GALC_DANRE
ID GALC_DANRE Reviewed; 660 AA.
AC Q5SNX7; Q5XJ01;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Galactocerebrosidase {ECO:0000250|UniProtKB:P54803};
DE Short=GALCERase;
DE EC=3.2.1.46 {ECO:0000250|UniProtKB:P54803};
DE AltName: Full=Galactosylceramidase;
DE Flags: Precursor;
GN Name=galc {ECO:0000250|UniProtKB:P54803}; Synonyms=galca;
GN ORFNames=si:ch211-199l3.4, zgc:92561;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes the galactose ester bonds of glycolipids such as
CC galactosylceramide and galactosylsphingosine.
CC {ECO:0000250|UniProtKB:P54803}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H2O = an
CC N-acylsphing-4-enine + D-galactose; Xref=Rhea:RHEA:14297,
CC ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:18390,
CC ChEBI:CHEBI:52639; EC=3.2.1.46;
CC Evidence={ECO:0000250|UniProtKB:P54803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14298;
CC Evidence={ECO:0000250|UniProtKB:P54803};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1<->1)-sphing-4-enine + H2O = D-galactose +
CC sphing-4-enine; Xref=Rhea:RHEA:43908, ChEBI:CHEBI:4139,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57756, ChEBI:CHEBI:57934;
CC Evidence={ECO:0000250|UniProtKB:P54803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43909;
CC Evidence={ECO:0000250|UniProtKB:P54803};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-galactosylceramide + H2O = an N-acyl-sphingoid base + D-
CC galactose; Xref=Rhea:RHEA:43412, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:36498, ChEBI:CHEBI:83273;
CC Evidence={ECO:0000250|UniProtKB:P54818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43413;
CC Evidence={ECO:0000250|UniProtKB:P54818};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 59 family. {ECO:0000305}.
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DR EMBL; AL953887; CAI11729.1; -; Genomic_DNA.
DR EMBL; BC083517; AAH83517.1; -; mRNA.
DR RefSeq; NP_001005921.1; NM_001005921.1.
DR AlphaFoldDB; Q5SNX7; -.
DR SMR; Q5SNX7; -.
DR STRING; 7955.ENSDARP00000053869; -.
DR CAZy; GH59; Glycoside Hydrolase Family 59.
DR PaxDb; Q5SNX7; -.
DR Ensembl; ENSDART00000053870; ENSDARP00000053869; ENSDARG00000037064.
DR GeneID; 449649; -.
DR KEGG; dre:449649; -.
DR CTD; 449649; -.
DR ZFIN; ZDB-GENE-040724-243; galca.
DR eggNOG; ENOG502QQ1Q; Eukaryota.
DR GeneTree; ENSGT00390000003303; -.
DR HOGENOM; CLU_015456_2_0_1; -.
DR InParanoid; Q5SNX7; -.
DR OMA; HEAWDEN; -.
DR OrthoDB; 364933at2759; -.
DR PhylomeDB; Q5SNX7; -.
DR TreeFam; TF312985; -.
DR PRO; PR:Q5SNX7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000037064; Expressed in intestine and 23 other tissues.
DR GO; GO:0005764; C:lysosome; IDA:ZFIN.
DR GO; GO:0004336; F:galactosylceramidase activity; IDA:ZFIN.
DR GO; GO:0006683; P:galactosylceramide catabolic process; ISS:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001286; Glyco_hydro_59.
DR InterPro; IPR035394; Glyco_hydro_59_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR15172; PTHR15172; 1.
DR Pfam; PF02057; Glyco_hydro_59; 1.
DR Pfam; PF17387; Glyco_hydro_59M; 1.
DR PRINTS; PR00850; GLHYDRLASE59.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lysosome; Reference proteome; Signal;
KW Sphingolipid metabolism.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..660
FT /note="Galactocerebrosidase"
FT /id="PRO_0000370713"
FT ACT_SITE 176
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 251
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 264..371
FT /evidence="ECO:0000250"
FT CONFLICT 11
FT /note="S -> F (in Ref. 2; AAH83517)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> V (in Ref. 2; AAH83517)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="K -> R (in Ref. 2; AAH83517)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="T -> I (in Ref. 2; AAH83517)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="R -> G (in Ref. 2; AAH83517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 73820 MW; AC70CBB2903A9B77 CRC64;
MQTHNFLCII SVILGCSAQF YVIDDRIGLG REFDGIGGLS GGGATSRLLV NYEEPYRSQI
LDYLFKPNFG ASLHILKVEI GGDAQTTDGT EPSHMHSKDE GNFFRGYEWW LMKEAKKRNP
NIKLIGLPWA FPGWVGYGTQ WPYFFPNVTA NYVITWVMGA KQHHNLDIDY IGIWNEKAFD
PTYIKVLRDA LDRAGFTNIG IIAADGDWSI ASAMLDDPYL NDAVEVIGVH YPGTNTVKEA
LLTERKLWSS EDYSTYNDDI GAGCWARILN QNYVNGKMTS TISWNVIASY YENLSFGRDG
LMTAEEPWSG HYIVESPIWM TAHTTQFTQP GWFYLQTVGK LNHGGSYVAL TDRKGNLTII
IETMTHEHSQ CIRPPLPHFD VSPQIATFEL KGSFAHLADL QVWYSKLDFK SGNGTLFKQL
RPIRAHNGLL SLKLDVDEVF TITTVTTAQR GFYPEPPKSC PFPKNYTDDF TIDNPPFSEA
PYFADQTGVF EYFRNTTDNS SHAFTLRQVV TERPVAWAKD ADQTISIIGD YSWSDVNVSC
DVFIETPKTG GVFLAARVDQ GGESVRQAKG VFYWIYANGT YRVTNDIGGK RVLAEGLSGT
KAGVWYTLTL SVKGYFATGS LNGFPLWKNA AVLEPKSGWA ALGTLSFEYA QFDNFNVIAG
