ID   XPT1_CRYGW              Reviewed;         865 AA.
AC   E6RCE9;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 40.
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=CGB_I4040W;
OS   Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS   (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=367775;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM276 / ATCC MYA-4071;
RX   PubMed=21304167; DOI=10.1128/mbio.00342-10;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 2:E342-E342(2011).
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; CP000294; ADV24468.1; -; Genomic_DNA.
DR   RefSeq; XP_003196255.1; XM_003196207.1.
DR   AlphaFoldDB; E6RCE9; -.
DR   EnsemblFungi; ADV24468; ADV24468; CGB_I4040W.
DR   GeneID; 10186567; -.
DR   KEGG; cgi:CGB_I4040W; -.
DR   VEuPathDB; FungiDB:CGB_I4040W; -.
DR   eggNOG; ENOG502QV1P; Eukaryota.
DR   HOGENOM; CLU_005484_2_0_1; -.
DR   Proteomes; UP000007805; Chromosome I.
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:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
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; Transferase; Transmembrane;
KW   Transmembrane helix; Xylose metabolism.
FT   CHAIN           1..865
FT                   /note="3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose
FT                   xylosylphosphotransferase"
FT                   /id="PRO_0000418547"
FT   TOPO_DOM        1..84
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..865
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   865 AA;  99891 MW;  8B323A4DF38D2088 CRC64;
     MLSTALSPSS PHADYNSYSS SLSPTSPRFH ASSAPHGRRS PSPSRLESLL DAPLPSCRPS
     RSPRSRKIRD ALARHIRPHL TPRTLTMLFL WMLSVWSIHH FFLPISSLSR LSNPRAEEHF
     LSTAFPPPPQ RIGDDHLDSV DPRWRAYHPL PAPDPPFPRL RPTRFLPPQC LEQWFAEGET
     LCGAKELGEE EKLDATWLWV NGSDHRWRDS MIEWREKENV NSPERHFREQ NELVHSMRSV
     LDALPGHLRT FHLILADYTF NYPEDLELVP FSIIPDLEKV ASKSKGRRHP RDLPGTPPSF
     SNLTERVTPE SISASLASHL QSEWRIVQTP TWLDFSRRDP SDPSHPFHPY SVSKAGERGQ
     HYAEASYPTL RYASHWEVFH TPSVDRDGRQ ELMGEREWRE NEWKKKALPT FNSMAIESRI
     GWLPGLADAI IALNDDFFLL RPHAVSDFHS PLYGSVIRFD HGYNQQVRPE VVKSHINDPG
     EIGGLYHANA ILSQRFPHRL RPYFAHVPKV ITRGLHHEAS LMFKEALTES STRRFREMKI
     GEGDVQMQWL LTSLRVERWR EALLWTWVVA NMGTISGSQD RWDDATRTAI KDMFGFTEND
     NDVVKIEVHR GERWTLEPGR MQKAFEQAGW EAPKATEFLF SSMDGTMPPL LKHGEDPAQN
     DRCMIDLNRC FGVFWTREED ILSTDMMKRL TFQYPECGDC MIMALVTASG TLGLNAFFPP
     KETTVTAPEL APGDGYPKFL PPPHLPLTPT WHEADFSLAN ILSTTALPGE QVDIRQYCMR
     LLSRYLYLDA RSVSHFHMLK SAEHAQRVFK MIQDNPRVSI LGMNDDIESD YDEVKRLMNE
     WFEMRWPRKA VWEREWDPVK DRYID