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Database: UniProt
Entry: A0A2Y9QEL1_DELLE
LinkDB: A0A2Y9QEL1_DELLE
Original site: A0A2Y9QEL1_DELLE 
ID   A0A2Y9QEL1_DELLE        Unreviewed;       365 AA.
AC   A0A2Y9QEL1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Chemerin-like receptor 1 {ECO:0000256|ARBA:ARBA00026211};
DE   AltName: Full=Chemokine-like receptor 1 {ECO:0000256|ARBA:ARBA00030532};
GN   Name=CMKLR1 {ECO:0000313|RefSeq:XP_022456050.1,
GN   ECO:0000313|RefSeq:XP_022456051.1, ECO:0000313|RefSeq:XP_022456052.1,
GN   ECO:0000313|RefSeq:XP_022456053.1, ECO:0000313|RefSeq:XP_022456054.1};
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_022456051.1};
RN   [1] {ECO:0000313|RefSeq:XP_022456050.1, ECO:0000313|RefSeq:XP_022456051.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022456050.1,
RC   ECO:0000313|RefSeq:XP_022456051.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
CC   -!- SIMILARITY: Belongs to the chemokine-like receptor (CMKLR) family.
CC       {ECO:0000256|ARBA:ARBA00025736}.
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DR   RefSeq; XP_022456050.1; XM_022600342.2.
DR   RefSeq; XP_022456051.1; XM_022600343.2.
DR   RefSeq; XP_022456052.1; XM_022600344.2.
DR   RefSeq; XP_022456053.1; XM_022600345.2.
DR   RefSeq; XP_022456054.1; XM_022600346.2.
DR   STRING; 9749.A0A2Y9QEL1; -.
DR   Ensembl; ENSDLET00000030786; ENSDLEP00000028016; ENSDLEG00000020161.
DR   KEGG; dle:111188134; -.
DR   OrthoDB; 5384006at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0097004; F:adipokinetic hormone binding; IEA:Ensembl.
DR   GO; GO:0097003; F:adipokinetic hormone receptor activity; IEA:Ensembl.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:Ensembl.
DR   GO; GO:0032695; P:negative regulation of interleukin-12 production; IEA:Ensembl.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl.
DR   GO; GO:0050848; P:regulation of calcium-mediated signaling; IEA:Ensembl.
DR   CDD; cd15116; 7tmA_CMKLR1; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR002258; CML1.
DR   InterPro; IPR000826; Formyl_rcpt-rel.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24225:SF49; CHEMERIN-LIKE RECEPTOR 1; 1.
DR   PANTHER; PTHR24225; CHEMOTACTIC RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01126; DEZORPHANR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|RuleBase:RU000688,
KW   ECO:0000313|RefSeq:XP_022456050.1};
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        39..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        220..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        296..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          55..314
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   REGION          339..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   365 AA;  41219 MW;  FAE735513CEE247A CRC64;
     MEDEDSNTSL TYEYVYSDDF DPIVVLEELS PLEGRVVRIF LVVVYSIICF LGILGNGLVI
     IIATCKMKKT VNTVWFLNLA VADFLFNVFL PIHITYAAMD YHWVFGTAMC KISNFLLIHN
     MYTSVFLLTV ISSDRCISVL LPVWSQNHRS VRLAYMACMV IWVLAFFLSS PSLVFRDTAH
     VHGKISCFNN FSLSATSSSS WPTHPQVDAV GFGRHVAVTI TRFLCGFLTP MLIITACYVT
     IVCKLRRNRL AKTKKPFKVI VTIIITFFLC WCPYHTLYLL ELHHSAMPGS VFSLGVPLAT
     AIAIANSCMN PILYVFVGQD FKKFKVALFS RLVHALSEDT GHSSYPSHRS FTKMSSMNER
     ETSML
//
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