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

 FA20C_HUMAN             Reviewed;         584 AA.
Q8IXL6; A4D2Q5; L8B5W8; Q5I0W9; Q7Z4I0; Q9NPT2;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 2.
25-OCT-2017, entry version 123.
RecName: Full=Extracellular serine/threonine protein kinase FAM20C {ECO:0000305};
EC=2.7.11.1 {ECO:0000269|PubMed:22582013, ECO:0000269|PubMed:23754375, ECO:0000269|PubMed:25789606};
AltName: Full=Dentin matrix protein 4 {ECO:0000250|UniProtKB:Q5MJS3};
Short=DMP-4 {ECO:0000250|UniProtKB:Q5MJS3};
AltName: Full=Golgi casein kinase {ECO:0000303|PubMed:22582013};
AltName: Full=Golgi-enriched fraction casein kinase {ECO:0000303|PubMed:22582013};
Short=GEF-CK {ECO:0000303|PubMed:22582013};
Flags: Precursor;
Name=FAM20C {ECO:0000312|HGNC:HGNC:22140};
Synonyms=DMP4 {ECO:0000250|UniProtKB:Q5MJS3};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Wu C., Ding P., Han W., Rui M., Wang Y., Song Q., Ma D.;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Kitagawa H., Izumikawa T., Koike T.;
"Molecular cloning and characterization of a novel xylosylkinase.";
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBCELLULAR LOCATION,
AUTOPHOSPHORYLATION, GLYCOSYLATION AT ASN-101; ASN-335 AND ASN-470,
AND MUTAGENESIS OF 93-LEU--ASP-95; ASN-101; ASN-335; ASN-470 AND
ASP-478.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[9]
TISSUE SPECIFICITY.
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).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-470.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[11]
FUNCTION, CATALYTIC ACTIVITY, MANGANESE-BINDING, MUTAGENESIS OF
ASP-478, VARIANTS RNS ASN-258; ARG-280; SER-328; ARG-379; GLU-379;
ARG-388; ASN-451 AND TRP-549, AND CHARACTERIZATION OF VARIANTS RNS
SER-328 AND ASN-451.
PubMed=22582013; DOI=10.1126/science.1217817;
Tagliabracci V.S., Engel J.L., Wen J., Wiley S.E., Worby C.A.,
Kinch L.N., Xiao J., Grishin N.V., Dixon J.E.;
"Secreted kinase phosphorylates extracellular proteins that regulate
biomineralization.";
Science 336:1150-1153(2012).
[12]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
ACTIVE SITE, AND MUTAGENESIS OF LYS-271; LYS-285; GLU-306; GLU-311;
ARG-408; ASP-458 AND ASP-458.
PubMed=23754375; DOI=10.1073/pnas.1309211110;
Xiao J., Tagliabracci V.S., Wen J., Kim S.A., Dixon J.E.;
"Crystal structure of the Golgi casein kinase.";
Proc. Natl. Acad. Sci. U.S.A. 110:10574-10579(2013).
[13]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH
FAM20A, MUTAGENESIS OF GLU-306 AND ASP-478, VARIANTS RNS MET-268 AND
SER-328, AND CHARACTERIZATION OF VARIANTS RNS MET-268 AND SER-328.
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).
[14]
VARIANTS RNS ARG-379; GLU-379; ARG-388 AND TRP-549.
PubMed=17924334; DOI=10.1086/522240;
Simpson M.A., Hsu R., Keir L.S., Hao J., Sivapalan G., Ernst L.M.,
Zackai E.H., Al-Gazali L.I., Hulskamp G., Kingston H.M.,
Prescott T.E., Ion A., Patton M.A., Murday V., George A., Crosby A.H.;
"Mutations in FAM20C are associated with lethal osteosclerotic bone
dysplasia (Raine syndrome), highlighting a crucial molecule in bone
development.";
Am. J. Hum. Genet. 81:906-912(2007).
-!- 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:22582013, PubMed:23754375, PubMed:25789606).
