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Q5RJI4 (PKDCC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processDifferentiation
Osteogenesis
Protein transport
Transport
   Cellular componentGolgi apparatus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone 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_componentGolgi apparatus

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Protein kinase domain-containing protein, cytoplasmic
PRO_0000263011

Regions

Domain138 – 422285Protein kinase
Nucleotide binding144 – 1529ATP By similarity
Compositional bias75 – 12854Pro-rich

Sites

Active site2781Proton acceptor By similarity
Binding site1661ATP By similarity

Amino acid modifications

Modified residue1481Phosphotyrosine Ref.2
Modified residue1771Phosphoserine Ref.2

Natural variations

Alternative sequence72 – 11847Missing in isoform 2.
VSP_038822

Experimental info

Mutagenesis1661K → M: Complete loss of phosphorylation. Phosphorylation is restored by co-transfection with wild-type protein. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 23, 2010. Version 2.
Checksum: AD95CAF730625FF9

FASTA49253,841
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5329234F964F15E9
Show »

FASTA44548,988

References

« Hide '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. expand/collapse author list , 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.
RefSeqNP_598878.2. NM_134117.2.
UniGeneMm.311974.

3D structure databases

ProteinModelPortalQ5RJI4.
SMRQ5RJI4. Positions 134-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000025094.

PTM databases

PhosphoSiteQ5RJI4.

Proteomic databases

PRIDEQ5RJI4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000170794; ENSMUSP00000129238; ENSMUSG00000024247. [Q5RJI4-1]
GeneID106522.
KEGGmmu:106522.
UCSCuc012axu.1. mouse. [Q5RJI4-1]

Organism-specific databases

CTD91461.
MGIMGI:2147077. Pkdcc.

Phylogenomic databases

eggNOGNOG254379.
GeneTreeENSGT00390000001205.
HOGENOMHOG000054185.
HOVERGENHBG079871.
InParanoidQ5RJI4.
KOK17548.
OMAYVGSGYT.
OrthoDBEOG7034GV.
PhylomeDBQ5RJI4.
TreeFamTF329248.

Gene expression databases

BgeeQ5RJI4.
GenevestigatorQ5RJI4.

Family and domain databases

InterProIPR022049. FAM69_kinase_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
[Graphical view]
PfamPF12260. PIP49_C. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio358240.
PROQ5RJI4.
SOURCESearch...

Entry information

Entry namePKDCC_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot