Q5RJI4 (PKDCC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein kinase domain-containing protein, cytoplasmic
EC=2.7.-.-

Alternative name(s):
Protein kinase-like protein SgK493
Sugen kinase 493
Vertebrate lonesome kinase

Gene names

Name:	Pkdcc
Synonyms:	Sgk493, Vlk

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein kinase which is required for longitudinal bone growth through regulation of chondrocyte differentiation. Involved in protein transport from the Golgi apparatus to the plasma membrane. Ref.1 Ref.2
Subcellular location	Golgi apparatus Ref.2.
Tissue specificity	Strongly expressed in adult heart, liver and testis with weak expression in brain, spleen, lung and thymus. In the humerus, strongly expressed in early flat proliferative chondrocytes. In the embryo, expressed in the anterior visceral endoderm and anterior primitive streak at E6.5. At E7.5, expressed in the anterior definitive endoderm (ADE) and anterior mesoderm but not in the notochord. At E8.0, expressed in the ADE and anterior embryonic mesoderm. At E8.5, expressed more broadly in anterior tissues and at the midline of the neural plate in the midbrain region as well as the lateral margins of the neural plate posterior to the metencephalic region. Also weakly expressed in the anterior mesenchyme. At E9.5, strongest expression in branchial arches and limb buds. During mid-gestation, expression continues in mesenchymal cells, particularly in areas where these cells condense. Ref.1 Ref.2
Developmental stage	Expressed throughout embryogenesis and in adulthood. During embryogenesis, expression is high at transition phases of mesenchymal cell differentiation such as from mesenchymal cells to chondrocytes and from mesenchymal to mesothelial cells. Expressed throughout all stages of humerus bone formation. During lung development, expressed in all mesenchymal cells at the early pseudoglandular stage. Expression is rapidly lost from the mesenchyme of the lung interstitium during the mid-to-late pseudoglandular stage but continues throughout life in the mesothelial pleural cells. Ref.1 Ref.2
Disruption phenotype	Morphological defects at birth including growth retardation, short limbs, cleft palate, sternal dysraphia, shortened intestine and cyanosis. Long bones display reduced mineralization due to delayed chondrocyte differentiation. Neonates breathe abnormally, do not suckle and die within a day after birth, probably due to insufficient respiration as a result of the cleft palate. Ref.1 Ref.2
Sequence similarities	Belongs to the protein kinase superfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence AAH86639.1 differs from that shown. Reason: Frameshift at position 72.

