ID   BMT1_KOMPG              Reviewed;         652 AA.
AC   C4R7X9;
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 1;
DE            EC=2.4.1.-;
GN   Name=BMT1; OrderedLocusNames=PAS_chr4_0451;
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       Involved in the beta-mannosylation of outer chains of N-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: Impaired expression of beta-mannose epitopes and
CC       decreases alpha-mannosidase resistant glycans.
CC       {ECO:0000269|PubMed:18234669, ECO:0000269|PubMed:21840970}.
CC   -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR   EMBL; FN392322; CAY71704.1; -; Genomic_DNA.
DR   RefSeq; XP_002493883.1; XM_002493838.1.
DR   AlphaFoldDB; C4R7X9; -.
DR   SMR; C4R7X9; -.
DR   CAZy; GT91; Glycosyltransferase Family 91.
DR   PRIDE; C4R7X9; -.
DR   EnsemblFungi; CAY71704; CAY71704; PAS_chr4_0451.
DR   GeneID; 8201400; -.
DR   KEGG; ppa:PAS_chr4_0451; -.
DR   eggNOG; ENOG502QTZG; Eukaryota.
DR   HOGENOM; CLU_013841_2_1_1; -.
DR   InParanoid; C4R7X9; -.
DR   OMA; WKRAMYI; -.
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..652
FT                   /note="Beta-mannosyltransferase 1"
FT                   /id="PRO_0000426098"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..652
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          536..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          535..652
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   652 AA;  74338 MW;  F03E379001B1058A CRC64;
     MVDLFQWLKF YSMRRLGQVA ITLVLLNLFV FLGYKFTPST VIGSPSWEPA VVPTVFNESY
     LDSLQFTDIN VDSFLSDTNG RISVTCDSLA YKGLVKTSKK KELDCDMAYI RRKIFSSEEY
     GVLADLEAQD ITEEQRIKKH WFTFYGSSVY LPEHEVHYLV RRVLFSKVGR ADTPVISLLV
     AQLYDKDWNE LTPHTLEIVN PATGNVTPQT FPQLIHVPIE WSVDDKWKGT EDPRVFLKPS
     KTGVSEPIVL FNLQSSLCDG KRGMFVTSPF RSDKVNLLDI EDKERPNSEK NWSPFFLDDV
     EVSKYSTGYV HFVYSFNPLK VIKCSLDTGA CRMIYESPEE GRFGSELRGA TPMVKLPVHL
     SLPKGKEVWV AFPRTRLRDC GCSRTTYRPV LTLFVKEGNK FYTELISSSI DFHIDVLSYD
     AKGESCSGSI SVLIPNGIDS WDVSKKQGGK SDILTLTLSE ADRNTVVVHV KGLLDYLLVL
     NGEGPIHDSH SFKNVLSTNH FKSDTTLLNS VKAAECAIFS SRDYCKKYGE TRGEPARYAK
     QMENERKEKE KKEKEAKEKL EAEKAEMEEA VRKAQEAIAQ KEREKEEAEQ EKKAQQEAKE
     KEAEEKAAKE KEAKENEAKK KIIVEKLAKE QEEAEKLEAK KKLYQLQEEE RS