ID   FA20A_HUMAN             Reviewed;         541 AA.
AC   Q96MK3; B2RN47; B2RN49; Q9UF95;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 4.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Pseudokinase FAM20A {ECO:0000305};
DE   Flags: Precursor;
GN   Name=FAM20A {ECO:0000312|HGNC:HGNC:23015};
GN   ORFNames=UNQ9388/PRO34279 {ECO:0000303|PubMed:12975309};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-332 AND SER-530.
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-332 AND SER-530.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-332 AND SER-530.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-541, AND VARIANT SER-530.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=15676076; DOI=10.1186/1471-2164-6-11;
RA   Nalbant D., Youn H., Nalbant S.I., Sharma S., Cobos E., Beale E.G., Du Y.,
RA   Williams S.C.;
RT   "FAM20: an evolutionarily conserved family of secreted proteins expressed
RT   in hematopoietic cells.";
RL   BMC Genomics 6:11-11(2005).
RN   [7]
RP   INVOLVEMENT IN AI1G.
RX   PubMed=21549343; DOI=10.1016/j.ajhg.2011.04.005;
RA   O'Sullivan J., Bitu C.C., Daly S.B., Urquhart J.E., Barron M.J.,
RA   Bhaskar S.S., Martelli-Junior H., dos Santos Neto P.E., Mansilla M.A.,
RA   Murray J.C., Coletta R.D., Black G.C., Dixon M.J.;
RT   "Whole-exome sequencing identifies FAM20A mutations as a cause of
RT   amelogenesis imperfecta and gingival hyperplasia syndrome.";
RL   Am. J. Hum. Genet. 88:616-620(2011).
RN   [8]
RP   INVOLVEMENT IN AI1G.
RX   PubMed=23697977; DOI=10.1038/jhg.2013.44;
RA   Cabral R.M., Kurban M., Rothman L., Wajid M., Shimomura Y., Petukhova L.,
RA   Christiano A.M.;
RT   "Autosomal recessive gingival hyperplasia and dental anomalies caused by a
RT   29-base pair duplication in the FAM20A gene.";
RL   J. Hum. Genet. 58:566-567(2013).
RN   [9]
RP   INVOLVEMENT IN AI1G.
RX   PubMed=24259279; DOI=10.1002/ajmg.a.36187;
RA   Kantaputra P.N., Kaewgahya M., Khemaleelakul U., Dejkhamron P.,
RA   Sutthimethakorn S., Thongboonkerd V., Iamaroon A.;
RT   "Enamel-renal-gingival syndrome and FAM20A mutations.";
RL   Am. J. Med. Genet. A 164A:1-9(2014).
RN   [10]
RP   INVOLVEMENT IN AI1G.
RX   PubMed=24756937; DOI=10.1002/ajmg.a.36579;
RA   Kantaputra P.N., Bongkochwilawan C., Kaewgahya M., Ohazama A.,
RA   Kayserili H., Erdem A.P., Aktoren O., Guven Y.;
RT   "Enamel-Renal-Gingival syndrome, hypodontia, and a novel FAM20A mutation.";
RL   Am. J. Med. Genet. A 164A:2124-2128(2014).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   INVOLVEMENT IN AI1G.
RX   PubMed=25827751; DOI=10.1016/j.archoralbio.2015.02.018;
RA   Volodarsky M., Zilberman U., Birk O.S.;
RT   "Novel FAM20A mutation causes autosomal recessive amelogenesis
RT   imperfecta.";
RL   Arch. Oral Biol. 60:919-922(2015).
RN   [13]
RP   INVOLVEMENT IN AI1G.
RX   PubMed=25636655; DOI=10.1186/1472-6831-15-14;
RA   Cherkaoui Jaouad I., El Alloussi M., Chafai El Alaoui S., Laarabi F.Z.,
RA   Lyahyai J., Sefiani A.;
RT   "Further evidence for causal FAM20A mutations and first case of
RT   amelogenesis imperfecta and gingival hyperplasia syndrome in Morocco: a
RT   case report.";
RL   BMC Oral Health 15:14-14(2015).
