BMT6_CANAL
ID BMT6_CANAL Reviewed; 646 AA.
AC Q5ABU8; A0A1D8PQ28; Q5AC72;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Beta-mannosyltransferase 6;
DE EC=2.4.1.-;
DE AltName: Full=WRY family protein 2;
GN Name=BMT6; Synonyms=WRY2; OrderedLocusNames=CAALFM_C603160CA;
GN ORFNames=CaO19.13045, CaO19.5602;
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 [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 [2]
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 [3]
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 [4]
RP IDENTIFICATION.
RX PubMed=18234669; DOI=10.1074/jbc.m708825200;
RA Mille C., Bobrowicz P., Trinel P.A., Li H., Maes E., Guerardel Y.,
RA Fradin C., Martinez-Esparza M., Davidson R.C., Janbon G., Poulain D.,
RA Wildt S.;
RT "Identification of a new family of genes involved in beta-1,2-mannosylation
RT of glycans in Pichia pastoris and Candida albicans.";
RL J. Biol. Chem. 283:9724-9736(2008).
RN [5]
RP INDUCTION.
RX PubMed=21414038; DOI=10.1111/j.1365-2958.2011.07626.x;
RA Bonhomme J., Chauvel M., Goyard S., Roux P., Rossignol T., d'Enfert C.;
RT "Contribution of the glycolytic flux and hypoxia adaptation to efficient
RT biofilm formation by Candida albicans.";
RL Mol. Microbiol. 80:995-1013(2011).
RN [6]
RP FUNCTION.
RX PubMed=22745283; DOI=10.1093/glycob/cws097;
RA Mille C., Fradin C., Delplace F., Trinel P.A., Masset A., Francois N.,
RA Coddeville B., Bobrowicz P., Jouault T., Guerardel Y., Wildt S., Janbon G.,
RA Poulain D.;
RT "Members 5 and 6 of the Candida albicans BMT family encode enzymes acting
RT specifically on beta-mannosylation of the phospholipomannan cell-wall
RT glycosphingolipid.";
RL Glycobiology 22:1332-1342(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24367694; DOI=10.1371/journal.pone.0084771;
RA Devillers A., Courjol F., Fradin C., Coste A., Poulain D., Pipy B.,
RA Bernardes E.S., Jouault T.;
RT "Deficient beta-mannosylation of Candida albicans phospholipomannan affects
RT the proinflammatory response in macrophages.";
RL PLoS ONE 8:E84771-E84771(2013).
CC -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis.
CC Required for beta-1,2-mannose transfer on phospholipomannan. Required
CC for pro-inflammatory response in macrophages through phospholipomannan-
CC induced TNF-alpha production. {ECO:0000269|PubMed:22745283,
CC ECO:0000269|PubMed:24367694}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Expression is induced in biofilm.
CC {ECO:0000269|PubMed:21414038}.
CC -!- DISRUPTION PHENOTYPE: Leads to the production of phospholipomannan with
CC short truncated oligomannosidic chain and impairs induction of TNF-
CC alpha production in macrophages. {ECO:0000269|PubMed:24367694}.
CC -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR EMBL; CP017628; AOW30247.1; -; Genomic_DNA.
DR RefSeq; XP_719163.2; XM_714070.2.
DR AlphaFoldDB; Q5ABU8; -.
DR STRING; 237561.Q5ABU8; -.
DR CAZy; GT91; Glycosyltransferase Family 91.
DR GeneID; 3639258; -.
DR KEGG; cal:CAALFM_C603160CA; -.
DR CGD; CAL0000178153; BMT6.
DR VEuPathDB; FungiDB:C6_03160C_A; -.
DR eggNOG; ENOG502QTZG; Eukaryota.
DR HOGENOM; CLU_013841_1_0_1; -.
DR InParanoid; Q5ABU8; -.
DR OrthoDB; 487566at2759; -.
DR PRO; PR:Q5ABU8; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR021988; BMT1.
DR PANTHER; PTHR37989; PTHR37989; 1.
DR Pfam; PF12141; DUF3589; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..646
FT /note="Beta-mannosyltransferase 6"
FT /id="PRO_0000426074"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..646
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 646 AA; 74499 MW; CC68F74BAEFAA6CE CRC64;
MGNYKPSIKQ YVVTVKAIKS SQFGRLGICA VVLLFVLGYP FYFISNNPFD TSIRYQYVDP
YNDTTRKYTT IEKQHTDIGG NGTTILYPKN LQLDQTALSQ LLNTTETTNP FVQYIGNSSS
IAFSQLNQTL VNHSIQVFDP FSNSDNCSDL MTETQLTISQ NIIIKESFEI MVKRLMHQLD
TEPAFKELAP FFQNKLSLHL RMRSYHKHFY KFARTSVWLK DYGVHLMISR VIYSQKGKKG
DPQISLLYTQ LYDTNWQELT NTDLLVSMQD ITGEYKLEKL QFPRFLPMPF YYNPKLTKGR
WYGPEDARIM LVKNQLDMEE PVVIYNSYHR QIANHTTTGK TDGSVELNFE FYRSMFVGWP
FRYQLGKSNT DGFVDDRFDN VKFTRVAELK IHNQTRASIE KNWTPFVDPS ERDPEDKSLY
IVYQWDKLRI LKCDISNLVT DDGFIHYSAC RFKQDTKHDE VEKVGPIRGG TELIPTIINN
KQLWVGFLRA HIDKCGCGKA MYRPNMVVLQ KTDMGTFQVA YLSSYISFNI PVPGWKTHEI
QCGKRDPNVL IPNGISNWEV ATIDGIERDV LTMTLSAADE DNILMDIHGL KTVIKNLITN
QKHGNEFNSD SVQMKCVVAY SIEFCRAYGE EQARLGLTGG WLPSHN
