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Database: UniProt
Entry: E3M0P5_CAERE
LinkDB: E3M0P5_CAERE
Original site: E3M0P5_CAERE 
ID   E3M0P5_CAERE            Unreviewed;       492 AA.
AC   E3M0P5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN   ORFNames=CRE_05469 {ECO:0000313|EMBL:EFO87966.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; DS268420; EFO87966.1; -; Genomic_DNA.
DR   RefSeq; XP_003110673.1; XM_003110625.1.
DR   AlphaFoldDB; E3M0P5; -.
DR   STRING; 31234.E3M0P5; -.
DR   EnsemblMetazoa; CRE05469.1; CRE05469.1; WBGene00052973.
DR   GeneID; 9825175; -.
DR   KEGG; crq:GCK72_018739; -.
DR   CTD; 9825175; -.
DR   eggNOG; KOG2516; Eukaryota.
DR   HOGENOM; CLU_008917_0_1_1; -.
DR   InParanoid; E3M0P5; -.
DR   OMA; WWVEVRM; -.
DR   OrthoDB; 122000at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
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, ECO:0000256|RuleBase:RU363075};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
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   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        140..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        169..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        199..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        255..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        283..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        308..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        341..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
SQ   SEQUENCE   492 AA;  57182 MW;  62D92F317837B8F0 CRC64;
     MEGTEWIVII VSLVHIILAP GTKVEESFNV QATHDLLFHL PTNLSNYDHS QFPGVVPRTF
     LGPIFLAALS SPMSFIFRFW AIPKMWQLLL IRSTLGLMNT MAFLYFARSV SRCFGRDTAM
     FLRIITCTQF HYIFYMSRPL PNSFALVLVM IVYERIFDGR YESAVRYATA CVILFRCELL
     LLFGPLFLGY MILGKLKTFG FDGAIAIGVR VASACLAISI PIDSYFWGRP VWPEGEVMFF
     NVVENRSHEY GTQHFLWYFY SALPRCLLTS LALIPLGCLV DRRIPQVLFP SVVFVFLYSF
     LPHKELRFII YVLPIFSLAA AVFCAKMFIN KWKSLFRTIL YFGVVMHLFA NILCTAMFLL
     VASKNYPGFD ALNYLQFQHR FDARKPVTVY IDNACAQTGV NRFLHSYDAW TYNKTENLKP
     EDLEHFDFLV LGTYGNTLKT EVETKFMKWH RPLFFVNSFH KFNIKHSKKF PYVYPEIVYT
     EKSAVLKNRN YR
//
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