CXT1_CRYNJ
ID CXT1_CRYNJ Reviewed; 694 AA.
AC Q5K8R6; A5JSV9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Beta-1,2-xylosyltransferase 1;
DE Short=Cxt1p;
DE EC=2.4.1.-;
GN Name=CXT1; OrderedLocusNames=CNL04750;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP GLYCOSYLATION AT ASN-141, AND MUTAGENESIS OF ASN-141; ASP-550 AND ASP-659.
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=17430900; DOI=10.1074/jbc.m701941200;
RA Klutts J.S., Levery S.B., Doering T.L.;
RT "A beta-1,2-xylosyltransferase from Cryptococcus neoformans defines a new
RT family of glycosyltransferases.";
RL J. Biol. Chem. 282:17890-17899(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=18347023; DOI=10.1074/jbc.m708927200;
RA Klutts J.S., Doering T.L.;
RT "Cryptococcal xylosyltransferase 1 (Cxt1p) from Cryptococcus neoformans
RT plays a direct role in the synthesis of capsule polysaccharides.";
RL J. Biol. Chem. 283:14327-14334(2008).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=18676952; DOI=10.1128/ec.00458-07;
RA Castle S.A., Owuor E.A., Thompson S.H., Garnsey M.R., Klutts J.S.,
RA Doering T.L., Levery S.B.;
RT "Beta1,2-xylosyltransferase Cxt1p is solely responsible for xylose
RT incorporation into Cryptococcus neoformans glycosphingolipids.";
RL Eukaryot. Cell 7:1611-1615(2008).
CC -!- FUNCTION: Beta-1,2-xylosyltransferase that plays a key role in capsule
CC polysaccharide synthesis by transferring xylose to alpha-1,3-
CC dimannoside in a beta-1,2-linkage. Also mediates glycosylation of
CC glycosphingolipids; constitutes the unique xylosyltransferase
CC responsible for adding xylose to glycosphingolipids.
CC {ECO:0000269|PubMed:17430900, ECO:0000269|PubMed:18347023,
CC ECO:0000269|PubMed:18676952}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Attenuation of cryptococcal growth in a mouse
CC model of infection due to defects in capsule polysaccharide content.
CC The general morphology of the capsule is normal but two main capsule
CC polysaccharides, glucuronoxylomannan (GXM) and galactoxylomannan
CC (GalXM), lack beta-1,2-xylose residues. {ECO:0000269|PubMed:18347023,
CC ECO:0000269|PubMed:18676952}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 90 family.
CC {ECO:0000305}.
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DR EMBL; EF564628; ABQ42713.1; -; mRNA.
DR EMBL; AE017352; AAW46501.1; -; Genomic_DNA.
DR RefSeq; XP_568018.1; XM_568018.1.
DR AlphaFoldDB; Q5K8R6; -.
DR STRING; 5207.AAW46501; -.
DR CAZy; GT90; Glycosyltransferase Family 90.
DR iPTMnet; Q5K8R6; -.
DR PaxDb; Q5K8R6; -.
DR EnsemblFungi; AAW46501; AAW46501; CNL04750.
DR GeneID; 3254907; -.
DR KEGG; cne:CNL04750; -.
DR VEuPathDB; FungiDB:CNL04750; -.
DR eggNOG; KOG2458; Eukaryota.
DR HOGENOM; CLU_005027_3_3_1; -.
DR InParanoid; Q5K8R6; -.
DR OMA; FTIHDQP; -.
DR OrthoDB; 547457at2759; -.
DR BRENDA; 2.4.2.38; 1723.
DR PHI-base; PHI:2822; -.
DR Proteomes; UP000002149; Chromosome 12.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR006598; CAP10.
DR Pfam; PF05686; Glyco_transf_90; 1.
DR SMART; SM00672; CAP10; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..694
FT /note="Beta-1,2-xylosyltransferase 1"
FT /id="PRO_0000404583"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..694
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 661..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:17430900"
FT MUTAGEN 141
FT /note="N->Q: Affects the apparent gel mobility without
FT affecting enzymatic activity."
FT /evidence="ECO:0000269|PubMed:17430900"
FT MUTAGEN 550
FT /note="D->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:17430900"
FT MUTAGEN 659
FT /note="D->A: Impairs enzymatic activity."
FT /evidence="ECO:0000269|PubMed:17430900"
SQ SEQUENCE 694 AA; 78970 MW; 011B8A9945404153 CRC64;
MPLNLPFSSP LKLPLPRRFI ILILSASILI LFLHTFAPST LPPVLTPNLP HHEPDASYFS
PSKWLPPILN PNAPTRPLEF DEDGQCLFLS PFDALSAAEK ARARVLSLDE ISPGIVRADA
PPAEGTDADP DFDDEFSELS NATRKMPAGL THPILGLLRD GEAKWNSMVT MQSQTLEQAV
DVYMDRWGRR PPKGFDEWWH FAKANNVLLP DEYDPIMNSL LPFYALPIDT LKERLVEAEK
IPETFTLIVH DGKVELKWND DYSRDTWWAS RPRADSQINL MEPFIKHIGT FRATFTIHDQ
PSILLDHERQ EELLTAARHG KISTHPNELD RAEQNWRKAC PPDSPLNKGE EELEAPDSFI
SSHLAAMDIC QHPSYMENHG MLLEEKNSDS HPKPHTKLYP ILVPSKTALN GDIPVTPIGK
DGRRDDIGHD PEWNRKSGKL YWRGLATGLQ HNKKAGAKWR QSHRERLHFL ANDKSDTYTE
VLSPVGSSGE AELARMPLRE LGQYYMDVKL AGGNWQCDWG DGTCEEMEKE IDFAPKDSSE
RSNDFKYVFD TDGNAWSSRF PRLMASNNVV IKSTVFPEWN TNSLPEWYAY VPSKMDYSDL
FSIMTFFRGT PSGRGAHDEV ARRIALNGQC WVERTWRRED LQAYMFRLYL EYARLTSPDR
DNGKMDYVST QKKASKEADD VPAAADIETP VIDQ