RN   [14]
RP   FUNCTION, INTERACTION WITH FAM20C, MUTAGENESIS OF GLN-258, AND
RP   CHARACTERIZATION OF VARIANTS AI1G ARG-173; ASP-331 AND ASN-403.
RX   PubMed=25789606; DOI=10.7554/elife.06120;
RA   Cui J., Xiao J., Tagliabracci V.S., Wen J., Rahdar M., Dixon J.E.;
RT   "A secretory kinase complex regulates extracellular protein
RT   phosphorylation.";
RL   Elife 4:0-0(2015).
RN   [15]
RP   VARIANT AI1G 197-ASP--ILE-214 DELINS VAL-197.
RX   PubMed=21990045; DOI=10.1002/humu.21621;
RA   Cho S.H., Seymen F., Lee K.E., Lee S.K., Kweon Y.S., Kim K.J., Jung S.E.,
RA   Song S.J., Yildirim M., Bayram M., Tuna E.B., Gencay K., Kim J.W.;
RT   "Novel FAM20A mutations in hypoplastic amelogenesis imperfecta.";
RL   Hum. Mutat. 33:91-94(2012).
RN   [16]
RP   VARIANT AI1G ARG-173.
RX   PubMed=23434854; DOI=10.1159/000349989;
RA   Jaureguiberry G., De la Dure-Molla M., Parry D., Quentric M., Himmerkus N.,
RA   Koike T., Poulter J., Klootwijk E., Robinette S.L., Howie A.J., Patel V.,
RA   Figueres M.L., Stanescu H.C., Issler N., Nicholson J.K., Bockenhauer D.,
RA   Laing C., Walsh S.B., McCredie D.A., Povey S., Asselin A., Picard A.,
RA   Coulomb A., Medlar A.J., Bailleul-Forestier I., Verloes A., Le Caignec C.,
RA   Roussey G., Guiol J., Isidor B., Logan C., Shore R., Johnson C.,
RA   Inglehearn C., Al-Bahlani S., Schmittbuhl M., Clauss F., Huckert M.,
RA   Laugel V., Ginglinger E., Pajarola S., Sparta G., Bartholdi D., Rauch A.,
RA   Addor M.C., Yamaguti P.M., Safatle H.P., Acevedo A.C., Martelli-Junior H.,
RA   dos Santos Netos P.E., Coletta R.D., Gruessel S., Sandmann C., Ruehmann D.,
RA   Langman C.B., Scheinman S.J., Ozdemir-Ozenen D., Hart T.C., Hart P.S.,
RA   Neugebauer U., Schlatter E., Houillier P., Gahl W.A., Vikkula M.,
RA   Bloch-Zupan A., Bleich M., Kitagawa H., Unwin R.J., Mighell A., Berdal A.,
RA   Kleta R.;
RT   "Nephrocalcinosis (enamel renal syndrome) caused by autosomal recessive
RT   FAM20A mutations.";
RL   Nephron Physiol. 122:1-6(2012).
RN   [17]
RP   VARIANT AI1G ASP-331, AND SUBCELLULAR LOCATION.
RX   PubMed=23468644; DOI=10.1371/journal.pgen.1003302;
RA   Wang S.K., Aref P., Hu Y., Milkovich R.N., Simmer J.P., El-Khateeb M.,
RA   Daggag H., Baqain Z.H., Hu J.C.;
RT   "FAM20A mutations can cause enamel-renal syndrome (ERS).";
RL   PLoS Genet. 9:E1003302-E1003302(2013).
RN   [18]
RP   VARIANT AI1G ASN-403.
RX   PubMed=24196488; DOI=10.1177/0022034513512653;
RA   Wang S.K., Reid B.M., Dugan S.L., Roggenbuck J.A., Read L., Aref P.,
RA   Taheri A.P., Yeganeh M.Z., Simmer J.P., Hu J.C.;
RT   "FAM20A mutations associated with enamel renal syndrome.";
RL   J. Dent. Res. 93:42-48(2014).
