ID   BMT7_CANAL              Reviewed;         651 AA.
AC   Q5AEC6; A0A1D8PJS0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Beta-mannosyltransferase 7;
DE            EC=2.4.1.-;
DE   AltName: Full=WRY family protein 8;
GN   Name=BMT7; Synonyms=WRY8; OrderedLocusNames=CAALFM_C303450CA;
GN   ORFNames=CaO19.342, CaO19.7975;
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=15273122; DOI=10.1128/aac.48.8.3064-3079.2004;
RA   Karababa M., Coste A.T., Rognon B., Bille J., Sanglard D.;
RT   "Comparison of gene expression profiles of Candida albicans azole-resistant
RT   clinical isolates and laboratory strains exposed to drugs inducing
RT   multidrug transporters.";
RL   Antimicrob. Agents Chemother. 48:3064-3079(2004).
RN   [5]
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   [6]
RP   INDUCTION.
RX   PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA   Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT   "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT   contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL   J. Biol. Chem. 286:25154-25170(2011).
CC   -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis
CC       through beta-1,2-mannosylation of cell wall phosphopeptidomannan.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Expression is induced by HAP43 and down-regulated in an
CC       azole-resistant strain. {ECO:0000269|PubMed:15273122,
CC       ECO:0000269|PubMed:21592964}.
CC   -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR   EMBL; CP017625; AOW28373.1; -; Genomic_DNA.
DR   RefSeq; XP_720037.1; XM_714944.1.
DR   AlphaFoldDB; Q5AEC6; -.
DR   STRING; 237561.Q5AEC6; -.
DR   CAZy; GT91; Glycosyltransferase Family 91.
DR   PRIDE; Q5AEC6; -.
DR   GeneID; 3638357; -.
DR   KEGG; cal:CAALFM_C303450CA; -.
DR   CGD; CAL0000190174; BMT7.
DR   VEuPathDB; FungiDB:C3_03450C_A; -.
DR   eggNOG; ENOG502QTZG; Eukaryota.
DR   HOGENOM; CLU_013841_3_1_1; -.
DR   InParanoid; Q5AEC6; -.
DR   OrthoDB; 487566at2759; -.
DR   PRO; PR:Q5AEC6; -.
DR   Proteomes; UP000000559; Chromosome 3.
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.
FT   CHAIN           1..651
FT                   /note="Beta-mannosyltransferase 7"
FT                   /id="PRO_0000426075"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..651
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   651 AA;  75191 MW;  1EB1B79EABAB0785 CRC64;
     MKLEMSSYLH KVPNTGITNL SNSKSIVFIM FCATLLFIIT SSRYLTGSES LGQIPSEIPK
     SSEQLNEELS QQINSKLHKL ASFDKFNSFP LLNKHMKDDI YGLMTLETFT DPLPYLENYN
     EEEYSQQNYP ICSEKLMFPS KIKLTKQQYL PADLQQFLGV LNNMRPYHDM VEKAKAYFIS
     DLREEKKWFR FAGSSIWLPQ FQCHYMVSRY LYSPNGVANH AFASFLYIQL FDSDWKELPS
     HTTLDIPFEQ TEANSIFKIF KPKQKYANFR NSTYPQILPI PFDYKLPIET KKYYYGPEDP
     RILLRSNPLG FDEPLIVFNM KGLKLTKRVM YSYLPFSNTL KLLKKRREPF ANIEKNWTPF
     KSVAQPSKTQ TTIHFIYSMI PLEVLACDID SGLCDILQKP AKHDFNYVGG LRGGTQLVSL
     PLNETIPSEI RAKLPIPKNR QVYIGWARTH LNNCGCGDSM YRPNFITLVE DYDDVTDKYY
     YKIGDISGYF DFAAKIEPWS KQVLDEEGNL YEKAEQCQGR NVLIPNSIAY WDVGSIKLAG
     TEYQKHDFKD MFSSGKVSDF NANEIVFNDY MGVTLSSADR DVSIVHVKGL LNYILQLPSL
     VDDSLVINKE WTFQKKGHDL NVRCAMIASK EYCKSYAIKQ GVKIDEKSEE T