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Protein

Pseudokinase FAM20A

Gene

Fam20a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Biological processi

  • calcium ion homeostasis Source: MGI
  • enamel mineralization Source: MGI
  • tooth eruption Source: MGI
Complete GO annotation...

Keywords - Biological processi

Biomineralization

Names & Taxonomyi

Protein namesi
Recommended name:
Pseudokinase FAM20ACurated
Gene namesi
Name:Fam20aImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2388266. Fam20a.

Subcellular locationi

GO - Cellular componenti

  • cell Source: UniProtKB
  • extracellular exosome Source: MGI
  • Golgi apparatus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Secreted

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 152LL → DE: Not secreted; nuclear localization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence AnalysisAdd
BLAST
Chaini34 – 541508Pseudokinase FAM20APRO_0000008744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi314 ↔ 330By similarity
Disulfide bondi319 ↔ 323By similarity
Disulfide bondi378 ↔ 452By similarity
Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi453 ↔ 512By similarity
Glycosylationi538 – 5381N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8CID3.
PRIDEiQ8CID3.

PTM databases

PhosphoSiteiQ8CID3.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

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.1 Publication

Inductioni

By all-trans retinoic acid (atRA) and IL3 in EML cell line.1 Publication

Gene expression databases

BgeeiQ8CID3.
GenevisibleiQ8CID3. MM.

Interactioni

Subunit structurei

Interacts with FAM20C; probably forming a heterotetramer of 2 subunits of FAM20A and 2 subunits of FAM20C.1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020938.

Structurei

3D structure databases

ProteinModelPortaliQ8CID3.
SMRiQ8CID3. Positions 160-533.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FAM20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG238678.
GeneTreeiENSGT00390000007484.
HOGENOMiHOG000231437.
HOVERGENiHBG051635.
InParanoidiQ8CID3.
OMAiEASWVQF.
OrthoDBiEOG7JX33T.
PhylomeDBiQ8CID3.
TreeFamiTF313276.

Family and domain databases

InterProiIPR009581. DUF1193.
IPR024869. FAM20.
[Graphical view]
PANTHERiPTHR12450. PTHR12450. 1 hit.
PfamiPF06702. DUF1193. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8CID3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGLRRDRLL ALLLLGALFS ADLYFHLWPQ VQRQLRPGER PAACPCSGRA
60 70 80 90 100
PSASLHSAAA SRDLGTASHN FSGALPRVEH PSRGHPAPRS KLQALFAHSL
110 120 130 140 150
YQVLEDPPLL GPEDWLLASQ EALRYYRRKV ARWNRRHKIY KEQFNLTSLD
160 170 180 190 200
PPLQFRPEAS WVQFHLGINS HGLYSRSSLA ISKLLHDMRH FPTISADYSQ
210 220 230 240 250
DEKALLGACD CSQIVKPSGV HLKLVLRFSD FGKAMFKPMR QQREEETPED
260 270 280 290 300
FFYFIDFQRH NAEIAAFHLD RILDFRRVPP TVGRLVNVTK EILEVTKNEI
310 320 330 340 350
LQSVFFVSPA NNVCFFAKCP YMCKTEYAVC GNPHLLEGSL SAFLPSLNLA
360 370 380 390 400
PRLSVPNPWI RSYSLSGKEE WELNPLYCDT VKQIYPYNSS NRLLGIIDMA
410 420 430 440 450
VFDFLIGNMD RHHYEMFTKF GDDGYLIHLD NARGFGRHSQ DEISILAPLA
460 470 480 490 500
QCCMIKRKTL LHLQLLAQAD YRLSDVMRES LLEDQLSPVL TEPHLLALDR
510 520 530 540
RLQIILKTVE DCIEAHGERR VIAEGSAQRS APDSGQANLT S
Length:541
Mass (Da):61,526
Last modified:March 1, 2003 - v1
Checksum:i2F6B2DCF9A447CDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC029169 mRNA. Translation: AAH29169.1.
CCDSiCCDS25584.1.
RefSeqiNP_722477.1. NM_153782.1.
UniGeneiMm.208662.

Genome annotation databases

EnsembliENSMUST00000020938; ENSMUSP00000020938; ENSMUSG00000020614.
ENSMUST00000155559; ENSMUSP00000116687; ENSMUSG00000020614.
GeneIDi208659.
KEGGimmu:208659.
UCSCiuc007mcw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC029169 mRNA. Translation: AAH29169.1.
CCDSiCCDS25584.1.
RefSeqiNP_722477.1. NM_153782.1.
UniGeneiMm.208662.

3D structure databases

ProteinModelPortaliQ8CID3.
SMRiQ8CID3. Positions 160-533.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020938.

PTM databases

PhosphoSiteiQ8CID3.

Proteomic databases

PaxDbiQ8CID3.
PRIDEiQ8CID3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020938; ENSMUSP00000020938; ENSMUSG00000020614.
ENSMUST00000155559; ENSMUSP00000116687; ENSMUSG00000020614.
GeneIDi208659.
KEGGimmu:208659.
UCSCiuc007mcw.1. mouse.

Organism-specific databases

CTDi54757.
MGIiMGI:2388266. Fam20a.

Phylogenomic databases

eggNOGiNOG238678.
GeneTreeiENSGT00390000007484.
HOGENOMiHOG000231437.
HOVERGENiHBG051635.
InParanoidiQ8CID3.
OMAiEASWVQF.
OrthoDBiEOG7JX33T.
PhylomeDBiQ8CID3.
TreeFamiTF313276.

Miscellaneous databases

NextBioi372371.
PROiQ8CID3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CID3.
GenevisibleiQ8CID3. MM.

Family and domain databases

InterProiIPR009581. DUF1193.
IPR024869. FAM20.
[Graphical view]
PANTHERiPTHR12450. PTHR12450. 1 hit.
PfamiPF06702. DUF1193. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: FVB/N.
  2. "FAM20: an evolutionarily conserved family of secreted proteins expressed in hematopoietic cells."
    Nalbant D., Youn H., Nalbant S.I., Sharma S., Cobos E., Beale E.G., Du Y., Williams S.C.
    BMC Genomics 6:11-11(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, DEVELOPMENTAL STAGE, INDUCTION, MUTAGENESIS OF 14-LEU-LEU-15.
  3. "Whole-exome sequencing identifies FAM20A mutations as a cause of amelogenesis imperfecta and gingival hyperplasia syndrome."
    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.
    Am. J. Hum. Genet. 88:616-620(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "The Raine syndrome protein FAM20C is a Golgi kinase that phosphorylates bio-mineralization proteins."
    Ishikawa H.O., Xu A., Ogura E., Manning G., Irvine K.D.
    PLoS ONE 7:E42988-E42988(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Amelogenesis imperfecta and other biomineralization defects in Fam20a and Fam20c null mice."
    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.
    Vet. Pathol. 49:998-1017(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  6. "A secretory kinase complex regulates extracellular protein phosphorylation."
    Cui J., Xiao J., Tagliabracci V.S., Wen J., Rahdar M., Dixon J.E.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FAM20C.

Entry informationi

Entry nameiFA20A_MOUSE
AccessioniPrimary (citable) accession number: Q8CID3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: March 1, 2003
Last modified: July 22, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.