Reviewed, UniProtKB/Swiss-Prot Q8BZ03 (KPCD2_MOUSE)

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	875 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Calcium-independent, phospholipid-dependent, serine- and threonine-specific protein kinase By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by diacylglycerol and phorbol esters.
Post-translational modification	Autophosphorylated. Phorbol esters stimulates autophosphorylation. 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.

Ontologies

Keywords
Domain	Phorbol-ester binding Repeat Zinc-finger
Ligand	ATP-binding 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
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW diacylglycerol 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...

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_0000260436
Regions
	Domain	398 – 510	113	PH
	Domain	552 – 808	257	Protein kinase
	Zinc finger	138 – 188	51	Phorbol-ester/DAG-type 1
	Zinc finger	265 – 315	51	Phorbol-ester/DAG-type 2
	Nucleotide binding	558 – 566	9	ATP By similarity
Sites
	Active site	675	1	Proton acceptor By similarity
	Binding site	581	1	ATP By similarity
Amino acid modifications
	Modified residue	197	1	Phosphoserine By similarity
	Modified residue	198	1	Phosphoserine By similarity
	Modified residue	200	1	Phosphoserine Ref.3
	Modified residue	203	1	Phosphoserine By similarity
	Modified residue	206	1	Phosphoserine By similarity
	Modified residue	211	1	Phosphoserine Ref.3
	Modified residue	212	1	Phosphoserine Ref.3
	Modified residue	214	1	Phosphoserine Ref.3
	Modified residue	376	1	Phosphoserine By similarity
	Modified residue	397	1	Phosphoserine By similarity
	Modified residue	519	1	Phosphoserine By similarity
	Modified residue	707	1	Phosphoserine By similarity
	Modified residue	711	1	Phosphoserine By similarity
	Modified residue	873	1	Phosphoserine; by autocatalysis By similarity
Experimental info
	Sequence conflict	213	1	E → G in BAE42012. Ref.1
	Sequence conflict	220	1	E → G in BAE41652. Ref.1
	Sequence conflict	310	1	R → H in BAE32326. Ref.1
	Sequence conflict	310	1	R → H in BAE41652. Ref.1
	Sequence conflict	630	1	K → N in BAE42012. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8BZ03-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: C7173546FA1E6DB1	FASTA	875	96,542
	10 20 30 40 50 60 MAAAPSHPAG LPGSPGPGSP PPPGGLDLQS PPPLLPQIPA 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 ISDELEDSGV IPGSHSESAL 370 380 390 400 410 420 HASEEEEGEG HKAQSSLGYI PLMRVVQSVR HTTRKSSTTL REGWVVHYSN KDTLRKRHYW 430 440 450 460 470 480 RLDCKCITLF QNNTTNRYYK EIPLSEILAV EPAQNFSLVP PGTNPHCFEI ITANVTYFVG 490 500 510 520 530 540 ETPGGAPGGP SGQGTEAVRG 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 FVAERHGTPA EGDLGGACLP QDHEMQGLAE RISIL

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Thymus and Vagina.
[2]	"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]. Strain: FVB/N. Tissue: Colon and Mammary tumor.
[3]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-211; SER-212 AND SER-214, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK037030 mRNA. Translation: BAC29677.1. AK154029 mRNA. Translation: BAE32326.1. AK170236 mRNA. Translation: BAE41652.1. AK170761 mRNA. Translation: BAE42012.1. BC095949 mRNA. Translation: AAH95949.1. BC096444 mRNA. Translation: AAH96444.1.
IPI	IPI00227209.
RefSeq	NP_849231.1.
UniGene	Mm.1881
3D structure databases
HSSP	HSSP built from PDB template 1NY3 based on UniProtKB P49137.
SMR	Q8BZ03. Positions 396-510.
ModBase	Search...
PTM databases
PhosphoSite	Q8BZ03.
Genome annotation databases
Ensembl	ENSMUSG00000041187. Mus musculus. [Contig view]
GeneID	101540.
KEGG	mmu:101540.
Organism-specific databases
MGI	MGI:2141917. Prkd2.
Phylogenomic databases
HOVERGEN	Q8BZ03.
OMA	Q8BZ03. LDCKCIT.
Enzyme and pathway databases
BRENDA	2.7.11.13. 244.
Gene expression databases
ArrayExpress	Q8BZ03.
Bgee	Q8BZ03.
CleanEx	MM_PRKD2.
GermOnline	ENSMUSG00000041187. Mus musculus.
Family and domain databases
InterPro	IPR002219. DAG_PE_bd. IPR011993. PH_type. IPR001849. Pleckstrin_homology. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR015727. Protein_Kinase_C_mu-related. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [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]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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	355000.
SOURCE	Search...

Entry information

Entry name

KPCD2_MOUSE

Accession

Primary (citable) accession number: Q8BZ03
Secondary accession number(s): Q3TCE5, Q3TDF0, Q3U4V4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)