GALC_SALSA
ID GALC_SALSA Reviewed; 666 AA.
AC B5X3C1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 46.
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};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
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; BT045540; ACI33802.1; -; mRNA.
DR RefSeq; NP_001133732.1; NM_001140260.1.
DR AlphaFoldDB; B5X3C1; -.
DR SMR; B5X3C1; -.
DR STRING; 8030.ENSSSAP00000044309; -.
DR CAZy; GH59; Glycoside Hydrolase Family 59.
DR GeneID; 100195231; -.
DR KEGG; sasa:100195231; -.
DR CTD; 406385; -.
DR OrthoDB; 364933at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR Bgee; ENSSSAG00000046330; Expressed in digestive tract and 15 other tissues.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004336; F:galactosylceramidase activity; ISS:UniProtKB.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..666
FT /note="Galactocerebrosidase"
FT /id="PRO_0000370714"
FT ACT_SITE 180
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 269..376
FT /evidence="ECO:0000250"
SQ SEQUENCE 666 AA; 74494 MW; 7169F6D7ADD8CA67 CRC64;
MIYKLYFAIA LCFSLCFDLC IAESYVLDDK VGLGRTFDGI GGLSGGGATS RLLVNYAEPY
RSQILDYLFK PNFGASLHIL KVEIGGDAQT TDGTEPSHMH YENDENFFRG YEWWLMREAK
KRNPNITLIG LPWAFPGWVG HGKNWPYDFP DITASYVVSW ILGAKHYHDL NIDYVGIWNE
RNFDSKYIKL LRYTLDKSGL ERVRIIASDN LWQPITYSLC VDQELADAVD VIGAHYPGTT
TVIEALKTQK KLWSSEDYST FNDEVGGGCW ARILNQNYVN GLMTATISWN LVASYYEDLP
FGRDGLMTAE EPWTGNYVVE SPIWITAHTT QFSQPGWTYL QTVGHLVHGG SYVALTDSNG
NLTVVIETMT HDHSVCIRPP LLPFNVTAQN VTFQLKGSFA LIKELQVWQS RFDFKTKKPF
FFKKLSPLKI SDGSFTLSLD VDEVYTLTTI STGLKGTYPD PPTSGPFPKV YFDDFNVANP
SFSEAPDFAD QTGVFEYYIN LTDPGPHVFT LRQVVTQMPV TWATDADQTI SVIGDYKWQN
LTVTCDVFME TVKTGGVFIA ARVDKGGQSV RSAKGVFFWV FADGSYKVTN DLVGKTVLAE
GLSGTRAYGW HTLTLTVEGQ YATGLLNGYP LWKDAVVLGP KNGWAAIGTH SFELAQFDNF
AVEAKL
