ID   XPT1_CRYNV              Reviewed;         864 AA.
AC   D0U690;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 28.
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;
OS   Cryptococcus neoformans var. grubii (Filobasidiella neoformans var.
OS   grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=178876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, AND FUNCTION.
RC   STRAIN=KN99alpha;
RX   PubMed=19864415; DOI=10.1074/jbc.m109.056226;
RA   Reilly M.C., Levery S.B., Castle S.A., Klutts J.S., Doering T.L.;
RT   "A novel xylosylphosphotransferase activity discovered in Cryptococcus
RT   neoformans.";
RL   J. Biol. Chem. 284:36118-36127(2009).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21606487; DOI=10.1074/jbc.m111.262162;
RA   Reilly M.C., Aoki K., Wang Z.A., Skowyra M.L., Williams M., Tiemeyer M.,
RA   Doering T.L.;
RT   "A xylosylphosphotransferase of Cryptococcus neoformans acts in protein O-
RT   glycan synthesis.";
RL   J. Biol. Chem. 286:26888-26899(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. {ECO:0000269|PubMed:19864415,
CC       ECO:0000269|PubMed:21606487}.
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         Evidence={ECO:0000269|PubMed:19864415};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:19864415};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:21606487}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:21606487}.
CC   -!- SIMILARITY: Belongs to the XPT1 family. {ECO:0000305}.
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DR   EMBL; GQ403790; ACY41153.1; -; mRNA.
DR   AlphaFoldDB; D0U690; -.
DR   KEGG; ag:ACY41153; -.
DR   BioCyc; MetaCyc:MON-15994; -.
DR   BRENDA; 2.7.8.32; 1723.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Manganese; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix; Xylose metabolism.
FT   CHAIN           1..864
FT                   /note="3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose
FT                   xylosylphosphotransferase"
FT                   /id="PRO_0000418544"
FT   TOPO_DOM        1..82
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..864
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        583
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   864 AA;  99527 MW;  CC5F36B99DD513E7 CRC64;
     MPSTALSPPS RPPAQSYDSY SSSLSPSSPR FHAAAGSHGR RSPSPSRLES LLDGPHVPPR
     SPSRKIRSAL SRHIRPHITP RTLTPVFLWT LALWLIHHFL FPLSSPFAKL AKPKAEEHFL
     STTFPPPAQR LGDDRLDSVD PRWRAYHPLP APEPPFPRLR PTRFLPPQCL EQWFAEGETL
     CGAKEMGEEE TLDATWLWVN GSDHRWRDSM VEWREKENVN SPERHYREQN ELVHSMRSVL
     DALPGHLRTF HLILADYPFN YPEDLELVPS SIIPDLEVAA SKSKGRRHPR ELPGAPASLA
     NLTERVTPES ISPTLASHLQ SEWRILQTPT WLDFSRRDPS DPSHPFHPYS VSKAGEIRQH
     YAEASYPTLR YASHWEVFHI PSVDRDGRQE LMGEREWREN EWKKKALPSF NSMAIESRIG
     WLPGLADAII ALNDDFFLLR PHAVSDFHSP LYGSVIRFEH GYNQQVKPDV EKNHINDPGE
     MGGLYHANAL LSRRFPRRLR PYFAHVPKVI TRGLHHEASL MFQEALTESS TRRFREMKIG
     EGDVQMQWLL TSLRVERWRE ALLWTWTVAN MGTLGGSQDH WDNDTRRAIK NLFGFTENDD
     DVVKIEVHRG ERWTLEPGRM QRVFRQAGWE APKATEFLFS SMDGIMPPLL RSGEDPAQND
     RCIIDLNRCF GLFWTREEDV LSSDMMKRLT FQYPECGDCM IMALVTASGT LGLNAFFPPK
     ETTITAPELG PGDAYPKFLP PPHLPLTPTW HEADFSLANI LSTTALPGEQ VDIRQYCMRL
     LSRYLYLDAK SVSHFHMMKS AEHARRVFRM IQGDPKVSIL GMNDDIESDY DEVRGLMNEW
     FEMRWPRKAV WERDWDPVKD RYND