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NK2R_MESAU
ID   NK2R_MESAU              Reviewed;         384 AA.
AC   P51144;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Substance-K receptor;
DE            Short=SKR;
DE   AltName: Full=NK-2 receptor;
DE            Short=NK-2R;
DE   AltName: Full=Neurokinin A receptor;
DE   AltName: Full=Tachykinin receptor 2;
GN   Name=TACR2; Synonyms=TAC2R;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Urinary bladder;
RX   PubMed=8302285;
RA   Aharony D., Little J., Thomas C., Powell S., Berry D., Graham A.;
RT   "Isolation and pharmacological characterization of a hamster urinary
RT   bladder neurokinin A receptor cDNA.";
RL   Mol. Pharmacol. 45:9-19(1994).
CC   -!- FUNCTION: This is a receptor for the tachykinin neuropeptide substance
CC       K (neurokinin A). It is associated with G proteins that activate a
CC       phosphatidylinositol-calcium second messenger system. The rank order of
CC       affinity of this receptor to tachykinins is: substance K > neuromedin-K
CC       > substance P.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; S68899; AAC60680.1; -; mRNA.
DR   RefSeq; XP_005070883.1; XM_005070826.2.
DR   AlphaFoldDB; P51144; -.
DR   SMR; P51144; -.
DR   STRING; 10036.XP_005070883.1; -.
DR   BindingDB; P51144; -.
DR   ChEMBL; CHEMBL2304405; -.
DR   GeneID; 101839819; -.
DR   CTD; 6865; -.
DR   eggNOG; KOG4219; Eukaryota.
DR   OrthoDB; 715197at2759; -.
DR   Proteomes; UP000189706; 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:0061827; C:sperm head; IEA:Ensembl.
DR   GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR   GO; GO:0004995; F:tachykinin receptor activity; IEA:InterPro.
DR   GO; GO:1902093; P:positive regulation of flagellated sperm motility; IEA:Ensembl.
DR   GO; GO:0070472; P:regulation of uterine smooth muscle contraction; IEA:Ensembl.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001681; Neurokn_rcpt.
DR   InterPro; IPR000913; NK2_rcpt.
DR   PANTHER; PTHR46925:SF3; PTHR46925:SF3; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01025; NEUROKININ2R.
DR   PRINTS; PR00244; NEUROKININR.
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   Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..384
FT                   /note="Substance-K receptor"
FT                   /id="PRO_0000069894"
FT   TOPO_DOM        1..32
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..56
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..107
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..129
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..196
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..218
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..251
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..290
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..310
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        311..384
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           324
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        106..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   384 AA;  43418 MW;  524BECFC3D0067F3 CRC64;
     MGGRAIVTDT NIFSGLESNT TGVTAFSMPA WQLALWATAY LGLVLVAVTG NATVIWIILA
     HERMRTVTNY FIINLALADL CMAAFNATFN FVYASHNIWY FGRAFCYFQN LFPITAMFVS
     IYSMTAIAAD RYMAIVHPFQ PRLSAPITKA TIAGIWLVAL ALASPQCFYS TITVDQGATK
     CVVAWPNDNG GKMLLLYHLV VFVLVYFLPL VVMFVAYSVI GLTLWKRAVP RHQAHGANLR
     HLHAKKKFVK AMVLVVLTFA ICWLPYHLYF ILGSFQKDIY YRKFIQQVYL ALFWLAMSST
     MYNPIIYCCL NHRFRSGFRL AFRCCPWVTP TEEDRLELTR TPSLSRRVNR CHTKETLFMT
     ADMTHSEATN GQVGSPQDVE PAAP
 
 
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