ID M7BN75_CHEMY Unreviewed; 2328 AA.
AC M7BN75;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=[beta-adrenergic-receptor] kinase {ECO:0000256|ARBA:ARBA00012427};
DE EC=2.7.11.15 {ECO:0000256|ARBA:ARBA00012427};
GN ORFNames=UY3_05711 {ECO:0000313|EMBL:EMP37180.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP37180.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(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 TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. GPRK subfamily. {ECO:0000256|ARBA:ARBA00009793}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAFAC class
CC myosin-kinesin ATPase superfamily. Myosin family.
CC {ECO:0000256|ARBA:ARBA00006998}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KB523138; EMP37180.1; -; Genomic_DNA.
DR STRING; 8469.M7BN75; -.
DR eggNOG; KOG0161; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
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 GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd01386; MYSc_Myo18; 1.
DR CDD; cd05633; STKc_GRK3; 1.
DR Gene3D; 1.10.287.1270; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 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; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036064; MYSc_Myo18.
DR InterPro; IPR027417; P-loop_NTPase.
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 PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF8; UNCONVENTIONAL MYOSIN-XVIIIB; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00717; GPCRKINASE.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 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; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT DOMAIN 15..42
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 48..76
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 92..354
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 355..422
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 459..489
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 831..1634
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 597..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1698..1894
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1923..2056
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2112..2202
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 621..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600239-51"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 920..927
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2328 AA; 266026 MW; 3057DAAE258DC8D5 CRC64;
MATAALHKTP VSYNIKDYEK LDSEEERLSR SRQIYDTYIM KELLSCSHPY IEEICDSLRG
KIFQKFMESD RFTRFCQWKN VELNIHLTMN DFSVHRIIGR GGFGEVYGCR KADTGKMYAM
KCLDKKRIKM KQGETLALNE RIMLSLVSTG DCPFIVCMTY AFHTPDKLCF ILDLMNGGDL
HYHLSQHGVF SEKEMRFYAT EIILGLEHMH NRFVVYRDLK PANILLDEHG HVRISDLGLA
CDFSKKKPHA SVGTHGYMAP EVLQKGTAYD SSADWFSLGC MLFKLLRGHS PFRQHKTKDK
HEIDRMTLTV NVELPDSFSP ELKSLLEGLL QRDVSKRLGC QGSSAQEIKE HHFFKGIDWQ
QVYLQKYSPP LIPPRGEVNA ADAFDIGSFD EEDTKGIKLV DSDQELYKNF PLVISERWQQ
EVAETVYDAV NADTDKIEAR KRTKNKQLGH EEDYALGKDC IMHGYMLKLG NPFLTQWQRR
YFYLFPNRLE WRGEGESRNY AMLEKLQWEA AIGRGPRLLY STAQPPGKDN HHVQQFVTKD
ENILEVGGEM ASEGQLMQNG LNGEQHEGEV AAEIAPRKPL PFKRVVKRSN IMKATSLAPE
KAAATPKPGK TIPPDESKVA RLPSSEQSPK EQSKGENAPA GAPTTSKDFQ RHREDPAKEG
DALRRKCPES SGREKVVTKK QWEPQIKAEI KKGQGEIKEK PGEIKAEPVE INEEQGEVKE
EPVEIKEEQG EVKEKPGQIK EEPVENKKEP GEIKEPGEST DSDKVHDDVW YETEKVWLVQ
KDGFTLATVL KPDVGTPELP AGRVRIRLEA DNTVTEVDEE DIHRTNPSKL DYTEDLAALL
SLNESSIINT LQHRYQSQLC NTYAGPSLIA LKPSWATTSY SGKVFKGKRD SMPPHISSVA
QRAYWNLLMH RQDQAIVPLG RSGAGKTTCC QSALEYLVGA ARSVDNRVSV EKIQAMFTIL
KAFGTVTTCH NSTSTRFSMV MSLDFNATGR ITAAHLQTML LERVRVAQQP EGESNFNVFS
QMLAGLDMAH RTMLHLHQMA ESNSFGIGPC SKQNFWLQTK PKLHPNPGKV TVQLHGRVMG
TGMKHNEIGC TWSYGIKRTG NFAFSPEKQK ASVAFVQLQA AMETLGITVD EQTAIWRVLA
GIYHLGAAGA CKVGRKQFMK FEWANNAADV LGCDFEELTT AVFKHHLKQI IEQVTSGTSR
LSKDEERNAG PKMTGVECVE GMAAGLYEEL FAAVVSLINR SFSSSHLSMA SIMVVDTPGF
HNPRHQKKER AATFEELCHN YVHEQLQALF YKRTFMSELE RYREENVKVP FDLPELSPMA
TVAVVDQNSS QLQVPPGGQA EEPKGLLWIL DEEVLIPGSS DSVVLNRLCS YFAKKGTASE
EEGFLRKCEQ MLQFEIFHQL GKDPVRYDLT GWMNKAKLNL SAQNSIEVLQ QSKIDALKKL
FLLRSKMPLI CRSVAGLEGN SQQALQRTGC VRKTFTSSFA AVKKKSVCAQ IKLQMDALTN
LVKRSQIHFV HCLVPRVGAE GKPSQPCVTG EVGLTLDVPT LRVQLSGAQL LDALRLYRIG
YVDRMVLTQF RRRFQVLAQP VMKKYTSAYE IPDENKAIEE LFQVLDLEKK SVAVGHSQVF
LKPGIVSRLE KQREKLISQN MILLQAACKG FLSRQKFKRL KIQRLAIRCI QKNLAVFHVV
KDWPWWQLMS YVRPLLSVNI VEDQLRVKNE ELAVLRRKLE KSEQSRSELR QNTELLESKQ
ALEVERAERL RGSREIKELQ SKYDQVQKKL ESVEKQLEEA QQQIQLREIG ISGAAGEEEW
HMRFDCAQME ITFLRKRLAQ FEERLESELN CRKELEQKLS EVQSTYEVAK KVAQQMKRKC
KHLACDLEDT RVLMESLQSR NHELEKKQKK FDMQLAQALG ESAFEKSLRE KVTQENTTIR
WELGKLQQRL EQKDLETSDL NQRIAVLAIR VQELTSPEAW DKDAVAALRK KLWELESSAA
EQQKALSRHA NAVEQLEQLH MRLEMEIERM KQMHQKELED KEEELEDVRQ SCQRRLRQLE
MQLEQEFEEK QMVLHEKQDL EGLIGTLCEQ IGHRDFDVEK RLRRDLKRTH ALLADVQLLL
VTAGEPSPSV SKEELENVRS QVDEQLYQLQ HEKADLLKRI DEDQEDLNEL MTKHKALIAQ
SAVDITQIRE LQTQLEEVKK EKQSLQEKLQ AARARIAYVE QSMVERSIVS RQEALICDLE
NKLEFQSVQI KRFEMLVLRL RDSVIKMGEE LEKAVESEAR EKENTKYYQM RMEEMKADMN
ELVQRELEAS RRRMELAGFQ VDYKVLQLQS IPAVQTGACW PESLQALG
//
