ID   MNT2_CANAL              Reviewed;         461 AA.
AC   P46592; A0A1D8PJA0; Q5AJC8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 4.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Glycolipid 2-alpha-mannosyltransferase 2;
DE            EC=2.4.1.-;
DE   AltName: Full=Alpha-1,2-mannosyltransferase 2;
GN   Name=MNT2; OrderedLocusNames=CAALFM_C301830CA;
GN   ORFNames=CaO19.1663, CaO19.9232;
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], AND 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).
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).
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 third
CC       mannose residue in an O-linked mannose pentamer. Can also substitute
CC       for MNT1 by adding the second mannose residue. Important for adherence
CC       to host surfaces and for virulence. {ECO:0000269|PubMed:15519997}.
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; X89263; CAA61538.1; -; Genomic_DNA.
DR   EMBL; CP017625; AOW28224.1; -; Genomic_DNA.
DR   PIR; S57713; S57713.
DR   RefSeq; XP_721740.2; XM_716647.2.
DR   AlphaFoldDB; P46592; -.
DR   SMR; P46592; -.
DR   STRING; 237561.P46592; -.
DR   CAZy; GT15; Glycosyltransferase Family 15.
DR   PRIDE; P46592; -.
DR   GeneID; 3636583; -.
DR   KEGG; cal:CAALFM_C301830CA; -.
DR   CGD; CAL0000188888; MNT2.
DR   VEuPathDB; FungiDB:C3_01830C_A; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   HOGENOM; CLU_024327_1_0_1; -.
DR   InParanoid; P46592; -.
DR   OrthoDB; 948664at2759; -.
DR   PHI-base; PHI:392; -.
DR   PRO; PR:P46592; -.
DR   Proteomes; UP000000559; Chromosome 3.
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: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; IBA:GO_Central.
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   PIRSF; PIRSF018153; Glyco_trans_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..461
FT                   /note="Glycolipid 2-alpha-mannosyltransferase 2"
FT                   /id="PRO_0000208251"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..35
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..461
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          35..138
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   COMPBIAS        79..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        349
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   461 AA;  54562 MW;  9A374446C5116335 CRC64;
     MKPSIFYSSR QPYLKYLAII LTTITIYVLT HSSYSADPNI NDVTTKPISE TVPQPPPQSP
     SSPEQQQQQP ANQDQIVKVP EELKNKPQDL VVDNNKDQKP AVSGVPKSSS SSPQQQEKQD
     TKKESENSSS SKDPVKPEKV KATFVTLARN SELYDLIKSI RNVEDRFNRK FNYDWVFLND
     DDFTQEFKDL TTALVSGKTK YGKIPKEHWS YPDWIDLKRA EETRKNMKLQ KIIYGDSESY
     RHMCRFESGF FWRHPLLDDY DWYWRVEPSI DIHCDLNYDL FKYMEDNNKV YGFTISIHEF
     RATIPTLWDT TKKFIKENPQ YLAENNFMDF ISDDKGETYN LCHFWSNFEI ANLNFWRGEA
     YRKYFDYLDQ TGGFFYERWG DAPIHSIAAA LFLPKDKIHY FDDVGYKHSV YTQCPLNPQF
     RYEHKCHCNP DNDFTFRGYS CGKKYFEKMG LQKPKEWEKY Q