MANBA_CAEEL
ID MANBA_CAEEL Reviewed; 900 AA.
AC Q93324;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable beta-mannosidase;
DE EC=3.2.1.25;
DE AltName: Full=Mannanase;
DE Short=Mannase;
DE Flags: Precursor;
GN ORFNames=C33G3.4;
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-131 AND ASN-477, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC in beta-D-mannosides.; EC=3.2.1.25;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR EMBL; Z78540; CAB01737.1; -; Genomic_DNA.
DR PIR; T19689; T19689.
DR RefSeq; NP_510342.1; NM_077941.5.
DR AlphaFoldDB; Q93324; -.
DR SMR; Q93324; -.
DR STRING; 6239.C33G3.4; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR iPTMnet; Q93324; -.
DR EPD; Q93324; -.
DR PaxDb; Q93324; -.
DR PeptideAtlas; Q93324; -.
DR EnsemblMetazoa; C33G3.4.1; C33G3.4.1; WBGene00007904.
DR GeneID; 181517; -.
DR KEGG; cel:CELE_C33G3.4; -.
DR UCSC; C33G3.4; c. elegans.
DR CTD; 181517; -.
DR WormBase; C33G3.4; CE08560; WBGene00007904; -.
DR eggNOG; KOG2230; Eukaryota.
DR GeneTree; ENSGT00390000001670; -.
DR HOGENOM; CLU_005015_3_1_1; -.
DR InParanoid; Q93324; -.
DR OMA; PFWNYTT; -.
DR OrthoDB; 517710at2759; -.
DR PhylomeDB; Q93324; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8853383; Lysosomal oligosaccharide catabolism.
DR PRO; PR:Q93324; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00007904; Expressed in embryo and 3 other tissues.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004567; F:beta-mannosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR041625; Beta-mannosidase_Ig.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF17753; Ig_mannosidase; 1.
DR SUPFAM; SSF49303; SSF49303; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Lysosome; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..900
FT /note="Probable beta-mannosidase"
FT /id="PRO_0000012167"
FT ACT_SITE 463
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 900 AA; 103978 MW; C6B90C25517579C7 CRC64;
MRTSLVVCLF WLLFQLHTTH GYNTLVNLAG NWEFSSSNKT VNGTGTVPGD IYSDLYASGI
IDNPLFGENH LNLKWIAEDD WTYSRKFRLI DLDDTVGAFL EIESVDTIAT VYVNGQKVLH
SRNQFLPYHV NVTDIIALGE NDITIKFKSS VKYAEKRADE YKKIFGHSLP PDCNPDIYHG
ECHQNFIRKA QYSFAWDWGP SFPTVGIPST ITINIYRGQY FHDFNWKTRF AHGKWKVAFE
FDTFHYGART IEYSVQIPEL GIKESDYYRL SATKSLQTRS KNIMSLSIPM EHEPERWWPN
GMGEQKLYDV VVSMGGQVKE KKIGFKTVEL VQDLIDPKKP EKGRNFYFKI NDEPVFLKGT
NWIPVSMFRS DRENIAKTEF LLDSVAEVGM NAIRVWGGGF YESNHFYYYA SKKGILVWQD
LMFACALYPT TEEFIQNAEE EVSYNVDRIS QHTSVIVFSG NNENEAAIRG HWWKASNYTE
SQQVKDYVLL YQRLAKIAKK VAPTIPFIMS SPSNGVETEE EGGVSKNPYD VRYGDIHYYN
EFVNLWRDDT YLTPRCASEY GVQSYPMKET MLNWINESDW EYTSKAMFHR QHHPGGIATN
LLMIFQHLPI PAECGSKSVS DVPSCKYISS ASYMSRLAYF SQVHQSIALK TQTLHYRRFR
NTTTNEGLGN TMCAMYWQLN DVWAAPTWST IDFEQNWKMA HYEARRFFSN VAVYSFADET
DFNLKVFLLN DNPYLLHNIT VNVQMLSWGN GLDPILTNEF HIDSVPAGSS EVLKTGITFS
KITELSEYLY VSTLYDSSGV KIHEDVLVPD FLFEVDFNTF GDVQISDVQR IDEKTYDLTI
TTDRVSPFTW ITCKKPFTGW FSDNGFHMIQ RLRKIRLIAK FEVDLEKSDF TVCNLKNCYV
