CML1_HUMAN
ID CML1_HUMAN Reviewed; 373 AA.
AC Q99788; A8K6Y5; O75748; Q3KP37; Q5U0H0; Q99789;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Chemerin-like receptor 1 {ECO:0000303|PubMed:29279348};
DE AltName: Full=Chemokine-like receptor 1;
DE AltName: Full=G-protein coupled receptor ChemR23;
DE AltName: Full=G-protein coupled receptor DEZ;
GN Name=CMKLR1 {ECO:0000312|HGNC:HGNC:2121}; Synonyms=CHEMR23, DEZ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=9144535; DOI=10.1006/bbrc.1997.6455;
RA Methner A., Hermey G., Schinke B., Hermans-Borgmeyer I.;
RT "A novel G protein-coupled receptor with homology to neuropeptide and
RT chemoattractant receptors expressed during bone development.";
RL Biochem. Biophys. Res. Commun. 233:336-342(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B), AND FUNCTION (MICROBIAL
RP INFECTION).
RX PubMed=9603476;
RX DOI=10.1002/(sici)1521-4141(199805)28:05<1689::aid-immu1689>3.0.co;2-i;
RA Samson M., Edinger A.L., Stordeur P., Rucker J., Verhasselt V., Sharron M.,
RA Govaerts C., Mollereau C., Vassart G., Doms R.W., Parmentier M.;
RT "ChemR23, a putative chemoattractant receptor, is expressed in monocyte-
RT derived dendritic cells and macrophages and is a coreceptor for SIV and
RT some primary HIV-1 strains.";
RL Eur. J. Immunol. 28:1689-1700(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B).
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Kidney;
RA King M.M., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=8976386; DOI=10.1159/000134436;
RA Gantz I., Konda Y., Yang Y.K., Miller D.E., Dierick H.A., Yamada T.;
RT "Molecular cloning of a novel receptor (CMKLR1) with homology to the
RT chemotactic factor receptors.";
RL Cytogenet. Cell Genet. 74:286-290(1996).
RN [11]
RP LIGAND-BINDING.
RX PubMed=14675762; DOI=10.1016/s0014-5793(03)01312-7;
RA Meder W., Wendland M., Busmann A., Kutzleb C., Spodsberg N., John H.,
RA Richter R., Schleuder D., Meyer M., Forssmann W.G.;
RT "Characterization of human circulating TIG2 as a ligand for the orphan
RT receptor ChemR23.";
RL FEBS Lett. 555:495-499(2003).
RN [12]
RP TISSUE SPECIFICITY, LIGAND-BINDING, AND INDUCTION.
RX PubMed=14530373; DOI=10.1084/jem.20030382;
RA Wittamer V., Franssen J.D., Vulcano M., Mirjolet J.F., Le Poul E.,
RA Migeotte I., Brezillon S., Tyldesley R., Blanpain C., Detheux M.,
RA Mantovani A., Sozzani S., Vassart G., Parmentier M., Communi D.;
RT "Specific recruitment of antigen-presenting cells by chemerin, a novel
RT processed ligand from human inflammatory fluids.";
RL J. Exp. Med. 198:977-985(2003).
RN [13]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [14]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15728234; DOI=10.1084/jem.20041310;
RA Vermi W., Riboldi E., Wittamer V., Gentili F., Luini W., Marrelli S.,
RA Vecchi A., Franssen J.D., Communi D., Massardi L., Sironi M., Mantovani A.,
RA Parmentier M., Facchetti F., Sozzani S.;
RT "Role of ChemR23 in directing the migration of myeloid and plasmacytoid
RT dendritic cells to lymphoid organs and inflamed skin.";
RL J. Exp. Med. 201:509-515(2005).
