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Extracellular serine/threonine protein kinase FAM20C (EC 2.7.11.1) (Dentin matrix protein 4) (DMP-4) (Golgi-enriched fraction casein kinase) (GEF-CK)

 FA20C_MOUSE             Reviewed;         579 AA.
Q5MJS3; Q4FJP0; Q571A3; Q6PKA8; Q8JZP7;
21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 1.
20-JUN-2018, entry version 93.
RecName: Full=Extracellular serine/threonine protein kinase FAM20C {ECO:0000305};
EC=2.7.11.1 {ECO:0000269|PubMed:22900076};
AltName: Full=Dentin matrix protein 4 {ECO:0000303|PubMed:17369251};
Short=DMP-4 {ECO:0000303|PubMed:17369251};
AltName: Full=Golgi-enriched fraction casein kinase {ECO:0000250|UniProtKB:Q8IXL6};
Short=GEF-CK {ECO:0000250|UniProtKB:Q8IXL6};
Flags: Precursor;
Name=Fam20c {ECO:0000312|MGI:MGI:2136853};
Synonyms=Dmp4 {ECO:0000303|PubMed:17369251},
Kiaa4081 {ECO:0000303|Ref.2};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND DEVELOPMENTAL STAGE.
PubMed=17369251; DOI=10.1074/jbc.M701547200;
Hao J., Narayanan K., Muni T., Ramachandran A., George A.;
"Dentin matrix protein 4, a novel secretory calcium-binding protein
that modulates odontoblast differentiation.";
J. Biol. Chem. 282:15357-15365(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreatic islet;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 331-579.
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
TISSUE SPECIFICITY.
PubMed=21549343; DOI=10.1016/j.ajhg.2011.04.005;
O'Sullivan J., Bitu C.C., Daly S.B., Urquhart J.E., Barron M.J.,
Bhaskar S.S., Martelli-Junior H., dos Santos Neto P.E., Mansilla M.A.,
Murray J.C., Coletta R.D., Black G.C., Dixon M.J.;
"Whole-exome sequencing identifies FAM20A mutations as a cause of
amelogenesis imperfecta and gingival hyperplasia syndrome.";
Am. J. Hum. Genet. 88:616-620(2011).
[6]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-241; GLY-261; GLY-374;
LEU-383; ASP-446; ASP-453; 473-ASP-ASN-474 AND ARG-544.
PubMed=22900076; DOI=10.1371/journal.pone.0042988;
Ishikawa H.O., Xu A., Ogura E., Manning G., Irvine K.D.;
"The Raine syndrome protein FAM20C is a Golgi kinase that
phosphorylates bio-mineralization proteins.";
PLoS ONE 7:E42988-E42988(2012).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22732358; DOI=10.1177/0300985812453177;
Vogel P., Hansen G.M., Read R.W., Vance R.B., Thiel M., Liu J.,
Wronski T.J., Smith D.D., Jeter-Jones S., Brommage R.;
"Amelogenesis imperfecta and other biomineralization defects in Fam20a
and Fam20c null mice.";
Vet. Pathol. 49:998-1017(2012).
[8]
FUNCTION, INTERACTION WITH FAM20A, AND ENZYME REGULATION.
PubMed=25789606; DOI=10.7554/eLife.06120;
Cui J., Xiao J., Tagliabracci V.S., Wen J., Rahdar M., Dixon J.E.;
"A secretory kinase complex regulates extracellular protein
phosphorylation.";
Elife 4:0-0(2015).
-!- FUNCTION: Golgi serine/threonine protein kinase that
phosphorylates secretory pathway proteins within Ser-x-Glu/pSer
motifs and plays a key role in biomineralization of bones and
teeth (PubMed:22900076, PubMed:22732358, PubMed:25789606).
Constitutes the main protein kinase for extracellular proteins,
generating the majority of the extracellular phosphoproteome (By
similarity). Mainly phosphorylates proteins within the Ser-x-
Glu/pSer motif, but also displays a broader substrate specificity
(By similarity). Phosphorylates casein as well as a number of
proteins involved in biomineralization such as AMELX, AMTN, ENAM
and SPP1 (PubMed:25789606). In addition to its role in
biomineralization, also plays a role in lipid homeostasis, wound
healing and cell migration and adhesion (By similarity).
{ECO:0000250|UniProtKB:Q8IXL6, ECO:0000269|PubMed:22732358,
ECO:0000269|PubMed:22900076, ECO:0000269|PubMed:25789606}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:22900076}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q8IXL6};
-!- ENZYME REGULATION: Serine/threonine protein kinase activity is
increased upon interaction with FAM20A.
