MNT3_CANAL
ID MNT3_CANAL Reviewed; 378 AA.
AC P87207; A0A1D8PSZ3; Q59KJ8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Probable mannosyltransferase MNT3;
DE EC=2.4.1.-;
GN Name=MNT3; OrderedLocusNames=CAALFM_CR05290WA; ORFNames=CaO19.8624;
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=SGY243;
RA Buurman E.T., Gow N.A.R.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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: 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.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 15 family.
CC {ECO:0000305}.
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DR EMBL; Y13642; CAA73985.1; -; Genomic_DNA.
DR EMBL; CP017630; AOW31254.1; -; Genomic_DNA.
DR RefSeq; XP_710275.2; XM_705183.2.
DR AlphaFoldDB; P87207; -.
DR SMR; P87207; -.
DR STRING; 237561.P87207; -.
DR CAZy; GT15; Glycosyltransferase Family 15.
DR GeneID; 3648123; -.
DR KEGG; cal:CAALFM_CR05290WA; -.
DR CGD; CAL0000188769; MNT3.
DR VEuPathDB; FungiDB:CR_05290W_A; -.
DR eggNOG; KOG4472; Eukaryota.
DR HOGENOM; CLU_024327_4_2_1; -.
DR InParanoid; P87207; -.
DR OrthoDB; 948664at2759; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000031; F:mannosylphosphate transferase activity; IGI:CGD.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR GO; GO:0097502; P:mannosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IGI:CGD.
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 Glycoprotein; Glycosyltransferase; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..378
FT /note="Probable mannosyltransferase MNT3"
FT /id="PRO_0000208249"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..378
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="W -> R (in Ref. 1; CAA73985)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="S -> P (in Ref. 1; CAA73985)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="T -> I (in Ref. 1; CAA73985)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="T -> I (in Ref. 1; CAA73985)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="I -> T (in Ref. 1; CAA73985)"
FT /evidence="ECO:0000305"
FT CONFLICT 81..85
FT /note="RNSDV -> QNSDI (in Ref. 1; CAA73985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 45322 MW; 60ECA41C81668152 CRC64;
MLWHLVFILI AILLLTFSPK IESLFKSFTI NKPTKTTCYQ YTTREQLKSI LESDTHETNF
CIEKPSISPP KTNSTLLMLC RNSDVFSVLE TIQNIQDRFN DKYNYDYTFL NDVPFNYEFI
YLVSSIIPHG KINFGLIPIE HWSYPSHINI SLATEIRQNY ANVPYGDSES YRHMCRFYSG
FFYKHELVKQ YQYYWRIEPG IKIYCDIDYD VFEYMIINDK KYGFVISLFE YSETIPTLWN
HVVQYINDNE IKSELLPLLT NKYNWYNLCH FWSNFEIANL DIFNNDDYEN FFQYLDNLGG
FYYERWGDAP IHSIAIALFL QKKDIHWFEN IGYYHVPYLQ CPQDIDLYVK NKCTCNPDED
FTWSDLSCTN HFLNILHN