G protein-coupled receptor kinase 7 precursor

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Q8WP15 (GRK7_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. 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 7
EC=2.7.11.14
EC=2.7.11.16

Alternative name(s):
G protein-coupled receptor kinase GRK7

Gene names

Name:

GRK7

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	553 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.
Enzyme regulation	Inhibited by phosphorylation of Ser-36 By similarity.
Subcellular location	Membrane; Lipid-anchor By similarity.
Post-translational modification	Autophosphorylated in vitro at Ser-490 By similarity. Phosphorylation at Ser-36 is regulated by light and activated by cAMP. Ref.2
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	protein autophosphorylation Inferred from electronic annotation. Source: Compara 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 – 550

550

G protein-coupled receptor kinase 7

PRO_0000024334

Propeptide

551 – 553

Removed in mature form By similarity

PRO_0000024335

Regions

Domain

56 – 176

121

RGS

Domain

191 – 454

264

Protein kinase

Domain

455 – 520

AGC-kinase C-terminal

Nucleotide binding

197 – 205

ATP By similarity

Sites

Active site

316

Proton acceptor By similarity

Binding site

220

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine; by PKA Ref.2

Modified residue

550

Cysteine methyl ester Potential

Lipidation

550

S-geranylgeranyl cysteine Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q8WP15 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 9BAD6E91BF31D33E
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FASTA

553

62,299

        10         20         30         40         50         60 
MVDMGGLDNL IANTAYLQAR KTSDADSKEL QRRRRSLMLP GPQSCEQLRQ AMPADFNSLC 

        70         80         90        100        110        120 
EQQPIGRRLF RDFLATVPAY QEAMGFLEEV QSWELAEEGP AKGSTLQALV ATCAVAPNPG 

       130        140        150        160        170        180 
QPHSFLSPAL VTKCQAATTD EERASLVEQA KAEAMAFLQD QPFREFLVSP FYDKFLQWKV 

       190        200        210        220        230        240 
FEMQPVSDKY FEEFRVLGKG GFGEVCAVQV KNTGKMYACK KLDKKRLKKK SGEKMALSEK 

       250        260        270        280        290        300 
EILEKVSSPF VVSLAYAFES KSHLCLVMSL MNGGDLKFHI YSVGERGLDM NRVIFYSAQM 

       310        320        330        340        350        360 
TCGVLHLHSL GIVYRDLKPE NVLLDDLGNC RLSDLGLAVQ IQDGKPVTQR AGTNGYMAPE 

       370        380        390        400        410        420 
ILMEKASYSY PVDWFAMGCS IYEMVAGRTP FKDYKEKISK EDLKQRTLKE EVRFQHQSFT 

       430        440        450        460        470        480 
EEAKDICRLF LAKTPEQRLG SREKSDDPRK HHFFKTINFP RLEAGLVDPP FVPDPSVVYA 

       490        500        510        520        530        540 
KDVDEIEDFS EVRGVEFDDK DKQFFQRFAT GAVPIAWQEE IIETGLFEEL NDPNRPAGCG 

       550 
EGNSSRSGVC LLL

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References

[1]	"Species-specific differences in expression of G-protein-coupled receptor kinase (GRK) 7 and GRK1 in mammalian cone photoreceptor cells: implications for cone cell phototransduction." Weiss E.R., Ducceschi M.H., Horner T.J., Li A., Craft C.M., Osawa S. J. Neurosci. 21:9175-9184(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[2]	"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: PHOSPHORYLATION AT SER-36.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF282270 mRNA. Translation: AAL33881.1.
RefSeq	NP_999212.1. NM_214047.1.
UniGene	Ssc.165.
3D structure databases
ProteinModelPortal	Q8WP15.
ModBase	Search...
Protein-protein interaction databases
STRING	9823.ENSSSCP00000012443.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSSSCT00000012780; ENSSSCP00000012443; ENSSSCG00000011675.
GeneID	397114.
KEGG	ssc:397114.
Organism-specific databases
CTD	131890.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00550000074318.
HOGENOM	HOG000006742.
HOVERGEN	HBG004532.
KO	K00909.
OMA	ESKSHLC.
OrthoDB	EOG4TTGJ1.
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

GRK7_PIG

Accession

Primary (citable) accession number: Q8WP15

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	March 1, 2002
Last modified:	April 3, 2013
This is version 75 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

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents