BMT2_KOMPC
ID BMT2_KOMPC Reviewed; 635 AA.
AC F2QZ66;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Beta-mannosyltransferase 2;
DE EC=2.4.1.-;
GN Name=BMT2; OrderedLocusNames=PP7435_Chr4-0530;
OS Komagataella phaffii (strain ATCC 76273 / CBS 7435 / CECT 11047 / NRRL
OS Y-11430 / Wegner 21-1) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=981350;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX PubMed=21575661; DOI=10.1016/j.jbiotec.2011.04.014;
RA Kueberl A., Schneider J., Thallinger G.G., Anderl I., Wibberg D., Hajek T.,
RA Jaenicke S., Brinkrolf K., Goesmann A., Szczepanowski R., Puehler A.,
RA Schwab H., Glieder A., Pichler H.;
RT "High-quality genome sequence of Pichia pastoris CBS7435.";
RL J. Biotechnol. 154:312-320(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX PubMed=27388471; DOI=10.1093/femsyr/fow051;
RA Valli M., Tatto N.E., Peymann A., Gruber C., Landes N., Ekker H.,
RA Thallinger G.G., Mattanovich D., Gasser B., Graf A.B.;
RT "Curation of the genome annotation of Pichia pastoris (Komagataella
RT phaffii) CBS7435 from gene level to protein function.";
RL FEMS Yeast Res. 16:0-0(2016).
CC -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis.
CC Initiates the beta-mannosylation of core N-linked glycans (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR EMBL; FR839631; CCA40694.1; -; Genomic_DNA.
DR AlphaFoldDB; F2QZ66; -.
DR SMR; F2QZ66; -.
DR CAZy; GT91; Glycosyltransferase Family 91.
DR EnsemblFungi; CCA40694; CCA40694; PP7435_CHR4-0530.
DR HOGENOM; CLU_013841_2_1_1; -.
DR Proteomes; UP000006853; 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; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..635
FT /note="Beta-mannosyltransferase 2"
FT /id="PRO_0000426101"
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..635
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 517..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 512..635
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 635 AA; 73436 MW; DB5480C45B9F7E61 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 EKKGK