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Database: UniProt
Entry: A0A1E5R690_9ASCO
LinkDB: A0A1E5R690_9ASCO
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ID   A0A1E5R690_9ASCO        Unreviewed;       478 AA.
AC   A0A1E5R690;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase {ECO:0000256|ARBA:ARBA00015841};
DE            EC=2.4.1.142 {ECO:0000256|ARBA:ARBA00012611};
DE   AltName: Full=Asparagine-linked glycosylation protein 1 {ECO:0000256|ARBA:ARBA00030745};
DE   AltName: Full=Beta-1,4-mannosyltransferase {ECO:0000256|ARBA:ARBA00031566};
DE   AltName: Full=GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase {ECO:0000256|ARBA:ARBA00033088};
DE   AltName: Full=GDP-mannose-dolichol diphosphochitobiose mannosyltransferase {ECO:0000256|ARBA:ARBA00031434};
GN   ORFNames=AWRI3578_g3391 {ECO:0000313|EMBL:OEJ82412.1};
OS   Hanseniaspora opuntiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=211096 {ECO:0000313|EMBL:OEJ82412.1, ECO:0000313|Proteomes:UP000095605};
RN   [1] {ECO:0000313|Proteomes:UP000095605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI3578 {ECO:0000313|Proteomes:UP000095605};
RX   PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA   Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT   "Genome sequences of three species of Hanseniaspora isolated from
RT   spontaneous wine fermentations.";
RL   Genome Announc. 4:E01287-E01287(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEJ82412.1}.
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DR   EMBL; LPNL01000008; OEJ82412.1; -; Genomic_DNA.
DR   OrthoDB; 1219598at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000095605; 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   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR026051; ALG1-like.
DR   PANTHER; PTHR13036; BETA1,4 MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR13036:SF0; CHITOBIOSYLDIPHOSPHODOLICHOL BETA-MANNOSYLTRANSFERASE; 1.
DR   Pfam; PF13692; Glyco_trans_1_4; 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:OEJ82412.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OEJ82412.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   478 AA;  55408 MW;  7236B6A230CA85A2 CRC64;
     MRTGDYVLIV SSIIVSFIPI FFYYVLPFIK DTKHMNAFKR KACVIVIGPL VRSPRMMNHI
     KALLLSGYDV EVISQATPNE LNELNSKYST IIKSIHXDDD QEXLNNVPTI NFHLLESEKY
     KKQSYIMKAL SQMFTLLKMI WSVRSCDYAL VQNPPSIPIL PILITSKLIF NWKVIIDWHN
     FGYSIFLMKG NSSKIKLLGN LYFKLELYFG RLADHHLVVT KMMADVLIKT WRWESKYPKV
     EGDGFKVNDK ITVCYDYPDV QFQPYVNKVQ DRLELINNIP DVADLKNVDI TEYTIGVTST
     SFTPDEDLQL LLDSLKDLDS ILKXKGKKFM LIITGKGPLK DXFIKSFEEQ XFHNIQYRFY
     YLKLEDYPKI LQLADFGISL HSSSSGWDLP MKVWDMIGCG LPCVAYSFPA LDKELVHANK
     TGLLFKDKSE LVHCLEEMLT NXDLMRXLTR NSLXNLNQMD RWVESWNKSV RKYIQPGC
//
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