G protein-coupled receptor kinase 7B precursor - Xenopus laevis (African clawed frog)

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B6CZ18 (GRK7B_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 11, 2012. Version 31. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
G protein-coupled receptor kinase 7B
EC=2.7.11.14
EC=2.7.11.16

Gene names

Name:

grk7-b

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	550 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Retina-specific kinase involved in the shutoff of the photoresponse and adaptation to changing light conditions via cone opsin phosphorylation, including rhodopsin (RHO) By similarity.
Catalytic activity	ATP + [G-protein-coupled receptor] = ADP + [G-protein-coupled receptor] phosphate. ATP + [rhodopsin] = ADP + [rhodopsin] phosphate.
Subcellular location	Membrane; Lipid-anchor By similarity.
Tissue specificity	Retina, cones. Ref.1
Post-translational modification	Autophosphorylated in vitro at Ser-487 By similarity. Phosphorylation at Ser-36 is regulated by light and activated by cAMP. Ref.1
Miscellaneous	Although the protein is present in a diversity of vertebrates ranging from bony fish to mammals, the mouse and rat orthologous proteins do not exist.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain. Contains 1 RGS domain.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Methylation Phosphoprotein Prenylation
Gene Ontology (GO)
Biological_process	signal transduction Inferred from electronic annotation. Source: InterPro termination of G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW G-protein coupled receptor kinase activity Inferred from electronic annotation. Source: EC rhodopsin kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 547

547

G protein-coupled receptor kinase 7B

PRO_0000412818

Propeptide

548 – 550

Removed in mature form By similarity

PRO_0000412819

Regions

Domain

57 – 174

118

RGS

Domain

189 – 451

263

Protein kinase

Domain

452 – 517

AGC-kinase C-terminal

Nucleotide binding

195 – 203

ATP By similarity

Sites

Active site

314

Proton acceptor By similarity

Binding site

218

ATP By similarity

Amino acid modifications

Modified residue

547

Cysteine methyl ester Potential

Lipidation

547

S-geranylgeranyl cysteine Potential

Sequences

Sequence

Length

Mass (Da)

Tools

B6CZ18 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 86F610D8275855CF
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FASTA

550

62,493

        10         20         30         40         50         60 
MCDMGGLDNL IANTAYLQAR KSSEGDAKEL QKRRKSLSLP PPDVSRNEVK ETITLDYQSI 

        70         80         90        100        110        120 
CVEQPIGQRL FKDFLATVPE YKLAEDFLEE VKEWELEEGS AKEQLMEKLV SRRFKEPAEG 

       130        140        150        160        170        180 
SLNFLGKDLS SRIQQAQSKD MPELILLAKD SGNAFLMDAP FQDFQNSPFY DRFLQWKAFE 

       190        200        210        220        230        240 
RQPINQKYFY EFRILGKGGF GEVCAIQVKN TGQMYACKKL DKKRLKKKNG EKMALLEKEI 

       250        260        270        280        290        300 
LEKVHSPFIV SLAYAYETKT HLCLVMSLMN GGDLKFHIYN VGDKGVEIKR VIFYSAQICC 

       310        320        330        340        350        360 
GILHLHSLKI VYRDMKPENV LLDDHGNCRL SDLGLAVKVK EGKAITQRAG TNGYMAPEIL 

       370        380        390        400        410        420 
TDEDYSYPVD WFAMGCSIFE MIAAYTPFRD PKEKTSKEEL KRKTLEDEVV FPLPTFTEEA 

       430        440        450        460        470        480 
KDICRLFLAK KPQNRLGSRT NDDDPRKHAF FKSINFQRLE AGMVDPPFVP DPSVVYAKDI 

       490        500        510        520        530        540 
SDIADFSEVK GIEFDDKDAK LFKRFSTGAV PISWQKEIID TGLFDELNDP SREVTGGGNS 

       550 
GEKSGVCSIL

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References

[1]	"Phosphorylation of GRK7 by PKA in cone photoreceptor cells is regulated by light." Osawa S., Jo R., Weiss E.R. J. Neurochem. 107:1314-1324(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-36.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EU621674 mRNA. Translation: ACF28431.1.
RefSeq	NP_001131052.1. NM_001137580.1.
UniGene	Xl.85104.
3D structure databases
ProteinModelPortal	B6CZ18.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100192359.
KEGG	xla:100192359.
Organism-specific databases
CTD	100192359.
Xenbase	XB-GENE-6252064. grk7.
Phylogenomic databases
HOVERGEN	HBG004532.
KO	K00909.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR000239. GPCR_kinase. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR000342. Regulat_G_prot_signal. IPR016137. Regulat_G_prot_signal_superfam. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF00615. RGS. 1 hit. [Graphical view]
PRINTS	PR00717. GPCRKINASE.
SMART	SM00315. RGS. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF48097. Regulat_G_prot_signal_superfam. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS50132. RGS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GRK7B_XENLA

Accession

Primary (citable) accession number: B6CZ18

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	November 25, 2008
Last modified:	July 11, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents