ID GPR35_HUMAN Reviewed; 309 AA.
AC Q9HC97; J3KR30; O43495; Q17R58; Q4VBN5; Q4ZFV2; Q6FHI8; Q86UH4;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 4.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=G-protein coupled receptor 35;
DE AltName: Full=Kynurenic acid receptor;
DE Short=KYNA receptor;
GN Name=GPR35;
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 [GENOMIC DNA], AND VARIANT ARG-294.
RX PubMed=9479505; DOI=10.1006/geno.1998.5095;
RA O'Dowd B.F., Nguyen T., Marchese A., Cheng R., Lynch K.R., Heng H.H.Q.,
RA Kolakowski L.F. Jr., George S.R.;
RT "Discovery of three novel G-protein-coupled receptor genes.";
RL Genomics 47:310-313(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-25; ILE-29;
RP MET-108; SER-125 AND MET-253.
RX PubMed=11017071; DOI=10.1038/79876;
RA Horikawa Y., Oda N., Cox N.J., Li X., Orho-Melander M., Hara M.,
RA Hinokio Y., Lindner T.H., Mashima H., Schwarz P.E.H., del Bosque-Plata L.,
RA Horikawa Y., Oda Y., Yoshiuchi I., Colilla S., Polonsky K.S., Wei S.,
RA Concannon P., Iwasaki N., Schulze J., Baier L.J., Bogardus C., Groop L.,
RA Boerwinkle E., Hanis C.L., Bell G.I.;
RT "Genetic variation in the gene encoding calpain-10 is associated with type
RT 2 diabetes mellitus.";
RL Nat. Genet. 26:163-175(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Warren C.N., Aronstam R.S., Sharma S.V.;
RT "Isolation of complete coding sequence for G-protein coupled receptor 35
RT (GPR35).";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ARG-294.
RC TISSUE=Hepatoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-294.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-294.
RC TISSUE=Brain;
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16754668; DOI=10.1074/jbc.m603503200;
RA Wang J., Simonavicius N., Wu X., Swaminath G., Reagan J., Tian H., Ling L.;
RT "Kynurenic acid as a ligand for orphan G protein-coupled receptor GPR35.";
RL J. Biol. Chem. 281:22021-22028(2006).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20361937; DOI=10.1016/j.bbrc.2010.03.169;
RA Oka S., Ota R., Shima M., Yamashita A., Sugiura T.;
RT "GPR35 is a novel lysophosphatidic acid receptor.";
RL Biochem. Biophys. Res. Commun. 395:232-237(2010).
RN [10]
RP FUNCTION.
RX PubMed=35148838; DOI=10.1016/j.cell.2022.01.010;
RA De Giovanni M., Tam H., Valet C., Xu Y., Looney M.R., Cyster J.G.;
RT "GPR35 promotes neutrophil recruitment in response to serotonin metabolite
RT 5-HIAA.";
RL Cell 185:815-830(2022).
RN [11]
RP FUNCTION, MUTAGENESIS OF SER-287; SER-300; SER-303 AND THR-307,
RP PHOSPHORYLATION AT SER-287; SER-294; SER-300; SER-303 AND THR-307,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ARRB2.
RX PubMed=35101446; DOI=10.1016/j.jbc.2022.101655;
RA Divorty N., Jenkins L., Ganguly A., Butcher A.J., Hudson B.D., Schulz S.,
RA Tobin A.B., Nicklin S.A., Milligan G.;
RT "Agonist-induced phosphorylation of orthologues of the orphan receptor
RT GPR35 functions as an activation sensor.";
RL J. Biol. Chem. 298:101655-101655(2022).
RN [12]
RP FUNCTION, PHOSPHORYLATION AT SER-300 AND SER-303, AND INTERACTION WITH
RP ARRB2.
RX PubMed=37660910; DOI=10.1016/j.jbc.2023.105218;
RA Ganguly A., Quon T., Jenkins L., Joseph B., Al-Awar R., Chevigne A.,
RA Tobin A.B., Uehling D.E., Hoffmann C., Drube J., Milligan G.;
RT "G protein-receptor kinases 5/6 are the key regulators of G protein-coupled
RT receptor 35-arrestin interactions.";
RL J. Biol. Chem. 0:0-0(2023).
