XPT1_CRYNJ
ID XPT1_CRYNJ Reviewed; 864 AA.
AC Q5KA65; Q55LC0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose xylosylphosphotransferase;
DE EC=2.7.8.32;
DE AltName: Full=Xylosylphosphotransferase 1;
GN Name=XPT1; OrderedLocusNames=CNJ02890;
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 [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).
CC -!- FUNCTION: Xylosylphosphotransferase that is specific for UDP-xylose as
CC a donor and mannose as an acceptor to form a xylose-alpha-1-phosphate-
CC 6-mannose linkage. Functions in the O-glycosylation of proteins en
CC route through the secretory pathway (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-alpha-D-mannopyranosyl-alpha-D-mannopyranose + UDP-alpha-D-
CC xylose = 3-O-(6-O-alpha-D-xylosylphospho-alpha-D-mannopyranosyl)-
CC alpha-D-mannopyranose + H(+) + UMP; Xref=Rhea:RHEA:28262,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:61663, ChEBI:CHEBI:61665; EC=2.7.8.32;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the XPT1 family. {ECO:0000305}.
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DR EMBL; AE017350; AAW46052.1; -; Genomic_DNA.
DR RefSeq; XP_567569.1; XM_567569.1.
DR AlphaFoldDB; Q5KA65; -.
DR STRING; 5207.AAW46052; -.
DR PaxDb; Q5KA65; -.
DR EnsemblFungi; AAW46052; AAW46052; CNJ02890.
DR GeneID; 3254180; -.
DR KEGG; cne:CNJ02890; -.
DR VEuPathDB; FungiDB:CNJ02890; -.
DR eggNOG; ENOG502QV1P; Eukaryota.
DR HOGENOM; CLU_005484_2_0_1; -.
DR InParanoid; Q5KA65; -.
DR OMA; FLIYTSW; -.
DR OrthoDB; 851009at2759; -.
DR Proteomes; UP000002149; Chromosome 10.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003976; F:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; IBA:GO_Central.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016256; P:N-glycan processing to lysosome; IBA:GO_Central.
DR InterPro; IPR031357; Stealth_CR3.
DR InterPro; IPR031356; Stealth_CR4.
DR Pfam; PF17102; Stealth_CR3; 1.
DR Pfam; PF17103; Stealth_CR4; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Xylose metabolism.
FT CHAIN 1..864
FT /note="3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose
FT xylosylphosphotransferase"
FT /id="PRO_0000418545"
FT TOPO_DOM 1..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..864
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 864 AA; 99644 MW; 0D18064BD3014B5F CRC64;
MPPTALPPLR PPAQPYDSYS SSLSPSSPRF HPASAPHGRR APSPSRLESL LDAPHAPARS
PSRKIRSALS RHIRPHLTPR TLTPLLLWTL ALWLVHHFLF PFSSPLAALS RPKAEQHFLS
TTFPPPPQRL GDDRLDSVDP RWRAFHPLPP PEPPFPRLRP TRFLPPQCLE QWFADGETLC
GAKEMGEEET LDATWLWVNG SDHRWRDSMA EWREKENVNS PERHFREQNE LVHSMRSVLD
ALPGHLRTFH LILADYPFNY PEDLDLVPPS IIPDLEVAAS KGGQGRRHPR ELARAPASVS
NLTERLTPES ISPSLARHLQ SEWRILQTPT WLDFSRRDPS DPSHPFHPYS VSKAGEMRQH
YAEASYPTLR YASHWEVFHI PSVDRDGREE LMGEREWREN EWKKKALPSF NSMAIESRIG
WLPGLADAII ALNDDFFLLR PHAVSDFHSP LYGSVIRFEH SYNQQVKPDV EKNHINDPGE
MGGLYHANAL LSRRFPHRLR PYFAHVPKVI TRGLHHEASL MFQEALTLSS TRKFREMKIG
EGDVQMQWLL TSLRVERWRE ALLWTWVVAN MGTLSGSHDR WDSDTRSAIK HLFGFTEDDD
DVVKIEVHRG ERWTLEPGRM QKVFHQAGWE APKATEFLFS SMDGIMPPLL RSGEDPSQND
RCIIDLNRCF GVFWTRQEDV LSADMMKRLT FQYPECGDCM IMALVTASGT LGLNAFFPPK
ETTITAPELG PGDAYPKYLP PPHLPLTPTW HEADYSLSNI LSTTALPGEQ VDIRQYCMRL
LSRYLYLDAK SVSHFHMMKS AEHAKRVFKM IQDNPKVSIL GMNDDIESDY DEVKRLMNEW
FEMRWPRKAV WERDWDPVKD RYHD
