MAN12_CAEEL
ID MAN12_CAEEL Reviewed; 590 AA.
AC Q18788; E1B6T6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Mannosyl-oligosaccharide 1,2-alpha-mannosidase C52E4.5;
DE EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906};
DE AltName: Full=Processing alpha-1,2-mannosidase C52E4.5;
DE Short=Alpha-1,2-mannosidase C52E4.5;
GN ORFNames=C52E4.5;
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], AND ALTERNATIVE SPLICING.
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-373, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156; ASN-373 AND ASN-402, AND
RP IDENTIFICATION BY MASS 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: Involved in the maturation of Asn-linked oligosaccharides.
CC Progressively trim alpha-1,2-linked mannose residues from
CC Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2) (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 H2O + N(4)-(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)-L-asparaginyl-[protein] (N-
CC glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-
CC (alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-
CC asparaginyl-[protein] (N-glucan mannose isomer 5A1,2);
CC Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087,
CC ChEBI:CHEBI:139493; EC=3.2.1.113;
CC Evidence={ECO:0000250|UniProtKB:P32906};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer
CC 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[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)-beta-D-GlcNAc)-L-asparaginyl-[protein]
CC (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-
CC COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628;
CC EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P45700};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P32906}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q18788-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q18788-2; Sequence=VSP_044102;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR EMBL; Z78012; CAB01415.1; -; Genomic_DNA.
DR EMBL; Z78012; CBW48349.1; -; Genomic_DNA.
DR PIR; T20153; T20153.
DR RefSeq; NP_001256388.1; NM_001269459.1.
DR RefSeq; NP_001256389.1; NM_001269460.1. [Q18788-1]
DR AlphaFoldDB; Q18788; -.
DR SMR; Q18788; -.
DR BioGRID; 44666; 1.
DR IntAct; Q18788; 1.
DR MINT; Q18788; -.
DR STRING; 6239.C52E4.5b; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR iPTMnet; Q18788; -.
DR EPD; Q18788; -.
DR PaxDb; Q18788; -.
DR PeptideAtlas; Q18788; -.
DR PRIDE; Q18788; -.
DR EnsemblMetazoa; C52E4.5.1; C52E4.5.1; WBGene00008258. [Q18788-1]
DR GeneID; 179642; -.
DR KEGG; cel:CELE_C52E4.5; -.
DR UCSC; C52E4.5; c. elegans. [Q18788-1]
DR CTD; 179642; -.
DR WormBase; C52E4.5a; CE08947; WBGene00008258; -.
DR WormBase; C52E4.5b; CE45297; WBGene00008258; -.
DR eggNOG; KOG2204; Eukaryota.
DR GeneTree; ENSGT00940000167910; -.
DR HOGENOM; CLU_003818_3_2_1; -.
DR InParanoid; Q18788; -.
DR OMA; CESFWMA; -.
DR OrthoDB; 693882at2759; -.
DR PhylomeDB; Q18788; -.
DR Reactome; R-CEL-964827; Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q18788; -.
DR Proteomes; UP000001940; Chromosome V.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001382; Glyco_hydro_47.
DR InterPro; IPR036026; Seven-hairpin_glycosidases.
DR Pfam; PF01532; Glyco_hydro_47; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF48225; SSF48225; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..590
FT /note="Mannosyl-oligosaccharide 1,2-alpha-mannosidase
FT C52E4.5"
FT /id="PRO_0000248514"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..590
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 88..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 470
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 423..456
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT VAR_SEQ 1
FT /note="M -> MIDVSSSITNMNVTIVESFLDFFKILAYVSKFSSWKEPNKTTFPHAM
FT (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_044102"
SQ SEQUENCE 590 AA; 66950 MW; B0714A3671204843 CRC64;
MKTVRFNKQA LAILAACFIF LLCVVCYFSA SSESHNAVVV GERARGHIAV RDVENRHLAE
EKHAVIHAKT VGKIERVVSQ EKVEILRPAR VESKPPGEKT STEPEETGVG KAPIQTSEGL
EKLIGKIHYE NKDEENDLRR QKVKEMMIHA WEGYKNYSWG ANELRPMSKK PNSQNIFGGS
QMPATIVDAA DTLFIMDLKD KYKEARDYIE NNFSMAKSTS TLSVFETTIR FLGGLLSLYA
LTQESFYIEK AREVGEALLP AFNTPSGIPK SNLDVASKHA SNYGWANGGQ SILSEIGSLH
LEFLYLSRIS NAPIFEKKVK KVRDALEKAE KPNGLYSNYI NPDTGKFTGS HMSLGALGDS
FYEYLIKSYV QSNYTDTQAK NMYWDVSDAI QKHMIKVSKQ SNLTYTVELN NGQAQHKMGH
LACFVPGMFA LQAINEDTEE EKLRIMTLAE ELAKTCHESY IRSETHIGPE MFYFNERDEA
TSKHSENGYI QRPEVIEGWF YLWRLTGKTM YRDWVWDAVQ AIEKYCRVDS GFTGLQNVYN
PKAGREDVMQ SFFLAEFLKY AYLTFADESL ISLDKWVFNT EAHPVPVLTN
