ID   CMT1_CRYNJ              Reviewed;         466 AA.
AC   Q6U1Z4; Q5KDG4;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Alpha-1,3-mannosyltransferase CMT1;
DE            EC=2.4.1.-;
GN   Name=CMT1 {ECO:0000312|EMBL:AAQ86764.1}; OrderedLocusNames=CNG04090;
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] {ECO:0000305, ECO:0000312|EMBL:AAQ86764.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 74-93; 220-235 AND 327-332,
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=14504286; DOI=10.1074/jbc.m307223200;
RA   Sommer U., Liu H., Doering T.L.;
RT   "An alpha-1,3-mannosyltransferase of Cryptococcus neoformans.";
RL   J. Biol. Chem. 278:47724-47730(2003).
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).
CC   -!- FUNCTION: Responsible for addition of mannose residues in an alpha-1,3
CC       linkage to a polymannosly precursor. May be involved in synthesis of
CC       capsule glucuronoxylomannan. {ECO:0000269|PubMed:14504286}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC       Note=Divalent metal cations. Mg(2+), Mn(2+) or Co(2+) can be used.;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000305|PubMed:14504286}; Single-pass type II membrane protein
CC       {ECO:0000305|PubMed:14504286}.
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DR   EMBL; AY380340; AAQ86764.1; -; mRNA.
DR   EMBL; AE017347; AAW44851.1; -; Genomic_DNA.
DR   RefSeq; XP_572158.1; XM_572158.1.
DR   AlphaFoldDB; Q6U1Z4; -.
DR   CAZy; GT69; Glycosyltransferase Family 69.
DR   PaxDb; Q6U1Z4; -.
DR   EnsemblFungi; AAW44851; AAW44851; CNG04090.
DR   GeneID; 3258835; -.
DR   KEGG; cne:CNG04090; -.
DR   VEuPathDB; FungiDB:CNG04090; -.
DR   eggNOG; ENOG502QRBX; Eukaryota.
DR   HOGENOM; CLU_036740_0_0_1; -.
DR   InParanoid; Q6U1Z4; -.
DR   OMA; NDIALCM; -.
DR   OrthoDB; 841960at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002149; Chromosome 7.
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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR021047; Mannosyltransferase_CMT1.
DR   PANTHER; PTHR34144; PTHR34144; 1.
DR   Pfam; PF11735; CAP59_mtransfer; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..466
FT                   /note="Alpha-1,3-mannosyltransferase CMT1"
FT                   /id="PRO_0000080584"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..466
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   466 AA;  53035 MW;  F5BA33EDC958A788 CRC64;
     MFRNTLRTFP RPATPSLPTS SHSPIARASL SKSPLFVLSL VLVCIFFLSF LSHPDPSARK
     LQWPGLFPSP SPSVIHTKDL FLERALNATS EAFREICPSA GDPVHLDPDL TEAQKKRYLP
     LKRSKRGRYL LVTNTRQIEA HLPDLLNTLI VLLRYLAPEH LAVSILEGPS SDCTQKAIEQ
     VLKPMLDDQG LESAWTRIET GESKIDWGKH NRIEKIAELR NTALAPLWQG EGDQKWEDEI
     EAVVFFNDVY LHAADILELV YQHVKNGAGI TTAMDWWKKR PEYYYDVWVG RTIDTGDLFY
     PIDNPWWSPS SDLFPNSPNS RNAYSRLEPF QVFSSWNALA VLSPKPFLPP HNVRFRRGDV
     EKGECAASEC TLIATDFWKA GFGKVAVVPS VQLAYERDVA KDIIEDVGKQ KEQLGWIDGV
     PPEHLDDKIE WSTKPPKKVR CHPWPEVNGL SANVWEETRW VQPWLE