CC   -!- FUNCTION: Pseudokinase that acts as an allosteric activator of the
CC       Golgi serine/threonine protein kinase FAM20C and is involved in
CC       biomineralization of teeth. Forms a complex with FAM20C and increases
CC       the ability of FAM20C to phosphorylate the proteins that form the
CC       'matrix' that guides the deposition of the enamel minerals.
CC       {ECO:0000269|PubMed:25789606}.
CC   -!- SUBUNIT: Interacts with FAM20C; probably forming a heterotetramer of 2
CC       subunits of FAM20A and 2 subunits of FAM20C.
CC       {ECO:0000269|PubMed:25789606}.
CC   -!- INTERACTION:
CC       Q96MK3; Q8IXL6: FAM20C; NbExp=3; IntAct=EBI-11892970, EBI-7147442;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8CID3}. Golgi
CC       apparatus {ECO:0000269|PubMed:23468644}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q8CID3}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung and liver. Intermediate
CC       levels in thymus and ovary. {ECO:0000269|PubMed:15676076}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8CID3}.
CC   -!- DISEASE: Amelogenesis imperfecta 1G (AI1G) [MIM:204690]: A disorder
CC       characterized by dental anomalies, gingival overgrowth, and
CC       nephrocalcinosis. Dental anomalies include hypoplastic amelogenesis
CC       imperfecta, intrapulpal calcifications, delay of tooth eruption,
CC       hypodontia/oligodontia, pericoronal radiolucencies and unerupted teeth.
CC       {ECO:0000269|PubMed:21549343, ECO:0000269|PubMed:21990045,
CC       ECO:0000269|PubMed:23434854, ECO:0000269|PubMed:23468644,
CC       ECO:0000269|PubMed:23697977, ECO:0000269|PubMed:24196488,
CC       ECO:0000269|PubMed:24259279, ECO:0000269|PubMed:24756937,
CC       ECO:0000269|PubMed:25636655, ECO:0000269|PubMed:25789606,
CC       ECO:0000269|PubMed:25827751}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
CC   -!- CAUTION: Although strongly related to other members of the family,
CC       lacks the kinase activity. A conserved Asp/Glu residue present in other
CC       members of the family, which coordinates the Mn(2+) ion and the ion-
CC       pair Lys and is indispensable for kinase activity, is replaced by a Gln
CC       in position 258. {ECO:0000269|PubMed:25789606}.
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DR   EMBL; AK056789; BAB71285.1; -; mRNA.
DR   EMBL; AY358197; AAQ88564.1; -; mRNA.
DR   EMBL; AC079210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC136686; AAI36687.1; -; mRNA.
DR   EMBL; BC136689; AAI36690.1; -; mRNA.
DR   EMBL; AL133105; CAB61412.1; -; mRNA.
DR   CCDS; CCDS11679.1; -.
DR   PIR; T42684; T42684.
DR   RefSeq; NP_001230675.1; NM_001243746.1.
DR   RefSeq; NP_060035.2; NM_017565.3.
DR   PDB; 5WRR; X-ray; 2.51 A; A/B=89-526.
DR   PDB; 5WRS; X-ray; 2.75 A; A/B=89-526.
DR   PDB; 5YH2; X-ray; 3.55 A; A/B=63-529.
DR   PDB; 5YH3; X-ray; 3.30 A; A/B=63-529.
DR   PDBsum; 5WRR; -.
DR   PDBsum; 5WRS; -.
DR   PDBsum; 5YH2; -.
DR   PDBsum; 5YH3; -.
DR   AlphaFoldDB; Q96MK3; -.
DR   SMR; Q96MK3; -.
DR   BioGRID; 120133; 1.
DR   IntAct; Q96MK3; 5.
DR   STRING; 9606.ENSP00000468308; -.
DR   GlyCosmos; Q96MK3; 7 sites, 1 glycan.
