Serine/threonine-protein kinase D2 - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot Q5XIS9 (KPCD2_RAT)

Last modified February 9, 2010. Version 61. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase D2
    EC=2.7.11.13
Alternative name(s):
    nPKC-D2

Gene names

Name:

Prkd2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	875 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domains bind DAG, mediating translocation to membranes. Autophosphorylation of Ser-711 and phosphorylation of Ser-707 by PKC relieves auto-inhibition by the PH domain By similarity.
Subcellular location	Cytoplasm By similarity. Membrane By similarity. Note: Translocation to the cell membrane is required for kinase activation By similarity.
Post-translational modification	Phosphorylation of Ser-873 correlates with the activation status of the kinase By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily. Contains 1 PH domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain.

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Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Domain	Repeat Zinc-finger
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase C activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 875

875

Serine/threonine-protein kinase D2

PRO_0000260437

Regions

Domain

398 – 510

113

Domain

552 – 808

257

Protein kinase

Zinc finger

138 – 188

Phorbol-ester/DAG-type 1

Zinc finger

265 – 315

Phorbol-ester/DAG-type 2

Nucleotide binding

558 – 566

ATP By similarity

Sites

Active site

675

Proton acceptor By similarity

Binding site

581

ATP By similarity

Amino acid modifications

Modified residue

189

Phosphoserine By similarity

Modified residue

197

Phosphoserine By similarity

Modified residue

198

Phosphoserine By similarity

Modified residue

199

Phosphothreonine By similarity

Modified residue

200

Phosphoserine By similarity

Modified residue

203

Phosphoserine By similarity

Modified residue

206

Phosphoserine By similarity

Modified residue

211

Phosphoserine Ref.2

Modified residue

212

Phosphoserine By similarity

Modified residue

214

Phosphoserine Ref.2

Modified residue

225

Phosphoserine By similarity

Modified residue

227

Phosphothreonine By similarity

Modified residue

236

Phosphoserine By similarity

Modified residue

237

Phosphoserine By similarity

Modified residue

238

Phosphoserine By similarity

Modified residue

339

Phosphoserine By similarity

Modified residue

354

Phosphoserine By similarity

Modified residue

363

Phosphoserine By similarity

Modified residue

375

Phosphoserine By similarity

Modified residue

376

Phosphoserine By similarity

Modified residue

397

Phosphoserine By similarity

Modified residue

519

Phosphoserine By similarity

Modified residue

707

Phosphoserine; by PKC By similarity

Modified residue

711

Phosphoserine; by autocatalysis By similarity

Modified residue

718

Phosphotyrosine By similarity

Modified residue

873

Phosphoserine; by autocatalysis By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q5XIS9-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 789FD9853EEDF6A1
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FASTA

875

96,497

        10         20         30         40         50         60 
MAAAPSHPAG LPCSPGPGSP PPPGGSDLQS LPPLLPQIPA PGSGVSFHIQ IGLTREFVLL 

        70         80         90        100        110        120 
PAASELAHVK QLACSIVDQK FPECGFYGLY DKILLFKHDP TSANLLQLVR SAADIQEGDL 

       130        140        150        160        170        180 
VEVVLSASAT FEDFQIRPHA LTVHSYRAPA FCDHCGEMLF GLVRQGLKCD GCGLNYHKRC 

       190        200        210        220        230        240 
AFSIPNNCSG ARKRRLSSTS LASGHSVRLG SSESLPCTAE ELSRSTTDLL PRRPPSSSSS 

       250        260        270        280        290        300 
SSSSSFYTGR PIELDKMLMS KVKVPHTFLI HSYTRPTVCQ ACKKLLKGLF RQGLQCKDCK 

       310        320        330        340        350        360 
FNCHKRCATR VPNDCLGEAL INGDVPMEEA ADYSEADKSS LSDELEDSGV IPGSHAENAL 

