ID   BMT4_KOMPG              Reviewed;         503 AA.
AC   C4R7Z8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 2.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Beta-mannosyltransferase 4;
DE            EC=2.4.1.-;
GN   Name=BMT4; OrderedLocusNames=PAS_chr4_0471;
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       Responsible for addition of a hexose to the beta-mannose chain. Beta-
CC       mannosylation catalyzed by BMT4 masks beta-mannose epitopes recognized
CC       by monoclonal antibody (mAb) 5B2 reacting with beta-1,2-linked
CC       mannobiose as a minimal epitope. {ECO:0000269|PubMed:18234669,
CC       ECO:0000269|PubMed:21840970}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Leads to a size reduction of glycans resistant to
CC       alpha-mannosidase treatment. {ECO:0000269|PubMed:18234669,
CC       ECO:0000269|PubMed:21840970}.
CC   -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAY71723.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; FN392322; CAY71723.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002493902.1; XM_002493857.1.
DR   AlphaFoldDB; C4R7Z8; -.
DR   EnsemblFungi; CAY71723; CAY71723; PAS_chr4_0471.
DR   GeneID; 8201418; -.
DR   KEGG; ppa:PAS_chr4_0471; -.
DR   eggNOG; ENOG502QTZG; Eukaryota.
DR   HOGENOM; CLU_013841_3_0_1; -.
DR   InParanoid; C4R7Z8; -.
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; Glycoprotein; Glycosyltransferase;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..503
FT                   /note="Beta-mannosyltransferase 4"
FT                   /id="PRO_0000426104"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..503
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        468
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   503 AA;  56665 MW;  CD914139E9E988A5 CRC64;
     MKLDTQQISH LLSRQMYHLA PRKKLLIWGG SLGFVLLLLI VASSHQRIRS TILHRTPIST
     LPVISQEVIT ADYHPTLLTG FIPTDSDDSD CADFSPSGVI YSTDKLVLHD SLKDIRDSLL
     KTQYKDLVTL EDEEKMNIDD ILKRWYTLSG SSVWIPGMKA HLVVSRVMYL GTNGRSDPLV
     SFVRVQLFDP DFNELKDIAL KFSDKPDGTV IFPYILPVDI PREGSRWLGP EDAKIAVNPE
     TPDDPIVIFN MQNSVNRAMY GFYPFRPENK QVLFSIKDEE PRKKEKNWTP FFVPGSPTTV
     NFVYDLQKLT ILKCSIITGI CEKEFVSGDD GQNHGIGIFR GGSNLVPFPT SFTDKDVWVG
     FPKTHMESCG CSSHIYRPYL MVLVRKGDFY YKAFVSTPLD FGIDVRSWES AESTSCQTAK
     NVLAVNSISN WDLLDDGLDK DYMTITLSEA DVVNSVLRVR GIAKFVDNLT MDDGSTTLST
     SNKIDECATT GSKQYCQRYG ELH