ID G7XCS4_ASPKW Unreviewed; 244 AA.
AC G7XCS4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Dolichol-phosphate mannosyltransferase subunit 1 {ECO:0000256|RuleBase:RU365083};
DE EC=2.4.1.83 {ECO:0000256|RuleBase:RU365083};
GN ORFNames=AKAW_03130 {ECO:0000313|EMBL:GAA85016.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA85016.1};
RN [1] {ECO:0000313|EMBL:GAA85016.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA85016.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate
CC to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl
CC donor in pathways leading to N-glycosylation, glycosyl
CC phosphatidylinositol membrane anchoring, and O-mannosylation of
CC proteins. {ECO:0000256|RuleBase:RU365083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-
CC D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:58211;
CC Evidence={ECO:0000256|RuleBase:RU365083};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU365083}.
CC -!- SUBUNIT: Component of the dolichol-phosphate mannose (DPM) synthase
CC complex. {ECO:0000256|RuleBase:RU365083}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|RuleBase:RU365083}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739, ECO:0000256|RuleBase:RU365083}.
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DR EMBL; DF126452; GAA85016.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XCS4; -.
DR STRING; 1033177.G7XCS4; -.
DR VEuPathDB; FungiDB:AKAW_03130; -.
DR eggNOG; KOG2978; Eukaryota.
DR InParanoid; G7XCS4; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
DR CDD; cd06442; DPM1_like; 1.
DR InterPro; IPR039528; DPM1-like.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43398; DOLICHOL-PHOSPHATE MANNOSYLTRANSFERASE SUBUNIT 1; 1.
DR PANTHER; PTHR43398:SF1; DOLICHOL-PHOSPHATE MANNOSYLTRANSFERASE SUBUNIT 1; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU365083};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU365083};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365083}.
FT DOMAIN 8..182
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 244 AA; 27578 MW; 4A25213BF4982FDC CRC64;
MGAENKYSVI LPTYNERRNL PIIVWLLERT FRENNLDWEI IIVDDGSPDG TLDIAKQLQK
HYGANHILLH PRAGKLGLGT AYIHGLQFTT GNYVIIMDAD FSHHPKFIPE MIRIQKLGDA
DIVTGTRYAS RDGIKGGVYG WDLFRKFTSR TANLIADVML MPGVSDLTGS FRLYKKSVLE
KVIHSTQSKG YSFQMEMMVR AKAMGFRVAE CPITFVDRLY GESKLGGSEI VEYLKGVVTL
WLKV
//