RN [13] {ECO:0007744|PDB:8H8J}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 2-309, DISULFIDE
RP BONDS, AND INTERACTION WITH GNA13.
RX PubMed=36543774; DOI=10.1038/s41421-022-00499-8;
RA Duan J., Liu Q., Yuan Q., Ji Y., Zhu S., Tan Y., He X., Xu Y., Shi J.,
RA Cheng X., Jiang H., Eric Xu H., Jiang Y.;
RT "Insights into divalent cation regulation and G13-coupling of orphan
RT receptor GPR35.";
RL Cell Discov. 8:135-135(2022).
CC -!- FUNCTION: G-protein coupled receptor that binds to several ligands
CC including the tryptophan metabolite kynurenic acid (KYNA),
CC lysophosphatidic acid (LPA) or 5-hydroxyindoleacetic acid (5-HIAA) with
CC high affinity, leading to rapid and transient activation of numerous
CC intracellular signaling pathways (PubMed:16754668, PubMed:20361937,
CC PubMed:35148838). Plays a role in neutrophil recruitment to sites of
CC inflammation and bacterial clearance through the major serotonin
CC metabolite 5-HIAA that acts as a physiological ligand
CC (PubMed:35148838). Stimulates lipid metabolism, thermogenic, and anti-
CC inflammatory gene expression in adipose tissue once activated by
CC kynurenic acid (By similarity). In macrophages, activation by
CC lysophosphatidic acid promotes GPR35-induced signaling with a distinct
CC transcriptional profile characterized by TNF production associated with
CC ERK and NF-kappa-B activation. In turn, induces chemotaxis of
CC macrophages (By similarity). {ECO:0000250|UniProtKB:Q9ES90,
CC ECO:0000269|PubMed:20361937, ECO:0000269|PubMed:35148838}.
CC -!- SUBUNIT: Interacts with GNA13 (PubMed:36543774). Interacts with ARRB2
CC (PubMed:35101446, PubMed:37660910). {ECO:0000269|PubMed:35101446,
CC ECO:0000269|PubMed:36543774, ECO:0000269|PubMed:37660910}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16754668,
CC ECO:0000269|PubMed:20361937, ECO:0000269|PubMed:35101446}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16754668}. Note=Internalized to
CC the cytoplasm after exposure to kynurenic acid.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HC97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HC97-2; Sequence=VSP_045871;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in immune and
CC gastrointestinal tissues. {ECO:0000269|PubMed:16754668}.
CC -!- PTM: Multiply phosphorylated in clusters of serines and threonines in
CC the C-terminal tail (PubMed:35101446). Phosphorylation of Ser-300 and
CC Ser-303 is mediated by GRK5 and/or GRK6 (PubMed:37660910).
CC {ECO:0000269|PubMed:35101446, ECO:0000269|PubMed:37660910}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF027957; AAC52028.1; -; Genomic_DNA.
DR EMBL; AF089087; AAG17965.1; -; mRNA.
DR EMBL; AY275467; AAP32299.1; -; Genomic_DNA.
DR EMBL; AK172786; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR541765; CAG46564.1; -; mRNA.
DR EMBL; AC124862; AAX88945.1; -; Genomic_DNA.
DR EMBL; BC095500; AAH95500.1; -; mRNA.
DR EMBL; BC117453; AAI17454.2; -; mRNA.
DR EMBL; BC117455; AAI17456.2; -; mRNA.
DR CCDS; CCDS2541.1; -. [Q9HC97-1]
DR CCDS; CCDS56174.1; -. [Q9HC97-2]
DR RefSeq; NP_001182310.1; NM_001195381.1. [Q9HC97-2]
DR RefSeq; NP_001182311.1; NM_001195382.1. [Q9HC97-2]
DR RefSeq; NP_005292.2; NM_005301.3. [Q9HC97-1]
DR PDB; 8H8J; EM; 3.20 A; C=2-309.
DR PDBsum; 8H8J; -.
DR AlphaFoldDB; Q9HC97; -.
DR EMDB; EMD-34549; -.
DR SMR; Q9HC97; -.
DR BioGRID; 109117; 146.
DR IntAct; Q9HC97; 64.
DR MINT; Q9HC97; -.
DR STRING; 9606.ENSP00000411788; -.
DR BindingDB; Q9HC97; -.
DR ChEMBL; CHEMBL1293267; -.
