Q9WTQ1 (KPCD1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase D1
EC=2.7.11.13

Alternative name(s):
Protein kinase C mu type
Protein kinase D
nPKC-D1
nPKC-mu

Gene names

Name:	Prkd1
Synonyms:	Pkcm, Pkd, Prkcm

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	918 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-469 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor. Ref.3 Ref.4 Ref.6 Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domain 1 binds DAG with high affinity and appears to play the dominant role in mediating translocation to the cell membrane and trans-Golgi network. Phorbol-ester/DAG-type domain 2 binds phorbol ester with higher affinity. Autophosphorylation of Ser-748 and phosphorylation of Ser-744 by PKC relieves auto-inhibition by the PH domain. Phosphorylation on Tyr-469 by the SRC-ABL1 pathway in response to oxidative stress, is also required for activation. Activated by DAPK1 under oxidative stress By similarity.
Subunit structure	Interacts (via N-terminus) with ADAP1/CENTA1. Interacts with MAPK13 and SRC By similarity. Interacts with DAPK1 in an oxidative stress-regulated manner By similarity.
Subcellular location	Cytoplasm By similarity. Cell membrane By similarity. Golgi apparatus › trans-Golgi network By similarity. Note: Translocation to the cell membrane is required for kinase activation By similarity.
Post-translational modification	Phosphorylated at Ser-403 and Ser-407 by MAPK13 during regulation of insulin secretion in pancreatic beta cells. Phosphorylated by DAPK1. Phosphorylated by ABL at Tyr-469, which primes the kinase in response to oxidative stress, and promotes a second step activating phosphorylation at Ser-744/Ser-748 by PKRD By similarity. Ref.5
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
Biological process	Angiogenesis Apoptosis Differentiation Immunity Inflammatory response Innate immunity Neurogenesis
Cellular component	Cell membrane Cytoplasm Golgi apparatus Membrane
Domain	Repeat Zinc-finger
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi organization Inferred from sequence or structural similarity. Source: UniProtKB Golgi vesicle transport Inferred from sequence or structural similarity. Source: UniProtKB angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular response to oxidative stress Inferred from sequence or structural similarity. Source: UniProtKB cellular response to vascular endothelial growth factor stimulus Inferred from sequence or structural similarity. Source: UniProtKB inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW intracellular protein kinase cascade Inferred from electronic annotation. Source: Compara intracellular signal transduction Inferred from direct assay PubMed 12057008. Source: RGD negative regulation of cell death Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-serine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of CREB transcription factor activity Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of blood vessel endothelial cell migration Inferred from electronic annotation. Source: Compara positive regulation of endothelial cell chemotaxis Inferred from electronic annotation. Source: Compara positive regulation of endothelial cell migration Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of osteoblast differentiation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara regulation of keratinocyte proliferation Inferred from sequence or structural similarity. Source: UniProtKB vascular endothelial growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell cell cortex Inferred from electronic annotation. Source: Compara cell-cell junction Inferred from electronic annotation. Source: Compara cytosol Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB trans-Golgi network Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid binding Inferred from electronic annotation. Source: InterPro protein kinase C activity Inferred from electronic annotation. Source: EC protein serine/threonine kinase activity Inferred from direct assay PubMed 12057008. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 918	918	Serine/threonine-protein kinase D1		PRO_0000333881
Regions
	Domain	428 – 547	120	PH
	Domain	589 – 845	257	Protein kinase
	Zinc finger	144 – 194	51	Phorbol-ester/DAG-type 1
	Zinc finger	276 – 326	51	Phorbol-ester/DAG-type 2
	Nucleotide binding	595 – 603	9	ATP By similarity
	Compositional bias	16 – 26	11	Poly-Ala
	Compositional bias	198 – 201	4	Poly-Arg
Sites
	Active site	712	1	Proton acceptor By similarity
	Binding site	618	1	ATP By similarity
Amino acid modifications
	Modified residue	93	1	Phosphotyrosine By similarity
	Modified residue	203	1	Phosphoserine By similarity
	Modified residue	206	1	Phosphoserine By similarity
	Modified residue	253	1	Phosphoserine By similarity
	Modified residue	351	1	Phosphoserine By similarity
	Modified residue	403	1	Phosphoserine; by MAPK13 By similarity
	Modified residue	407	1	Phosphoserine; by MAPK13 By similarity
	Modified residue	438	1	Phosphotyrosine By similarity
	Modified residue	454	1	Phosphoserine By similarity
	Modified residue	469	1	Phosphotyrosine; by ABL By similarity
	Modified residue	508	1	Phosphotyrosine By similarity
	Modified residue	744	1	Phosphoserine; by PKC/PRKCD By similarity
