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   27-MAR-2024, entry version 151.
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.C33G3.4.1; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   iPTMnet; Q93324; -.
DR   EPD; Q93324; -.
DR   PaxDb; 6239-C33G3-4; -.
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   AGR; WB:WBGene00007904; -.
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; QFACASY; -.
DR   OrthoDB; 2504097at2759; -.
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 cell types or 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; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF17753; Ig_mannosidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 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
//