB; P50129; -.
DR SMR; P50129; -.
DR STRING; 9823.ENSSSCP00000010037; -.
DR BindingDB; P50129; -.
DR ChEMBL; CHEMBL2490; -.
DR DrugCentral; P50129; -.
DR PaxDb; P50129; -.
DR GeneID; 397432; -.
DR KEGG; ssc:397432; -.
DR CTD; 3356; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P50129; -.
DR PRO; PR:P50129; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IEA:InterPro.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR InterPro; IPR000455; 5HT2A_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF30; PTHR24247:SF30; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00516; 5HT2ARECEPTR.
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 Behavior; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Synapse; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..470
FT /note="5-hydroxytryptamine receptor 2A"
FT /id="PRO_0000068949"
FT TOPO_DOM 1..75
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 76..99
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 100..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 111..132
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 133..148
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 149..171
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 172..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 192..215
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 216..233
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 234..254
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 255..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 324..345
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 346..361
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 362..383
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 384..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 448..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..174
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT MOTIF 375..379
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT MOTIF 468..470
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:P28223"
FT COMPBIAS 454..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT BINDING 160
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT BINDING 229
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT SITE 229
FT /note="Hydrophobic barrier that decreases the speed of
FT ligand binding and dissociation"
FT /evidence="ECO:0000250|UniProtKB:P28223"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28223"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 148..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 348..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 184
FT /note="R -> S (in Ref. 2; CAA88169)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="M -> K (in Ref. 2; CAA88169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 52676 MW; 8231AD580BEE2A8F CRC64;
MDVLCEENTS LSSPTNSFMQ LNDDTRLYHN DFNSGEANTS DAFNWTVDSE NRTNLSCEGC
LSPPCFSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD
MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP
IHHRRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF
VSFFIPLTIM VITYFLTIKS LQKEATLCVS DLGTRAKLAS FSFLPQSSLS SEKLFQRSIH
REPGSYGRRT MQSISNEQKA CKVLGIVFFL FVVMWCPFFI TNIMAVICKE SCNEDVIGAL
LNVFVWIGYL SSAVNPLVYT LFNKTYRSAF SRYIQCQYKE NKKPLQLILV NTIPALAYKS
SQLQTGQKEN SKQDDKATEN DCTMVALGKQ HSEDAPADNS NTVNEKVSCV