DR   GlyGen; Q96MK3; 7 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q96MK3; -.
DR   PhosphoSitePlus; Q96MK3; -.
DR   BioMuta; FAM20A; -.
DR   DMDM; 269849750; -.
DR   jPOST; Q96MK3; -.
DR   MassIVE; Q96MK3; -.
DR   PaxDb; 9606-ENSP00000468308; -.
DR   PeptideAtlas; Q96MK3; -.
DR   ProteomicsDB; 77370; -.
DR   Antibodypedia; 31793; 136 antibodies from 23 providers.
DR   DNASU; 54757; -.
DR   Ensembl; ENST00000592554.2; ENSP00000468308.1; ENSG00000108950.12.
DR   GeneID; 54757; -.
DR   KEGG; hsa:54757; -.
DR   MANE-Select; ENST00000592554.2; ENSP00000468308.1; NM_017565.4; NP_060035.2.
DR   UCSC; uc002jho.4; human.
DR   AGR; HGNC:23015; -.
DR   CTD; 54757; -.
DR   DisGeNET; 54757; -.
DR   GeneCards; FAM20A; -.
DR   HGNC; HGNC:23015; FAM20A.
DR   HPA; ENSG00000108950; Tissue enhanced (liver).
DR   MalaCards; FAM20A; -.
DR   MIM; 204690; phenotype.
DR   MIM; 611062; gene.
DR   neXtProt; NX_Q96MK3; -.
DR   OpenTargets; ENSG00000108950; -.
DR   Orphanet; 1031; Enamel-renal syndrome.
DR   PharmGKB; PA134888583; -.
DR   VEuPathDB; HostDB:ENSG00000108950; -.
DR   eggNOG; KOG3829; Eukaryota.
DR   GeneTree; ENSGT00950000182951; -.
DR   HOGENOM; CLU_028926_2_0_1; -.
DR   InParanoid; Q96MK3; -.
DR   OMA; PLTQCCI; -.
DR   OrthoDB; 5382325at2759; -.
DR   PhylomeDB; Q96MK3; -.
DR   PathwayCommons; Q96MK3; -.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SignaLink; Q96MK3; -.
DR   BioGRID-ORCS; 54757; 21 hits in 1146 CRISPR screens.
DR   ChiTaRS; FAM20A; human.
DR   GeneWiki; FAM20A; -.
DR   GenomeRNAi; 54757; -.
DR   Pharos; Q96MK3; Tbio.
DR   PRO; PR:Q96MK3; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q96MK3; Protein.
DR   Bgee; ENSG00000108950; Expressed in right lobe of liver and 128 other cell types or tissues.
DR   ExpressionAtlas; Q96MK3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
DR   GO; GO:0031214; P:biomineral tissue development; IMP:UniProtKB.
DR   GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0070166; P:enamel mineralization; IMP:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   GO; GO:0044691; P:tooth eruption; IMP:UniProtKB.
DR   CDD; cd10469; FAM20A_C; 1.
DR   InterPro; IPR024869; FAM20.
DR   InterPro; IPR009581; FAM20_C.
DR   PANTHER; PTHR12450; DENTIN MATRIX PROTEIN 4 PROTEIN FAM20; 1.
DR   PANTHER; PTHR12450:SF12; PSEUDOKINASE FAM20A; 1.
DR   Pfam; PF06702; Fam20C; 1.
