BMT2_CANAL
ID BMT2_CANAL Reviewed; 654 AA.
AC Q59MA6; A0A1D8PDF6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Beta-mannosyltransferase 2;
DE EC=2.4.1.-;
DE AltName: Full=Repressed during hyphae development protein 1;
DE AltName: Full=WRY family protein 7;
GN Name=RHD1; Synonyms=BMT2, IFQ3, WRY7; OrderedLocusNames=CAALFM_C105000WA;
GN ORFNames=CaO19.54, CaO19.7715;
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 INDUCTION.
RX PubMed=12388749; DOI=10.1091/mbc.e02-05-0272;
RA Nantel A., Dignard D., Bachewich C., Harcus D., Marcil A., Bouin A.P.,
RA Sensen C.W., Hogues H., van het Hoog M., Gordon P., Rigby T., Benoit F.,
RA Tessier D.C., Thomas D.Y., Whiteway M.;
RT "Transcription profiling of Candida albicans cells undergoing the yeast-to-
RT hyphal transition.";
RL Mol. Biol. Cell 13:3452-3465(2002).
RN [5]
RP INDUCTION.
RX PubMed=12397174; DOI=10.1073/pnas.232566499;
RA Lan C.Y., Newport G., Murillo L.A., Jones T., Scherer S., Davis R.W.,
RA Agabian N.;
RT "Metabolic specialization associated with phenotypic switching in
RT Candidaalbicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14907-14912(2002).
RN [6]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, AND FUNCTION.
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 [7]
RP INDUCTION.
RX PubMed=22265407; DOI=10.1016/j.cell.2011.10.048;
RA Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT "A recently evolved transcriptional network controls biofilm development in
RT Candida albicans.";
RL Cell 148:126-138(2012).
CC -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis.
CC Required for the addition of beta-mannose to the acid-labile fraction
CC of cell wall phosphopeptidomannan. {ECO:0000269|PubMed:18234669}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Regulated on yeast-hypha and white-opaque switches, and
CC repressed in biofilm. {ECO:0000269|PubMed:12388749,
CC ECO:0000269|PubMed:12397174, ECO:0000269|PubMed:22265407}.
CC -!- DISRUPTION PHENOTYPE: Impairs the elongation of beta-mannose chains on
CC the acid-labile fraction of cell wall phosphopeptidomannan.
CC {ECO:0000269|PubMed:18234669}.
CC -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26172.1; -; Genomic_DNA.
DR RefSeq; XP_710865.2; XM_705773.2.
DR AlphaFoldDB; Q59MA6; -.
DR SMR; Q59MA6; -.
DR CAZy; GT91; Glycosyltransferase Family 91.
DR PRIDE; Q59MA6; -.
DR GeneID; 3647531; -.
DR KEGG; cal:CAALFM_C105000WA; -.
DR CGD; CAL0000199919; RHD1.
DR VEuPathDB; FungiDB:C1_05000W_A; -.
DR eggNOG; ENOG502QTZG; Eukaryota.
DR HOGENOM; CLU_013841_1_1_1; -.
DR InParanoid; Q59MA6; -.
DR OrthoDB; 487566at2759; -.
DR PRO; PR:Q59MA6; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0070135; P:beta-1,2-oligomannoside metabolic process; IMP:CGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IGI:CGD.
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; Glycosyltransferase; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..654
FT /note="Beta-mannosyltransferase 2"
FT /id="PRO_0000426070"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..654
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 654 AA; 75813 MW; 0C2ADD765D42F3F0 CRC64;
MLAWLRHRIR SYNTSTYSSI LPSASFGKVY KIGTKLNFTL LALCLLLACS VFFNYFYLAD
NNGLDIDTKG EEEENVFKDR KMVIFPNNFE ITDKNLLEYY LKTLEEPLHP QDTIYRNRFI
YKVPDVSYTS QTINLFSGLS QNSQSSKCED LSSSYSFDVS GPQNKNCDLY KVLGKFLNDD
SEYFQEISPL FPKLKEMLVK KEIEKHWFQL IGSSVWLEQY GVHLMTSRIF YSSTGDKVKP
VVSLTYVQVF DHEWREIENV ELIVPDGEGK YKPMTYPTFL PMSVYHNEKQ QQGRFYGVED
PRITLVRNKL GYDEPIIVYN SHHRKITDAK SDNDGESNIH FKAYRSIFMA WLWQNQKGKN
NVEEIETGKM KNRVYVKSKE LIKPNNKRED KEKNWAPFIN YQQRLQQGFD SHVYFMYQFQ
DLKILKCSLL DEEDCVWEYQ FNDKNGAGRL RGGTELVNIN QLLTTFDHPE IKRVKDLMPQ
NREIWIGVAR AALEKCGCGD KMYRPNIVIL IKDGDDQYRL SHVSPFVGLG IPILPWWPDK
GLCDGKNLII PNGISSWHLN KDEDNSVQDY LTLSISRADS TVDLLHIKGL LKSILFDDPN
SKLLELNDYG FNNKNIECAV KSSDAFCKKY GSEYKLNNNK EEDKANGNGK GSSS