ID J8PXM4_SACAR Unreviewed; 555 AA.
AC J8PXM4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN ORFNames=SU7_2889 {ECO:0000313|EMBL:EJS42088.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS42088.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS42088.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a
CC dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+);
CC Xref=Rhea:RHEA:29539, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:12630, Rhea:RHEA-COMP:12631, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132519,
CC ChEBI:CHEBI:132520; EC=2.4.1.261;
CC Evidence={ECO:0000256|ARBA:ARBA00034020};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:29531,
CC Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12628,
CC Rhea:RHEA-COMP:12629, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58211, ChEBI:CHEBI:132516, ChEBI:CHEBI:132517;
CC EC=2.4.1.259; Evidence={ECO:0000256|ARBA:ARBA00033991};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU363075}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000256|ARBA:ARBA00007063, ECO:0000256|RuleBase:RU363075}.
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:EJS42088.1}.
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DR EMBL; ALIE01000166; EJS42088.1; -; Genomic_DNA.
DR AlphaFoldDB; J8PXM4; -.
DR HOGENOM; CLU_018152_1_1_1; -.
DR OrthoDB; 162888at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000006968; Chromosome XIV.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052926; F:dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052918; F:dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760:SF2; ALPHA-1,2-MANNOSYLTRANSFERASE ALG9; 1.
DR PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU363075};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363075};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW Reference proteome {ECO:0000313|Proteomes:UP000006968};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363075};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363075}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..555
FT /note="Mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003812598"
FT TRANSMEM 111..129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 136..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 173..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 211..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 265..286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 293..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
SQ SEQUENCE 555 AA; 63772 MW; 8D438BFF5A5D69B9 CRC64;
MNCKAVTICL LLLLFVTRVY IQPTFSLISD CDETFNYWEP LNLLVRGFGK QTWEYSPEYS
IRSWAFLLPF YTILYPINKF TELETHWNFF ITRACLGFFS FVMEFKLHRE IAGTLALQIA
NAWIIFQLFN PGWFHASVEL LPSAVAMLLY VGATTHSLRY LSTGSTSNFT KSLAYNFLAS
ILGWPFVLVL SVPLCLHYLF NHRIISTIRT AFDCCLIFSL TAFTVIATDS IFYGKLAPVS
WNILFYNVIN ANEETGPNIF GIEPWYYYPL NLILNFPLPV LILCTLGVFH LRLWPLWASL
FTWLAIFIQQ PHKEERFLYP IYSLITLSAS IAFYKVLSLF NKKSVLKKVV KLSVLLTVAV
QAMSRIVALV NNYTAPIAVY EQFSSLNQGS VNTPMVNVCT GREWYHFPTS FLLPDNHRLR
FVKSGFGGLL PGDFPENGSI FKKIRAIPKG MNNKNLYDAG KEWPIAKCDY FVDIVAPIDL
TKDVFNPLHL MDNWNKLACA AFIDTDSSKI FGRAFYVPES INQIMQTILP KQWNQVYGIH
YIDYCLFEKP TETIN
//