Constitutes the main protein kinase for extracellular proteins,
generating the majority of the extracellular phosphoproteome
(PubMed:26091039). Mainly phosphorylates proteins within the Ser-
x-Glu/pSer motif, but also displays a broader substrate
specificity (PubMed:26091039). Phosphorylates casein as well as a
number of proteins involved in biomineralization such as AMELX,
AMTN, ENAM and SPP1 (PubMed:22582013, PubMed:25789606). In
addition to its role in biomineralization, also plays a role in
lipid homeostasis, wound healing and cell migration and adhesion
(PubMed:26091039). {ECO:0000269|PubMed:22582013,
ECO:0000269|PubMed:23754375, ECO:0000269|PubMed:25789606,
ECO:0000269|PubMed:26091039}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:22582013, ECO:0000269|PubMed:23754375,
ECO:0000269|PubMed:25789606}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:23754375,
ECO:0000305|PubMed:22582013};
-!- ENZYME REGULATION: Serine/threonine protein kinase activity is
increased upon interaction with FAM20A.
{ECO:0000269|PubMed:25789606}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.8 uM for manganese/ATP {ECO:0000269|PubMed:23754375};
-!- SUBUNIT: Interacts with FAM20A; probably forming a heterotetramer
of 2 subunits of FAM20A and 2 subunits of FAM20C.
{ECO:0000269|PubMed:25789606}.
-!- INTERACTION:
Q9NP70:AMBN; NbExp=2; IntAct=EBI-7147442, EBI-11893530;
Q6UX39:AMTN; NbExp=2; IntAct=EBI-7147442, EBI-11892684;
O14791:APOL1; NbExp=2; IntAct=EBI-7147442, EBI-1221934;
P05060:CHGB; NbExp=2; IntAct=EBI-7147442, EBI-712619;
P02666:CSN2 (xeno); NbExp=3; IntAct=EBI-7147442, EBI-5260183;
Q9NRM1:ENAM; NbExp=2; IntAct=EBI-7147442, EBI-11892601;
Q96MK3:FAM20A; NbExp=3; IntAct=EBI-7147442, EBI-11892970;
P02671:FGA; NbExp=2; IntAct=EBI-7147442, EBI-348571;
P08833:IGFBP1; NbExp=2; IntAct=EBI-7147442, EBI-13646303;
P02810:PRH2; NbExp=2; IntAct=EBI-7147442, EBI-738601;
P01008:SERPINC1; NbExp=2; IntAct=EBI-7147442, EBI-1039832;
P10451:SPP1; NbExp=3; IntAct=EBI-7147442, EBI-723648;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26091039}.
Golgi apparatus {ECO:0000250|UniProtKB:Q5MJS3}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8IXL6-1; Sequence=Displayed;
Name=2;
IsoId=Q8IXL6-2; Sequence=VSP_040834;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:15676076}.
-!- PTM: N-glycosylation is required for folding.
{ECO:0000305|PubMed:26091039}.
-!- PTM: Autophosphorylated. {ECO:0000269|PubMed:26091039}.
-!- DISEASE: Raine syndrome (RNS) [MIM:259775]: Autosomal recessive
osteosclerotic bone dysplasia with neonatal lethal outcome.
Clinical features include generalized osteosclerosis, craniofacial
dysplasia and microcephaly. {ECO:0000269|PubMed:17924334,
ECO:0000269|PubMed:22582013, ECO:0000269|PubMed:25789606}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH40074.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=EAL23705.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF533706; AAQ09019.1; -; mRNA.
EMBL; AB545605; BAM78534.1; -; mRNA.
EMBL; AC093627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC145676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC187652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236966; EAL23705.1; ALT_INIT; Genomic_DNA.
EMBL; CH471144; EAW87149.1; -; Genomic_DNA.
EMBL; BC040074; AAH40074.1; ALT_INIT; mRNA.
EMBL; BC087853; AAH87853.1; -; mRNA.
EMBL; AL390147; CAB99089.2; -; mRNA.
CCDS; CCDS47522.1; -. [Q8IXL6-1]
PIR; T51872; T51872.
RefSeq; NP_064608.2; NM_020223.3. [Q8IXL6-1]
UniGene; Hs.134742; -.
UniGene; Hs.733582; -.
ProteinModelPortal; Q8IXL6; -.
SMR; Q8IXL6; -.
BioGrid; 121294; 7.
IntAct; Q8IXL6; 71.
MINT; MINT-6940404; -.
STRING; 9606.ENSP00000322323; -.
iPTMnet; Q8IXL6; -.
PhosphoSitePlus; Q8IXL6; -.
BioMuta; FAM20C; -.
DMDM; 327478506; -.
EPD; Q8IXL6; -.
MaxQB; Q8IXL6; -.
PaxDb; Q8IXL6; -.
PeptideAtlas; Q8IXL6; -.
PRIDE; Q8IXL6; -.
