5HT5B_MOUSE
ID 5HT5B_MOUSE Reviewed; 370 AA.
AC P31387; Q1RME2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=5-hydroxytryptamine receptor 5B;
DE Short=5-HT-5B;
DE Short=5-HT5B;
DE AltName: Full=Serotonin receptor 5B;
GN Name=Htr5b; Synonyms=5ht5b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8450829;
RA Matthes H., Boschert U., Amlaiky N., Grailhe R., Plassat J.-L.,
RA Muscatelli F., Mattei M.-G., Hen R.;
RT "Mouse 5-hydroxytryptamine5A and 5-hydroxytryptamine5B receptors define a
RT new family of serotonin receptors: cloning, functional expression, and
RT chromosomal localization.";
RL Mol. Pharmacol. 43:313-319(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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. The activity of this
CC receptor is mediated by G proteins. Probably involved in anxiety and
CC depression.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the central nervous
CC system; in the hippocampus, habenula, and the doral raphe.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X69867; CAA49501.1; -; mRNA.
DR EMBL; BC114988; AAI14989.1; -; mRNA.
DR EMBL; BC115825; AAI15826.1; -; mRNA.
DR CCDS; CCDS15239.1; -.
DR PIR; I48231; I48231.
DR AlphaFoldDB; P31387; -.
DR SMR; P31387; -.
DR STRING; 10090.ENSMUSP00000057212; -.
DR BindingDB; P31387; -.
DR GuidetoPHARMACOLOGY; 648; -.
DR GlyGen; P31387; 1 site.
DR iPTMnet; P31387; -.
DR PhosphoSitePlus; P31387; -.
DR PaxDb; P31387; -.
DR PRIDE; P31387; -.
DR MGI; MGI:96284; Htr5b.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P31387; -.
DR PhylomeDB; P31387; -.
DR PRO; PR:P31387; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P31387; protein.
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:GOC.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IBA:GO_Central.
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 InterPro; IPR000431; 5HT5B_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00519; 5HT5BRECEPTR.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..370
FT /note="5-hydroxytryptamine receptor 5B"
FT /id="PRO_0000068972"
FT TOPO_DOM 1..52
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 53..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 76..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 91..111
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 112..128
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 129..150
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 151..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 172..194
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 195..211
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 212..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 233..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 296..316
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 317..333
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 334..354
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 355..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 127..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 370 AA; 41201 MW; 0553C62B12DAAD84 CRC64;
MEVSNLSGAT PGLAFPPGPE SCSDSPSSGR SMGSTPGGLI LPGREPPFSA FTVLVVTLLV
LLIAATFLWN LLVLVTILRV RAFHRVPHNL VASTAVSDVL VAVLVMPLSL VSELSAGRRW
QLGRSLCHVW ISFDVLCCTA SIWNVAAIAL DRYWTITRHL QYTLRTRSRA SALMIAITWA
LSALIALAPL LFGWGEAYDA RLQRCQVSQE PSYAVFSTCG AFYLPLAVVL FVYWKIYKAA
KFRFGRRRRA VVPLPATTQA KEAPPESEMV FTARRRATVT FQTSGDSWRE QKEKRAAMMV
GILIGVFVLC WIPFFLTELI SPLCACSLPP IWKSIFLWLG YSNSFFNPLI YTAFNKNYNN
AFKSLFTKQR
