XYLK_MOUSE
ID XYLK_MOUSE Reviewed; 409 AA.
AC Q8VCS3; Q3V201; Q6ZQA3; Q8BWX2;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Glycosaminoglycan xylosylkinase {ECO:0000250|UniProtKB:O75063};
DE EC=2.7.1.- {ECO:0000250|UniProtKB:O75063};
DE AltName: Full=Xylose kinase;
GN Name=Fam20b {ECO:0000312|MGI:MGI:2443990};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-409.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP TISSUE SPECIFICITY.
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=22900076; DOI=10.1371/journal.pone.0042988;
RA Ishikawa H.O., Xu A., Ogura E., Manning G., Irvine K.D.;
RT "The Raine syndrome protein FAM20C is a Golgi kinase that phosphorylates
RT bio-mineralization proteins.";
RL PLoS ONE 7:E42988-E42988(2012).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=22732358; DOI=10.1177/0300985812453177;
RA Vogel P., Hansen G.M., Read R.W., Vance R.B., Thiel M., Liu J.,
RA Wronski T.J., Smith D.D., Jeter-Jones S., Brommage R.;
RT "Amelogenesis imperfecta and other biomineralization defects in Fam20a and
RT Fam20c null mice.";
RL Vet. Pathol. 49:998-1017(2012).
CC -!- FUNCTION: Responsible for the 2-O-phosphorylation of xylose in the
CC glycosaminoglycan-protein linkage region of proteoglycans thereby
CC regulating the amount of mature GAG chains. Sulfated glycosaminoglycans
CC (GAGs), including heparan sulfate and chondroitin sulfate, are
CC synthesized on the so-called common GAG-protein linkage region
CC (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser) of core proteins,
CC which is formed by the stepwise addition of monosaccharide residues by
CC the respective specific glycosyltransferases. Xylose 2-O-
CC phosphorylation may influence the catalytic activity of B3GAT3 (GlcAT-
CC I) which completes the precursor tetrasaccharide of GAG-protein linkage
CC regions on which the repeating disaccharide region is synthesized.
CC {ECO:0000250|UniProtKB:O75063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
CC xylosyl)-L-seryl-[protein] + ATP = 3-O-(beta-D-galactosyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-2-O-phosphoxylosyl)-L-seryl-[protein]
CC + ADP + H(+); Xref=Rhea:RHEA:19461, Rhea:RHEA-COMP:12571, Rhea:RHEA-
CC COMP:14558, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:132090,
CC ChEBI:CHEBI:140494, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O75063};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9XTW2};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22900076}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Little expression detected in the secretory stage
CC enamel. Weak to moderate expression is observed in the gingivae and
CC odontoblasts. Strong expression in maturation stage ameloblasts.
CC {ECO:0000269|PubMed:21549343}.
CC -!- DISRUPTION PHENOTYPE: Embryos show severe stunting and increased
CC mortality at 13.5 dpc. {ECO:0000269|PubMed:22732358}.
CC -!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
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DR EMBL; AK049705; BAC33883.1; -; mRNA.
DR EMBL; AK132149; BAE20998.1; -; mRNA.
DR EMBL; CH466520; EDL39377.1; -; Genomic_DNA.
DR EMBL; BC019381; AAH19381.1; -; mRNA.
DR EMBL; BC023737; AAH23737.1; -; mRNA.
DR EMBL; BC024412; AAH24412.1; -; mRNA.
DR EMBL; BC031473; AAH31473.1; -; mRNA.
DR EMBL; AK129154; BAC97964.1; -; mRNA.
DR CCDS; CCDS15395.1; -.
DR RefSeq; NP_663388.1; NM_145413.4.
DR RefSeq; XP_006496799.1; XM_006496736.2.
DR RefSeq; XP_006496800.1; XM_006496737.2.
DR AlphaFoldDB; Q8VCS3; -.
DR SMR; Q8VCS3; -.
DR STRING; 10090.ENSMUSP00000083322; -.
DR GlyGen; Q8VCS3; 1 site.
DR PhosphoSitePlus; Q8VCS3; -.
DR SwissPalm; Q8VCS3; -.
DR EPD; Q8VCS3; -.
DR jPOST; Q8VCS3; -.
DR MaxQB; Q8VCS3; -.
DR PaxDb; Q8VCS3; -.
DR PeptideAtlas; Q8VCS3; -.
DR PRIDE; Q8VCS3; -.
DR ProteomicsDB; 275225; -.
DR Antibodypedia; 34415; 19 antibodies from 10 providers.
DR DNASU; 215015; -.
DR Ensembl; ENSMUST00000086153; ENSMUSP00000083322; ENSMUSG00000033557.
DR Ensembl; ENSMUST00000122424; ENSMUSP00000112534; ENSMUSG00000033557.
DR GeneID; 215015; -.
DR KEGG; mmu:215015; -.
DR UCSC; uc007dcp.1; mouse.
DR CTD; 9917; -.
DR MGI; MGI:2443990; Fam20b.
DR VEuPathDB; HostDB:ENSMUSG00000033557; -.
DR eggNOG; KOG3829; Eukaryota.
DR GeneTree; ENSGT00950000182951; -.
DR HOGENOM; CLU_028926_1_1_1; -.
DR InParanoid; Q8VCS3; -.
DR OMA; EGDIMEG; -.
DR OrthoDB; 484324at2759; -.
DR PhylomeDB; Q8VCS3; -.
DR TreeFam; TF313276; -.
DR BioGRID-ORCS; 215015; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Fam20b; mouse.
DR PRO; PR:Q8VCS3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VCS3; protein.
DR Bgee; ENSMUSG00000033557; Expressed in prostate gland ventral lobe and 243 other tissues.
DR Genevisible; Q8VCS3; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
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 ATP-binding; Disulfide bond; Glycoprotein; Golgi apparatus; Kinase;
KW Manganese; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..409
FT /note="Glycosaminoglycan xylosylkinase"
FT /id="PRO_0000008746"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..409
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 289
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 222..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 309
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 196..211
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 201..204
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 257..331
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 332..389
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
SQ SEQUENCE 409 AA; 46581 MW; 4BDD0C89D48C4187 CRC64;
MKLKQRVVLL AILLVIFIFT KVFLIDNLDT SAANREDQRA FHRMMTGLRV ELVPKLDHTL
QSPWEIAAQW VVPREVYPEE TPELGAIMHA MATKKIIKAD VGYKGTQLKA LLILEGGQKV
VFKPKRYSRD YVVEGEPYAG YDRHNAEVAA FHLDRILGFR RAPLVVGRYV NLRTEVKPVA
TEQLLSTFLT VGNNTCFYGK CYYCRETEPA CADGDMMEGS VTLWLPDVWP LQKHRHPWGR
TYREGKLARW EYDESYCDAV KKTSPYDSGP RLLDIIDTAV FDYLIGNADR HHYESFQDDE
GASMLILLDN AKSFGNPSLD ERSILAPLYQ CCIIRVSTWN RLNYLKNGVL KSALKSAMAH
DPISPVLSDP HLDTVDQRLL NVLATIKQCT DQFGTDTVLV EDRMPLSHL
