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TAAR1_MACMU
ID   TAAR1_MACMU             Reviewed;         338 AA.
AC   Q8HZ64;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Trace amine-associated receptor 1;
DE            Short=TaR-1;
DE            Short=Trace amine receptor 1;
GN   Name=TAAR1; Synonyms=TA1, TAR1, TRAR1;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Miller G.M., Madras B.K.;
RT   "Cloning of trace amine receptor 1 (TAR1) from Rhesus monkey.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for trace amines, including beta-phenylethylamine
CC       (b-PEA), p-tyramine (p-TYR), octopamine and tryptamine, with highest
CC       affinity for b-PEA and p-TYR. Unresponsive to classical biogenic
CC       amines, such as epinephrine and histamine and only partially activated
CC       by dopamine and serotonin. Trace amines are biogenic amines present in
CC       very low levels in mammalian tissues. Although some trace amines have
CC       clearly defined roles as neurotransmitters in invertebrates, the extent
CC       to which they function as true neurotransmitters in vertebrates has
CC       remained speculative. Trace amines are likely to be involved in a
CC       variety of physiological functions that have yet to be fully
CC       understood. The signal transduced by this receptor is mediated by the
CC       G(s)-class of G-proteins which activate adenylate cyclase (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AY135366; AAN06172.1; -; Genomic_DNA.
DR   RefSeq; NP_001074234.1; NM_001080765.1.
DR   AlphaFoldDB; Q8HZ64; -.
DR   SMR; Q8HZ64; -.
DR   STRING; 9544.ENSMMUP00000019771; -.
DR   BindingDB; Q8HZ64; -.
DR   ChEMBL; CHEMBL1926495; -.
DR   DrugCentral; Q8HZ64; -.
DR   GeneID; 708944; -.
DR   KEGG; mcc:708944; -.
DR   CTD; 134864; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   HOGENOM; CLU_009579_11_0_1; -.
DR   InParanoid; Q8HZ64; -.
DR   OMA; YIPGFVM; -.
DR   OrthoDB; 913195at2759; -.
DR   PRO; PR:Q8HZ64; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001594; F:trace-amine receptor activity; IBA:GO_Central.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR009133; TAAR1.
DR   InterPro; IPR009132; TAAR_fam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01831; TRACEAMINE1R.
DR   PRINTS; PR01830; TRACEAMINER.
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   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..338
FT                   /note="Trace amine-associated receptor 1"
FT                   /id="PRO_0000070142"
FT   TOPO_DOM        1..24
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80..97
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..187
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        209..251
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..286
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..307
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        308..338
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        9
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        16
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        95..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   338 AA;  38797 MW;  9EE7B35456BB409B CRC64;
     MPFCHNIINI SCVKNNWSND VRASLYSLMA LIILTTLVGN LIVIVSISHF KQLHTPTNWL
     IHSMATVDFL LGCLVMPYSM VRSAEHCWYF GEVFCKIHTS TDIMLSSASI FHLSFISIDR
     YYAVCDPLRY KAKINILVVC VMIFISWSVP AVFAFGMIFL ELNFKGAEEI YYKHVHCRGG
     CSVFFSKISG VLAFMTSFYI PGSIMLCIYY RIYLIAKEQA RSINDANQKL QIGLEMKNGI
     SQSKERKAVK TLGIVMGVFL ICWCPFFVCT VIDPFLHYTI PPTLNDVLIW FGYLNSTFNP
     MVYAFFYPWF RKALKMILFG KIFQKDSSRC KLFLESSS
 
 
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