Ontologies

Keywords
Biological process	Differentiation Osteogenesis Protein transport Transport
Cellular component	Golgi apparatus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bone mineralization Inferred from mutant phenotype PubMed 21553379. Source: MGI cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW embryonic digestive tract development Inferred from mutant phenotype Ref.1. Source: UniProtKB lung alveolus development Inferred from mutant phenotype Ref.2. Source: UniProtKB multicellular organism growth Inferred from mutant phenotype PubMed 21553379. Source: MGI negative regulation of Golgi to plasma membrane protein transport Inferred from direct assay Ref.2. Source: UniProtKB palate development Inferred from mutant phenotype Ref.1Ref.2. Source: UniProtKB positive regulation of bone mineralization Inferred from mutant phenotype Ref.1. Source: UniProtKB positive regulation of chondrocyte differentiation Inferred from mutant phenotype Ref.1Ref.2. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW skeletal system development Inferred from mutant phenotype PubMed 21553379. Source: MGI
Cellular_component	Golgi apparatus Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5RJI4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q5RJI4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     72-118: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 492	492	Protein kinase domain-containing protein, cytoplasmic		PRO_0000263011
Regions
	Domain	138 – 422	285	Protein kinase
	Nucleotide binding	144 – 152	9	ATP By similarity
	Compositional bias	75 – 128	54	Pro-rich
Sites
	Active site	278	1	Proton acceptor By similarity
	Binding site	166	1	ATP By similarity
Amino acid modifications
	Modified residue	148	1	Phosphotyrosine Ref.2
	Modified residue	177	1	Phosphoserine Ref.2
Natural variations
	Alternative sequence	72 – 118	47	Missing in isoform 2.		VSP_038822
Experimental info
	Mutagenesis	166	1	K → M: Complete loss of phosphorylation. Phosphorylation is restored by co-transfection with wild-type protein. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 23, 2010. Version 2. Checksum: AD95CAF730625FF9	FASTA	492	53,841
	10 20 30 40 50 60 MRRRRAAVAA GFCASFLLGS VLNVLFAPGS EPPRPGQSPG SSAAPGPGRR GGRGELARQI 70 80 90 100 110 120 RERYEEVQRY SRGGPGPGAG RPERRRLMDL APGGPGLQRP RPPRVRSPPD GAPGWPPAPG 130 140 150 160 170 180 PGSPGPGPRL GCAALRNVSG AQYVGSGYTK AVYRVRLPGG AAVALKAVDF SGHDLGSCVR 190 200 210 220 230 240 EFGARRGCYR LAAHKLLKEM VLLERLRHPN VLQLYGYCYQ DSEGIPDTLT TITELGAPVE 250 260 270 280 290 300 MIQLLQTSWE DRFRICLSLG RLLHHLAHSP LGSVTLLDFR PRQFVLVNGE LKVTDLDDAR 310 320 330 340 350 360 VEETPCTSSA DCTLEFPARN FSLPCSAQGW CEGMNEKRNL YNAYRFFFTY LLPHSAPPSL 370 380 390 400 410 420 RPLLDSIVNA TGELAWGVDE TLAQLETALH LFRSGQYLQN STSSRAEYQR IPDSAITQED 430 440 450 460 470 480 YRCWPSYHHG GCLLSVFNLA EAIDVCESHA QCRAFVVTNQ TTWTGRKLVF FKTGWNQVVP 490 DAGKTTYVKA PG
	Isoform 2 [UniParc]. Checksum: 5329234F964F15E9	FASTA	445	48,988
	10 20 30 40 50 60 MRRRRAAVAA GFCASFLLGS VLNVLFAPGS EPPRPGQSPG SSAAPGPGRR GGRGELARQI 70 80 90 100 110 120 RERYEEVQRY SPGPGSPGPG PRLGCAALRN VSGAQYVGSG YTKAVYRVRL PGGAAVALKA 130 140 150 160 170 180 VDFSGHDLGS CVREFGARRG CYRLAAHKLL KEMVLLERLR HPNVLQLYGY CYQDSEGIPD 190 200 210 220 230 240 TLTTITELGA PVEMIQLLQT SWEDRFRICL SLGRLLHHLA HSPLGSVTLL DFRPRQFVLV 250 260 270 280 290 300 NGELKVTDLD DARVEETPCT SSADCTLEFP ARNFSLPCSA QGWCEGMNEK RNLYNAYRFF 310 320 330 340 350 360 FTYLLPHSAP PSLRPLLDSI VNATGELAWG VDETLAQLET ALHLFRSGQY LQNSTSSRAE 370 380 390 400 410 420 YQRIPDSAIT QEDYRCWPSY HHGGCLLSVF NLAEAIDVCE SHAQCRAFVV TNQTTWTGRK 430 440 LVFFKTGWNQ VVPDAGKTTY VKAPG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Short limbs, cleft palate, and delayed formation of flat proliferative chondrocytes in mice with targeted disruption of a putative protein kinase gene, Pkdcc (AW548124)." Imuta Y., Nishioka N., Kiyonari H., Sasaki H. Dev. Dyn. 238:210-222(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING. Tissue: Embryo.
[2]	"The novel protein kinase Vlk is essential for stromal function of mesenchymal cells." Kinoshita M., Era T., Jakt L.M., Nishikawa S. Development 136:2069-2079(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT TYR-148 AND SER-177, MUTAGENESIS OF LYS-166.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6 and FVB/N. Tissue: Brain and Liver.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 381-492 (ISOFORMS 1/2). Strain: C57BL/6J. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB436780 mRNA. Translation: BAG82823.1. AB381893 mRNA. Translation: BAH66379.1. BC022157 mRNA. Translation: AAH22157.1. BC086639 mRNA. Translation: AAH86639.1. Frameshift. AK133913 mRNA. Translation: BAE21924.1.
IPI	IPI00348562. IPI00914148.
RefSeq	NP_598878.2. NM_134117.2.
UniGene	Mm.311974.
3D structure databases
ProteinModelPortal	Q5RJI4.
SMR	Q5RJI4. Positions 272-304.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000025094.
PTM databases
PhosphoSite	Q5RJI4.
Proteomic databases
PRIDE	Q5RJI4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000170794; ENSMUSP00000129238; ENSMUSG00000024247.
GeneID	106522.
KEGG	mmu:106522.
UCSC	uc012axu.1. mouse.
Organism-specific databases
CTD	91461.
MGI	MGI:2147077. Pkdcc.
Phylogenomic databases
eggNOG	NOG254379.
GeneTree	ENSGT00390000001205.
HOGENOM	HOG000054185.
HOVERGEN	HBG079871.
InParanoid	Q5RJI4.
OMA	PRLGCAA.
OrthoDB	EOG4WQ13D.
Gene expression databases
Bgee	Q5RJI4.
Genevestigator	Q5RJI4.
GermOnline	ENSMUSG00000024247. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	358240.
SOURCE	Search...

Entry information

Entry name

PKDCC_MOUSE

Accession

Primary (citable) accession number: Q5RJI4
Secondary accession number(s): B6F136, Q3UZD3, Q8VBZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	March 23, 2010
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