GenomeNet

Database: UniProt
Entry: Q96MK3
LinkDB: Q96MK3
Original site: Q96MK3 
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   10-APR-2019, entry version 134.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-332 AND
RP   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP   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.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics 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.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   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
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-332 AND
RP   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
RT   project: 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
RP   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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.,
RA   Du Y., Williams S.C.;
RT   "FAM20: an evolutionarily conserved family of secreted proteins
RT   expressed 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.,
RA   Petukhova L., Christiano A.M.;
RT   "Autosomal recessive gingival hyperplasia and dental anomalies caused
RT   by a 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
RT   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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver 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.,
RA   Laarabi F.Z., Lyahyai J., Sefiani A.;
RT   "Further evidence for causal FAM20A mutations and first case of
RT   amelogenesis imperfecta and gingival hyperplasia syndrome in Morocco:
RT   a 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.,
RA   Jung S.E., Song S.J., Yildirim M., Bayram M., Tuna E.B., Gencay K.,
RA   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.,
RA   Himmerkus N., Koike T., Poulter J., Klootwijk E., Robinette S.L.,
RA   Howie A.J., Patel V., Figueres M.L., Stanescu H.C., Issler N.,
RA   Nicholson J.K., Bockenhauer D., Laing C., Walsh S.B., McCredie D.A.,
RA   Povey S., Asselin A., Picard A., Coulomb A., Medlar A.J.,
RA   Bailleul-Forestier I., Verloes A., Le Caignec C., Roussey G.,
RA   Guiol J., Isidor B., Logan C., Shore R., Johnson C., Inglehearn C.,
RA   Al-Bahlani S., Schmittbuhl M., Clauss F., Huckert M., Laugel V.,
RA   Ginglinger E., Pajarola S., Sparta G., Bartholdi D., Rauch A.,
RA   Addor M.C., Yamaguti P.M., Safatle H.P., Acevedo A.C.,
RA   Martelli-Junior H., dos Santos Netos P.E., Coletta R.D., Gruessel S.,
RA   Sandmann C., Ruehmann D., Langman C.B., Scheinman S.J.,
RA   Ozdemir-Ozenen D., Hart T.C., Hart P.S., Neugebauer U., Schlatter E.,
RA   Houillier P., Gahl W.A., Vikkula M., Bloch-Zupan A., Bleich M.,
RA   Kitagawa H., Unwin R.J., Mighell A., Berdal A., Kleta R.;
RT   "Nephrocalcinosis (enamel renal syndrome) caused by autosomal
RT   recessive 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
CC       increases the ability of FAM20C to phosphorylate the proteins that
CC       form the 'matrix' that guides the deposition of the enamel
CC       minerals. {ECO:0000269|PubMed:25789606}.
CC   -!- SUBUNIT: Interacts with FAM20C; probably forming a heterotetramer
CC       of 2 subunits of FAM20A and 2 subunits of FAM20C.
CC       {ECO:0000269|PubMed:25789606}.
CC   -!- INTERACTION:
CC       Q8IXL6:FAM20C; NbExp=3; IntAct=EBI-11892970, EBI-7147442;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8CID3}.
CC       Golgi apparatus {ECO:0000269|PubMed:23468644}. Endoplasmic
CC       reticulum {ECO:0000250|UniProtKB:Q8CID3}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung and liver.
CC       Intermediate levels in thymus and ovary.
CC       {ECO:0000269|PubMed:15676076}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8CID3}.
CC   -!- DISEASE: Amelogenesis imperfecta 1G (AI1G) [MIM:204690]: A
CC       disorder characterized by dental anomalies, gingival overgrowth,
CC       and nephrocalcinosis. Dental anomalies include hypoplastic
CC       amelogenesis imperfecta, intrapulpal calcifications, delay of
CC       tooth eruption, hypodontia/oligodontia, pericoronal radiolucencies
CC       and unerupted teeth. {ECO:0000269|PubMed:21549343,
CC       ECO:0000269|PubMed:21990045, ECO:0000269|PubMed:23434854,
CC       ECO:0000269|PubMed:23468644, ECO:0000269|PubMed:23697977,
CC       ECO:0000269|PubMed:24196488, ECO:0000269|PubMed:24259279,
CC       ECO:0000269|PubMed:24756937, ECO:0000269|PubMed:25636655,
CC       ECO:0000269|PubMed:25789606, ECO:0000269|PubMed:25827751}.
