ID   EGCSE_HYDVU             Reviewed;         517 AA.
AC   Q6L6S1;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Endoglycoceramidase {ECO:0000312|EMBL:BAD20464.1};
DE            Short=EGCase {ECO:0000303|PubMed:15320336};
DE            EC=3.2.1.123;
DE   AltName: Full=Glycosphingolipid-specific enzyme {ECO:0000303|PubMed:15320336};
DE            Short=GSL-specific enzyme {ECO:0000303|PubMed:15320336};
DE   Flags: Precursor;
OS   Hydra vulgaris (Hydra) (Hydra attenuata).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC   Aplanulata; Hydridae; Hydra.
OX   NCBI_TaxID=6087;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAD20464.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=105 {ECO:0000269|PubMed:15320336};
RX   PubMed=15320336; DOI=10.1074/jbc.m401460200;
RA   Horibata Y., Sakaguchi K., Okino N., Iida H., Inagaki M., Fujisawa T.,
RA   Hama Y., Ito M.;
RT   "Unique catabolic pathway of glycosphingolipids in a hydrozoan, Hydra
RT   magnipapillata, involving endoglycoceramidase.";
RL   J. Biol. Chem. 279:33379-33389(2004).
CC   -!- FUNCTION: Hydrolysis of the glycosidic linkage between oligosaccharides
CC       and ceramides of glycosphingolipids, optimal substrates appear to be
CC       the glycosphingolipids with a gangliotetraose structure.
CC       {ECO:0000269|PubMed:15320336}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an oligoglycosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H2O
CC         = an N-acyl-sphingoid base + an oligoglycosyl-(1->4)-D-glucose;
CC         Xref=Rhea:RHEA:22288, ChEBI:CHEBI:15377, ChEBI:CHEBI:83273,
CC         ChEBI:CHEBI:136875, ChEBI:CHEBI:156536; EC=3.2.1.123;
CC         Evidence={ECO:0000269|PubMed:15320336};
CC   -!- ACTIVITY REGULATION: Cu(2+), zinc, manganese, calcium, magnesium and
CC       EDTA have no significant effects on enzyme activity. Enzyme requires
CC       presence of detergents such as Triton X-100 and Lubrol PX for the
CC       hydrolysis of glycosphingolipids. Taurodeoxycholate strongly inhibits
CC       the enzyme activity. {ECO:0000269|PubMed:15320336}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 3.0-4.0. Highly stable at acidic pH.
CC         {ECO:0000269|PubMed:15320336};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15320336}.
CC       Note=Released from digestive cells into the gastric cavity, and
CC       eventually into the surrounding medium, during the digestive process.
CC       {ECO:0000269|PubMed:15320336}.
CC   -!- TISSUE SPECIFICITY: Expressed uniformly in digestive cells, tentacles
CC       and peduncle regions suggesting expression in the endoderm throughout
CC       the whole body (at protein level). {ECO:0000269|PubMed:15320336}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000255}.
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DR   EMBL; AB179748; BAD20464.1; -; mRNA.
DR   AlphaFoldDB; Q6L6S1; -.
DR   SMR; Q6L6S1; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   BioCyc; MetaCyc:MON-18387; -.
DR   Proteomes; UP000694840; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0047876; F:endoglycosylceramidase activity; IDA:UniProtKB.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046479; P:glycosphingolipid catabolic process; IDA:UniProtKB.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR041036; GH5_C.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF18564; Glyco_hydro_5_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..517
FT                   /note="Endoglycoceramidase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000390382"
FT   ACT_SITE        230
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        380
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   517 AA;  59685 MW;  9042532367D263F4 CRC64;
     MISVALIILF LAKVISGKSD DFISVNPETN MLIDGYGRER FFHGTNVVVK HFPFHPETTG
     FNKDTFSEDD MKILQKFGLN SIRLGMMLPG YVPKREEYNE TYIKVIQSIV TTAAKYGIYT
     LLDMHQDVFS PKFCVEGMPD WIVNTQGAKD FPMPLHKPFN LDPKTGYPYP EDCAKFSWAD
     YYFTEAAGQA FQNLYDNVDG LRDEWAQFWK KTADVFKEEP SVIGYELINE PFCGNVFKHP
     TLLIPGVADY LNLQPTYDAL QKAIRQVDEE HNIFFEGVTW DFFEVGFTEV PGGKQYQNRS
     VLSYHYYEPP DFSKKLNFEA RLLDLKRLKC GGFLTEMFTV GTDFNSMFEM FDLCDKFKQS
     WHGWMYKSYG CIEQNLGCLN MSSPGKESIQ IANTSRTYPQ AVAGRTQSYA FDIKTKVFTL
     VYETVGSCKS GRTIVYFNKN LHYPNGYRYE INPNFKVTPS ENEYFLYLDE VNKVPNTVVT
     FKLFPLSFTD SEDIHPVTVM GDKHLSENHN ENEKKKK