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 10-JUN-2026, entry version 114. 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; Pichiomycetes; OC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P87207; 2 sites, No reported glycans. DR PaxDb; 237561-P87207; -. DR EnsemblFungi; CR_05290W_A-T; CR_05290W_A-T-p1; CR_05290W_A. 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; 439943at2759; -. DR Proteomes; UP000000559; Chromosome R. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. 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:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central. DR FunFam; 3.90.550.10:FF:000051; Alpha-1,2-mannosyltransferase (Ktr4); 1. DR Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1. DR InterPro; IPR002685; Glyco_trans_15. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR31121; ALPHA-1,2 MANNOSYLTRANSFERASE KTR1; 1. DR PANTHER; PTHR31121:SF6; ALPHA-1,2 MANNOSYLTRANSFERASE KTR1; 1. DR Pfam; PF01793; Glyco_transf_15; 1. DR PIRSF; PIRSF018153; Glyco_trans_15; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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 //