{ECO:0000269|PubMed:25789606}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.5 uM for casein {ECO:0000269|PubMed:22900076};
KM=78 uM for ATP {ECO:0000269|PubMed:22900076};
Vmax=0.7 umol/min/mg enzyme {ECO:0000269|PubMed:22900076};
Note=kcat is 52 min(-1). {ECO:0000269|PubMed:22900076};
-!- SUBUNIT: Interacts with FAM20A; probably forming a heterotetramer
of 2 subunits of FAM20A and 2 subunits of FAM20C.
{ECO:0000269|PubMed:25789606}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17369251}.
Golgi apparatus {ECO:0000269|PubMed:22900076}.
-!- TISSUE SPECIFICITY: Highly expressed in the tooth. No expression
in the dental pulp. At the secretory stage of amelogenesis, it is
detected in the matrix of the enamel, in the ameloblasts, and
within the cells adjoining the stratum intermedium (a tissue layer
analogous to the stellate reticulum seen in the developing molar).
Strong expression is observed in maturation stage ameloblasts and
throughout the non-cornified layers of the gingival epithelium.
Expressed at moderate levels in bone and at low levels in kidney,
liver, brain and lung. Very low expression, if any, in spleen and
skeletal muscle. {ECO:0000269|PubMed:17369251,
ECO:0000269|PubMed:21549343}.
-!- DEVELOPMENTAL STAGE: In the developing tooth, initial expression
observed in odontoblasts at all stages of development. At later
stages, restricted expression pattern in ameloblasts. Also
observed in osteoblasts in the alveolar bone.
{ECO:0000269|PubMed:17369251}.
-!- PTM: N-glycosylation is required for folding.
{ECO:0000250|UniProtKB:Q8IXL6}.
-!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q8IXL6}.
-!- DISRUPTION PHENOTYPE: Mice survive to adulthood and show
biomineralization defects, suc as severe amelogenesis imperfecta
(AI). In addition, mice are severely hypophosphatemic and develop
notable lesions in both dentin and bone.
{ECO:0000269|PubMed:22732358}.
-!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH04044.3; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH04044.3; Type=Frameshift; Positions=294; Evidence={ECO:0000305};
Sequence=AAH25814.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH25826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAD90211.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAD90211.1; Type=Frameshift; Positions=296; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AY778962; AAV91326.1; -; mRNA.
EMBL; AK220286; BAD90211.1; ALT_SEQ; mRNA.
EMBL; BC004044; AAH04044.3; ALT_SEQ; mRNA.
EMBL; BC025814; AAH25814.1; ALT_INIT; mRNA.
EMBL; BC025826; AAH25826.1; ALT_INIT; mRNA.
EMBL; CT010363; CAJ18570.1; -; mRNA.
CCDS; CCDS51681.1; -.
RefSeq; NP_085042.2; NM_030565.6.
UniGene; Mm.320355; -.
ProteinModelPortal; Q5MJS3; -.
SMR; Q5MJS3; -.
IntAct; Q5MJS3; 1.
STRING; 10090.ENSMUSP00000026972; -.
iPTMnet; Q5MJS3; -.
PhosphoSitePlus; Q5MJS3; -.
MaxQB; Q5MJS3; -.
PaxDb; Q5MJS3; -.
PeptideAtlas; Q5MJS3; -.
PRIDE; Q5MJS3; -.
DNASU; 80752; -.
Ensembl; ENSMUST00000026972; ENSMUSP00000026972; ENSMUSG00000025854.
GeneID; 80752; -.
KEGG; mmu:80752; -.
UCSC; uc009afv.2; mouse.
CTD; 56975; -.
MGI; MGI:2136853; Fam20c.
eggNOG; KOG3829; Eukaryota.
eggNOG; ENOG410XQEJ; LUCA.
GeneTree; ENSGT00390000007484; -.
HOGENOM; HOG000231437; -.
HOVERGEN; HBG051635; -.
InParanoid; Q5MJS3; -.
KO; K21958; -.
OMA; LPLRQCC; -.
OrthoDB; EOG091G1BEO; -.
PhylomeDB; Q5MJS3; -.
TreeFam; TF313276; -.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
ChiTaRS; Fam20c; mouse.
PRO; PR:Q5MJS3; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000025854; -.
ExpressionAtlas; Q5MJS3; baseline and differential.
Genevisible; Q5MJS3; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IDA:MGI.
GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
GO; GO:0031214; P:biomineral tissue development; ISS:UniProtKB.
GO; GO:0097187; P:dentinogenesis; IMP:MGI.
GO; GO:0070166; P:enamel mineralization; IMP:MGI.
GO; GO:0071895; P:odontoblast differentiation; IDA:MGI.
