GenomeNet

Database: UniProt
Entry: A0A183WCM6_TRIRE
LinkDB: A0A183WCM6_TRIRE
Original site: A0A183WCM6_TRIRE 
ID   A0A183WCM6_TRIRE        Unreviewed;       147 AA.
AC   A0A183WCM6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
OS   Trichobilharzia regenti (Nasal bird schistosome).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Trichobilharzia.
OX   NCBI_TaxID=157069 {ECO:0000313|WBParaSite:TRE_0001049201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TRE_0001049201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
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)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC         (1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate +
CC         alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC         Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-
CC         (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC         diphosphodolichol + H(+); Xref=Rhea:RHEA:29535, Rhea:RHEA-COMP:9517,
CC         Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12629, Rhea:RHEA-COMP:12630,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC         ChEBI:CHEBI:132517, ChEBI:CHEBI:132519; EC=2.4.1.260;
CC         Evidence={ECO:0000256|ARBA:ARBA00034044};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU363075}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU363075}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC       {ECO:0000256|ARBA:ARBA00007063, ECO:0000256|RuleBase:RU363075}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A183WCM6; -.
DR   STRING; 157069.A0A183WCM6; -.
DR   WBParaSite; TRE_0001049201-mRNA-1; TRE_0001049201-mRNA-1; TRE_0001049201.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052917; F:dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR005599; GPI_mannosylTrfase.
DR   PANTHER; PTHR22760:SF1; DOL-P-MAN:MAN(7)GLCNAC(2)-PP-DOL ALPHA-1,6-MANNOSYLTRANSFERASE; 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}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..147
FT                   /note="Mannosyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008155555"
SQ   SEQUENCE   147 AA;  16520 MW;  05AE25061273066E CRC64;
     LLISWVLLTI LSLKTFANSV KKVFGKHVCA RFLVICCSQF HFSFYASRTL PNSFANILVL
     YSLGQLINGN QAAFLVSAGV SVLVFRSELI LLFGPCLLYA LFTGRVSCSV LIDSYFWGRL
     IWPELEVFYF NTILNKSGQW GVSFCPL
//
DBGET integrated database retrieval system