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GRK7B_DANRE
ID   GRK7B_DANRE             Reviewed;         548 AA.
AC   Q1XHL7;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Rhodopsin kinase grk7-b;
DE            EC=2.7.11.14 {ECO:0000269|PubMed:16787417};
DE   AltName: Full=G protein-coupled receptor kinase 7-2;
DE   AltName: Full=G protein-coupled receptor kinase 7B;
DE   Flags: Precursor;
GN   Name=grk7b; Synonyms=grk7-2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=16787417; DOI=10.1111/j.1471-4159.2006.03920.x;
RA   Wada Y., Sugiyama J., Okano T., Fukada Y.;
RT   "GRK1 and GRK7: unique cellular distribution and widely different
RT   activities of opsin phosphorylation in the zebrafish rods and cones.";
RL   J. Neurochem. 98:824-837(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Retina-specific kinase involved in the shutoff of the
CC       photoresponse and adaptation to changing light conditions via cone
CC       opsin phosphorylation, including rhodopsin (RHO).
CC       {ECO:0000269|PubMed:16787417}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[rhodopsin] = ADP + H(+) + O-phospho-L-
CC         threonyl-[rhodopsin]; Xref=Rhea:RHEA:56552, Rhea:RHEA-COMP:14596,
CC         Rhea:RHEA-COMP:14597, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.14; Evidence={ECO:0000269|PubMed:16787417};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[rhodopsin] = ADP + H(+) + O-phospho-L-seryl-
CC         [rhodopsin]; Xref=Rhea:RHEA:23356, Rhea:RHEA-COMP:14594, Rhea:RHEA-
CC         COMP:14595, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.14;
CC         Evidence={ECO:0000269|PubMed:16787417};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8WMV0}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:Q8WMV0}.
CC   -!- TISSUE SPECIFICITY: Expressed in the eyes (at protein level). Expressed
CC       in the eyes, the pineal gland and in the brain.
CC       {ECO:0000269|PubMed:16787417}.
CC   -!- PTM: Phosphorylation at Ser-33 is regulated by light and activated by
CC       cAMP. {ECO:0000250|UniProtKB:B6CZ18}.
CC   -!- MISCELLANEOUS: Although the protein is present in a diversity of
CC       vertebrates ranging from bony fish to mammals, the mouse and rat
CC       orthologous proteins do not exist.
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; AB212996; BAE92859.1; -; mRNA.
DR   EMBL; BC162212; AAI62212.1; -; mRNA.
DR   EMBL; BC162221; AAI62221.1; -; mRNA.
DR   AlphaFoldDB; Q1XHL7; -.
DR   SMR; Q1XHL7; -.
DR   STRING; 7955.ENSDARP00000072364; -.
DR   PaxDb; Q1XHL7; -.
DR   PRIDE; Q1XHL7; -.
DR   Ensembl; ENSDART00000077898; ENSDARP00000072364; ENSDARG00000055534.
DR   ZFIN; ZDB-GENE-030904-3; grk7b.
DR   eggNOG; KOG0986; Eukaryota.
DR   GeneTree; ENSGT00940000160511; -.
DR   HOGENOM; CLU_000288_63_41_1; -.
DR   InParanoid; Q1XHL7; -.
DR   OMA; TLEDECQ; -.
DR   PhylomeDB; Q1XHL7; -.
DR   TreeFam; TF313940; -.
DR   BRENDA; 2.7.11.14; 928.
DR   PRO; PR:Q1XHL7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 18.
DR   Bgee; ENSDARG00000055534; Expressed in retina and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004703; F:G protein-coupled receptor kinase activity; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0050254; F:rhodopsin kinase activity; IDA:ZFIN.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.167.10; -; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000239; GPCR_kinase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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; PF00069; Pkinase; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR00717; GPCRKINASE.
DR   SMART; SM00315; RGS; 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; 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   1: Evidence at protein level;
KW   ATP-binding; Kinase; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome;
KW   Sensory transduction; Serine/threonine-protein kinase; Transferase; Vision.
FT   CHAIN           1..545
FT                   /note="Rhodopsin kinase grk7-b"
FT                   /id="PRO_0000412814"
FT   PROPEP          546..548
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000412815"
FT   DOMAIN          53..172
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   DOMAIN          187..446
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          447..512
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   REGION          520..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        312
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         193..201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         33
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:B6CZ18"
FT   MOD_RES         545
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           545
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        47
FT                   /note="V -> A (in Ref. 1; BAE92859 and 2; AAI62212)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="N -> D (in Ref. 1; BAE92859 and 2; AAI62212/
FT                   AAI62221)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        412
FT                   /note="R -> Q (in Ref. 1; BAE92859 and 2; AAI62212/
FT                   AAI62221)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        504
FT                   /note="V -> A (in Ref. 1; BAE92859 and 2; AAI62212/
FT                   AAI62221)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   548 AA;  62609 MW;  939D0B13095FECF2 CRC64;
     MSDMGGLKNL VANTDYLKAQ SLDEKEIKKR RCSLGLPHLG NCTDVRVSVS KGFEDICEQQ
     PIGRACFRQF LSVSSPEYLA AAELLDELNC WNLAEAEAKE EARLNIINKF CKADSKSFLA
     FLTEDEAEKC KAVSEKDFEE VMMGQVKEAT QKFLRGQPFE EYQTSLFFDR FVQWKKFEKQ
     PITDKYFYEF RTLGKGGFGE VCGVQVKTTG QMYACKKLDK KRLKKKSGEK MALLEKKILE
     MVNSLFIVNL AYAFDTKTHL CLVMTLMSGG DLKYHIFHVG EVGIEMERII HYTAQITSGI
     LHLHSMDIVY RDMKPENVLL DCQGQCRLSD LGLAVELPNG KTTTQKAGTK GYMAPEILKQ
     EPYRTSVDWW ALGCSIYEMV AGRVPFRDHK EKVAKEELLR RTLEDEVKFE HRNFDAPSKD
     IISLFLKRNI EDRLGSNDDP RKHEFFKSIN FPRLEAGLIP PPWEPKANVV YAKDTGDIRE
     FSDVKGVKFD ANDEKFFKEF STGVVPIAWQ QEMIDSGLFD ELSDPNRKES AAGLEDEEQQ
     KSKSCTLL
 
 
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