RN [15]
RP LIGAND-BINDING, INDUCTION, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15753205; DOI=10.1084/jem.20042031;
RA Arita M., Bianchini F., Aliberti J., Sher A., Chiang N., Hong S., Yang R.,
RA Petasis N.A., Serhan C.N.;
RT "Stereochemical assignment, antiinflammatory properties, and receptor for
RT the omega-3 lipid mediator resolvin E1.";
RL J. Exp. Med. 201:713-722(2005).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=16863918; DOI=10.1016/j.exphem.2006.03.011;
RA Zabel B.A., Ohyama T., Zuniga L., Kim J.Y., Johnston B., Allen S.J.,
RA Guido D.G., Handel T.M., Butcher E.C.;
RT "Chemokine-like receptor 1 expression by macrophages in vivo: regulation by
RT TGF-beta and TLR ligands.";
RL Exp. Hematol. 34:1106-1114(2006).
RN [17]
RP TISSUE SPECIFICITY.
RX PubMed=18242188; DOI=10.1016/j.febslet.2008.01.023;
RA Takahashi M., Takahashi Y., Takahashi K., Zolotaryov F.N., Hong K.S.,
RA Kitazawa R., Iida K., Okimura Y., Kaji H., Kitazawa S., Kasuga M.,
RA Chihara K.;
RT "Chemerin enhances insulin signaling and potentiates insulin-stimulated
RT glucose uptake in 3T3-L1 adipocytes.";
RL FEBS Lett. 582:573-578(2008).
RN [18]
RP TISSUE SPECIFICITY, INDUCTION, AND FUNCTION.
RX PubMed=20044979; DOI=10.1016/j.bbrc.2009.12.150;
RA Kaur J., Adya R., Tan B.K., Chen J., Randeva H.S.;
RT "Identification of chemerin receptor (ChemR23) in human endothelial cells:
RT chemerin-induced endothelial angiogenesis.";
RL Biochem. Biophys. Res. Commun. 391:1762-1768(2010).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27716822; DOI=10.1371/journal.pone.0164179;
RA De Henau O., Degroot G.N., Imbault V., Robert V., De Poorter C., Mcheik S.,
RA Gales C., Parmentier M., Springael J.Y.;
RT "Signaling properties of chemerin receptors CMKLR1, GPR1 and CCRL2.";
RL PLoS ONE 11:e0164179-e0164179(2016).
RN [20]
RP NOMENCLATURE.
RX PubMed=29279348; DOI=10.1124/pr.116.013177;
RA Kennedy A.J., Davenport A.P.;
RT "International Union of Basic and Clinical Pharmacology CIII: Chemerin
RT Receptors CMKLR1 (Chemerin1) and GPR1 (Chemerin2) Nomenclature,
RT Pharmacology, and Function.";
RL Pharmacol. Rev. 70:174-196(2018).
CC -!- FUNCTION: Receptor for the chemoattractant adipokine chemerin/RARRES2
CC and for the omega-3 fatty acid derived molecule resolvin E1.
CC Interaction with RARRES2 initiates activation of G proteins G(i)/G(o)
CC and beta-arrestin pathways inducing cellular responses via second
CC messenger pathways such as intracellular calcium mobilization,
CC phosphorylation of MAP kinases MAPK1/MAPK3 (ERK1/2), TYRO3,
CC MAPK14/P38MAPK and PI3K leading to multifunctional effects, like,
CC reduction of immune responses, enhancing of adipogenesis and angionesis
CC PubMed:27716822. Resolvin E1 down-regulates cytokine production in
CC macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-
CC kappa-B. Positively regulates adipogenesis and adipocyte metabolism.
CC {ECO:0000269|PubMed:15728234, ECO:0000269|PubMed:15753205,
CC ECO:0000269|PubMed:20044979, ECO:0000269|PubMed:27716822}.
