ID A0A2Y9QIK7_DELLE Unreviewed; 419 AA.
AC A0A2Y9QIK7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 2.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=LOW QUALITY PROTEIN: neuropeptide FF receptor 2 {ECO:0000313|RefSeq:XP_022455243.2};
GN Name=NPFFR2 {ECO:0000313|RefSeq:XP_022455243.2};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022455243.2};
RN [1] {ECO:0000313|RefSeq:XP_022455243.2}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022455243.2};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide)
CC neuropeptides, also known as morphine-modulating peptides. Can also be
CC activated by a variety of naturally occurring or synthetic FMRF-amide
CC like ligands. This receptor mediates its action by association with G
CC proteins that activate a phosphatidylinositol-calcium second messenger
CC system. {ECO:0000256|ARBA:ARBA00025478}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
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DR RefSeq; XP_022455243.2; XM_022599535.2.
DR STRING; 9749.A0A2Y9QIK7; -.
DR KEGG; dle:111187666; -.
DR InParanoid; A0A2Y9QIK7; -.
DR OrthoDB; 3150248at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008188; F:neuropeptide receptor activity; IEA:InterPro.
DR GO; GO:0031628; F:opioid receptor binding; IEA:InterPro.
DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:InterPro.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR005395; NPFF_rcpt.
DR InterPro; IPR005397; NPFF_rcpt_2.
DR PANTHER; PTHR24241:SF132; NEUROPEPTIDE FF RECEPTOR 2; 1.
DR PANTHER; PTHR24241; NEUROPEPTIDE RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01570; NPFFRECEPTOR.
DR PRINTS; PR01572; NPFFRECEPTR2.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU000688};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|RuleBase:RU000688,
KW ECO:0000313|RefSeq:XP_022455243.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Transducer {ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..333
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 419 AA; 48150 MW; 25DC6EDD866BE6DC CRC64;
MSENWESNSS ENWHPIWSVS DTKHDLYADS SITYVNYYLH QPQVAAIFVI SYFLTFFLCM
VGNTVVCFIV MRNTHMHTVT NLFILNLAVS DLLVGIFCMP ITLLDNIIAG WPFGSTMCKI
SGLVQGISVA ASVFTLVAIA VDRFQCVVYP FKPKLTIKTA SVIIMIIWIL AIVIMSPSAI
MLHVQEEKYY RVRLNSQNKT SPVYWCREDW PNREMRKIYT TVLFANIYLA PLSLNVIMYG
RIGIALSKTT VPPSGKQNQE QWHVVTKKQQ KVIKMLLTVA LLFILSWLPL WTXMMLSHYV
DLSLNELQVI NTYIYPLAHW LAFGNSSINP IIYGFFNENF RHGFQDAFRL HLCQXREKPK
EAYTLRAKNN VVINISHLSA QESTIKNPHE DIVLCRKSAE KPIQELMIKN XELTDSNEM
//