ID   BMT9_CANAL              Reviewed;         782 AA.
AC   Q5AMH3; A0A1D8PL96;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Beta-mannosyltransferase 9;
DE            EC=2.4.1.-;
DE   AltName: Full=WRY family protein 5;
GN   Name=BMT9; Synonyms=WRY5; OrderedLocusNames=CAALFM_C401170CA;
GN   ORFNames=CaO19.12143, CaO19.4673;
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=21843869; DOI=10.1016/j.chom.2011.07.005;
RA   Chen C., Pande K., French S.D., Tuch B.B., Noble S.M.;
RT   "An iron homeostasis regulatory circuit with reciprocal roles in Candida
RT   albicans commensalism and pathogenesis.";
RL   Cell Host Microbe 10:118-135(2011).
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 regulated by SEF1, SFU1, and HAP43.
CC       {ECO:0000269|PubMed:21592964, ECO:0000269|PubMed:21843869}.
CC   -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR   EMBL; CP017626; AOW28903.1; -; Genomic_DNA.
DR   RefSeq; XP_722742.2; XM_717649.2.
DR   AlphaFoldDB; Q5AMH3; -.
DR   CAZy; GT91; Glycosyltransferase Family 91.
DR   GeneID; 3635654; -.
DR   KEGG; cal:CAALFM_C401170CA; -.
DR   CGD; CAL0000183827; BMT9.
DR   VEuPathDB; FungiDB:C4_01170C_A; -.
DR   eggNOG; ENOG502QTZG; Eukaryota.
DR   HOGENOM; CLU_707868_0_0_1; -.
DR   InParanoid; Q5AMH3; -.
DR   OrthoDB; 487566at2759; -.
DR   PRO; PR:Q5AMH3; -.
DR   Proteomes; UP000000559; Chromosome 4.
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; 2.
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..782
FT                   /note="Beta-mannosyltransferase 9"
FT                   /id="PRO_0000426077"
FT   TOPO_DOM        1..26
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..782
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          66..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        648
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        699
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   782 AA;  89915 MW;  E8B6EBAFEE04B1B5 CRC64;
     MEKLIQSTIS LFISLSLKIS TKSYKSIISI LFIISLLSII LTTTITVYHD PERIITTTTT
     TTSASKSVFT ASSPKQQDKL QQEIDQHQSD NSHEQQGKRI IIFPNNFPLI KNDQLVKYYI
     DTMNQALQPH DLIYRNCFEY KIPQLSYSSQ KIDVFSDGGG GDQSGIKCRK LSSQVNVKVS
     PAINKNGNMR QILTRFMQDD GLYFQEFLPF FPNLKEQLQS ADDDIINKHW YQFIGSTVWL
     QQYGVHLMIS RIIYTEVDQG LPIISLAYLQ LFDRNWNELN DVELIIPDYE TTTTTTTQSK
     YKYKSIIYPY FAPIPIYHNV KQLNTGKFFG VEDPRIMLIT NEFGFEEPII IYNSHHRKIS
     NIDYENGGDN QGKINFKNYR SLFIGWLWKT QIGKFNLEQL PSEHTLDNHK ANKNDANNND
     YSKNEYIKIK ELTRPNNQRN LLEKNWSLFL NHQEKLNHGY HSFIYFIYQF KDLKILKCPL
     SSSTTKKNND GDDRFDSGCQ WEYQINDDDN FGSGYLHGGT ELINVNELLD NYLSKSSTST
     SINGKQLTNS IKDRLPLNRQ IWIGFARAAM RHCGCSETMY RPNMVILVKD DVPTNTNIAS
     GKSNYRLTHV SSFMDLGIEV LPWWEDKGLC EGKNVVIPNG ISSWTIENES NNLESESSTI
     TSNNLVDYLT ITITRRDTTI DLVYIKGLLN ALLLNPDNNN SNNDVDDTEE GSSIFKSSVL
     FNVDLVKDYS STTTTTTTKN VNKNLDCALQ YSHKYCQIYG EKLKIEDEFN NKGKDKGKDK
     SN