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OAR2_CAEEL
ID   OAR2_CAEEL              Reviewed;         468 AA.
AC   Q19084; Q3S1M1; Q7Z290;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 3.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Tyramine receptor tyra-2;
GN   Name=tyra-2; ORFNames=F01E11.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15953361; DOI=10.1111/j.1471-4159.2005.03180.x;
RA   Rex E., Hapiak V., Hobson R., Smith K., Xiao H., Komuniecki R.;
RT   "TYRA-2 (F01E11.5): a Caenorhabditis elegans tyramine receptor expressed in
RT   the MC and NSM pharyngeal neurons.";
RL   J. Neurochem. 94:181-191(2005).
CC   -!- FUNCTION: G-protein coupled receptor for tyramine, a known
CC       neurotransmitter and neuromodulator and direct precursor of octopamine.
CC       Expression in amphidial sensory neurons suggests a role in
CC       chemosensation. {ECO:0000269|PubMed:15953361}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=c;
CC         IsoId=Q19084-1; Sequence=Displayed;
CC       Name=a;
CC         IsoId=Q19084-2; Sequence=VSP_018118;
CC       Name=b;
CC         IsoId=Q19084-3; Sequence=VSP_018117;
CC   -!- TISSUE SPECIFICITY: Expressed in the pharyngeal neurons, MCL/R and
CC       NSML/R and the AS group of amphidial sensory neurons, ASEL/R, AGSL/R,
CC       ASHL/R and ASIL/R. {ECO:0000269|PubMed:15953361}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; FO080572; CCD83463.1; -; Genomic_DNA.
DR   EMBL; FO080572; CCD83464.1; -; Genomic_DNA.
DR   EMBL; FO080572; CCD83465.1; -; Genomic_DNA.
DR   PIR; T15941; T15941.
DR   RefSeq; NP_001024521.1; NM_001029350.4. [Q19084-2]
DR   RefSeq; NP_001024522.1; NM_001029351.3. [Q19084-3]
DR   RefSeq; NP_001033537.1; NM_001038448.2. [Q19084-1]
DR   AlphaFoldDB; Q19084; -.
DR   SMR; Q19084; -.
DR   STRING; 6239.F01E11.5c; -.
DR   PaxDb; Q19084; -.
DR   EnsemblMetazoa; F01E11.5a.1; F01E11.5a.1; WBGene00017157. [Q19084-2]
DR   EnsemblMetazoa; F01E11.5b.1; F01E11.5b.1; WBGene00017157. [Q19084-3]
DR   EnsemblMetazoa; F01E11.5b.2; F01E11.5b.2; WBGene00017157. [Q19084-3]
DR   EnsemblMetazoa; F01E11.5c.1; F01E11.5c.1; WBGene00017157. [Q19084-1]
DR   GeneID; 180970; -.
DR   KEGG; cel:CELE_F01E11.5; -.
DR   UCSC; F01E11.5c; c. elegans. [Q19084-1]
DR   CTD; 180970; -.
DR   WormBase; F01E11.5a; CE38313; WBGene00017157; tyra-2. [Q19084-2]
DR   WormBase; F01E11.5b; CE35711; WBGene00017157; tyra-2. [Q19084-3]
DR   WormBase; F01E11.5c; CE30931; WBGene00017157; tyra-2. [Q19084-1]
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q19084; -.
DR   OMA; NAHIEMF; -.
DR   OrthoDB; 737211at2759; -.
DR   PhylomeDB; Q19084; -.
DR   Reactome; R-CEL-390696; Adrenoceptors.
DR   Reactome; R-CEL-392023; Adrenaline signalling through Alpha-2 adrenergic receptor.
DR   Reactome; R-CEL-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR   Reactome; R-CEL-418594; G alpha (i) signalling events.
DR   Reactome; R-CEL-418597; G alpha (z) signalling events.
DR   PRO; PR:Q19084; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00017157; Expressed in larva and 4 other tissues.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0008227; F:G protein-coupled amine receptor activity; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
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   Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..468
FT                   /note="Tyramine receptor tyra-2"
FT                   /id="PRO_0000070223"
FT   TOPO_DOM        1..23
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..43
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..54
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..77
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..91
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..114
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..134
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..157
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..186
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..209
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..387
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        388..410
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        411..424
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..444
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        445..468
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          252..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        91..177
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VAR_SEQ         1..126
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018117"
FT   VAR_SEQ         225..230
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018118"
SQ   SEQUENCE   468 AA;  53051 MW;  52868B370274AF79 CRC64;
     MMSSYVMSPV DETYTLFQIL KGSALFLLVL WTIFANSLVF IVLYKNPRLQ TVPNLLVGNL
     AFSDLALGLI VLPLSSVYAI AGEWVFPDAL CEVFVSADIL CSTASIWNLS IVGLDRYWAI
     TSPVAYMSKR NKRTAGIMIL SVWISSALIS LAPLLGWKQT AQTPNLIYEK NNTVRQCTFL
     DLPSYTVYSA TGSFFIPTLL MFFVYFKIYQ AFAKHRARQI YRQKLAVSSH VIRKHIESTI
     LHEISHVLPT SDEFAKEEEE EEDSESSGQV ENGLGNGNDA IIEEDECEDE DSDEKRDDHT
     SMTTVTATVT GPTEAPYMKR EAKISKSVPI EKESAIQKRE AKPMRSVMAI SYEKVKRHKN
     RKERIYRKSL QRKPKAISAA KERRGVKVLG IILGCFTVCW APFFTMYVLV QFCKDCSPNA
     HIEMFITWLG YSNSAMNPII YTVFNRDYQI ALKRLFTSEK KPSSTSRV
 
 
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