ALG11_CAEEL
ID ALG11_CAEEL Reviewed; 470 AA.
AC P53993;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase {ECO:0000250|UniProtKB:Q2TAA5};
DE EC=2.4.1.131 {ECO:0000250|UniProtKB:Q2TAA5};
DE AltName: Full=Asparagine-linked glycosylation protein 11 homolog {ECO:0000312|WormBase:B0361.8};
GN Name=algn-11 {ECO:0000312|WormBase:B0361.8};
GN ORFNames=B0361.8 {ECO:0000312|WormBase:B0361.8};
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).
CC -!- FUNCTION: Mannosyltransferase involved in the last steps of the
CC synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the
CC cytoplasmic face of the endoplasmic reticulum. Catalyzes the addition
CC of the 4th and 5th mannose residues to the dolichol-linked
CC oligosaccharide chain. {ECO:0000250|UniProtKB:Q2TAA5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-
CC D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523,
CC Rhea:RHEA-COMP:12626, Rhea:RHEA-COMP:12627, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511,
CC ChEBI:CHEBI:132515; EC=2.4.1.131;
CC Evidence={ECO:0000250|UniProtKB:Q2TAA5};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q2TAA5}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q2TAA5}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; FO080185; CCD61823.1; -; Genomic_DNA.
DR RefSeq; NP_498606.1; NM_066205.4.
DR AlphaFoldDB; P53993; -.
DR SMR; P53993; -.
DR STRING; 6239.B0361.8; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EPD; P53993; -.
DR PaxDb; P53993; -.
DR PeptideAtlas; P53993; -.
DR EnsemblMetazoa; B0361.8.1; B0361.8.1; WBGene00015162.
DR GeneID; 176032; -.
DR KEGG; cel:CELE_B0361.8; -.
DR UCSC; B0361.8.1; c. elegans.
DR CTD; 176032; -.
DR WormBase; B0361.8; CE26792; WBGene00015162; algn-11.
DR eggNOG; KOG1387; Eukaryota.
DR GeneTree; ENSGT00550000075118; -.
DR HOGENOM; CLU_017896_1_1_1; -.
DR InParanoid; P53993; -.
DR OMA; RFNIHLH; -.
DR OrthoDB; 1051021at2759; -.
DR PhylomeDB; P53993; -.
DR PRO; PR:P53993; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015162; Expressed in germ line (C elegans) and 4 other tissues.
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:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd03806; GT4_ALG11-like; 1.
DR InterPro; IPR038013; ALG11.
DR InterPro; IPR031814; ALG11_N.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR45919; PTHR45919; 1.
DR Pfam; PF15924; ALG11_N; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..470
FT /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-
FT mannosyltransferase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000080281"
FT TOPO_DOM 1..15
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..470
FT /note="Lumenal"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 53647 MW; 7C5D9C4556F63E8A CRC64;
MSDTVISLIS HSITTVFYLV PLIIALIIPF SLYSGFRRKS KTVAFFHPYC NAGGGGERVL
WAAIRTMQKK FPDHKYFVYS GDTDATKEQI LLKARQRFGI ELDPSNIQFI YLHWRTLVEA
RHYKHCTMLF QALAGLILAL EAWFRMVPAV FIDSMGYPLS LPAFRLSGSK VVAYVHYPTI
SCDMLDVVES RQETFNNSST IAQSNVLSWG KLTYYRLFAC LYWLAGKAAH VGMVNGSWTQ
RHITSIWSRR DVSIVYPPCD VEAFLNIESV AESLLEDTKT VRLLSVGQIR PEKNHKLQLE
VLHDVKEPLE KMGYNVELCI AGGCRNEEDQ ERVKMLKNEA EKLDISEQLI WQLNVPYEDL
VVELSKALIS IHTMHNEHFG ISVVEAMAAS TIILSNDSGG PRMDIVKDYE GHCVGYLSIT
KEEYVETILK IVEEGLKKRN DTRKYARKSL TRFGEAAFET HWNKEIEKVL