DR   Genevisible; Q96MK3; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Amelogenesis imperfecta; Biomineralization; Disease variant;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..541
FT                   /note="Pseudokinase FAM20A"
FT                   /id="PRO_0000008743"
FT   REGION          38..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        538
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        314..330
FT                   /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT   DISULFID        319..323
FT                   /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT   DISULFID        378..452
FT                   /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT   DISULFID        453..512
FT                   /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT   VARIANT         173
FT                   /note="L -> R (in AI1G; impaired folding of the protein;
FT                   abolishes ability to activate FAM20C protein kinase
FT                   activity)"
FT                   /evidence="ECO:0000269|PubMed:23434854,
FT                   ECO:0000269|PubMed:25789606"
FT                   /id="VAR_072170"
FT   VARIANT         197..214
FT                   /note="DYSQDEKALLGACDCTQI -> V (in AI1G)"
FT                   /evidence="ECO:0000269|PubMed:21990045"
FT                   /id="VAR_066859"
FT   VARIANT         331
FT                   /note="G -> D (in AI1G; impaired folding of the protein;
FT                   abolishes ability to activate FAM20C protein kinase
FT                   activity; dbSNP:rs981673034)"
FT                   /evidence="ECO:0000269|PubMed:23468644,
FT                   ECO:0000269|PubMed:25789606"
FT                   /id="VAR_072171"
FT   VARIANT         332
FT                   /note="N -> K (in dbSNP:rs2302234)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_059282"
FT   VARIANT         403
FT                   /note="D -> N (in AI1G; impaired folding of the protein;
FT                   abolishes ability to activate FAM20C protein kinase
FT                   activity; dbSNP:rs377432171)"
FT                   /evidence="ECO:0000269|PubMed:24196488,
FT                   ECO:0000269|PubMed:25789606"
FT                   /id="VAR_072172"
FT   VARIANT         530
FT                   /note="L -> S (in dbSNP:rs2907373)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:17974005"
FT                   /id="VAR_059283"
FT   MUTAGEN         258
FT                   /note="Q->E: Able to hydrolyze ATP and display some protein
FT                   kinase activity."
FT                   /evidence="ECO:0000269|PubMed:25789606"
FT   HELIX           91..97
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           99..102
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   TURN            112..114
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           119..143
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           160..167
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          172..174
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           179..190
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          193..198
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           200..203
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   TURN            212..214
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:5YH3"
FT   STRAND          224..228
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          233..238
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           252..254
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           259..272
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          281..287
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           288..291
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   TURN            292..295
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           299..303
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          305..307
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          313..316
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           318..322
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          328..330
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          332..342
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   TURN            347..349
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          352..356
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:5YH3"
FT   TURN            371..373
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           376..381
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   TURN            385..388
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           390..406
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          413..417
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           418..420
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   STRAND          434..436
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           443..446
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           447..452
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           457..466
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           469..471
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           473..481
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   TURN            485..488
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           492..516
FT                   /evidence="ECO:0007829|PDB:5WRR"
FT   HELIX           518..521
FT                   /evidence="ECO:0007829|PDB:5WRR"
SQ   SEQUENCE   541 AA;  61417 MW;  B44A4655996279A1 CRC64;
     MPGLRRDRLL TLLLLGALLS ADLYFHLWPQ VQRQLRPRER PRGCPCTGRA SSLARDSAAA
     ASDPGTIVHN FSRTEPRTEP AGGSHSGSSS KLQALFAHPL YNVPEEPPLL GAEDSLLASQ
     EALRYYRRKV ARWNRRHKMY REQMNLTSLD PPLQLRLEAS WVQFHLGINR HGLYSRSSPV
     VSKLLQDMRH FPTISADYSQ DEKALLGACD CTQIVKPSGV HLKLVLRFSD FGKAMFKPMR
     QQRDEETPVD FFYFIDFQRH NAEIAAFHLD RILDFRRVPP TVGRIVNVTK EILEVTKNEI
     LQSVFFVSPA SNVCFFAKCP YMCKTEYAVC GNPHLLEGSL SAFLPSLNLA PRLSVPNPWI
     RSYTLAGKEE WEVNPLYCDT VKQIYPYNNS QRLLNVIDMA IFDFLIGNMD RHHYEMFTKF
     GDDGFLIHLD NARGFGRHSH DEISILSPLS QCCMIKKKTL LHLQLLAQAD YRLSDVMRES
     LLEDQLSPVL TEPHLLALDR RLQTILRTVE GCIVAHGQQS VIVDGPVEQL APDSGQANLT
     S
//