GO; GO:0036179; P:osteoclast maturation; IMP:MGI.
GO; GO:0030501; P:positive regulation of bone mineralization; IDA:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0051174; P:regulation of phosphorus metabolic process; IMP:MGI.
GO; GO:0001501; P:skeletal system development; IMP:MGI.
InterPro; IPR024869; FAM20.
InterPro; IPR009581; FAM20_C.
PANTHER; PTHR12450; PTHR12450; 1.
Pfam; PF06702; Fam20C; 1.
1: Evidence at protein level;
ATP-binding; Biomineralization; Calcium; Complete proteome;
Disulfide bond; Glycoprotein; Golgi apparatus; Kinase; Manganese;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Secreted; Serine/threonine-protein kinase; Signal; Transferase.
SIGNAL 1 26 {ECO:0000255}.
PROPEP 27 87 {ECO:0000250|UniProtKB:Q8IXL6}.
/FTId=PRO_0000433884.
CHAIN 88 579 Extracellular serine/threonine protein
kinase FAM20C.
/FTId=PRO_0000297978.
NP_BIND 384 387 ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
REGION 349 560 Kinase domain.
{ECO:0000250|UniProtKB:Q8IXL6}.
ACT_SITE 453 453 {ECO:0000250|UniProtKB:Q8IXL6}.
METAL 301 301 Manganese.
{ECO:0000250|UniProtKB:Q9XTW2}.
METAL 473 473 Manganese.
{ECO:0000250|UniProtKB:Q9XTW2}.
BINDING 264 264 ATP; via amide nitrogen.
{ECO:0000250|UniProtKB:Q9XTW2}.
BINDING 280 280 ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
BINDING 301 301 ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
BINDING 458 458 ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
BINDING 473 473 ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 357 373 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 362 366 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 421 495 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 496 555 {ECO:0000250|UniProtKB:Q9XTW2}.
MUTAGEN 241 241 I->N: Abrogates kinase activity.
{ECO:0000269|PubMed:22900076}.
MUTAGEN 261 261 G->R: Abrogates kinase activity.
{ECO:0000269|PubMed:22900076}.
MUTAGEN 374 374 G->E,R: Abrogates kinase activity.
{ECO:0000269|PubMed:22900076}.
MUTAGEN 383 383 L->R: Mislocalization of the protein from
Golgi apparatus to endoplasmic reticulum.
{ECO:0000269|PubMed:22900076}.
MUTAGEN 446 446 D->N: Mislocalization of the protein from
Golgi apparatus to endoplasmic reticulum.
{ECO:0000269|PubMed:22900076}.
MUTAGEN 453 453 D->G: Abrogates kinase activity without
affecting subcellular location.
{ECO:0000269|PubMed:22900076}.
MUTAGEN 473 474 DN->GG: Abrogates kinase activity.
{ECO:0000269|PubMed:22900076}.
MUTAGEN 544 544 R->W: Mislocalization of the protein from
Golgi apparatus to endoplasmic reticulum.
{ECO:0000269|PubMed:22900076}.
CONFLICT 333 333 K -> N (in Ref. 4; CAJ18570).
{ECO:0000305}.
SEQUENCE 579 AA; 65766 MW; 9DE5F5496AC117FE CRC64;
MKMILVRRFR VLILVVFLLA CALHIAVDLL PKLDRRATRS SGEPGCSCAQ PAAEAAGPGW
AQARSRPGES AGGDAGWPNK HTLRILQDFS SDPASNLTSH SLEKLPSAAE PVDHAPRGQE
PRSPPPRDPA HRPLLRDPGP RPRVPPPGPS GDGSLLAKLF EHPLYQGAVP PLTEDDVLFN
VNSDIRFNPK AAENPDWPHE GAEGAEFLPT GEAAVNLYPN WLKFHIGINR YELYSRHNPA
IDALLRDLGS QKITSVAMKS GGTQLKLIMT FQNYGQALFK PMKQTREQET PPDFFYFSDY
ERHNAEIAAF HLDRILDFRR VPPVAGRMIN MTKEIRDVTR DKKLWRTFFV SPANNICFYG
ECSYYCSTEH ALCGRPDQIE GSLAAFLPDL SLAKRKTWRN PWRRSYHKRK KAEWEVDPDY
CEEVKQTPPY DSGHRILDIM DMTVFDFLMG NMDRHHYETF EKFGNETFII HLDNGRGFGK
YSHDELSILA PLHQCCRIRR STYLRLQLLA KEEHKLSLLM AESLQHDKVA PVLYQLHLEA
LDRRLRIVLQ AVRDCVEKDG LSSVVEDDLA TEHRASTER


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