DR DrugBank; DB00695; Furosemide.
DR DrugBank; DB11937; Kynurenic Acid.
DR DrugBank; DB11156; Pyrantel.
DR DrugCentral; Q9HC97; -.
DR GuidetoPHARMACOLOGY; 102; -.
DR TCDB; 9.A.14.13.8; the g-protein-coupled receptor (gpcr) family.
DR GlyCosmos; Q9HC97; 1 site, No reported glycans.
DR GlyGen; Q9HC97; 1 site.
DR iPTMnet; Q9HC97; -.
DR PhosphoSitePlus; Q9HC97; -.
DR BioMuta; GPR35; -.
DR DMDM; 68068087; -.
DR jPOST; Q9HC97; -.
DR MassIVE; Q9HC97; -.
DR PaxDb; 9606-ENSP00000411788; -.
DR PeptideAtlas; Q9HC97; -.
DR Antibodypedia; 34526; 259 antibodies from 30 providers.
DR DNASU; 2859; -.
DR Ensembl; ENST00000319838.10; ENSP00000322731.5; ENSG00000178623.13. [Q9HC97-1]
DR Ensembl; ENST00000403859.1; ENSP00000385140.1; ENSG00000178623.13. [Q9HC97-1]
DR Ensembl; ENST00000407714.2; ENSP00000384263.1; ENSG00000178623.13. [Q9HC97-1]
DR Ensembl; ENST00000430267.2; ENSP00000411788.2; ENSG00000178623.13. [Q9HC97-2]
DR Ensembl; ENST00000438013.3; ENSP00000415890.3; ENSG00000178623.13. [Q9HC97-1]
DR GeneID; 2859; -.
DR KEGG; hsa:2859; -.
DR MANE-Select; ENST00000407714.2; ENSP00000384263.1; NM_005301.5; NP_005292.2.
DR UCSC; uc002vzs.4; human. [Q9HC97-1]
DR AGR; HGNC:4492; -.
DR CTD; 2859; -.
DR DisGeNET; 2859; -.
DR GeneCards; GPR35; -.
DR HGNC; HGNC:4492; GPR35.
DR HPA; ENSG00000178623; Tissue enhanced (intestine).
DR MalaCards; GPR35; -.
DR MIM; 602646; gene.
DR neXtProt; NX_Q9HC97; -.
DR OpenTargets; ENSG00000178623; -.
DR Orphanet; 171; Primary sclerosing cholangitis.
DR PharmGKB; PA28880; -.
DR VEuPathDB; HostDB:ENSG00000178623; -.
DR eggNOG; ENOG502S0QN; Eukaryota.
DR GeneTree; ENSGT01040000240444; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q9HC97; -.
DR OMA; YMSISLI; -.
DR OrthoDB; 5133474at2759; -.
DR PhylomeDB; Q9HC97; -.
DR TreeFam; TF335578; -.
DR PathwayCommons; Q9HC97; -.
DR Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
DR SignaLink; Q9HC97; -.
DR SIGNOR; Q9HC97; -.
DR BioGRID-ORCS; 2859; 14 hits in 1150 CRISPR screens.
DR ChiTaRS; GPR35; human.
DR GenomeRNAi; 2859; -.
DR Pharos; Q9HC97; Tchem.
DR PRO; PR:Q9HC97; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9HC97; Protein.
DR Bgee; ENSG00000178623; Expressed in mucosa of transverse colon and 109 other cell types or tissues.
DR Genevisible; Q9HC97; HS.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016494; F:C-X-C chemokine receptor activity; IMP:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:1904456; P:negative regulation of neuronal action potential; IEA:Ensembl.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IMP:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR CDD; cd15164; 7tmA_GPR35-like; 1.
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; IPR044734; GPR35_7tmA.
DR PANTHER; PTHR24232; G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24232:SF54; G-PROTEIN COUPLED RECEPTOR 35; 1.
DR Pfam; PF00001; 7tm_1; 1.