CC       Note=The disease is caused by mutations affecting the gene
CC       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
CC       other members of the family, which coordinates the Mn(2+) ion and
CC       the ion-pair Lys and is indispensable for kinase activity, is
CC       replaced by a Gln in position 258. {ECO:0000269|PubMed:25789606}.
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   UniGene; Hs.268874; -.
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   ProteinModelPortal; Q96MK3; -.
DR   SMR; Q96MK3; -.
DR   IntAct; Q96MK3; 5.
DR   STRING; 9606.ENSP00000468308; -.
DR   iPTMnet; Q96MK3; -.
DR   PhosphoSitePlus; Q96MK3; -.
DR   BioMuta; FAM20A; -.
DR   DMDM; 269849750; -.
DR   jPOST; Q96MK3; -.
DR   PaxDb; Q96MK3; -.
DR   PeptideAtlas; Q96MK3; -.
DR   PRIDE; Q96MK3; -.
DR   ProteomicsDB; 77370; -.
DR   Ensembl; ENST00000592554; ENSP00000468308; ENSG00000108950.
DR   GeneID; 54757; -.
DR   KEGG; hsa:54757; -.
DR   UCSC; uc002jho.4; human.
DR   CTD; 54757; -.
DR   DisGeNET; 54757; -.
DR   EuPathDB; HostDB:ENSG00000108950.11; -.
DR   GeneCards; FAM20A; -.
DR   H-InvDB; HIX0014117; -.
DR   HGNC; HGNC:23015; FAM20A.
DR   HPA; HPA048964; -.
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   eggNOG; KOG3829; Eukaryota.
DR   eggNOG; ENOG410XQEJ; LUCA.
DR   GeneTree; ENSGT00950000182951; -.
DR   HOGENOM; HOG000231437; -.
DR   HOVERGEN; HBG051635; -.
DR   InParanoid; Q96MK3; -.
DR   KO; K21957; -.
DR   OMA; LLHDMRH; -.
DR   OrthoDB; 484324at2759; -.
DR   PhylomeDB; 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   ChiTaRS; FAM20A; human.
DR   GeneWiki; FAM20A; -.
DR   GenomeRNAi; 54757; -.
DR   PRO; PR:Q96MK3; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000108950; Expressed in 133 organ(s), highest expression level in right lobe of liver.
DR   ExpressionAtlas; Q96MK3; baseline and differential.
DR   Genevisible; Q96MK3; HS.
DR   GO; GO:0005623; C:cell; 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:0006468; P:protein phosphorylation; IEA:GOC.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   GO; GO:0044691; P:tooth eruption; IMP:UniProtKB.
DR   InterPro; IPR024869; FAM20.
DR   InterPro; IPR009581; FAM20_C.
DR   PANTHER; PTHR12450; PTHR12450; 1.
DR   Pfam; PF06702; Fam20C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amelogenesis imperfecta; Biomineralization;
KW   Complete proteome; Disease mutation; Disulfide bond;
KW   Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Polymorphism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     33       {ECO:0000255}.
FT   CHAIN        34    541       Pseudokinase FAM20A.
FT                                /FTId=PRO_0000008743.
FT   CARBOHYD     70     70       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    145    145       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    287    287       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    388    388       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    538    538       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    314    330       {ECO:0000250|UniProtKB:Q9XTW2}.
FT   DISULFID    319    323       {ECO:0000250|UniProtKB:Q9XTW2}.
FT   DISULFID    378    452       {ECO:0000250|UniProtKB:Q9XTW2}.
FT   DISULFID    453    512       {ECO:0000250|UniProtKB:Q9XTW2}.
FT   VARIANT     173    173       L -> R (in AI1G; impaired folding of the
FT                                protein; abolishes ability to activate
FT                                FAM20C protein kinase activity).
FT                                {ECO:0000269|PubMed:23434854,
FT                                ECO:0000269|PubMed:25789606}.
FT                                /FTId=VAR_072170.
FT   VARIANT     197    214       DYSQDEKALLGACDCTQI -> V (in AI1G).
FT                                {ECO:0000269|PubMed:21990045}.
FT                                /FTId=VAR_066859.
FT   VARIANT     331    331       G -> D (in AI1G; impaired folding of the
FT                                protein; abolishes ability to activate
FT                                FAM20C protein kinase activity;
FT                                dbSNP:rs981673034).
FT                                {ECO:0000269|PubMed:23468644,
FT                                ECO:0000269|PubMed:25789606}.
FT                                /FTId=VAR_072171.
