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NTR2_CAEEL
ID   NTR2_CAEEL              Reviewed;         398 AA.
AC   O62169;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Nematocin receptor 2 {ECO:0000303|PubMed:23112336};
GN   Name=ntr-2 {ECO:0000303|PubMed:23112336};
GN   ORFNames=F14F4.1 {ECO:0000312|WormBase:F14F4.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|EMBL:AFJ42490.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=23112336; DOI=10.1126/science.1226860;
RA   Beets I., Janssen T., Meelkop E., Temmerman L., Suetens N., Rademakers S.,
RA   Jansen G., Schoofs L.;
RT   "Vasopressin/oxytocin-related signaling regulates gustatory associative
RT   learning in C. elegans.";
RL   Science 338:543-545(2012).
RN   [2] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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   [3] {ECO:0000305}
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=23112335; DOI=10.1126/science.1226201;
RA   Garrison J.L., Macosko E.Z., Bernstein S., Pokala N., Albrecht D.R.,
RA   Bargmann C.I.;
RT   "Oxytocin/vasopressin-related peptides have an ancient role in reproductive
RT   behavior.";
RL   Science 338:540-543(2012).
CC   -!- FUNCTION: Not directly activated by nematocin (PubMed:23112336,
CC       PubMed:23112335). May modulate activity of the nematocin receptor ntr-
CC       1, leading to reduced intracellular cAMP production (PubMed:23112335).
CC       Plays a role in male mating behavior (PubMed:23112335).
CC       {ECO:0000269|PubMed:23112335, ECO:0000269|PubMed:23112336}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23112336};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Detected in the ADL sensory neurons, the RMED and
CC       RMEV motor neurons, and the PQR tail neuron (PubMed:23112336). In
CC       males, detected in SPC tail neurons involved in spicule penetration and
CC       sperm transfer, and male-specific oblique muscles involved in vulval
CC       contact (PubMed:23112335). {ECO:0000269|PubMed:23112335,
CC       ECO:0000269|PubMed:23112336}.
CC   -!- DISRUPTION PHENOTYPE: Viable and fertile. Males have reduced
CC       reproductive success, due to a range of aberrant mating behaviors.
CC       Double knockouts with ntr-1 partially rescue the reproductive
CC       phenotypes. {ECO:0000269|PubMed:23112335}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Vasopressin/oxytocin receptor subfamily. {ECO:0000305}.
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DR   EMBL; JQ277479; AFJ42490.1; -; mRNA.
DR   EMBL; BX284606; CAA16265.1; -; Genomic_DNA.
DR   PIR; T20901; T20901.
DR   RefSeq; NP_510477.1; NM_078076.1.
DR   AlphaFoldDB; O62169; -.
DR   SMR; O62169; -.
DR   STRING; 6239.F14F4.1; -.
DR   PaxDb; O62169; -.
DR   EnsemblMetazoa; F14F4.1.1; F14F4.1.1; WBGene00008808.
DR   GeneID; 184471; -.
DR   KEGG; cel:CELE_F14F4.1; -.
DR   UCSC; F14F4.1; c. elegans.
DR   CTD; 184471; -.
DR   WormBase; F14F4.1; CE17670; WBGene00008808; ntr-2.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00970000195859; -.
DR   HOGENOM; CLU_009579_15_0_1; -.
DR   InParanoid; O62169; -.
DR   OMA; RAMDSQK; -.
DR   OrthoDB; 890925at2759; -.
DR   PhylomeDB; O62169; -.
DR   PRO; PR:O62169; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00008808; Expressed in larva and 1 other tissue.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..398
FT                   /note="Nematocin receptor 2"
FT                   /id="PRO_0000438125"
FT   TOPO_DOM        1..25
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        26..46
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        59..79
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80..99
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        100..120
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..143
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        144..164
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..187
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        188..208
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        209..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        272..292
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        303..325
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..398
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        7
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        98..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   398 AA;  45991 MW;  41AC4F9E56F3030D CRC64;
     MNNNTLNITN QRTAAAMSQI YFLVVYQTAV MIVSLLGNLF LLFVIFRANQ VMKRRVSPVQ
     LLIIHTCVAD LLFALLSLGT EILTLRTYPQ YYGSNFVCKL MRYVQMFPMY ASPFLLVAIS
     ADRYQAICRP LAHFRSSRYR RPNWMAAIAW GLALVLSIPQ FFVWTKHSKT GRCSTIYGQN
     KNTVKITYVI MFNTLAWLLP SILAAVFYYC VCKAVRLSST KSVRAMDSQK RNGKYSSGAT
     EDYIEELRKK SKGFRQQMSE FDRKRVQTVR LTITIVACNF FLWMPFCLIN VIQALWPEIS
     HIMFINYVAI LGNLNSCLNP WIYILFNRSH VRKALCRSRR SFTEVTKKRS FENFECSSTA
     TMNNNYNNCH AYTAFSNRSQ LKFDSYATDS TSLKTNSN
 
 
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