Ensembl; ENST00000313766; ENSP00000322323; ENSG00000177706. [Q8IXL6-1]
GeneID; 56975; -.
KEGG; hsa:56975; -.
UCSC; uc003sip.4; human. [Q8IXL6-1]
CTD; 56975; -.
DisGeNET; 56975; -.
EuPathDB; HostDB:ENSG00000177706.8; -.
GeneCards; FAM20C; -.
H-InvDB; HIX0019573; -.
HGNC; HGNC:22140; FAM20C.
HPA; HPA019823; -.
MalaCards; FAM20C; -.
MIM; 259775; phenotype.
MIM; 611061; gene.
neXtProt; NX_Q8IXL6; -.
OpenTargets; ENSG00000177706; -.
Orphanet; 1832; Lethal osteosclerotic bone dysplasia.
PharmGKB; PA134898453; -.
eggNOG; KOG3829; Eukaryota.
eggNOG; ENOG410XQEJ; LUCA.
GeneTree; ENSGT00390000007484; -.
HOGENOM; HOG000231437; -.
HOVERGEN; HBG051635; -.
InParanoid; Q8IXL6; -.
KO; K21958; -.
OMA; HRILDVM; -.
OrthoDB; EOG091G1BEO; -.
PhylomeDB; Q8IXL6; -.
TreeFam; TF313276; -.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
GeneWiki; FAM20C; -.
GenomeRNAi; 56975; -.
PRO; PR:Q8IXL6; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000177706; -.
CleanEx; HS_FAM20C; -.
Genevisible; Q8IXL6; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
GO; GO:0031214; P:biomineral tissue development; IMP:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0097187; P:dentinogenesis; IEA:Ensembl.
GO; GO:0070166; P:enamel mineralization; IEA:Ensembl.
GO; GO:0071895; P:odontoblast differentiation; IEA:Ensembl.
GO; GO:0036179; P:osteoclast maturation; IEA:Ensembl.
GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0051174; P:regulation of phosphorus metabolic process; IEA:Ensembl.
InterPro; IPR024869; FAM20.
InterPro; IPR009581; FAM20_C.
PANTHER; PTHR12450; PTHR12450; 1.
Pfam; PF06702; Fam20C; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Biomineralization; Calcium;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; Golgi apparatus; Kinase; Manganese;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Secreted; Serine/threonine-protein kinase; Signal; Transferase.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 92 {ECO:0000269|PubMed:26091039}.
/FTId=PRO_0000433883.
CHAIN 93 584 Extracellular serine/threonine protein
kinase FAM20C.
/FTId=PRO_0000008747.
NP_BIND 389 392 ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
REGION 354 565 Kinase domain.
{ECO:0000305|PubMed:22582013}.
ACT_SITE 458 458 {ECO:0000269|PubMed:23754375}.
METAL 306 306 Manganese.
{ECO:0000250|UniProtKB:Q9XTW2}.
METAL 478 478 Manganese. {ECO:0000305|PubMed:22582013}.
BINDING 269 269 ATP; via amide nitrogen.
{ECO:0000250|UniProtKB:Q9XTW2}.
BINDING 285 285 ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
BINDING 306 306 ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
BINDING 463 463 ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
BINDING 478 478 ATP. {ECO:0000250|UniProtKB:Q9XTW2}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 470 470 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:26091039}.
DISULFID 362 378 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 367 371 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 426 500 {ECO:0000250|UniProtKB:Q9XTW2}.
DISULFID 501 560 {ECO:0000250|UniProtKB:Q9XTW2}.
VAR_SEQ 1 332 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_040834.
VARIANT 258 258 I -> N (in RNS).
{ECO:0000269|PubMed:22582013}.
/FTId=VAR_073660.
VARIANT 268 268 T -> M (in RNS; mild non-lethal form;
decreased protein kinase activity;
dbSNP:rs778899041).
{ECO:0000269|PubMed:25789606}.
/FTId=VAR_073661.
VARIANT 280 280 G -> R (in RNS; dbSNP:rs779708323).
{ECO:0000269|PubMed:22582013}.
/FTId=VAR_073662.
VARIANT 328 328 P -> S (in RNS; mild non-lethal form;
decreased protein kinase activity; FAM20A
is still able to increase remaining
protein kinase activity;
dbSNP:rs797044462).
{ECO:0000269|PubMed:22582013,
ECO:0000269|PubMed:25789606}.
/FTId=VAR_073663.