FT   VARIANT     332    332       N -> K (in dbSNP:rs2302234).
FT                                {ECO:0000269|PubMed:12975309,
FT                                ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_059282.
FT   VARIANT     403    403       D -> N (in AI1G; impaired folding of the
FT                                protein; abolishes ability to activate
FT                                FAM20C protein kinase activity;
FT                                dbSNP:rs377432171).
FT                                {ECO:0000269|PubMed:24196488,
FT                                ECO:0000269|PubMed:25789606}.
FT                                /FTId=VAR_072172.
FT   VARIANT     530    530       L -> S (in dbSNP:rs2907373).
FT                                {ECO:0000269|PubMed:12975309,
FT                                ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:17974005}.
FT                                /FTId=VAR_059283.
FT   MUTAGEN     258    258       Q->E: Able to hydrolyze ATP and display
FT                                some protein kinase activity.
FT                                {ECO:0000269|PubMed:25789606}.
FT   HELIX        91     97       {ECO:0000244|PDB:5WRR}.
FT   HELIX        99    102       {ECO:0000244|PDB:5WRR}.
FT   TURN        112    114       {ECO:0000244|PDB:5WRR}.
FT   STRAND      115    117       {ECO:0000244|PDB:5WRR}.
FT   HELIX       119    143       {ECO:0000244|PDB:5WRR}.
FT   HELIX       160    167       {ECO:0000244|PDB:5WRR}.
FT   STRAND      172    174       {ECO:0000244|PDB:5WRR}.
FT   HELIX       179    190       {ECO:0000244|PDB:5WRR}.
FT   STRAND      193    198       {ECO:0000244|PDB:5WRR}.
FT   HELIX       200    203       {ECO:0000244|PDB:5WRR}.
FT   STRAND      206    208       {ECO:0000244|PDB:5WRR}.
FT   TURN        212    214       {ECO:0000244|PDB:5WRR}.
FT   STRAND      220    222       {ECO:0000244|PDB:5YH3}.
FT   STRAND      224    228       {ECO:0000244|PDB:5WRR}.
FT   STRAND      233    238       {ECO:0000244|PDB:5WRR}.
FT   HELIX       244    246       {ECO:0000244|PDB:5WRR}.
FT   HELIX       252    254       {ECO:0000244|PDB:5WRR}.
FT   HELIX       259    272       {ECO:0000244|PDB:5WRR}.
FT   STRAND      281    287       {ECO:0000244|PDB:5WRR}.
FT   HELIX       288    291       {ECO:0000244|PDB:5WRR}.
FT   TURN        292    295       {ECO:0000244|PDB:5WRR}.
FT   HELIX       299    303       {ECO:0000244|PDB:5WRR}.
FT   STRAND      305    307       {ECO:0000244|PDB:5WRR}.
FT   STRAND      313    316       {ECO:0000244|PDB:5WRR}.
FT   HELIX       318    322       {ECO:0000244|PDB:5WRR}.
FT   STRAND      328    330       {ECO:0000244|PDB:5WRR}.
FT   STRAND      332    342       {ECO:0000244|PDB:5WRR}.
FT   TURN        347    349       {ECO:0000244|PDB:5WRR}.
FT   STRAND      352    356       {ECO:0000244|PDB:5WRR}.
FT   STRAND      364    366       {ECO:0000244|PDB:5YH3}.
FT   TURN        371    373       {ECO:0000244|PDB:5WRR}.
FT   HELIX       376    381       {ECO:0000244|PDB:5WRR}.
FT   TURN        385    388       {ECO:0000244|PDB:5WRR}.
FT   HELIX       390    406       {ECO:0000244|PDB:5WRR}.
FT   STRAND      413    417       {ECO:0000244|PDB:5WRR}.
FT   HELIX       418    420       {ECO:0000244|PDB:5WRR}.
FT   STRAND      434    436       {ECO:0000244|PDB:5WRR}.
FT   HELIX       443    446       {ECO:0000244|PDB:5WRR}.
FT   HELIX       447    452       {ECO:0000244|PDB:5WRR}.
FT   HELIX       457    466       {ECO:0000244|PDB:5WRR}.
FT   HELIX       469    471       {ECO:0000244|PDB:5WRR}.
FT   HELIX       473    481       {ECO:0000244|PDB:5WRR}.
FT   TURN        485    488       {ECO:0000244|PDB:5WRR}.
FT   HELIX       492    516       {ECO:0000244|PDB:5WRR}.
FT   HELIX       518    521       {ECO:0000244|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
//
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