ID A0A3P9C1S6_9CICH Unreviewed; 575 AA.
AC A0A3P9C1S6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=G protein-coupled receptor kinase {ECO:0000256|RuleBase:RU000308};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU000308};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005016072.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005016072.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005016072.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[beta-adrenergic receptor] + ATP = [beta-adrenergic receptor]-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:19429, Rhea:RHEA-COMP:11222,
CC Rhea:RHEA-COMP:11223, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216;
CC EC=2.7.11.15; Evidence={ECO:0000256|ARBA:ARBA00036224};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19430;
CC Evidence={ECO:0000256|ARBA:ARBA00036224};
CC -!- SUBCELLULAR LOCATION: Postsynapse {ECO:0000256|ARBA:ARBA00034110}.
CC Presynapse {ECO:0000256|ARBA:ARBA00034106}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. GPRK subfamily. {ECO:0000256|ARBA:ARBA00009793,
CC ECO:0000256|RuleBase:RU000308}.
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DR AlphaFoldDB; A0A3P9C1S6; -.
DR Ensembl; ENSMZET00005016585.1; ENSMZEP00005016072.1; ENSMZEG00005012038.1.
DR GeneTree; ENSGT00940000157699; -.
DR Proteomes; UP000265160; LG7.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0047696; F:beta-adrenergic receptor kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004703; F:G protein-coupled receptor kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01240; PH_GRK2_subgroup; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000239; GPCR_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR24355:SF18; G PROTEIN-COUPLED RECEPTOR KINASE; 1.
DR PANTHER; PTHR24355; G PROTEIN-COUPLED RECEPTOR KINASE/RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR00717; GPCRKINASE.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50132; RGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000308};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000308};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000308}.
FT DOMAIN 1..62
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 78..340
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 341..408
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 445..539
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 575 AA; 65916 MW; 1C88AE16BF542E0F CRC64;
MKELLSCSHP FSKKAVDHVQ SHLAKKQVPP NLFQPYIVEI CDSLRGNIFQ KFIESDKFTR
FCQWKNVELN IHLTMNDFSV HRIIGRGGFG EVYGCRKADT GKMYAMKCLD KKRIKMKQGE
TLALNERIML SLVSTGDCPF IVCMTYAFHT PDKLCFILDL MNGNGNCNLS LELVSSPTLY
PMLYRVISHI LHHPLHHSAY VYVLPQPANI LLDEHGHVRI SDLGLACDFS KKKPHASVGT
HGYMAPEVLQ KGTAYDSSAD WFSLGCMLFK LLRGHSPFRQ HKTKDKHEID RMTLTMNVEL
PDSFTAELKD LLEGLLQRDV SKRLGCQGRG ASEVKEHQFF KGIDWQQVYL QKYSPPLIPP
RGEVNAADAF DIGSFDEEDT KGIKLLDSDQ ELYKNFPLVI SERWQQEVAE TVYEAVNLDT
DKNEARKRAK NKQLGHEEDY ALGKDCIMHG YMLKLGNPFL TQWQRRYFYL FPNRVEWRGE
GDTRQNLLTM EQIVTVEETQ IKDKKCILLR IKGGKQFVLQ CESDPEFVQW KKELTEAFTE
AQKLLRRAPK VIGKGRAGVV ELSKPPLTHR NSNGL
//
