ID   BMT8_CANAL              Reviewed;         694 AA.
AC   Q5AHD6; A0A1D8PH12; Q5AHR2;
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 8;
DE            EC=2.4.1.-;
DE   AltName: Full=WRY family protein 3;
GN   Name=BMT8; Synonyms=WRY3; OrderedLocusNames=CAALFM_C203600WA;
GN   ORFNames=CaO19.8479, CaO19.860;
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   DISRUPTION PHENOTYPE.
RX   PubMed=20141603; DOI=10.1111/j.1365-2958.2009.07038.x;
RA   Epp E., Walther A., Lepine G., Leon Z., Mullick A., Raymond M.,
RA   Wendland J., Whiteway M.;
RT   "Forward genetics in Candida albicans that reveals the Arp2/3 complex is
RT   required for hyphal formation, but not endocytosis.";
RL   Mol. Microbiol. 75:1182-1198(2010).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23951271; DOI=10.1371/journal.pone.0071939;
RA   Fox S.J., Shelton B.T., Kruppa M.D.;
RT   "Characterization of genetic determinants that modulate Candida albicans
RT   filamentation in the presence of bacteria.";
RL   PLoS ONE 8:E71939-E71939(2013).
CC   -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis
CC       through beta-1,2-mannosylation of cell wall phosphopeptidomannan (By
CC       similarity). Plays a role in the ability to produce hyphae in the
CC       presence of three bacterial species. {ECO:0000250,
CC       ECO:0000269|PubMed:23951271}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Leads to a hypo-filamentous phenotype.
CC       {ECO:0000269|PubMed:20141603, ECO:0000269|PubMed:23951271}.
CC   -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR   EMBL; CP017624; AOW27393.1; -; Genomic_DNA.
DR   RefSeq; XP_720983.1; XM_715890.2.
DR   AlphaFoldDB; Q5AHD6; -.
DR   CAZy; GT91; Glycosyltransferase Family 91.
DR   GeneID; 3637442; -.
DR   KEGG; cal:CAALFM_C203600WA; -.
DR   CGD; CAL0000195105; BMT8.
DR   VEuPathDB; FungiDB:C2_03600W_A; -.
DR   eggNOG; ENOG502QTZG; Eukaryota.
DR   HOGENOM; CLU_013841_1_1_1; -.
DR   InParanoid; Q5AHD6; -.
DR   OrthoDB; 487566at2759; -.
DR   PRO; PR:Q5AHD6; -.
DR   Proteomes; UP000000559; Chromosome 2.
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:0030447; P:filamentous growth; IMP:CGD.
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   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..694
FT                   /note="Beta-mannosyltransferase 8"
FT                   /id="PRO_0000426076"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..694
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   694 AA;  80590 MW;  197C0EBD519F1316 CRC64;
     MKFPKLRKRT VYWAVLTVFA LFTIHFVFQY KEHNSHRVQP IVLIPKAFPS LILNSFDTQN
     EELVPIKLLK NCQIIRSYHT GYEENTKLLG QEPQSNFHKF NFTVFSSMKP IGLDLKQCQL
     LSSSSQVEVN DAVNMDASLH DILGKLLQDI RHGKLEYLQE IAPFFLPELQ LQLNLNIVDR
     FWYRFSGSSI WLDQYNMYFM ISRIAYSPHG VKNQPVVSLT YGQLFDRNWN EVKNINLLVP
     SNDPSKNGGH DSFRIISFPY FLPIPFWHDI DNTDGNYFGP EDPRLILVRN KQGYEEPLLI
     FNSYHRKFVH YDDDEDSIMG QTVKFQRSMF MCWPWQYQMG KSNVEGTSNP EYDNKVYNRV
     IELKVKLLAD MKSQKNWTPF ISEDSTNKFD SYIYFVYRWA NLDVLKCSLL GDVAGDCVFD
     YRLDETLVPQ NKVGPLRGGT QLVNLRQVIP RSVYHRLLPS HREIFIGFAR THLDNCGCGK
     VMYRPNLVIL VKDAADKTYY KISHISSSLS FDVPIIGWNV YKPDDLCFDS NVLIPYSVSN
     WNITSLELDI EGGRWVSNDQ LTLTLSISDS TVHRLDIRGL FQSILDLADR SLFIPVDRET
     RVIDEFQNGL QNPGSNPLNQ DVNSLGVNND NIVCALDASV EFCFEYGAKF SIPKQEEFYE
     VEQQEFNEEL IDPKKHQYFK ILGKYLYDHA SVNS