EGCSE_CYANO
ID EGCSE_CYANO Reviewed; 503 AA.
AC Q9GV16; Q9GV15;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Endoglycoceramidase {ECO:0000312|EMBL:BAB16369.1};
DE Short=EGCase {ECO:0000303|PubMed:10882727};
DE EC=3.2.1.123;
DE AltName: Full=Glycosphingolipid-specific enzyme {ECO:0000303|PubMed:10882727};
DE Short=GSL-specific enzyme {ECO:0000303|PubMed:10882727};
DE Flags: Precursor;
OS Cyanea nozakii (Jellyfish).
OC Eukaryota; Metazoa; Cnidaria; Scyphozoa; Semaeostomeae; Cyaneidae; Cyanea.
OX NCBI_TaxID=135523;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB16369.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-42; 62-78; 230-251 AND
RP 299-318, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION AT ASN-72 AND ASN-307, AND
RP VARIANT PRO-172.
RC TISSUE=Tentacle {ECO:0000269|PubMed:10882727};
RX PubMed=10882727; DOI=10.1074/jbc.m003575200;
RA Horibata Y., Okino N., Ichinose S., Omori A., Ito M.;
RT "Purification, characterization, and cDNA cloning of a novel acidic
RT endoglycoceramidase from the jellyfish, Cyanea nozakii.";
RL J. Biol. Chem. 275:31297-31304(2000).
CC -!- FUNCTION: Hydrolysis of the glycosidic linkage between oligosaccharides
CC and ceramides of glycosphingolipids, especially b-series
CC polysialogangliosides. {ECO:0000269|PubMed:10882727}.
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:10882727};
CC -!- ACTIVITY REGULATION: Completely inhibited by Hg(2+). Cu(2+) and zinc
CC have no effect on enzyme activity. Lithium, potassium, manganese,
CC Ni(2+), calcium, magnesium and EDTA have no significant effect on
CC enzyme activity. Enzyme requires presence of detergents such as Triton
CC X-100 and Lubrol PX for the hydrolysis of glycosphingolipids.
CC Taurodeoxycholate strongly inhibits the enzyme activity and SDS
CC completely inhibits the enzyme activity. {ECO:0000269|PubMed:10882727}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.35 mM for GM1 {ECO:0000269|PubMed:10882727};
CC Vmax=4.4 uM/min/mg enzyme {ECO:0000269|PubMed:10882727};
CC pH dependence:
CC Optimum pH 3.0. Highly stable at acidic pH.
CC {ECO:0000269|PubMed:10882727};
CC -!- SUBCELLULAR LOCATION: Secreted. Nematocyst {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000255}.
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DR EMBL; AB047321; BAB16369.1; -; mRNA.
DR EMBL; AB047322; BAB16370.1; -; mRNA.
DR AlphaFoldDB; Q9GV16; -.
DR SMR; Q9GV16; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR iPTMnet; Q9GV16; -.
DR BRENDA; 3.2.1.123; 1767.
DR SABIO-RK; Q9GV16; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0047876; F:endoglycosylceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:1901136; P:carbohydrate derivative catabolic process; IEA:UniProt.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProt.
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; Direct protein sequencing;
KW Glycoprotein; Glycosidase; Hydrolase; Nematocyst;
KW Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..503
FT /note="Endoglycoceramidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390381"
FT ACT_SITE 239
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10882727"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10882727"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 172
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:10882727"
SQ SEQUENCE 503 AA; 57253 MW; 3383E64987E7B15A CRC64;
MAETQPLVFV LMSISAILTA GLPINDDASL LISVNPETQQ LVDSLGRERF FHGTNVVVKH
KPYHPSVEGY DNTSFSEVDM KILQDLGLNT IRLGMMLPGY VPTRGNYNET YLKIIQEIVS
KAAKYGIYTL LDMHQDVMSA KFCVEGFPDW AVNTGNADNF PFPLEDKYPL NLQTGYPYPK
DCAKHAWGDY YFTEAAAAAF QNFYNNTDGL LDAWADFWKK TAQGFKDYKS VIGYELINEP
FAGDIYRDPS LMIPGVADER NLAPAYDVIH KAIRTVDEQH SIFFEGVTWD YFAAGFSKVP
GGDAYRNRSV LSYHYYEPPD FNKKFQFEVR MEDLRRLKCG GFLTELLTVG DTAKDMSDML
ELFDICDQHK QSWMGWLYKS YGCYKQHLGC LTDSMHDETG HLRDIVLQNT TRTYPQAVAG
HTIGYKFDRI TKKFDLSFVV TADCRSTESI VYFNKDLHYS NGYDVTVFPK DSVTWKQVEK
KIIINHSQKL SAGTTVTFSL VAK
