ID S9X137_SCHCR Unreviewed; 422 AA.
AC S9X137;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase {ECO:0000256|ARBA:ARBA00015841};
DE EC=2.4.1.142 {ECO:0000256|ARBA:ARBA00012611};
GN ORFNames=SPOG_00665 {ECO:0000313|EMBL:EPY50797.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY50797.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY50797.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- FUNCTION: Participates in the formation of the lipid-linked precursor
CC oligosaccharide for N-glycosylation. Involved in assembling the
CC dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic
CC surface of the ER. {ECO:0000256|ARBA:ARBA00024899}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl
CC diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:13865,
CC Rhea:RHEA-COMP:9520, Rhea:RHEA-COMP:11044, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472; EC=2.4.1.142;
CC Evidence={ECO:0000256|ARBA:ARBA00001259};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
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DR EMBL; KE546992; EPY50797.1; -; Genomic_DNA.
DR RefSeq; XP_013024294.1; XM_013168840.1.
DR AlphaFoldDB; S9X137; -.
DR STRING; 653667.S9X137; -.
DR EnsemblFungi; EPY50797; EPY50797; SPOG_00665.
DR GeneID; 25034997; -.
DR eggNOG; KOG2941; Eukaryota.
DR HOGENOM; CLU_012079_1_0_1; -.
DR OMA; CKLIIDW; -.
DR OrthoDB; 1219598at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004578; F:chitobiosyldiphosphodolichol beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR026051; ALG1-like.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR13036; BETA1,4 MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR13036:SF0; CHITOBIOSYLDIPHOSPHODOLICHOL BETA-MANNOSYLTRANSFERASE; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:EPY50797.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPY50797.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..422
FT /note="Chitobiosyldiphosphodolichol beta-
FT mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004572907"
FT DOMAIN 236..396
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
SQ SEQUENCE 422 AA; 48235 MW; 2654295B50A347D8 CRC64;
MLAIRILLFL SAVIFINSRR SAKSKRIIIL VLGRIDQSPR MQYHALSFAK QGWKVDLVGY
QDKKGPGLFQ NHPNIQSYAI PTLPGSLTFR SRLSFLLVAP VKILHQLLSI LFILFKIKQA
SYFLVQNPPS IPTFLLGHVL YLLRGTRFVI DWHNFGYTIL ALKLGKEHPF VKLLRIYERV
LAKGAFLHIT VSYSMQQVLL EWGIRPCHVC YDRPPAHFQP VQDATRKSNL HVIPEEFNPE
KEKLLVTSTS WTPDENIYAL WDALKMYNET RNAVPLLVLV TGKGPGKPDF VKHLQKNPLG
KVRFCLPWFS SEDYPRAIAC ADFGVSLHQS SSGHDLPMKV VDLFGCGVPV VAWNFPAISE
LVHDHKNGFI ANDSNELFKK IELLCSDEHV LQSVRQGAFE ESKNRWDDEW NKKIPRLFTI
DS
//
