ALG9_CAEEL
ID ALG9_CAEEL Reviewed; 603 AA.
AC P54002;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Alpha-1,2-mannosyltransferase algn-9 {ECO:0000250|UniProtKB:Q9H6U8};
DE EC=2.4.1.259 {ECO:0000250|UniProtKB:Q9H6U8};
DE EC=2.4.1.261 {ECO:0000250|UniProtKB:Q9H6U8};
DE AltName: Full=Asparagine-linked glycosylation protein 9 homolog {ECO:0000312|WormBase:C14A4.3};
DE AltName: Full=Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase {ECO:0000250|UniProtKB:Q9H6U8};
DE AltName: Full=Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase {ECO:0000250|UniProtKB:Q9H6U8};
GN Name=algn-9 {ECO:0000312|WormBase:C14A4.3};
GN ORFNames=C14A4.3 {ECO:0000312|WormBase:C14A4.3};
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-443, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Catalyzes the transfer of mannose from Dol-P-Man to lipid-
CC linked oligosaccharides. {ECO:0000250|UniProtKB:Q9H6U8}.
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:0000250|UniProtKB:Q9H6U8};
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:0000250|UniProtKB:Q9H6U8};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9H6U8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9H6U8}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000305}.
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DR EMBL; BX284602; CAA90107.2; -; Genomic_DNA.
DR PIR; T19245; T19245.
DR RefSeq; NP_496282.2; NM_063881.4.
DR AlphaFoldDB; P54002; -.
DR STRING; 6239.C14A4.3; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR iPTMnet; P54002; -.
DR EPD; P54002; -.
DR PaxDb; P54002; -.
DR PeptideAtlas; P54002; -.
DR EnsemblMetazoa; C14A4.3.1; C14A4.3.1; WBGene00007556.
DR GeneID; 174633; -.
DR KEGG; cel:CELE_C14A4.3; -.
DR UCSC; C14A4.3; c. elegans.
DR CTD; 174633; -.
DR WormBase; C14A4.3; CE32796; WBGene00007556; algn-9.
DR eggNOG; KOG2515; Eukaryota.
DR GeneTree; ENSGT00950000183090; -.
DR HOGENOM; CLU_018152_1_1_1; -.
DR InParanoid; P54002; -.
DR OMA; GKDWHRY; -.
DR OrthoDB; 1396421at2759; -.
DR PhylomeDB; P54002; -.
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:P54002; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007556; Expressed in pharyngeal muscle cell (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:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
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:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR039484; ALG9-like.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR PANTHER; PTHR22760:SF2; PTHR22760:SF2; 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..603
FT /note="Alpha-1,2-mannosyltransferase algn-9"
FT /id="PRO_0000215791"
FT TOPO_DOM 1..108
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..166
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..218
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..310
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..370
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..603
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
SQ SEQUENCE 603 AA; 68912 MW; 6AFDD9F995CEC0C5 CRC64;
MVTHRRKGGS GPPQKPPPRI VDRSSFDADK KKIKVEKLYH KANNPDNDWP FSFGSVFKML
LSIRISGAIW GIINDCDEVY NYWEPLHLFL YGEGFQTWEY SPVYAIRSYF YIYLHYIPAS
LFANLFGDTK IVVFTLIRLT IGLFCLLGEY YAFDAICKKI NIATGRFFIL FSIFSSGMFL
ASTAFVPSSF CMAITFYILG AYLNENWTAG IFCVAFSTMV GWPFSAVLGL PIVADMLLLK
GLRIRFILTS LVIGLCIGGV QVITDSHYFG KTVLAPLNIF LYNVVSGPGP SLYGEEPLSF
YIKNLFNNWN IVIFAAPFGF PLSLAYFTKV WMSQDRNVAL YQRFAPIILL AVTTAAWLLI
FGSQAHKEER FLFPIYPFIA FFAALALDAT NRLCLKKLGM DNILSILFIL CFAILSASRT
YSIHNNYGSH VEIYRSLNAE LTNRTNFKNF HDPIRVCVGK EWHRFPSSFF IPQTVSDGKK
VEMRFIQSEF RGLLPKPFLK SDKLVEVTRH IPTEMNNLNQ EEISRYVDLD SCDYVVDVDM
PQSDREPDFR KMEDNWKPVD SLPFIDVSKS TGFHGLLRAF YVPFLSAKHN VMTTCTLYRK
SNL
