PKDCC

PKDCC (Protein Kinase Domain Containing, Cytoplasmic) is a protein coding gene. Gene Ontology annotations related to this gene include transferase activity, transferring phosphorus-containing groups and non-membrane spanning protein tyrosine kinase activity.

Protein Kinase Domain Containing, Cytoplasmic

Secreted tyrosine-protein kinase that mediates phosphorylation of extracellular proteins and endogenous proteins in the secretory pathway, which is essential for patterning at organogenesis stages. Mediates phosphorylation of MMP1, MMP13, MMP14, MMP19 and ERP29 (PubMed:25171405).
Probably plays a role in platelets: rapidly and quantitatively secreted from platelets in response to stimulation of platelet degranulation (PubMed:25171405).
May also have serine/threonine protein kinase activity. Required for longitudinal bone growth through regulation of chondrocyte differentiation. May be indirectly involved in protein transport from the Golgi apparatus to the plasma membrane (By similarity).

Bone mineralizationIEA:Ensembl
Cell differentiationIEA:UniProtKB-KW
Embryonic digestive tract developmentISS:UniProtKB
Limb morphogenesisIEA:Ensembl
Lung alveolus developmentISS:UniProtKB
Multicellular organism growthIEA:Ensembl
Negative regulation of Golgi to plasma membrane protein transportISS:UniProtKB
Peptidyl-tyrosine phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of bone mineralizationISS:UniProtKB
Positive regulation of chondrocyte differentiationISS:UniProtKB
Protein transportIEA:UniProtKB-KW
Roof of mouth developmentISS:UniProtKB
Skeletal system developmentManual Assertion Based On ExperimentIMP:UniProtKB

Secreted
Golgi apparatus

Secreted 1 Publication
Golgi apparatus:
An autosomal recessive skeletal dysplasia characterized by rhizomelic shortening of limbs as well as variable dysmorphic features, including macrocephaly, short neck, micrognathia, mild proptosis, downslanting palpebral fissures, depressed or broad nasal bridge and long philtrum.

N-glycosylated.
Phosphorylated on tyrosines; probably via autophosphorylation.