CC -!- FUNCTION: (Microbial infection) Acts as a coreceptor for several SIV
CC strains (SIVMAC316, SIVMAC239, SIVMACL7E-FR and SIVSM62A), as well as a
CC primary HIV-1 strain (92UG024-2). {ECO:0000269|PubMed:9603476}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15728234,
CC ECO:0000269|PubMed:16863918, ECO:0000269|PubMed:27716822}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Internalizes efficiently in
CC response to RARRES2. {ECO:0000269|PubMed:27716822}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q99788-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q99788-2; Sequence=VSP_001985;
CC -!- TISSUE SPECIFICITY: Prominently expressed in developing osseous and
CC cartilaginous tissue. Also found in adult parathyroid glands. Expressed
CC in cardiovascular system, brain, kidney, gastrointestinal tissues and
CC myeloid tissues. Expressed in a broad array of tissues associated with
CC hematopoietic and immune function including, spleen, thymus, appendix,
CC lymph node, bone marrow and fetal liver. Among leukocyte populations
CC abundant expression in monocyte-derived macrophage and immature
CC dendritic cells (DCs). High expression in blood monocytes and low
CC levels in polymorphonuclear cells and T-cells. Expressed on endothelial
CC cells. Highly expressed in differentiating adipocytes.
CC {ECO:0000269|PubMed:14530373, ECO:0000269|PubMed:15728234,
CC ECO:0000269|PubMed:15753205, ECO:0000269|PubMed:18242188,
CC ECO:0000269|PubMed:20044979, ECO:0000269|PubMed:8976386}.
CC -!- DEVELOPMENTAL STAGE: Expressed during bone development.
CC -!- INDUCTION: Up-regulated by inflammatory cytokines TNF-alpha and IFN-
CC gamma in monocytes. Up-regulated by TNF-alpha, IL-1-beta and IL-6 in
CC endothelial cells. {ECO:0000269|PubMed:14530373,
CC ECO:0000269|PubMed:15753205, ECO:0000269|PubMed:20044979}.
CC -!- MISCELLANEOUS: [Isoform A]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay.
CC -!- SIMILARITY: Belongs to the chemokine-like receptor (CMKLR) family.
CC {ECO:0000305}.
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DR EMBL; U79526; AAC51258.1; -; mRNA.
DR EMBL; U79527; AAC51259.1; -; mRNA.
DR EMBL; Y14838; CAA75112.1; -; Genomic_DNA.
DR EMBL; AB065871; BAC06089.1; -; Genomic_DNA.
DR EMBL; AY497547; AAR90850.1; -; mRNA.
DR EMBL; AK291800; BAF84489.1; -; mRNA.
DR EMBL; BT019556; AAV38363.1; -; mRNA.
DR EMBL; BT019557; AAV38364.1; -; mRNA.
DR EMBL; AC009729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC063957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97810.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97811.1; -; Genomic_DNA.
DR EMBL; BC106927; AAI06928.1; -; mRNA.
DR EMBL; BC106928; AAI06929.1; -; mRNA.
DR CCDS; CCDS41829.1; -. [Q99788-2]
DR CCDS; CCDS44965.1; -. [Q99788-1]
DR RefSeq; NP_001135815.1; NM_001142343.1. [Q99788-1]
DR RefSeq; NP_001135816.1; NM_001142344.1. [Q99788-1]
DR RefSeq; NP_001135817.1; NM_001142345.1. [Q99788-1]
DR RefSeq; NP_004063.1; NM_004072.2. [Q99788-2]
DR RefSeq; XP_016874309.1; XM_017018820.1. [Q99788-2]
DR AlphaFoldDB; Q99788; -.
DR SMR; Q99788; -.
DR BioGRID; 107644; 110.
DR STRING; 9606.ENSP00000311733; -.
DR BindingDB; Q99788; -.
DR ChEMBL; CHEMBL3540; -.
DR GuidetoPHARMACOLOGY; 79; -.
DR SwissLipids; SLP:000001606; -.
DR TCDB; 9.A.14.13.15; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q99788; 2 sites.
DR iPTMnet; Q99788; -.
DR PhosphoSitePlus; Q99788; -.
DR BioMuta; CMKLR1; -.
DR DMDM; 17380487; -.
DR jPOST; Q99788; -.
DR MassIVE; Q99788; -.
DR PaxDb; Q99788; -.
DR PeptideAtlas; Q99788; -.
DR PRIDE; Q99788; -.
DR ProteomicsDB; 78474; -. [Q99788-1]
DR ProteomicsDB; 78475; -. [Q99788-2]
DR ABCD; Q99788; 1 sequenced antibody.
DR Antibodypedia; 9299; 583 antibodies from 36 providers.
DR DNASU; 1240; -.
DR Ensembl; ENST00000312143.11; ENSP00000311733.7; ENSG00000174600.14. [Q99788-1]
DR Ensembl; ENST00000412676.5; ENSP00000401293.1; ENSG00000174600.14. [Q99788-1]
DR Ensembl; ENST00000550402.6; ENSP00000449716.1; ENSG00000174600.14. [Q99788-1]
DR Ensembl; ENST00000552995.5; ENSP00000447579.1; ENSG00000174600.14. [Q99788-2]
DR GeneID; 1240; -.
DR KEGG; hsa:1240; -.
DR MANE-Select; ENST00000550402.6; ENSP00000449716.1; NM_001142343.2; NP_001135815.1.
DR UCSC; uc001tmv.4; human. [Q99788-1]
DR CTD; 1240; -.
DR DisGeNET; 1240; -.
DR GeneCards; CMKLR1; -.
DR HGNC; HGNC:2121; CMKLR1.
DR HPA; ENSG00000174600; Tissue enhanced (lymphoid).
DR MIM; 602351; gene.
DR neXtProt; NX_Q99788; -.
DR OpenTargets; ENSG00000174600; -.
DR PharmGKB; PA26640; -.
DR VEuPathDB; HostDB:ENSG00000174600; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230438; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; Q99788; -.
DR OMA; TACVVIW; -.
DR OrthoDB; 910274at2759; -.
DR PhylomeDB; Q99788; -.
DR TreeFam; TF330976; -.
DR PathwayCommons; Q99788; -.
DR Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
DR SignaLink; Q99788; -.
DR BioGRID-ORCS; 1240; 99 hits in 1060 CRISPR screens.
DR ChiTaRS; CMKLR1; human.
DR GeneWiki; CMKLR1; -.
DR GenomeRNAi; 1240; -.
DR Pharos; Q99788; Tchem.
DR PRO; PR:Q99788; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q99788; protein.
DR Bgee; ENSG00000174600; Expressed in right coronary artery and 127 other tissues.
DR ExpressionAtlas; Q99788; baseline and differential.
DR Genevisible; Q99788; HS.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0097004; F:adipokinetic hormone binding; IDA:UniProtKB.
DR GO; GO:0097003; F:adipokinetic hormone receptor activity; IDA:UniProtKB.
DR GO; GO:0004950; F:chemokine receptor activity; TAS:ProtInc.
DR GO; GO:0004875; F:complement receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0006935; P:chemotaxis; IDA:UniProtKB.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; ISS:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:DFLAT.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IDA:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR InterPro; IPR002258; CML1.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; PTHR24225; 1.
DR PANTHER; PTHR24225:SF49; PTHR24225:SF49; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01126; DEZORPHANR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..373
FT /note="Chemerin-like receptor 1"
FT /id="PRO_0000069307"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..320
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 341..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97468"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35786"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..2
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4,
FT ECO:0000303|Ref.6"
FT /id="VSP_001985"
FT CONFLICT 248
FT /note="Q -> H (in Ref. 2; AAC51258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 42322 MW; 5244B9738EC93834 CRC64;
MRMEDEDYNT SISYGDEYPD YLDSIVVLED LSPLEARVTR IFLVVVYSIV CFLGILGNGL
VIIIATFKMK KTVNMVWFLN LAVADFLFNV FLPIHITYAA MDYHWVFGTA MCKISNFLLI
HNMFTSVFLL TIISSDRCIS VLLPVWSQNH RSVRLAYMAC MVIWVLAFFL SSPSLVFRDT
ANLHGKISCF NNFSLSTPGS SSWPTHSQMD PVGYSRHMVV TVTRFLCGFL VPVLIITACY
LTIVCKLQRN RLAKTKKPFK IIVTIIITFF LCWCPYHTLN LLELHHTAMP GSVFSLGLPL
ATALAIANSC MNPILYVFMG QDFKKFKVAL FSRLVNALSE DTGHSSYPSH RSFTKMSSMN
ERTSMNERET GML
