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TAAR1_PANTR
ID   TAAR1_PANTR             Reviewed;         339 AA.
AC   Q5QD29;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Trace amine-associated receptor 1;
DE            Short=TaR-1;
DE            Short=Trace amine receptor 1;
GN   Name=TAAR1; Synonyms=TRAR1;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15718104; DOI=10.1016/j.ygeno.2004.11.010;
RA   Lindemann L., Ebeling M., Kratochwil N.A., Bunzow J.R., Grandy D.K.,
RA   Hoener M.C.;
RT   "Trace amine-associated receptors form structurally and functionally
RT   distinct subfamilies of novel G protein-coupled receptors.";
RL   Genomics 85:372-385(2005).
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 {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AY702307; AAV70124.1; -; Genomic_DNA.
DR   RefSeq; NP_001009145.1; NM_001009145.1.
DR   AlphaFoldDB; Q5QD29; -.
DR   SMR; Q5QD29; -.
DR   STRING; 9598.ENSPTRP00000031769; -.
DR   PaxDb; Q5QD29; -.
DR   GeneID; 493908; -.
DR   KEGG; ptr:493908; -.
DR   CTD; 134864; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q5QD29; -.
DR   OrthoDB; 913195at2759; -.
DR   Proteomes; UP000002277; 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; IEA:InterPro.
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..339
FT                   /note="Trace amine-associated receptor 1"
FT                   /id="PRO_0000070144"
FT   TOPO_DOM        1..25
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..59
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..98
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..252
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        274..287
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..339
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        96..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   339 AA;  39086 MW;  1E36D67ED5E8C8EC CRC64;
     MMPFCHNIIN ISCVKNNWSN DVRASLYSLM VLIILTTLVG NLIVIVSISH FKELHTPTNW
     LIHSMATVDF LPGCLVMPYS MVRSAEHCWY FGEVFCKIHT STDIMLSSAS IFHLSFISID
     RYYAVCDPLR YKAKINILVI CVMIFISWSV PAVFAFGMIF LELNFKGAEE IYYKHVHCRG
     GCSVFFSKIS GVLTFMTSFY IPGSIMLCVY YRIYLIAKEQ ARLINDANQK LQIGLEMKNG
     ISQSKERKAV KTLGIVMGVF LICWCPFFIC TVMDPFLHYI IPPTLNDVLI WFGYLNSTFN
     PMVYAFFYPW FRKALKMMLF GKIFQKDSSR CKLFLELSS
 
 
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