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Database: UniProt
Entry: G2YNR1_BOTF4
LinkDB: G2YNR1_BOTF4
Original site: G2YNR1_BOTF4 
ID   G2YNR1_BOTF4            Unreviewed;       605 AA.
AC   G2YNR1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN   ORFNames=BofuT4P8000015001 {ECO:0000313|EMBL:CCD53259.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD53259.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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}.
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DR   EMBL; FQ790346; CCD53259.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2YNR1; -.
DR   STRING; 999810.G2YNR1; -.
DR   eggNOG; KOG2515; Eukaryota.
DR   HOGENOM; CLU_018152_0_0_1; -.
DR   InParanoid; G2YNR1; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008177; Unplaced contigs.
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:UP000008177};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCD53259.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363075};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363075}.
FT   TRANSMEM        32..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        143..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        168..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        198..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        241..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        302..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        367..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        406..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   605 AA;  68154 MW;  411F2CE23325CACF CRC64;
     MAPPQPTSLG SSRGAEASTA SHSKKKKPAT PFAVQPISAF YVFLGANILA ALYAPIQDCD
     ETFNYWEPTH YLSHHYGLQT WEYSPEYAIR SWLYVTLHAL MGNFRRLLPF PTKVGEFYFI
     RYCLAFICAL CQTQMFRVIN GTLNPRVAMF FMMANIFSPG FFHASASYLP SSFAMYTTML
     GMAAFMNWRG GLKTAQGIFW FAVGGILGWP FSMALSAPFL IEEVIFASLS DKDAVIDTVM
     RFVRGIVGGL LVLFSEFVVS GFFYRQLVIV PLNIVLYNIF SGEGRGPEIY GTEPWHFYIR
     NLILNFNIWF VLAISALPLF ILQKLFGSRE GGTTTALRSV VFMAPFYIWL AIFTFQPHKE
     ERFMYPAYPC LALNAAMSLH IVLAAFGHSD PKTLVGKIPA KLKLLFVSFF IIGSVDIGVA
     RIYGIYAAYS APLKIYSPLQ NGTLGARGDS VCFAKEWYRF PSSYHLPNGM KAKFVKSEFD
     GLLPGEFSEA STGFGIWSTW LIPSGMNDQN LEDMSKYVDL KTCNFLVDTY YPGSVASELE
     PHYIMDSENW ETVNCEPFLD ASRTHILART IWLPDLPFIP EKFRRNWGSH CLLKRAPKKA
     VVSSV
//
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