EGCR1_CRYNH
ID EGCR1_CRYNH Reviewed; 742 AA.
AC H1AE12; J9VH96;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Glucosylceramidase {ECO:0000303|PubMed:22072709};
DE EC=3.2.1.45 {ECO:0000269|PubMed:22072709};
DE AltName: Full=Endoglycoceramidase-related protein 1 {ECO:0000303|PubMed:22072709};
DE Short=EGCrP1 {ECO:0000303|PubMed:22072709};
DE AltName: Full=Glucocerebrosidase {ECO:0000303|PubMed:22072709};
GN Name=EGC1 {ECO:0000303|PubMed:22072709};
GN ORFNames=CNAG_00623 {ECO:0000312|EMBL:AFR92751.2};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000312|Proteomes:UP000010091};
RN [1] {ECO:0000312|EMBL:BAL46040.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000312|EMBL:BAL46040.1};
RX PubMed=22072709; DOI=10.1074/jbc.m111.311340;
RA Ishibashi Y., Ikeda K., Sakaguchi K., Okino N., Taguchi R., Ito M.;
RT "Quality control of fungus-specific glucosylceramide in Cryptococcus
RT neoformans by endoglycoceramidase-related protein 1 (EGCrP1).";
RL J. Biol. Chem. 287:368-381(2012).
RN [2] {ECO:0000312|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
CC -!- FUNCTION: Specifically hydrolyzes the glucosidic linkage in
CC glucosylceramide (PubMed:22072709). May prevent accumulation of
CC aberrent glucosylceramide containing immature ceramide
CC (PubMed:22072709). {ECO:0000269|PubMed:22072709}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-
CC acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269,
CC ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801,
CC ChEBI:CHEBI:52639; EC=3.2.1.45;
CC Evidence={ECO:0000269|PubMed:22072709};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13270;
CC Evidence={ECO:0000269|PubMed:22072709};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:22072709};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:22072709}; Single-
CC pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Decreases membrane glucosylceramidase activity at
CC neutral pH (PubMed:22072709). Increases cellular glucosylceramide
CC levels; levels of normal glucosylceramide containing mature ceramide
CC and abnormal glucosylceramide containing immature ceramide are both
CC increased (PubMed:22072709). Decreases capsule size during growth in
CC capsule-inducing conditions (PubMed:22072709).
CC {ECO:0000269|PubMed:22072709}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFR92751.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB669191; BAL46040.1; -; mRNA.
DR EMBL; CP003820; AFR92751.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_012046368.1; XM_012190978.1.
DR AlphaFoldDB; H1AE12; -.
DR SMR; H1AE12; -.
DR EnsemblFungi; AFR92751; AFR92751; CNAG_00623.
DR GeneID; 23884409; -.
DR VEuPathDB; FungiDB:CNAG_00623; -.
DR HOGENOM; CLU_009024_1_0_1; -.
DR BRENDA; 3.2.1.62; 1723.
DR Proteomes; UP000010091; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004348; F:glucosylceramidase activity; IDA:UniProtKB.
DR GO; GO:0043094; P:cellular metabolic compound salvage; IMP:UniProtKB.
DR GO; GO:0006680; P:glucosylceramide catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR041036; GH5_C.
DR InterPro; IPR001547; Glyco_hydro_5.
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.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..742
FT /note="Glucosylceramidase"
FT /id="PRO_0000451755"
FT TRANSMEM 701..721
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 258
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT ACT_SITE 492
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 742 AA; 83552 MW; 4F4F488B2B27FDAF CRC64;
MSGIQFDVSR LCAATISIQG RHFVDSHGRV LHLRGANVSA ASKVPATPAP KIHDHAQASY
VGRPFRLEEA DEHWARLKSW GLTFVRITVT WEALEHKERG VYDEDYLAYL RALLQSMEPY
GLVAYIALHQ DVWSRYCGGS GAPGWTLEAA GFDLSNEGEN LSLSGAAFLD GIKSGRLAGE
RGLWPTGYQK LAAATMNTLF WGGETFAPLL KVPGQIDGKW VSRNIQVYLQ EAFLAATAKL
VKAVGDLETV MGFELMNEPH PGFIGIQSIH EWDYTTDLHL GQFPSPLQSF SMGAGHPTPN
VPVYTRSFPF PTRVTSHVTA NPEGACAWAS KECPWEKHGV WRWSEAKQEA AALQQDYFVK
NRDGGKVDFY EDFYFPFVRK WEQVIGENIS STKGLKARMV EAIPNELCPE WKEESRPKNM
VYAPHWYDLN TLFKKKFGFM SVNVQGLARG MFILRALYFG TAAAKANYAL QIKTIVLAAR
LKLGPVPVIF GECGVPMDIN NEEAFRTGDW KWQERSMDAL ISAMEGALMG FNLWTYNPAN
RDDIGDDWNA ENFSWYSESN RTKLLKNAEK SSDGLDVGAR LLNVIVRPYP IATAGNPTSL
AYDANACAFT YRFRSPLRVS AAAPTPEEYT EIFLPRRVFR KESTEWTVTA GGKVHVDWER
ERVFVWFEDS SLTAASIKDD TRPRRIDIWV IGRKVEENWS IAQILVAVVI LLLGVLVAYY
AQLYEWEKDK MIFQHLREAN GM
