ID   BMT2_KOMPG              Reviewed;         644 AA.
AC   C4R7X8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Beta-mannosyltransferase 2;
DE            EC=2.4.1.-;
GN   Name=BMT2; OrderedLocusNames=PAS_chr4_0450;
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, 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   [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       Initiates the beta-mannosylation of core N-linked glycans.
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: Strongly reduces de degree of mannosylation of
CC       the core glycans and eliminates glycans resistant to alpha-1,2-
CC       mannosidase treatment. {ECO:0000269|PubMed:18234669,
CC       ECO:0000269|PubMed:21840970}.
CC   -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR   EMBL; FN392322; CAY71703.1; -; Genomic_DNA.
DR   RefSeq; XP_002493882.1; XM_002493837.1.
DR   AlphaFoldDB; C4R7X8; -.
DR   SMR; C4R7X8; -.
DR   CAZy; GT91; Glycosyltransferase Family 91.
DR   PRIDE; C4R7X8; -.
DR   EnsemblFungi; CAY71703; CAY71703; PAS_chr4_0450.
DR   GeneID; 8201399; -.
DR   KEGG; ppa:PAS_chr4_0450; -.
DR   eggNOG; ENOG502QTZG; Eukaryota.
DR   HOGENOM; CLU_013841_2_1_1; -.
DR   InParanoid; C4R7X8; -.
DR   OMA; PINNIMR; -.
DR   Proteomes; UP000000314; 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   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..644
FT                   /note="Beta-mannosyltransferase 2"
FT                   /id="PRO_0000426100"
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..644
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          517..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          512..644
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        484
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   644 AA;  74561 MW;  1B9177D5859239EA CRC64;
     MRTRLNFLLL CIASVLSVIW IGVLLTWNDN NLGGISLNGG KDSAYDDLLS LGSFNDMEVD
     SYVTNIYDNA PVLGCTDLSY HGLLKVTPKH DLACDLEFIR AQILDIDVYS AIKDLEDKAL
     TVKQKVEKHW FTFYGSSVFL PEHDVHYLVR RVIFSAEGKA NSPVTSIIVA QIYDKNWNEL
     NGHFLDILNP NTGKVQHNTF PQVLPIATNF VKGKKFRGAE DPRVVLRKGR FGPDPLVMFN
     SLTQDNKRRR IFTISPFDQF KTVMYDIKDY EMPRYEKNWV PFFLKDNQEA VHFVYSFNPL
     RVLKCSLDDG SCDIVFEIPK VDSMSSELRG ATPMINLPQA IPMAKDKEIW VSFPRTRIAN
     CGCSRTTYRP MLMLFVREGS NFFVELLSTS LDFGLEVLPY SGNGLPCSAD HSVLIPNSID
     NWEVVDSNGD DILTLSFSEA DKSTSVIHIR GLYNYLSELD GYQGPEAEDE HNFQRILSDL
     HFDNKTTVNN FIKVQSCALD AAKGYCKEYG LTRGEAERRR RVAEERKKKE KEEEEKKKKK
     EKEEEEKKRI EEEKKKIEEK ERKEKEKEEA ERKKLQEMKK KLEEITEKLE KGQRNKEIDP
     KEKQREEEER KERVRKIAEK QRKEAEKKEA EKKANDKKDL KIRQ