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NTR2_RAT
ID   NTR2_RAT                Reviewed;         416 AA.
AC   Q63384;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Neurotensin receptor type 2;
DE            Short=NT-R-2;
DE            Short=NTR2;
DE   AltName: Full=High-affinity levocabastine-sensitive neurotensin receptor;
GN   Name=Ntsr2; Synonyms=Ntr2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hypothalamus;
RX   PubMed=8647296; DOI=10.1016/0014-5793(96)00397-3;
RA   Chalon P., Vita N., Kaghad M., Guillemont M., Bonin J., Delpech B.,
RA   le Fur G., Ferrara P., Caput D.;
RT   "Molecular cloning of a levocabastine-sensitive neurotensin binding site.";
RL   FEBS Lett. 386:91-94(1996).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Receptor for the tridecapeptide neurotensin. It is associated
CC       with G proteins that activate a phosphatidylinositol-calcium second
CC       messenger system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Abundant in cortex and hypothalamus, and lower
CC       levels seen in the heart and intestine.
CC   -!- DEVELOPMENTAL STAGE: Expressed maximally in 7-day-old brain and
CC       expression decreases progressively until adulthood (35-day-old brain).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Neurotensin receptor subfamily. NTSR2 sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X97121; CAA65787.1; -; mRNA.
DR   PIR; S68822; S68822.
DR   RefSeq; NP_073186.1; NM_022695.2.
DR   AlphaFoldDB; Q63384; -.
DR   SMR; Q63384; -.
DR   STRING; 10116.ENSRNOP00000067549; -.
DR   BindingDB; Q63384; -.
DR   ChEMBL; CHEMBL5106; -.
DR   DrugCentral; Q63384; -.
DR   GuidetoPHARMACOLOGY; 310; -.
DR   iPTMnet; Q63384; -.
DR   PhosphoSitePlus; Q63384; -.
DR   PaxDb; Q63384; -.
DR   PRIDE; Q63384; -.
DR   GeneID; 64636; -.
DR   KEGG; rno:64636; -.
DR   CTD; 23620; -.
DR   RGD; 70962; Ntsr2.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q63384; -.
DR   OrthoDB; 890529at2759; -.
DR   PhylomeDB; Q63384; -.
DR   Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   PRO; PR:Q63384; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0043204; C:perikaryon; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR   GO; GO:0016492; F:G protein-coupled neurotensin receptor activity; ISO:RGD.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:RGD.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:RGD.
DR   GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR003986; NT2_rcpt.
DR   InterPro; IPR003984; NT_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01479; NEUROTENSINR.
DR   PRINTS; PR01481; NEUROTENSN2R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..416
FT                   /note="Neurotensin receptor type 2"
FT                   /id="PRO_0000069951"
FT   TOPO_DOM        1..32
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..55
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..87
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..109
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..131
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..176
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..297
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..337
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..416
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         410
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   LIPID           377
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        108..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   416 AA;  46266 MW;  127FC5F5CB6FE208 CRC64;
     METSSPWPPR PSPSAGLSLE ARLGVDTRLW AKVLFTALYS LIFAFGTAGN ALSVHVVLKA
     RAGRPGRLRY HVLSLALSAL LLLLVSMPME LYNFVWSHYP WVFGDLGCRG YYFVRELCAY
     ATVLSVASLS AERCLAVCQP LRARRLLTPR RTRRLLSLVW VASLGLALPM AVIMGQKHEV
     ESADGEPEPA SRVCTVLVSR ATLQVFIQVN VLVSFALPLA LTAFLNGITV NHLMALYSQV
     PSASAQVSSI PSRLELLSEE GLLGFITWRK TLSLGVQASL VRHKDASQIR SLQHSAQVLR
     AIVAVYVICW LPYHARRLMY CYIPDDGWTN ELYDFYHYFY MVTNTLFYVS SAVTPILYNA
     VSSSFRKLFL ESLGSLCGEQ HSLVPLPQEA PESTTSTYSF RLWGSPRNPS LGEIQV
 
 
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