G protein-coupled receptor kinase 7B precursor

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Q1XHL7 (GRK7B_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 57. 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

Alternative name(s):
G protein-coupled receptor kinase 7-2

Gene names

Name:	grk7b
Synonyms:	grk7-2

Organism

Danio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]

Taxonomic identifier

7955 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length	548 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). Ref.1
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	Expressed in the eyes (at protein level). Expressed in the eyes, the pineal gland and in the brain. Ref.1
Post-translational modification	Phosphorylation at Ser-33 is regulated by light and activated by cAMP By similarity.
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
Technical term	Complete proteome Reference proteome
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 – 545

545

G protein-coupled receptor kinase 7B

PRO_0000412814

Propeptide

546 – 548

Removed in mature form By similarity

PRO_0000412815

Regions

Domain

53 – 172

120

RGS

Domain

187 – 446

260

Protein kinase

Domain

447 – 512

AGC-kinase C-terminal

Nucleotide binding

193 – 201

ATP By similarity

Sites

Active site

312

Proton acceptor By similarity

Binding site

216

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine; by PKA

Modified residue

545

Cysteine methyl ester Potential

Lipidation

545

S-geranylgeranyl cysteine Potential

Experimental info

Sequence conflict

V → A in BAE92859. Ref.1

Sequence conflict

V → A in AAI62212. Ref.2

Sequence conflict

339

N → D in BAE92859. Ref.1

Sequence conflict

339

N → D in AAI62212. Ref.2

Sequence conflict

339

N → D in AAI62221. Ref.2

Sequence conflict

412

R → Q in BAE92859. Ref.1

Sequence conflict

412

R → Q in AAI62212. Ref.2

Sequence conflict

412

R → Q in AAI62221. Ref.2

Sequence conflict

504

V → A in BAE92859. Ref.1

Sequence conflict

504

V → A in AAI62212. Ref.2

Sequence conflict

504

V → A in AAI62221. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q1XHL7 [UniParc].

Last modified September 21, 2011. Version 2.
Checksum: 939D0B13095FECF2
Show »

FASTA

548

62,609

        10         20         30         40         50         60 
MSDMGGLKNL VANTDYLKAQ SLDEKEIKKR RCSLGLPHLG NCTDVRVSVS KGFEDICEQQ 

        70         80         90        100        110        120 
PIGRACFRQF LSVSSPEYLA AAELLDELNC WNLAEAEAKE EARLNIINKF CKADSKSFLA 

       130        140        150        160        170        180 
FLTEDEAEKC KAVSEKDFEE VMMGQVKEAT QKFLRGQPFE EYQTSLFFDR FVQWKKFEKQ 

       190        200        210        220        230        240 
PITDKYFYEF RTLGKGGFGE VCGVQVKTTG QMYACKKLDK KRLKKKSGEK MALLEKKILE 

       250        260        270        280        290        300 
MVNSLFIVNL AYAFDTKTHL CLVMTLMSGG DLKYHIFHVG EVGIEMERII HYTAQITSGI 

       310        320        330        340        350        360 
LHLHSMDIVY RDMKPENVLL DCQGQCRLSD LGLAVELPNG KTTTQKAGTK GYMAPEILKQ 

       370        380        390        400        410        420 
EPYRTSVDWW ALGCSIYEMV AGRVPFRDHK EKVAKEELLR RTLEDEVKFE HRNFDAPSKD 

       430        440        450        460        470        480 
IISLFLKRNI EDRLGSNDDP RKHEFFKSIN FPRLEAGLIP PPWEPKANVV YAKDTGDIRE 

       490        500        510        520        530        540 
FSDVKGVKFD ANDEKFFKEF STGVVPIAWQ QEMIDSGLFD ELSDPNRKES AAGLEDEEQQ 


KSKSCTLL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"GRK1 and GRK7: unique cellular distribution and widely different activities of opsin phosphorylation in the zebrafish rods and cones." Wada Y., Sugiyama J., Okano T., Fukada Y. J. Neurochem. 98:824-837(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, FUNCTION.
[2]	NIH - Zebrafish Gene Collection (ZGC) project Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB212996 mRNA. Translation: BAE92859.1. BC162212 mRNA. Translation: AAI62212.1. BC162221 mRNA. Translation: AAI62221.1.
IPI	IPI00609859.
UniGene	Dr.88577.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSDART00000077898; ENSDARP00000072364; ENSDARG00000055534.
Organism-specific databases
ZFIN	ZDB-GENE-030904-3. grk7b.
Phylogenomic databases
GeneTree	ENSGT00550000074318.
HOVERGEN	HBG004532.
InParanoid	Q1XHL7.
Enzyme and pathway databases
BRENDA	2.7.11.14. 96826.
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_DANRE

Accession

Primary (citable) accession number: Q1XHL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	September 21, 2011
Last modified:	April 3, 2013
This is version 57 of the entry and version 2 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents