ID   BMT3_KOMPG              Reviewed;         594 AA.
AC   C4QZ06;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Beta-mannosyltransferase 3;
DE            EC=2.4.1.-;
GN   Name=BMT3; OrderedLocusNames=PAS_chr1-4_0696;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
RN   [2]
RP   IDENTIFICATION, 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   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21840970; DOI=10.1093/glycob/cwr108;
RA   Hopkins D., Gomathinayagam S., Rittenhour A.M., Du M., Hoyt E., Karaveg K.,
RA   Mitchell T., Nett J.H., Sharkey N.J., Stadheim T.A., Li H., Hamilton S.R.;
RT   "Elimination of beta-mannose glycan structures in Pichia pastoris.";
RL   Glycobiology 21:1616-1626(2011).
CC   -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis.
CC       {ECO:0000269|PubMed:18234669, ECO:0000269|PubMed:21840970}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Decreases alpha-mannosidase resistant glycans.
CC       {ECO:0000269|PubMed:21840970}.
CC   -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR   EMBL; FN392319; CAY68480.1; -; Genomic_DNA.
DR   RefSeq; XP_002490760.1; XM_002490715.1.
DR   AlphaFoldDB; C4QZ06; -.
DR   CAZy; GT91; Glycosyltransferase Family 91.
DR   EnsemblFungi; CAY68480; CAY68480; PAS_chr1-4_0696.
DR   GeneID; 8197829; -.
DR   KEGG; ppa:PAS_chr1-4_0696; -.
DR   eggNOG; ENOG502QTZG; Eukaryota.
DR   HOGENOM; CLU_013841_3_0_1; -.
DR   InParanoid; C4QZ06; -.
DR   OMA; FNSYHRQ; -.
DR   Proteomes; UP000000314; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR021988; BMT1.
DR   PANTHER; PTHR37989; PTHR37989; 2.
DR   Pfam; PF12141; DUF3589; 2.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Coiled coil; Glycoprotein;
KW   Glycosyltransferase; Membrane; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..594
FT                   /note="Beta-mannosyltransferase 3"
FT                   /id="PRO_0000426102"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..594
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          517..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          512..594
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   594 AA;  68423 MW;  DB09B57D918FEB1A CRC64;
     MRIRSNVLLL STAGALALVW FAVVFSWDDK SIFGIPTPGH AVASAYDSSV TLGTFNDMEV
     DSYVTNIYDN APVLGCYDLS YHGLLKVSPK HEILCDMKFI RARVLETEAY AALKDLEHKK
     LTEEEKIEKH WFTFYGSSVF LPDHDVHYLV RRVVFSGEGK ANRPITSILV AQIYDKNWNE
     LNGHFLNVLN PNTGKLQHHA FPQVLPIAVN WDRNSKYRGQ EDPRVVLRRG RFGPDPLVMF
     NTLTQNNKLR RLFTISPFDQ YKTVMYRTNA FKMQTTEKNW VPFFLKDDQE SVHFVYSFNP
     LRVLNCSLDN GACDVLFELP HDFGMSSELR GATPMLNLPQ AIPMADDKEI WVSFPRTRIS
     DCGCSETMYR PMLMLFVREG TNFFAELLSS SIDFGLEVIP YTGDGLPCSS GQSVLIPNSI
     DNWEVTGSNG EDILSLTFSE ADKSTSVVHI RGLYKYLSEL DGYGGPEAED EHNFQRILSD
     LHFDGKKTIE NFKKVQSCAL DAAKAYCKEY GVTRGEEDRL KNKEKERKIE EKRKKEEERK
     KKEEEKKKKE EEEKKKKEEE EEEEKRLKEL KKKLKELQEE LEKQKDEVKD TKAK