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5HT2B_PIG
ID   5HT2B_PIG               Reviewed;          60 AA.
AC   Q29005;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=5-hydroxytryptamine receptor 2B;
DE            Short=5-HT-2B;
DE            Short=5-HT2B;
DE   AltName: Full=Serotonin receptor 2B;
DE   Flags: Fragment;
GN   Name=HTR2B;
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], AND TISSUE SPECIFICITY.
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 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. May play a role in the perception
CC       of pain. Plays a role in the regulation of behavior, including
CC       impulsive behavior. Required for normal proliferation of embryonic
CC       cardiac myocytes and normal heart development. Protects cardiomyocytes
CC       against apoptosis. Plays a role in the adaptation of pulmonary arteries
CC       to chronic hypoxia. Plays a role in vasoconstriction. Required for
CC       normal osteoblast function and proliferation, and for maintaining
CC       normal bone density. Required for normal proliferation of the
CC       interstitial cells of Cajal in the intestine (By similarity).
CC       {ECO:0000250|UniProtKB:P41595, ECO:0000250|UniProtKB:Q02152}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with MPDZ.
CC       {ECO:0000250|UniProtKB:P41595}.
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   -!- TISSUE SPECIFICITY: Detected in aorta, renal artery, jugular vein, vena
CC       cava and femoral vein. {ECO:0000269|PubMed:7656980}.
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}.
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DR   EMBL; Z48174; CAA88197.1; -; mRNA.
DR   PIR; S66491; S66491.
DR   AlphaFoldDB; Q29005; -.
DR   SMR; Q29005; -.
DR   STRING; 9823.ENSSSCP00000017240; -.
DR   PaxDb; Q29005; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   HOGENOM; CLU_009579_11_3_1; -.
DR   InParanoid; Q29005; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; Q29005; SS.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR   GO; GO:0007507; P:heart development; IEA:InterPro.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
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; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24247:SF31; PTHR24247:SF31; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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; G-protein coupled receptor; Lipoprotein; Membrane;
KW   Palmitate; Receptor; Reference proteome; Synapse; Synaptosome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           <1..>60
FT                   /note="5-hydroxytryptamine receptor 2B"
FT                   /id="PRO_0000068955"
FT   TOPO_DOM        <1..4
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   TRANSMEM        5..26
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   TOPO_DOM        27..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   TRANSMEM        47..60
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   MOTIF           27..29
FT                   /note="DRY motif; important for ligand-induced conformation
FT                   changes"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   BINDING         10
FT                   /ligand="ergotamine"
FT                   /ligand_id="ChEBI:CHEBI:190463"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   BINDING         15
FT                   /ligand="ergotamine"
FT                   /ligand_id="ChEBI:CHEBI:190463"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   NON_TER         1
FT   NON_TER         60
SQ   SEQUENCE   60 AA;  6725 MW;  920DCF0D76A8404B CRC64;
     VLCPAWLFLD VLFSTASIMH LCAISVDRYI AIKKPIQANQ YNSRATAFIK ITVVWLISIG
 
 
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