GLCM1_CAEEL
ID GLCM1_CAEEL Reviewed; 523 AA.
AC O16580; A8DZ32;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative glucosylceramidase 1;
DE EC=3.2.1.45;
DE Flags: Precursor;
GN Name=gba-1; ORFNames=C33C12.3;
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], AND ALTERNATIVE SPLICING.
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-168, AND IDENTIFICATION BY MASS
RP 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=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 -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=O16580-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O16580-2; Sequence=VSP_045724;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family. {ECO:0000305}.
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DR EMBL; FO080754; CCD66449.1; -; Genomic_DNA.
DR EMBL; FO080754; CCD66450.1; -; Genomic_DNA.
DR PIR; T31964; T31964.
DR RefSeq; NP_001040750.1; NM_001047285.2. [O16580-1]
DR RefSeq; NP_001040751.1; NM_001047286.1. [O16580-2]
DR AlphaFoldDB; O16580; -.
DR SMR; O16580; -.
DR BioGRID; 38942; 7.
DR DIP; DIP-24530N; -.
DR STRING; 6239.C33C12.3a; -.
DR CAZy; GH30; Glycoside Hydrolase Family 30.
DR iPTMnet; O16580; -.
DR EPD; O16580; -.
DR PaxDb; O16580; -.
DR PeptideAtlas; O16580; -.
DR EnsemblMetazoa; C33C12.3a.1; C33C12.3a.1; WBGene00016335. [O16580-1]
DR EnsemblMetazoa; C33C12.3b.1; C33C12.3b.1; WBGene00016335. [O16580-2]
DR GeneID; 173574; -.
DR KEGG; cel:CELE_C33C12.3; -.
DR UCSC; C33C12.3a; c. elegans.
DR CTD; 173574; -.
DR WormBase; C33C12.3a; CE29208; WBGene00016335; gba-1. [O16580-1]
DR WormBase; C33C12.3b; CE39682; WBGene00016335; gba-1. [O16580-2]
DR eggNOG; KOG2566; Eukaryota.
DR GeneTree; ENSGT00390000009464; -.
DR InParanoid; O16580; -.
DR OMA; QWKIPYI; -.
DR OrthoDB; 644299at2759; -.
DR PhylomeDB; O16580; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:O16580; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016335; Expressed in larva and 2 other tissues.
DR GO; GO:0004348; F:glucosylceramidase activity; IBA:GO_Central.
DR GO; GO:0006680; P:glucosylceramide catabolic process; IBA:GO_Central.
DR InterPro; IPR033452; GH30_C.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11069; PTHR11069; 1.
DR Pfam; PF02055; Glyco_hydro_30; 1.
DR Pfam; PF17189; Glyco_hydro_30C; 1.
DR PRINTS; PR00843; GLHYDRLASE30.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Hydrolase; Lipid metabolism;
KW Reference proteome; Signal; Sphingolipid metabolism.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..523
FT /note="Putative glucosylceramidase 1"
FT /id="PRO_0000421453"
FT ACT_SITE 358
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_045724"
SQ SEQUENCE 523 AA; 58167 MW; 428C0B2E6AE7AAD2 CRC64;
MKSRFLLKIF IFLAVFGVDS VRAADCTEKT FKTGTVCVCS LDSCDEIPPL DITMGQAALY
TTSHTGARLH RDVIYATDTE PFGTLHMTID SSKKYQTIQG FGSTFSDASG ANLKSLPDKL
SDLIMKQYFS DTGLNLQFGR VPIASTDFSG RVYSYNDVAN DYSMQNFNLT KEDFQWKIPY
IKNAQKYNPN LKLFAAPWAA PGWLKTTKEM TGPGALNGKA GDNYHQAYAK YFVRFLEEYG
KSGISFWGLS TQNQPTLGSD KKNKIQSTLF TAETQRDFIK TDLGPALAAS SSGKDVKLLI
LDDNRGNLPK WADTVLNDMD AAKYVGGIGV HAYQDGETDN HLDETHKKHP NFFILGTEAS
EGYGSKDTHV DYGNWDRAAD TASDILDNMN NWMTGWTERN LILDALGGPS WVSDYTDAPV
IAFPAMAQFY KQPMFYAIAH FSHFIKPGAV RIDHSLNVIE LEVETTAFLN PDGSKVIVML
NKGSLVSTEH TVVVQDAADS RNHYHFTLPH RAITTLYIQT SQF
