ID   MNT1_CANAL              Reviewed;         431 AA.
AC   Q00310; A0A1D8PJA3; Q5AJC6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Glycolipid 2-alpha-mannosyltransferase 1;
DE            EC=2.4.1.-;
DE   AltName: Full=Alpha-1,2-mannosyltransferase 1;
GN   Name=MNT1; Synonyms=KRE2, KTR1; OrderedLocusNames=CAALFM_C301810CA;
GN   ORFNames=CaO19.1665, CaO19.9234;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC5314 / CAI4 / ATCC MYA-682;
RX   PubMed=9636208; DOI=10.1073/pnas.95.13.7670;
RA   Buurman E.T., Westwater C., Hube B., Brown A.J., Odds F.C., Gow N.A.R.;
RT   "Molecular analysis of CaMnt1p, a mannosyl transferase important for
RT   adhesion and virulence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:7670-7675(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [5]
RP   FUNCTION.
RC   STRAIN=SC5314 / CAI4 / ATCC MYA-682;
RX   PubMed=15519997; DOI=10.1074/jbc.m411413200;
RA   Munro C.A., Bates S., Buurman E.T., Hughes H.B., MacCallum D.M.,
RA   Bertram G., Atrih A., Ferguson M.A.J., Bain J.M., Brand A., Hamilton S.,
RA   Westwater C., Thomson L.M., Brown A.J.P., Odds F.C., Gow N.A.R.;
RT   "Mnt1p and Mnt2p of Candida albicans are partially redundant alpha-1,2-
RT   mannosyltransferases that participate in O-linked mannosylation and are
RT   required for adhesion and virulence.";
RL   J. Biol. Chem. 280:1051-1060(2005).
CC   -!- FUNCTION: Involved in O-glycosylation of cell wall and secreted
CC       proteins. Transfers an alpha-D-mannosyl residue from GDP-mannose into
CC       lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-
CC       mannose linkage. Mainly responsible for the addition of the second
CC       mannose residue in an O-linked mannose pentamer. Can also substitute
CC       for MNT2 by adding the third mannose residue. Important for adherence
CC       to host surfaces and for virulence. {ECO:0000269|PubMed:15519997}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 15 family.
CC       {ECO:0000305}.
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DR   EMBL; X99619; CAA67930.1; -; Genomic_DNA.
DR   EMBL; CP017625; AOW28222.1; -; Genomic_DNA.
DR   RefSeq; XP_721742.1; XM_716649.1.
DR   AlphaFoldDB; Q00310; -.
DR   SMR; Q00310; -.
DR   STRING; 237561.Q00310; -.
DR   CAZy; GT15; Glycosyltransferase Family 15.
DR   PRIDE; Q00310; -.
DR   GeneID; 3636585; -.
DR   KEGG; cal:CAALFM_C301810CA; -.
DR   CGD; CAL0000188662; MNT1.
DR   VEuPathDB; FungiDB:C3_01810C_A; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   HOGENOM; CLU_024327_0_1_1; -.
DR   InParanoid; Q00310; -.
DR   OMA; WNGYSCT; -.
DR   OrthoDB; 948664at2759; -.
DR   UniPathway; UPA00378; -.
DR   PHI-base; PHI:104; -.
DR   PRO; PR:Q00310; -.
DR   Proteomes; UP000000559; Chromosome 3.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
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:0016020; C:membrane; IDA:CGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IDA:CGD.
DR   GO; GO:0043710; P:cell adhesion involved in multi-species biofilm formation; IMP:CGD.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IMP:CGD.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:CGD.
DR   GO; GO:0006057; P:mannoprotein biosynthetic process; IMP:CGD.
DR   GO; GO:0097502; P:mannosylation; IBA:GO_Central.
DR   GO; GO:0030682; P:mitigation of host defenses by symbiont; IMP:CGD.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IDA:CGD.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR002685; Glyco_trans_15.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR31121; PTHR31121; 1.
DR   Pfam; PF01793; Glyco_transf_15; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..431
FT                   /note="Glycolipid 2-alpha-mannosyltransferase 1"
FT                   /id="PRO_0000208240"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..431
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          35..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        318
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   431 AA;  50004 MW;  E8AC1FAE9010B763 CRC64;
     MASTRSNARL IRFGIFALVL IGCGYILTRG SSFQPPNYQQ TQSPAAHEKQ TGNVAAGGGA
     GSGSAGAQVP LGKNRGPIPK AIMGAGEGGS DAPVPQQDIP DSYTLNDKIK ATFVTLARNS
     DLYSLAESIR HVEDRFNKKF HYDWVFLNDE EFNDEFKETV GSLVSGNTKF GLIPKEHWSY
     PPWIDQEKAA LVREQMREKK IIYGHSESYR HMCRFESGFF WRQEILNDYD YYWRVEPDIK
     LYCDIDYDIF KWMKDNNKDY AFTISLPEYK ETIPTLWDTT KEFIEKNPQY LAQNNLMDWV
     SDDKGQTYNG CHFWSNFEIG SLAFWRSEAY RKYFEHLDKA GGFFYERWGD APVHSIAAAL
     FLPREKIHFF EDVGYYHVPF TNCPVDKEVR KARNCNCDPN KDFTWRGYSC TTKYYTLNNF
     KRQKGWEKYT A