XYLK_DROME
ID XYLK_DROME Reviewed; 421 AA.
AC Q95T10;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glycosaminoglycan xylosylkinase homolog {ECO:0000250|UniProtKB:O75063};
DE EC=2.7.1.- {ECO:0000250|UniProtKB:O75063};
DE AltName: Full=Xylose kinase homolog {ECO:0000250|UniProtKB:O75063};
DE Flags: Precursor;
GN ORFNames=CG3631 {ECO:0000312|FlyBase:FBgn0038268};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
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).
CC -!- FUNCTION: Kylose kinase that mediates the 2-O-phosphorylation of xylose
CC in the glycosaminoglycan-protein linkage region of proteoglycans.
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 {ECO:0000269|PubMed:22900076}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:22900076}.
CC -!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF55106.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN13620.2; -; Genomic_DNA.
DR EMBL; AE014297; AAS65154.1; -; Genomic_DNA.
DR EMBL; AY060387; AAL25426.1; -; mRNA.
DR RefSeq; NP_650398.3; NM_142141.3.
DR RefSeq; NP_731951.2; NM_169605.3.
DR RefSeq; NP_996212.1; NM_206490.3.
DR AlphaFoldDB; Q95T10; -.
DR SMR; Q95T10; -.
DR STRING; 7227.FBpp0113025; -.
DR GlyGen; Q95T10; 1 site.
DR PaxDb; Q95T10; -.
DR PRIDE; Q95T10; -.
DR DNASU; 41797; -.
DR EnsemblMetazoa; FBtr0082997; FBpp0082456; FBgn0038268.
DR EnsemblMetazoa; FBtr0114533; FBpp0113025; FBgn0038268.
DR EnsemblMetazoa; FBtr0344378; FBpp0310751; FBgn0038268.
DR GeneID; 41797; -.
DR KEGG; dme:Dmel_CG3631; -.
DR UCSC; CG3631-RC; d. melanogaster.
DR FlyBase; FBgn0038268; CG3631.
DR VEuPathDB; VectorBase:FBgn0038268; -.
DR eggNOG; KOG3829; Eukaryota.
DR GeneTree; ENSGT00950000182951; -.
DR HOGENOM; CLU_028926_1_1_1; -.
DR InParanoid; Q95T10; -.
DR OMA; KETEPAC; -.
DR OrthoDB; 484324at2759; -.
DR PhylomeDB; Q95T10; -.
DR BioGRID-ORCS; 41797; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41797; -.
DR PRO; PR:Q95T10; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038268; Expressed in cleaving embryo and 30 other tissues.
DR Genevisible; Q95T10; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; 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; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; ISS:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:FlyBase.
DR InterPro; IPR024869; FAM20.
DR InterPro; IPR009581; FAM20_C.
DR PANTHER; PTHR12450; PTHR12450; 1.
DR Pfam; PF06702; Fam20C; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Kinase; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..421
FT /note="Glycosaminoglycan xylosylkinase homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433615"
FT ACT_SITE 314
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 166
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 252..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 329
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 225..240
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 230..233
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 285..351
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 352..409
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
SQ SEQUENCE 421 AA; 49248 MW; 3C0175ACCE2393CA CRC64;
MNKRSVIIAG IVASLLGLAL GANFYFMYYL SAEEGHLASV RALENMIRHK MRHLKPNYLN
RNPRFFMFRN KLLKNYKAAP YENASVLWDI ANWWPHENEV YPLYDSSMGQ LLETLRREPI
TRVSNLGRGT QLKLLVRLSH QQKVIFKPQW YPREEVIDGM IYSGKDRHTA EVYAFYLGAV
LDFRWTPIVV GRVVNLKKEI YAKGDPELQQ TINIETDEDG REKYCLFGKC HYCNEEETVC
GDERHNIEGV LIYIVPGTLA KRRSPWQRTY KDDKRAPWED DMTYCKSLKN KMETIRLLDL
IDASIFDYLI QNGDRHHYET REERVVLIDN GKAFGNPNKD HLDILAPLYQ CCLLRKSTWD
RLQVFSGGVL TEIIDRLSKQ DALYPLITDK HKKGVERRLL VVYAVVEHCM DIEGDKMFKT
L
