ARBK2_BOVIN
ID ARBK2_BOVIN Reviewed; 688 AA.
AC P26818;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Beta-adrenergic receptor kinase 2;
DE Short=Beta-ARK-2;
DE EC=2.7.11.15 {ECO:0000250|UniProtKB:P26819};
DE AltName: Full=G-protein-coupled receptor kinase 3 {ECO:0000250|UniProtKB:P35626};
GN Name=GRK3 {ECO:0000250|UniProtKB:P35626}; Synonyms=ADRBK2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1869533; DOI=10.1016/s0021-9258(18)98568-6;
RA Benovic J.L., Onorato J.J., Arriza J.L., Stone W.C., Lohse M.,
RA Jenkins N.A., Gilbert D.J., Copeland N.G., Caron M.G., Lefkowitz R.J.;
RT "Cloning, expression, and chromosomal localization of beta-adrenergic
RT receptor kinase 2. A new member of the receptor kinase family.";
RL J. Biol. Chem. 266:14939-14946(1991).
CC -!- FUNCTION: Specifically phosphorylates the agonist-occupied form of the
CC beta-adrenergic and closely related receptors.
CC {ECO:0000250|UniProtKB:P26819}.
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:0000250|UniProtKB:P26819};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19430;
CC Evidence={ECO:0000250|UniProtKB:P26819};
CC -!- SUBUNIT: Interacts with GIT1. {ECO:0000250|UniProtKB:P26819}.
CC -!- SUBCELLULAR LOCATION: Postsynapse {ECO:0000250|UniProtKB:P26819}.
CC Presynapse {ECO:0000250|UniProtKB:P26819}.
CC -!- TISSUE SPECIFICITY: Ubiquitous; brain, spleen > heart, lung > kidney.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. GPRK subfamily. {ECO:0000305}.
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DR EMBL; M73216; AAA30406.1; -; mRNA.
DR PIR; A39336; A39336.
DR RefSeq; NP_776925.1; NM_174500.2.
DR AlphaFoldDB; P26818; -.
DR SMR; P26818; -.
DR STRING; 9913.ENSBTAP00000000005; -.
DR BindingDB; P26818; -.
DR ChEMBL; CHEMBL3711487; -.
DR PaxDb; P26818; -.
DR Ensembl; ENSBTAT00000000005; ENSBTAP00000000005; ENSBTAG00000000005.
DR GeneID; 282136; -.
DR KEGG; bta:282136; -.
DR CTD; 157; -.
DR VEuPathDB; HostDB:ENSBTAG00000000005; -.
DR VGNC; VGNC:53904; GRK3.
DR eggNOG; KOG0986; Eukaryota.
DR GeneTree; ENSGT00940000157699; -.
DR HOGENOM; CLU_000288_63_41_1; -.
DR InParanoid; P26818; -.
DR OMA; KHFSLTI; -.
DR OrthoDB; 1104340at2759; -.
DR BRENDA; 2.7.11.15; 908.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000000005; Expressed in monocyte and 104 other tissues.
DR ExpressionAtlas; P26818; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0098794; C:postsynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047696; F:beta-adrenergic receptor kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0004703; F:G protein-coupled receptor kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0002029; P:desensitization of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 2.30.29.30; -; 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 InterPro; IPR008271; Ser/Thr_kinase_AS.
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; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF56112; SSF56112; 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; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50132; RGS; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Synapse; Transferase;
KW Ubl conjugation.
FT CHAIN 1..688
FT /note="Beta-adrenergic receptor kinase 2"
FT /id="PRO_0000085631"
FT DOMAIN 54..175
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 191..453
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 454..521
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 558..652
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..190
FT /note="N-terminal"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 197..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 688 AA; 79804 MW; 820249EBD827D92F CRC64;
MADLEAVLAD VSYLMAMEKS KATPAARASK KIVLPEPSIR SVMQKYLEER HEITFDKIFN
QRIGFLLFKD FCLNEINEAV PQVKFYEEIK EYEKLENEED RLCRSRQIYD TYIMKELLSC
SHPFSKQAVE HVQSHLSKKQ VTSTLFQPYI EEICESLRGS IFQKFMESDK FTRFCQWKNV
ELNIHLTMND FSVHRIIGRG GFGEVYGCRK ADTGKMYAMK CLDKKRIKMK QGETLALNER
IMLSLVSTGD CPFIVCMTYA FHTPDKLCFI LDLMNGGDLH YHLSQHGVFS EKEMRFYATE
IILGLEHMHN RFVVYRDLKP ANILLDEHGH VRISDLGLAC DFSKKKPHAS VGTHGYMAPE
VLQKGTAYDS SADWFSLGCM LFKLLRGHSP FRQHKTKDKH EIDRMTLTMN VELPDVFSPE
LKSLLEGLLQ RDVSKRLGCH GGSAQELKTH DFFRGIDWQH VYLQKYPPPL IPPRGEVNAA
DAFDIGSFDE EDTKGIKLLD CDQELYKNFP LVISERWQQE VAETVYEAVN ADTDKIEARK
RAKNKQLGHE EDYALGRDCI VHGYMLKLGN PFLTQWQRRY FYLFPNRLEW RGEGESRQSL
LTMEQIVSVE ETQIKDKKCI LLRIKGGKQF VLQCESDPEF VQWKKELTET FMEAQRLLRR
APKFLNKSRS AVVELSKPPL CHRNSNGL
