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TAAR8_HUMAN
ID   TAAR8_HUMAN             Reviewed;         342 AA.
AC   Q969N4; Q5VUQ0;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Trace amine-associated receptor 8;
DE            Short=TaR-8;
DE            Short=Trace amine receptor 8;
DE   AltName: Full=G-protein coupled receptor 102;
DE   AltName: Full=Trace amine receptor 5;
DE            Short=TaR-5;
GN   Name=TAAR8; Synonyms=GPR102, TA5, TAR5, TRAR5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=11459929; DOI=10.1073/pnas.151105198;
RA   Borowsky B., Adham N., Jones K.A., Raddatz R., Artymyshyn R.,
RA   Ogozalek K.L., Durkin M.M., Lakhlani P.P., Bonini J.A., Pathirana S.,
RA   Boyle N., Pu X., Kouranova E., Lichtblau H., Ochoa F.Y., Branchek T.A.,
RA   Gerald C.;
RT   "Trace amines: identification of a family of mammalian G protein-coupled
RT   receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8966-8971(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11574155; DOI=10.1016/s0378-1119(01)00651-5;
RA   Lee D.K., Nguyen T., Lynch K.R., Cheng R., Vanti W.B., Arkhitko O.,
RA   Lewis T., Evans J.F., George S.R., O'Dowd B.F.;
RT   "Discovery and mapping of ten novel G protein-coupled receptor genes.";
RL   Gene 275:83-91(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
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).
RN   [6]
RP   VARIANT ASP-211.
RX   PubMed=21885028; DOI=10.1016/j.ajhg.2011.08.002;
RA   Parry D.A., Logan C.V., Hayward B.E., Shires M., Landolsi H., Diggle C.,
RA   Carr I., Rittore C., Touitou I., Philibert L., Fisher R.A., Fallahian M.,
RA   Huntriss J.D., Picton H.M., Malik S., Taylor G.R., Johnson C.A.,
RA   Bonthron D.T., Sheridan E.G.;
RT   "Mutations causing familial biparental hydatidiform mole implicate c6orf221
RT   as a possible regulator of genomic imprinting in the human oocyte.";
RL   Am. J. Hum. Genet. 89:451-458(2011).
CC   -!- FUNCTION: Orphan receptor. Could be a receptor for trace amines. Trace
CC       amines are biogenic amines present in very low levels in mammalian
CC       tissues. Although some trace amines have clearly defined roles as
CC       neurotransmitters in invertebrates, the extent to which they function
CC       as true neurotransmitters in vertebrates has remained speculative.
CC       Trace amines are likely to be involved in a variety of physiological
CC       functions that have yet to be fully understood.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney and amygdala. Not expressed in
CC       other tissues or brain regions tested. {ECO:0000269|PubMed:11459929}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF380193; AAK71244.1; -; Genomic_DNA.
DR   EMBL; AF411116; AAL26487.1; -; Genomic_DNA.
DR   EMBL; AY183468; AAO24659.1; -; mRNA.
DR   EMBL; AL513524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC069166; AAH69166.1; -; mRNA.
DR   CCDS; CCDS5154.1; -.
DR   RefSeq; NP_444508.1; NM_053278.2.
DR   AlphaFoldDB; Q969N4; -.
DR   SMR; Q969N4; -.
DR   IntAct; Q969N4; 1.
DR   STRING; 9606.ENSP00000275200; -.
DR   ChEMBL; CHEMBL4523902; -.
DR   GlyGen; Q969N4; 2 sites.
DR   BioMuta; TAAR8; -.
DR   DMDM; 38258876; -.
DR   PaxDb; Q969N4; -.
DR   PeptideAtlas; Q969N4; -.
DR   PRIDE; Q969N4; -.
DR   ProteomicsDB; 75805; -.
DR   Antibodypedia; 19706; 126 antibodies from 22 providers.
DR   DNASU; 83551; -.
DR   Ensembl; ENST00000275200.1; ENSP00000275200.1; ENSG00000146385.1.
DR   GeneID; 83551; -.
DR   KEGG; hsa:83551; -.
DR   MANE-Select; ENST00000275200.2; ENSP00000275200.1; NM_053278.3; NP_444508.1.
DR   UCSC; uc011ecj.2; human.
DR   CTD; 83551; -.
DR   GeneCards; TAAR8; -.
DR   HGNC; HGNC:14964; TAAR8.
DR   HPA; ENSG00000146385; Not detected.
DR   MIM; 606927; gene.
DR   neXtProt; NX_Q969N4; -.
DR   OpenTargets; ENSG00000146385; -.
DR   PharmGKB; PA28850; -.
DR   VEuPathDB; HostDB:ENSG00000146385; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000161306; -.
DR   HOGENOM; CLU_009579_11_0_1; -.
DR   InParanoid; Q969N4; -.
DR   OMA; GAKFCTL; -.
DR   OrthoDB; 995146at2759; -.
DR   PhylomeDB; Q969N4; -.
DR   TreeFam; TF343107; -.
DR   PathwayCommons; Q969N4; -.
DR   Reactome; R-HSA-375280; Amine ligand-binding receptors.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR   SignaLink; Q969N4; -.
DR   BioGRID-ORCS; 83551; 11 hits in 1025 CRISPR screens.
DR   GeneWiki; TAAR8; -.
DR   GenomeRNAi; 83551; -.
DR   Pharos; Q969N4; Tbio.
DR   PRO; PR:Q969N4; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q969N4; protein.
DR   Genevisible; Q969N4; HS.
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:0004930; F:G protein-coupled receptor activity; TAS:GDB.
DR   GO; GO:0001594; F:trace-amine receptor activity; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR009132; TAAR_fam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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   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..342
FT                   /note="Trace amine-associated receptor 8"
FT                   /id="PRO_0000070174"
FT   TOPO_DOM        1..31
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..67
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        89..111
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..195
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        217..258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..342
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        104..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         153
FT                   /note="S -> N (in dbSNP:rs8192626)"
FT                   /id="VAR_049447"
FT   VARIANT         211
FT                   /note="V -> D (in dbSNP:rs187426282)"
FT                   /evidence="ECO:0000269|PubMed:21885028"
FT                   /id="VAR_066638"
FT   VARIANT         328
FT                   /note="D -> A (in dbSNP:rs8192627)"
FT                   /id="VAR_049448"
SQ   SEQUENCE   342 AA;  38029 MW;  AB034E68F7D60388 CRC64;
     MTSNFSQPVV QLCYEDVNGS CIETPYSPGS RVILYTAFSF GSLLAVFGNL LVMTSVLHFK
     QLHSPTNFLI ASLACADFLV GVTVMLFSMV RTVESCWYFG AKFCTLHSCC DVAFCYSSVL
     HLCFICIDRY IVVTDPLVYA TKFTVSVSGI CISVSWILPL TYSGAVFYTG VNDDGLEELV
     SALNCVGGCQ IIVSQGWVLI DFLLFFIPTL VMIILYSKIF LIAKQQAIKI ETTSSKVESS
     SESYKIRVAK RERKAAKTLG VTVLAFVISW LPYTVDILID AFMGFLTPAY IYEICCWSAY
     YNSAMNPLIY ALFYPWFRKA IKLILSGDVL KASSSTISLF LE
 
 
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