	Modified residue	748	1	Phosphoserine; by autocatalysis and PKC/PRKCD By similarity
	Modified residue	916	1	Phosphoserine; by autocatalysis Ref.5
Experimental info
	Sequence conflict	718	1	V → G in BAA78373. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9WTQ1 [UniParc]. Last modified May 20, 2008. Version 2. Checksum: 93E46AF6C0242B86	FASTA	918	102,043
	10 20 30 40 50 60 MSAPPLLRPP SPLLPAAAAV AAAAAALVPG SGPAPFPAPG AAPAGGISFH LQIGLSREPV 70 80 90 100 110 120 LLLQDSSGDY SLAHVREMAC SIVDQKFPEC GFYGLYDKIL LFRHDPASEN ILQLVKIASD 130 140 150 160 170 180 IQEGDLIEVV LSASATFEDF QIRPHALFVH SYRAPAFCDH CGEMLWGLVR QGLKCEGCGL 190 200 210 220 230 240 NYHKRCAFKI PNNCSGVRRR RLSNVSLTGL GTVRTASAEF STSAPDEPLL SPVSPGFEQK 250 260 270 280 290 300 SPSESFIGRE KRSNSQSYVG RPIQLDKLLM SKVKVPHTFV IHSYTRPTVC QFCKKLLKGL 310 320 330 340 350 360 FRQGLQCKDC RFNCHKRCAP KVPNNCLGEV TINGELLSPG AESDVVMEEG SDDNDSERNS 370 380 390 400 410 420 GLMDDMDEAM VQDTEMALAE GQSDGAEMQD PDADQEDSNR TISPSTSNNI PLMRVVQSVK 430 440 450 460 470 480 HTKRRSSTVM KEGWMVHYTS KDTLRKRHYW RLDSKSITLF QNDTGSRYYK EIPLSEILCL 490 500 510 520 530 540 EPAKPSALIP TGANPHCFEI TTANVVYYVG ENVVNPSSPP PNNSVPPSGI GTDVARMWEV 550 560 570 580 590 600 AIQHALMPVI PKGSSVGSGT NSHKDISVSI SVSNSQIQEN VDISTVYQIF PDEVLGSGQF 610 620 630 640 650 660 GIVYGGKHRK TGRDVAIKII DKLRFPTKQE SQLRNEVAIL QNLHHPGVVN LECMFETPER 670 680 690 700 710 720 VFVVMEKLHG DMLEMILSSE KGRLPEHITK FLITQILVAL RHLHFKNIVH CDLKPENVLL 730 740 750 760 770 780 ASADPFPQVK LCDFGFARII GEKSFRRSVV GTPAYLAPEV LRNKGYNRSL DMWSVGVIIY 790 800 810 820 830 840 VSLSGTFPFN EDEDIHDQIQ NAAFMYPPNP WKEISHEAID LINNLLQVKM RKRYSVDKTL 850 860 870 880 890 900 SHPWLQDYQT WLDLRELECR IGERYITHES DDSRWEQYAG EQGLQYPAHL INLSASHGDS 910 PEAEEREMKA LSERVSIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"Rat PKC mu mRNA partial cds." Minami H., Owada Y., Kondo H. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 718-864. Strain: Wistar. Tissue: Brain.
[3]	"Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D." Jamora C., Yamanouye N., Van Lint J., Laudenslager J., Vandenheede J.R., Faulkner D.J., Malhotra V. Cell 98:59-68(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN GOLGI REGULATION.
[4]	"Protein kinase D is a novel mediator of cardiac troponin I phosphorylation and regulates myofilament function." Haworth R.S., Cuello F., Herron T.J., Franzen G., Kentish J.C., Gautel M., Avkiran M. Circ. Res. 95:1091-1099(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CARDIOMYOCYTE.
[5]	"Hepatocyte resistance to oxidative stress is dependent on protein kinase C-mediated down-regulation of c-Jun/AP-1." Wang Y., Schattenberg J.M., Rigoli R.M., Storz P., Czaja M.J. J. Biol. Chem. 279:31089-31097(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-744; SER-748 AND SER-916.
[6]	"Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5." Vega R.B., Harrison B.C., Meadows E., Roberts C.R., Papst P.J., Olson E.N., McKinsey T.A. Mol. Cell. Biol. 24:8374-8385(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CARDIAC HYPERTROPHY.
[7]	"Protein kinase d regulates trafficking of dendritic membrane proteins in developing neurons." Bisbal M., Conde C., Donoso M., Bollati F., Sesma J., Quiroga S., Diaz Anel A., Malhotra V., Marzolo M.P., Caceres A. J. Neurosci. 28:9297-9308(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NEURONAL POLARITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR03048549 Genomic DNA. No translation available. AABR03048623 Genomic DNA. No translation available. AABR03048825 Genomic DNA. No translation available. AABR03049215 Genomic DNA. No translation available. AABR03049278 Genomic DNA. No translation available. AABR03050321 Genomic DNA. No translation available. AABR03052344 Genomic DNA. No translation available. AB020616 mRNA. Translation: BAA78373.1.
IPI	IPI00948758.
RefSeq	NP_001263644.1. NM_001276715.1. XP_001078506.1. XM_001078506.3. XP_234108.4. XM_234108.6.
UniGene	Rn.144619.
3D structure databases
ProteinModelPortal	Q9WTQ1.
SMR	Q9WTQ1. Positions 425-552.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9WTQ1. 1 interaction.
STRING	10116.ENSRNOP00000005596.
PTM databases
PhosphoSite	Q9WTQ1.
Proteomic databases
PaxDb	Q9WTQ1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000068077; ENSRNOP00000063159; ENSRNOG00000004165.
GeneID	85421.
KEGG	rno:85421.
UCSC	RGD:620964. rat.
Organism-specific databases
CTD	5587.
RGD	620964. Prkd1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00680000099894.
HOGENOM	HOG000015135.
HOVERGEN	HBG003564.
InParanoid	Q9WTQ1.
KO	K06070.
Gene expression databases
Genevestigator	Q9WTQ1.
Family and domain databases
Gene3D	2.30.29.30. 1 hit.
InterPro	IPR020454. DAG/PE-bd. IPR011009. Kinase-like_dom. IPR011993. PH_like_dom. 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. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
PANTHER	PTHR22968. PTHR22968. 1 hit.
Pfam	PF00130. C1_1. 2 hits. PF00169. PH. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
PIRSF	PIRSF000552. PKC_mu_nu_D2. 1 hit.
PRINTS	PR00008. DAGPEDOMAIN.
SMART	SM00109. C1. 2 hits. SM00233. PH. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
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
NextBio	617508.

Entry information

Entry name

KPCD1_RAT

Accession

Primary (citable) accession number: Q9WTQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program