BMT1_CANAL
ID BMT1_CANAL Reviewed; 684 AA.
AC Q5ADQ9; A0A1D8PKP2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Beta-mannosyltransferase 1;
DE EC=2.4.1.-;
DE AltName: Full=WRY family protein 4;
GN Name=BMT1; Synonyms=IFQ2, WRY4; OrderedLocusNames=CAALFM_C307180CA;
GN ORFNames=CaO19.14074, CaO19.6782;
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, 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 [5]
RP FUNCTION.
RX PubMed=23101887; DOI=10.3109/13693786.2012.733892;
RA Ueno K., Okawara A., Yamagoe S., Naka T., Umeyama T., Utena-Abe Y.,
RA Tarumoto N., Niimi M., Ohno H., Doe M., Fujiwara N., Kinjo Y., Miyazaki Y.;
RT "The mannan of Candida albicans lacking beta-1,2-linked oligomannosides
RT increases the production of inflammatory cytokines by dendritic cells.";
RL Med. Mycol. 51:385-395(2013).
CC -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis.
CC Required for addition of the first beta-mannose residue to acid-stable
CC fraction of cell wall phosphopeptidomannan. Plays a key role in
CC reducing host inflammatory response. {ECO:0000269|PubMed:18234669,
CC ECO:0000269|PubMed:23101887}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Impairs the mannosylation of beta-mannose chains
CC on the acid-stable fraction of cell wall phosphopeptidomannan.
CC {ECO:0000269|PubMed:18234669}.
CC -!- SIMILARITY: Belongs to the BMT family. {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; CP017625; AOW28721.1; -; Genomic_DNA.
DR RefSeq; XP_719878.1; XM_714785.1.
DR AlphaFoldDB; Q5ADQ9; -.
DR STRING; 237561.Q5ADQ9; -.
DR CAZy; GT91; Glycosyltransferase Family 91.
DR PRIDE; Q5ADQ9; -.
DR GeneID; 3638535; -.
DR KEGG; cal:CAALFM_C307180CA; -.
DR CGD; CAL0000201954; BMT1.
DR VEuPathDB; FungiDB:C3_07180C_A; -.
DR eggNOG; ENOG502QTZG; Eukaryota.
DR HOGENOM; CLU_013841_1_1_1; -.
DR InParanoid; Q5ADQ9; -.
DR OrthoDB; 487566at2759; -.
DR PRO; PR:Q5ADQ9; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000030; F:mannosyltransferase activity; IDA:CGD.
DR GO; GO:0070136; P:beta-1,2-oligomannoside biosynthetic process; IDA:CGD.
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; IBA:GO_Central.
DR GO; GO:0035269; P:protein O-linked mannosylation; IMP:CGD.
DR InterPro; IPR021988; BMT1.
DR PANTHER; PTHR37989; PTHR37989; 1.
DR Pfam; PF12141; DUF3589; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..684
FT /note="Beta-mannosyltransferase 1"
FT /id="PRO_0000426069"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..684
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 684 AA; 79603 MW; AA70FF9D5A5C7E2E CRC64;
MDKFIQSFSH QYLDSSSSLK LTARRKRKLT ILGLFLFSLI SLMIIISYSN NNILPGLSGI
SISSTFSDYY SNPKQQNKFE QQIQDHQTTK KGKRTIIFPN NFNHVHDHKG SYMMKDSELV
KYYVETMEQA LDPEDLIYRN RFTYKLPNIP YTEQKIEMFS DGGGGGGDTS DSNTDMCPKL
STTIKVEASP AMNKNGDLKK ILKTFLQEDS FYYRELSPFF PDLKKHFDED TIDKHWYQFI
GSTVWLEQYG VHLMVSRIIY TEKDQGSPKF SLAYLQVFDR NWKELDNVEL IVPDPENIST
TNNKNKNKKP YGYKSVLYPT IAPIPVYHNS KQTGGRFYGI EDPRIVLIKT RHGYEEPVLI
YNSHHRKISE KHFDNDQEGK INFNNYRSLF IGWIWQTQLG KIHLEELPNN EFKKNEYIKI
KEFVKPNNNR GRTEKNWALF INYNQRLNQG FDSHVYFANQ LKNLKILKCS ILNDNDDDCE
WEFQMDDYED AGVLHGGTEL ININQLLHQY DYPELNSIKD LIPNGREYWV GFARASLKNC
GCGSRMYRPN LIVLMKDGKN YKFAYVSSFV GLGIEILPWY LDKGLCEHYN LIIPNGISSW
TIEKDLHQKE KDKQVMDYMA FTISRRDATV DVVYVKGLLK ALFTDSSSSK HLLAVEQTGF
KSVTNVDCAL KNSEKFCKIY GETF
