ALG12_CAEEL
ID ALG12_CAEEL Reviewed; 492 AA.
AC Q23361;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase;
DE EC=2.4.1.260 {ECO:0000250|UniProtKB:P53730};
DE AltName: Full=Asparagine-linked glycosylation protein 12 homolog;
DE AltName: Full=Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase;
DE AltName: Full=Mannosyltransferase ALG12 homolog;
GN Name=algn-12 {ECO:0000312|WormBase:ZC513.5};
GN ORFNames=ZC513.5 {ECO:0000312|WormBase:ZC513.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-413, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
CC -!- FUNCTION: Adds the eighth mannose residue in an alpha-1,6 linkage onto
CC the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2))
CC required for protein glycosylation. {ECO:0000250|UniProtKB:P53730}.
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:0000250|UniProtKB:P53730};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P53730}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P53730}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P53730}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000305}.
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DR EMBL; BX284605; CCD64068.1; -; Genomic_DNA.
DR PIR; T28996; T28996.
DR RefSeq; NP_505071.1; NM_072670.3.
DR AlphaFoldDB; Q23361; -.
DR STRING; 6239.ZC513.5; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR iPTMnet; Q23361; -.
DR EPD; Q23361; -.
DR PaxDb; Q23361; -.
DR PeptideAtlas; Q23361; -.
DR EnsemblMetazoa; ZC513.5.1; ZC513.5.1; WBGene00022629.
DR GeneID; 179185; -.
DR KEGG; cel:CELE_ZC513.5; -.
DR UCSC; ZC513.5; c. elegans.
DR CTD; 179185; -.
DR WormBase; ZC513.5; CE29152; WBGene00022629; algn-12.
DR eggNOG; KOG2516; Eukaryota.
DR GeneTree; ENSGT00950000183090; -.
DR HOGENOM; CLU_008917_0_1_1; -.
DR InParanoid; Q23361; -.
DR OMA; FTQYDHH; -.
DR OrthoDB; 330169at2759; -.
DR PhylomeDB; Q23361; -.
DR Reactome; R-CEL-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q23361; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00022629; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:InterPro.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052917; F:dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR039485; ALG12.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR PANTHER; PTHR22760:SF1; PTHR22760:SF1; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..492
FT /note="Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-
FT mannosyltransferase"
FT /id="PRO_0000215783"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633"
SQ SEQUENCE 492 AA; 57150 MW; 73BC4F72ADA6B643 CRC64;
MEGTEWIVII VTIIHIILAP GTKVEESFNV QATHDLMFHL PTNLSNYDHS QFPGVVPRTF
IGPISLAILS SPMSFIFRFW AIPKMWQLLL IRATLGLMNA MAFLYFARSV NRKFGRETAM
YLRLIMCTQF HYIFYMSRPL PNTFALILVM IVFERLLEGR YESAVRYATA SVILFRCELV
LLYGPIFLGY MISGRLKVFG FDGAIAIGVR IAAMCLAVSI PIDSYFWGRP LWPEGEVMFF
NVVENRSHEY GTQPFLWYFY SALPRCLLTT TLLVPLGLLV DRRLPQIVLP SVIFIFLYSF
LPHKELRFII YVLPIFCLSA AVFCARMLIN RHKSFFRMIL FFGVILHLLA NVLCTGMFLL
VASKNYPGFD ALNYLQFQNR FDAKKPVTVY IDNACAQTGV NRFLHINDAW TYNKTENLKP
ADLENFDFLV LGTYGNTLKT EVESKFVTWH RPLFFVNSFH QYKIKKSRQF PWIYPEIIYT
EKAVVLKNRN YK