VARIANT 379 379 G -> E (in RNS; dbSNP:rs796051852).
{ECO:0000269|PubMed:17924334,
ECO:0000269|PubMed:22582013}.
/FTId=VAR_037530.
VARIANT 379 379 G -> R (in RNS).
{ECO:0000269|PubMed:17924334,
ECO:0000269|PubMed:22582013}.
/FTId=VAR_037531.
VARIANT 388 388 L -> R (in RNS; dbSNP:rs796051849).
{ECO:0000269|PubMed:17924334,
ECO:0000269|PubMed:22582013}.
/FTId=VAR_037532.
VARIANT 451 451 D -> N (in RNS; mild non-lethal form;
decreased protein kinase activity).
{ECO:0000269|PubMed:22582013}.
/FTId=VAR_073664.
VARIANT 549 549 R -> W (in RNS; dbSNP:rs796051850).
{ECO:0000269|PubMed:17924334,
ECO:0000269|PubMed:22582013}.
/FTId=VAR_037533.
MUTAGEN 91 93 LQD->AAA: Does not affect secretion or
activity. {ECO:0000269|PubMed:26091039}.
MUTAGEN 101 101 N->A: Impaired secretion; when associated
with A-335 and A-470.
{ECO:0000269|PubMed:26091039}.
MUTAGEN 271 271 K->A: Reduced kinase activity.
{ECO:0000269|PubMed:23754375}.
MUTAGEN 285 285 K->A: Reduced kinase activity.
{ECO:0000269|PubMed:23754375}.
MUTAGEN 306 306 E->A,Q: Strongly reduced kinase activity.
{ECO:0000269|PubMed:23754375,
ECO:0000269|PubMed:25789606}.
MUTAGEN 311 311 E->A: Reduced kinase activity.
{ECO:0000269|PubMed:23754375}.
MUTAGEN 335 335 N->A: Impaired secretion; when associated
with A-101 and A-470.
{ECO:0000269|PubMed:26091039}.
MUTAGEN 408 408 R->A: Reduced kinase activity.
{ECO:0000269|PubMed:23754375}.
MUTAGEN 458 458 D->A: Abrogates kinase activity.
{ECO:0000269|PubMed:23754375}.
MUTAGEN 470 470 N->A: Impaired secretion; when associated
with A-101 and A-335.
{ECO:0000269|PubMed:26091039}.
MUTAGEN 478 478 D->A: Unable to bind manganese; abrogates
kinase activity.
{ECO:0000269|PubMed:22582013,
ECO:0000269|PubMed:23754375,
ECO:0000269|PubMed:25789606,
ECO:0000269|PubMed:26091039}.
CONFLICT 274 288 MTFQNYGQALFKPMK -> FLSDKPFLFLSCFLR (in
Ref. 6; CAB99089). {ECO:0000305}.
CONFLICT 564 564 N -> D (in Ref. 5; AAH87853 and 6;
CAB99089). {ECO:0000305}.
SEQUENCE 584 AA; 66234 MW; ECD278B5EA681FEF CRC64;
MKMMLVRRFR VLILMVFLVA CALHIALDLL PRLERRGARP SGEPGCSCAQ PAAEVAAPGW
AQVRGRPGEP PAASSAAGDA GWPNKHTLRI LQDFSSDPSS NLSSHSLEKL PPAAEPAERA
LRGRDPGALR PHDPAHRPLL RDPGPRRSES PPGPGGDASL LARLFEHPLY RVAVPPLTEE
DVLFNVNSDT RLSPKAAENP DWPHAGAEGA EFLSPGEAAV DSYPNWLKFH IGINRYELYS
RHNPAIEALL HDLSSQRITS VAMKSGGTQL KLIMTFQNYG QALFKPMKQT REQETPPDFF
YFSDYERHNA EIAAFHLDRI LDFRRVPPVA GRMVNMTKEI RDVTRDKKLW RTFFISPANN
ICFYGECSYY CSTEHALCGK PDQIEGSLAA FLPDLSLAKR KTWRNPWRRS YHKRKKAEWE
VDPDYCEEVK QTPPYDSSHR ILDVMDMTIF DFLMGNMDRH HYETFEKFGN ETFIIHLDNG
RGFGKYSHDE LSILVPLQQC CRIRKSTYLR LQLLAKEEYK LSLLMAESLR GDQVAPVLYQ
PHLEALDRRL RVVLKAVRDC VERNGLHSVV DDDLDTEHRA ASAR


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