ID L5LZP7_MYODS Unreviewed; 676 AA.
AC L5LZP7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=G protein-coupled receptor kinase {ECO:0000256|RuleBase:RU000308};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU000308};
GN ORFNames=MDA_GLEAN10018473 {ECO:0000313|EMBL:ELK31475.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK31475.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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|RuleBase:RU000308}.
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DR EMBL; KB106121; ELK31475.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LZP7; -.
DR eggNOG; KOG0986; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
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 CDD; cd08747; RGS_GRK2_GRK3; 1.
DR Gene3D; 1.10.287.1270; -; 3.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24355:SF17; BETA-ADRENERGIC RECEPTOR KINASE 2; 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; SM00315; RGS; 1.
DR SMART; SM00220; S_TKc; 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; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 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|RuleBase:RU000308, ECO:0000313|EMBL:ELK31475.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000313|EMBL:ELK31475.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000308};
KW Transferase {ECO:0000256|RuleBase:RU000308}.
FT DOMAIN 55..176
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 192..454
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 546..640
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600239-51"
FT BINDING 221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 676 AA; 78053 MW; 1890B427A5B0BCC2 CRC64;
MNGSEGGFVA FSSSCDMLVA SCTGPPRPGP GPGRNLQPSI RSVMQKYLEE RNEITFDKIF
NQKIGFLLFK DFCLNEINEA VPQVKFYEEI KEYEKLDNEE DRLSRSRQIY DTYIMKELLS
CSHPFSKQAV DHVQYLLSKK QVTSALFQPY IEEICESLRG NIFQKFMESD KFTRFCQWKN
VELNIHLTMN DFSVHRIIGR GGFGEVYGCR KADTGKMYAM KCLDKKRIKM KQGETLALNE
RIMLSLVSTG DCPFIVCMTY AFHTPDKLCF ILDLMNGGDL HYHLSQHGVF SEKEMRFYAT
EIILGLEHMH HRFVVYRDLK PANILLDEYG HVRISDLGLA CDFSKKKPHA SVGTHGYMAP
EVLQKGTAYD SSADWFSLGC MLFKLLRGHS PFRQHKTKDK HEIDRMTLTV NADLPDVFSP
ELRSLLEGLL QREVGKRLGC RGGGSQEVKE HSFYPPPLIP PRGEVNAADA FDIGSFDEED
TRGIKLLDCD QELYKNFPLV ISERWQQEVV ETIYETVNSD TDKIEARKRA KNKQLGHEED
YAMGKDCIMH GYMLKLGNPF LTQWQRRYFY LFPNRLEWRG EGESRQNLLT MEQIMSVEET
QFKDKKCILL RIKGGKQFVL QCESDPEFVQ WKKELTETFT EAQRLLRRAP KFLNKPRAGT
VELSKPPLCH RSSNGL
//
