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Pseudokinase FAM20A

 FA20A_MOUSE             Reviewed;         541 AA.
Q8CID3;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 104.
RecName: Full=Pseudokinase FAM20A {ECO:0000305};
Flags: Precursor;
Name=Fam20a {ECO:0000312|MGI:MGI:2388266};
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 [LARGE SCALE MRNA].
STRAIN=FVB/N;
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).
[2]
SUBCELLULAR LOCATION, GLYCOSYLATION, DEVELOPMENTAL STAGE, INDUCTION,
AND MUTAGENESIS OF 14-LEU-LEU-15.
PubMed=15676076; DOI=10.1186/1471-2164-6-11;
Nalbant D., Youn H., Nalbant S.I., Sharma S., Cobos E., Beale E.G.,
Du Y., Williams S.C.;
"FAM20: an evolutionarily conserved family of secreted proteins
expressed in hematopoietic cells.";
BMC Genomics 6:11-11(2005).
[3]
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).
[4]
SUBCELLULAR LOCATION.
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).
[5]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
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).
[6]
FUNCTION, AND INTERACTION WITH FAM20C.
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: Pseudokinase that acts as an allosteric activator of the
Golgi serine/threonine protein kinase FAM20C and is involved in
biomineralization of teeth. Forms a complex with FAM20C and
increases the ability of FAM20C to phosphorylate the proteins that
form the 'matrix' that guides the deposition of the enamel
minerals. {ECO:0000269|PubMed:25789606}.
-!- SUBUNIT: Interacts with FAM20C; probably forming a heterotetramer
of 2 subunits of FAM20A and 2 subunits of FAM20C.
{ECO:0000269|PubMed:25789606}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15676076}.
Golgi apparatus {ECO:0000269|PubMed:22900076}. Endoplasmic
reticulum {ECO:0000269|PubMed:22900076}.
-!- TISSUE SPECIFICITY: Observed throughout the tissues of the
mandibular incisor, including the secretory and maturation stage
ameloblasts, the suprabasal layers of the gingival epithelium and
the odontoblasts. Weak expression in the enamel matrix.
{ECO:0000269|PubMed:21549343, ECO:0000269|PubMed:22732358}.
-!- DEVELOPMENTAL STAGE: In EML and MPRO cell lines, low levels in
undifferentiated cells. Induced during maturation to promyelocyte
stage of neutrophil differentiation. Decreased during neutrophil
terminal differentiation. {ECO:0000269|PubMed:15676076}.
-!- INDUCTION: By all-trans retinoic acid (atRA) and IL3 in EML cell
line. {ECO:0000269|PubMed:15676076}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:15676076}.
-!- DISRUPTION PHENOTYPE: Mice survive to adulthood and show
biomineralization defects such as severe amelogenesis imperfecta
(AI). In addition, mice develop disseminated calcifications of
muscular arteries and intrapulmonary calcifications, similar to
those of fetuin-A (Ahsg) deficient mice, although they are
normocalcemic and normophosphatemic, with normal dentin and bone.
{ECO:0000269|PubMed:22732358}.
-!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC029169; AAH29169.1; -; mRNA.
CCDS; CCDS25584.1; -.
RefSeq; NP_722477.1; NM_153782.1.
UniGene; Mm.208662; -.
ProteinModelPortal; Q8CID3; -.
SMR; Q8CID3; -.
IntAct; Q8CID3; 1.
STRING; 10090.ENSMUSP00000020938; -.
iPTMnet; Q8CID3; -.
PhosphoSitePlus; Q8CID3; -.
EPD; Q8CID3; -.
MaxQB; Q8CID3; -.
PaxDb; Q8CID3; -.
PeptideAtlas; Q8CID3; -.
PRIDE; Q8CID3; -.
Ensembl; ENSMUST00000020938; ENSMUSP00000020938; ENSMUSG00000020614.
Ensembl; ENSMUST00000155559; ENSMUSP00000116687; ENSMUSG00000020614.
GeneID; 208659; -.
KEGG; mmu:208659; -.
UCSC; uc007mcw.1; mouse.
CTD; 54757; -.
MGI; MGI:2388266; Fam20a.
eggNOG; KOG3829; Eukaryota.
eggNOG; ENOG410XQEJ; LUCA.
GeneTree; ENSGT00390000007484; -.
HOGENOM; HOG000231437; -.
HOVERGEN; HBG051635; -.
InParanoid; Q8CID3; -.
KO; K21957; -.
OMA; EASWVQF; -.
OrthoDB; EOG091G1BEO; -.
PhylomeDB; Q8CID3; -.
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.
PRO; PR:Q8CID3; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020614; -.
Genevisible; Q8CID3; MM.
GO; GO:0005623; C:cell; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:UniProtKB.
GO; GO:0031214; P:biomineral tissue development; ISS:UniProtKB.
GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
GO; GO:0070166; P:enamel mineralization; IMP:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0044691; P:tooth eruption; ISO:MGI.
InterPro; IPR024869; FAM20.
InterPro; IPR009581; FAM20_C.
PANTHER; PTHR12450; PTHR12450; 1.
Pfam; PF06702; Fam20C; 1.
1: Evidence at protein level;
Biomineralization; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
Reference proteome; Secreted; Signal.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 541 Pseudokinase FAM20A.
/FTId=PRO_0000008744.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 287 287 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 388 388 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 538 538 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 314 330 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 319 323 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 378 452 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 453 512 {ECO:0000250|UniProtKB:Q9XTW2}.
MUTAGEN 14 15 LL->DE: Not secreted; nuclear
localization.
{ECO:0000269|PubMed:15676076}.
SEQUENCE 541 AA; 61526 MW; 2F6B2DCF9A447CDA CRC64;
MPGLRRDRLL ALLLLGALFS ADLYFHLWPQ VQRQLRPGER PAACPCSGRA PSASLHSAAA
SRDLGTASHN FSGALPRVEH PSRGHPAPRS KLQALFAHSL YQVLEDPPLL GPEDWLLASQ
EALRYYRRKV ARWNRRHKIY KEQFNLTSLD PPLQFRPEAS WVQFHLGINS HGLYSRSSLA
ISKLLHDMRH FPTISADYSQ DEKALLGACD CSQIVKPSGV HLKLVLRFSD FGKAMFKPMR
QQREEETPED FFYFIDFQRH NAEIAAFHLD RILDFRRVPP TVGRLVNVTK EILEVTKNEI
LQSVFFVSPA NNVCFFAKCP YMCKTEYAVC GNPHLLEGSL SAFLPSLNLA PRLSVPNPWI
RSYSLSGKEE WELNPLYCDT VKQIYPYNSS NRLLGIIDMA VFDFLIGNMD RHHYEMFTKF
GDDGYLIHLD NARGFGRHSQ DEISILAPLA QCCMIKRKTL LHLQLLAQAD YRLSDVMRES
LLEDQLSPVL TEPHLLALDR RLQIILKTVE DCIEAHGERR VIAEGSAQRS APDSGQANLT
S


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