NK2R_CAVPO
ID NK2R_CAVPO Reviewed; 402 AA.
AC Q64077;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 112.
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;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Dunkin-Hartley; TISSUE=Lung;
RX PubMed=7877137; DOI=10.3109/10799899409101512;
RA Aharony D., Little J., Thomas C., Powell S., Downey-Jones M., Graham A.;
RT "Isolation and characterization of neurokinin A receptor cDNAs from guinea-
RT pig lung and rabbit pulmonary artery.";
RL J. Recept. Res. 14:399-421(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.
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; S76253; AAB33553.1; -; mRNA.
DR PIR; I56595; I56595.
DR RefSeq; XP_003473635.1; XM_003473587.3.
DR AlphaFoldDB; Q64077; -.
DR SMR; Q64077; -.
DR STRING; 10141.ENSCPOP00000005425; -.
DR BindingDB; Q64077; -.
DR ChEMBL; CHEMBL2647; -.
DR Ensembl; ENSCPOT00000006074; ENSCPOP00000005425; ENSCPOG00000006011.
DR GeneID; 100720631; -.
DR KEGG; cpoc:100720631; -.
DR CTD; 6865; -.
DR eggNOG; KOG4219; Eukaryota.
DR GeneTree; ENSGT00940000155512; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; Q64077; -.
DR OrthoDB; 715197at2759; -.
DR PRO; PR:Q64077; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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 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 Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..402
FT /note="Substance-K receptor"
FT /id="PRO_0000069892"
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..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 365..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 324
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
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 402 AA; 45092 MW; D4FA803E4363376F CRC64;
MGACVIVTNT NISSGLESNT TGITAFSMPT WQLALWATAY LALVLVAVTG NATVTWIILA
HQRMRTVTNY FIVNLALADL CMAAFNAAFN FVYASHNIWY FGRAFCYFQN LFPITAMFVS
IYSMTAIAID RYMAIVHPFQ PRLSAPSTKA VIGGIWLVAL ALAFPQCFYS TITEDEGATK
CVVAWPEDSR DKSLLLYHLV VIVLIYLLPL TVMFVAYSII GLTLWRRAVP RHQAHGANLR
HLQAKKKFVK TMVLVVVTFA ICWLPYHLYF ILGSFQEDIY CHKFIQQVYL ALFWLAMSST
MYNPIIYCCL NRRFRSGFRL AFRCCPWVTP TEEDKLELTH TPSFSLRVNR CHTKEILFMA
GDTVPSEATN GQAGGPQDRE SVELSSLPGC RAGPSILAKA SS