NK2R_CANLF
ID NK2R_CANLF Reviewed; 384 AA.
AC Q5DUB2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Engberg S., Drmota T.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
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; AJ884916; CAI58657.1; -; mRNA.
DR RefSeq; NP_001012635.1; NM_001012617.1.
DR AlphaFoldDB; Q5DUB2; -.
DR SMR; Q5DUB2; -.
DR STRING; 9615.ENSCAFP00000020552; -.
DR PaxDb; Q5DUB2; -.
DR Ensembl; ENSCAFT00030029652; ENSCAFP00030025835; ENSCAFG00030016045.
DR Ensembl; ENSCAFT00845006466; ENSCAFP00845005144; ENSCAFG00845003627.
DR GeneID; 489020; -.
DR KEGG; cfa:489020; -.
DR CTD; 6865; -.
DR VEuPathDB; HostDB:ENSCAFG00845003627; -.
DR VGNC; VGNC:47067; TACR2.
DR eggNOG; KOG4219; Eukaryota.
DR GeneTree; ENSGT00940000155512; -.
DR InParanoid; Q5DUB2; -.
DR OrthoDB; 715197at2759; -.
DR Proteomes; UP000002254; Chromosome 4.
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..384
FT /note="Substance-K receptor"
FT /id="PRO_0000069891"
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 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
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 384 AA; 43359 MW; A7C3D524AEBC2BDF CRC64;
MGAHAIVTDA NISSSLENNT TGITAFSMPG WQLALWATAY LVLVLVAVTG NATVIWIILA
HQRMRTVTNY FIVNLALADL CMAAFNAAFN FVYASHNIWY FGRAFCHFQN LFPITAMFVS
IYSMTAIAAD RYVAIVHPFQ PRLSAPGTRA VIAGIWLLAL ALAFPQCFYS TITMDQGATK
CVVVWPEDNG SKMLLLYHLV VIALIYVLPL LVMLLAYSVI GLTLWRREVP RHQVHGASLR
HLRAKKKFVK TMVLVVVTFA ICWLPYHFYF ILGSFQEDIY YHKFIQQVYL ALFWLAMSST
MYNPIIYCCL NHRFRSGFRL AFRCCPWVTP TEEDKIELTH TPSLSARINR CHTKETFFMA
GETALSPATN GQARGPQDGL PDEP