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 1: Evidence at protein level;
KW 3D-structure; 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..309
FT /note="G-protein coupled receptor 35"
FT /id="PRO_0000069563"
FT TOPO_DOM 1..24
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..90
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..112
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..258
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35101446"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:35101446"
FT MOD_RES 300
FT /note="Phosphoserine; by GRK5 and GRK6"
FT /evidence="ECO:0000269|PubMed:35101446"
FT MOD_RES 303
FT /note="Phosphoserine; by GRK5 and GRK6"
FT /evidence="ECO:0000269|PubMed:35101446"
FT MOD_RES 307
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:35101446"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..162
FT /evidence="ECO:0000269|PubMed:36543774,
FT ECO:0007744|PDB:8H8J"
FT VAR_SEQ 1
FT /note="M -> MLSGSRAVPTPHRGSEELLKYMLHSPCVSLTM (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045871"
FT VARIANT 25
FT /note="A -> T (in dbSNP:rs35146537)"
FT /evidence="ECO:0000269|PubMed:11017071"
FT /id="VAR_013601"
FT VARIANT 29
FT /note="V -> I (in dbSNP:rs139197368)"
FT /evidence="ECO:0000269|PubMed:11017071"
FT /id="VAR_013602"
FT VARIANT 76
FT /note="V -> M (in dbSNP:rs13387859)"
FT /id="VAR_033467"
FT VARIANT 108
FT /note="T -> M (in dbSNP:rs3749171)"
FT /evidence="ECO:0000269|PubMed:11017071"
FT /id="VAR_013603"
FT VARIANT 125
FT /note="R -> S (in dbSNP:rs34778053)"
FT /evidence="ECO:0000269|PubMed:11017071"
FT /id="VAR_013604"
FT VARIANT 253
FT /note="T -> M (in dbSNP:rs12468485)"
FT /evidence="ECO:0000269|PubMed:11017071"
FT /id="VAR_013605"
FT VARIANT 294
FT /note="S -> R (in dbSNP:rs3749172)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9479505,
FT ECO:0000269|Ref.5"
FT /id="VAR_013606"
FT MUTAGEN 287
FT /note="S->A: About 40% loss of ARRB2 recruitment."
FT /evidence="ECO:0000269|PubMed:35101446"
FT MUTAGEN 300
FT /note="S->A: About 50% loss of ARRB2 recruitment."
FT /evidence="ECO:0000269|PubMed:35101446"
FT MUTAGEN 303
FT /note="S->A: Almost complete loss of ARRB2 recruitment."
FT /evidence="ECO:0000269|PubMed:35101446"
FT MUTAGEN 307
FT /note="T->A: About 75% loss of ARRB2 recruitment."
FT /evidence="ECO:0000269|PubMed:35101446"
FT CONFLICT 174
FT /note="A -> R (in Ref. 1; AAC52028)"
FT /evidence="ECO:0000305"
FT HELIX 17..44
FT /evidence="ECO:0007829|PDB:8H8J"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:8H8J"
FT HELIX 54..78
FT /evidence="ECO:0007829|PDB:8H8J"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:8H8J"
FT HELIX 87..118
FT /evidence="ECO:0007829|PDB:8H8J"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:8H8J"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:8H8J"
FT HELIX 130..157
FT /evidence="ECO:0007829|PDB:8H8J"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:8H8J"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:8H8J"
FT HELIX 181..197
FT /evidence="ECO:0007829|PDB:8H8J"
FT HELIX 206..240
FT /evidence="ECO:0007829|PDB:8H8J"
FT HELIX 250..266
FT /evidence="ECO:0007829|PDB:8H8J"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:8H8J"
FT TURN 272..277
FT /evidence="ECO:0007829|PDB:8H8J"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:8H8J"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:8H8J"
FT CONFLICT Q9HC97-2:13
FT /note="R -> H (in Ref. 4; AK172786)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34072 MW; 97734FB7231B26F0 CRC64;
MNGTYNTCGS SDLTWPPAIK LGFYAYLGVL LVLGLLLNSL ALWVFCCRMQ QWTETRIYMT
NLAVADLCLL CTLPFVLHSL RDTSDTPLCQ LSQGIYLTNR YMSISLVTAI AVDRYVAVRH
PLRARGLRSP RQAAAVCAVL WVLVIGSLVA RWLLGIQEGG FCFRSTRHNF NSMAFPLLGF
YLPLAVVVFC SLKVVTALAQ RPPTDVGQAE ATRKAARMVW ANLLVFVVCF LPLHVGLTVR
LAVGWNACAL LETIRRALYI TSKLSDANCC LDAICYYYMA KEFQEASALA VAPSAKAHKS
QDSLCVTLA
//