       370        380        390        400        410        420 
HASEEEEGEG GKAQSSLGYI PLMRVVQSVR HTTRKSSTTL REGWVVHYSN KDTLRKRHYW 

       430        440        450        460        470        480 
RLDCKCITLF QNNTTNRYYK EIPLSEILAV EPAQNFSLVP PGTNPHCFEI ITANVTYFVG 

       490        500        510        520        530        540 
ETPGGAPGGP SGQGTEAARG WETAIRQALM PVILQDAPSA PGHTPHRQAS LSISVSNSQI 

       550        560        570        580        590        600 
QENVDIATVY QIFPDEVLGS GQFGVVYGGK HRKTGRDVAV KVIDKLRFPT KQESQLRNEV 

       610        620        630        640        650        660 
AILQSLRHPG IVNLECMFET PEKVFVVMEK LHGDMLEMIL SSEKGRLPER LTKFLITQIL 

       670        680        690        700        710        720 
VALRHLHFKN IVHCDLKPEN VLLASADPFP QVKLCDFGFA RIIGEKSFRR SVVGTPAYLA 

       730        740        750        760        770        780 
PEVLLNQGYN RSLDMWSVGV IMYVSLSGTF PFNEDEDIND QIQNAAFMYP ASPWSHISSG 

       790        800        810        820        830        840 
AIDLINNLLQ VKMRKRYSVD KSLSHPWLQE YQTWLDLREL EGKMGERYIT HESDDARWDQ 

       850        860        870 
FVSERHGTPA EGDLGGACLP QDHEMQGLAE RISIL

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References

[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[2]	"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed: 16641100] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-214, MASS SPECTROMETRY. Tissue: Kidney.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	BC083592 mRNA. Translation: AAH83592.1.
IPI	IPI00364038.
RefSeq	NP_001013917.1.
UniGene	Rn.15035
3D structure databases
HSSP	HSSP built from PDB template 2COA based on UniProtKB Q9BZL6.
SMR	Q5XIS9. Positions 130-192, 263-315, 396-510, 542-812.
ModBase	Search...
PTM databases
PhosphoSite	Q5XIS9.
Genome annotation databases
Ensembl	ENSRNOT00000022360; ENSRNOP00000022360; ENSRNOG00000016434; Rattus norvegicus. [Genome view]
GeneID	292658.
KEGG	rno:292658.
NMPDR	fig\|10116.3.peg.1129.
UCSC	NM_001013895. rat.
Organism-specific databases
CTD	292658.
RGD	1308054. Prkd2.
Phylogenomic databases
eggNOG	maNOG12873.
HOVERGEN	Q5XIS9.
InParanoid	Q5XIS9.
OMA	ASPWSHI.
OrthoDB	EOG9FXTT2.
PhylomeDB	Q5XIS9.
Enzyme and pathway databases
BRENDA	2.7.11.13. 248.
Gene expression databases
ArrayExpress	Q5XIS9.
Genevestigator	Q5XIS9.
GermOnline	ENSRNOG00000016434. Rattus norvegicus.
Family and domain databases
InterPro	IPR020454. DAG/PE_bd. IPR011009. Kinase-like_dom. IPR011993. PH_type. IPR001849. Pleckstrin_homology. IPR002219. Prot_Kinase_C-like_PE/DAG_bd. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR015727. Protein_Kinase_C_mu-related. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
PANTHER	PTHR22968. PKC_mu_like. 1 hit.
Pfam	PF00130. C1_1. 2 hits. PF00169. PH. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR00008. DAGPEDOMAIN.
SMART	SM00109. C1. 2 hits. SM00233. PH. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS50003. PH_DOMAIN. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS00479. ZF_DAG_PE_1. 2 hits. PS50081. ZF_DAG_PE_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	634460.

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Entry information

Entry name

KPCD2_RAT

Accession

Primary (citable) accession number: Q5XIS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	November 23, 2004
Last modified:	February 9, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

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

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents