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Protein

Galactocerebrosidase

Gene

galc

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride.By similarity

Catalytic activityi

D-galactosyl-N-acylsphingosine + H2O = D-galactose + N-acylsphingosine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei87 – 871SubstrateBy similarity
Binding sitei129 – 1291SubstrateBy similarity
Binding sitei175 – 1751SubstrateBy similarity
Active sitei176 – 1761Proton donor/acceptorBy similarity
Active sitei251 – 2511NucleophileBy similarity
Binding sitei373 – 3731SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

ReactomeiR-DRE-1660662. Glycosphingolipid metabolism.

Protein family/group databases

CAZyiGH59. Glycoside Hydrolase Family 59.

Names & Taxonomyi

Protein namesi
Recommended name:
Galactocerebrosidase (EC:3.2.1.46)
Short name:
GALCERase
Alternative name(s):
Galactosylceramidase
Gene namesi
Name:galc
Synonyms:galca
ORF Names:si:ch211-199l3.4, zgc:92561
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 20

Organism-specific databases

ZFINiZDB-GENE-040724-243. galca.

Subcellular locationi

GO - Cellular componenti

  • lysosome Source: ZFIN
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 660642GalactocerebrosidasePRO_0000370713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence analysis
Disulfide bondi264 ↔ 371By similarity
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence analysis
Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence analysis
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence analysis
Glycosylationi465 – 4651N-linked (GlcNAc...)Sequence analysis
Glycosylationi495 – 4951N-linked (GlcNAc...)Sequence analysis
Glycosylationi499 – 4991N-linked (GlcNAc...)Sequence analysis
Glycosylationi537 – 5371N-linked (GlcNAc...)Sequence analysis
Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ5SNX7.

Expressioni

Gene expression databases

BgeeiQ5SNX7.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000053869.

Structurei

3D structure databases

ProteinModelPortaliQ5SNX7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 59 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IITE. Eukaryota.
ENOG410XTIS. LUCA.
GeneTreeiENSGT00390000003303.
HOGENOMiHOG000068033.
InParanoidiQ5SNX7.
KOiK01202.
OMAiCIRPALP.
OrthoDBiEOG77WWCH.
PhylomeDBiQ5SNX7.
TreeFamiTF312985.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001286. Glyco_hydro_59.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR15172. PTHR15172. 1 hit.
PfamiPF02057. Glyco_hydro_59. 1 hit.
[Graphical view]
PRINTSiPR00850. GLHYDRLASE59.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5SNX7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTHNFLCII SVILGCSAQF YVIDDRIGLG REFDGIGGLS GGGATSRLLV
60 70 80 90 100
NYEEPYRSQI LDYLFKPNFG ASLHILKVEI GGDAQTTDGT EPSHMHSKDE
110 120 130 140 150
GNFFRGYEWW LMKEAKKRNP NIKLIGLPWA FPGWVGYGTQ WPYFFPNVTA
160 170 180 190 200
NYVITWVMGA KQHHNLDIDY IGIWNEKAFD PTYIKVLRDA LDRAGFTNIG
210 220 230 240 250
IIAADGDWSI ASAMLDDPYL NDAVEVIGVH YPGTNTVKEA LLTERKLWSS
260 270 280 290 300
EDYSTYNDDI GAGCWARILN QNYVNGKMTS TISWNVIASY YENLSFGRDG
310 320 330 340 350
LMTAEEPWSG HYIVESPIWM TAHTTQFTQP GWFYLQTVGK LNHGGSYVAL
360 370 380 390 400
TDRKGNLTII IETMTHEHSQ CIRPPLPHFD VSPQIATFEL KGSFAHLADL
410 420 430 440 450
QVWYSKLDFK SGNGTLFKQL RPIRAHNGLL SLKLDVDEVF TITTVTTAQR
460 470 480 490 500
GFYPEPPKSC PFPKNYTDDF TIDNPPFSEA PYFADQTGVF EYFRNTTDNS
510 520 530 540 550
SHAFTLRQVV TERPVAWAKD ADQTISIIGD YSWSDVNVSC DVFIETPKTG
560 570 580 590 600
GVFLAARVDQ GGESVRQAKG VFYWIYANGT YRVTNDIGGK RVLAEGLSGT
610 620 630 640 650
KAGVWYTLTL SVKGYFATGS LNGFPLWKNA AVLEPKSGWA ALGTLSFEYA
660
QFDNFNVIAG
Length:660
Mass (Da):73,820
Last modified:December 21, 2004 - v1
Checksum:iAC70CBB2903A9B77
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111S → F in AAH83517 (Ref. 2) Curated
Sequence conflicti190 – 1901A → V in AAH83517 (Ref. 2) Curated
Sequence conflicti418 – 4181K → R in AAH83517 (Ref. 2) Curated
Sequence conflicti511 – 5111T → I in AAH83517 (Ref. 2) Curated
Sequence conflicti591 – 5911R → G in AAH83517 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL953887 Genomic DNA. Translation: CAI11729.1.
BC083517 mRNA. Translation: AAH83517.1.
RefSeqiNP_001005921.1. NM_001005921.1.
UniGeneiDr.106140.

Genome annotation databases

EnsembliENSDART00000053870; ENSDARP00000053869; ENSDARG00000037064.
GeneIDi449649.
KEGGidre:449649.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL953887 Genomic DNA. Translation: CAI11729.1.
BC083517 mRNA. Translation: AAH83517.1.
RefSeqiNP_001005921.1. NM_001005921.1.
UniGeneiDr.106140.

3D structure databases

ProteinModelPortaliQ5SNX7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000053869.

Protein family/group databases

CAZyiGH59. Glycoside Hydrolase Family 59.

Proteomic databases

PaxDbiQ5SNX7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000053870; ENSDARP00000053869; ENSDARG00000037064.
GeneIDi449649.
KEGGidre:449649.

Organism-specific databases

CTDi449649.
ZFINiZDB-GENE-040724-243. galca.

Phylogenomic databases

eggNOGiENOG410IITE. Eukaryota.
ENOG410XTIS. LUCA.
GeneTreeiENSGT00390000003303.
HOGENOMiHOG000068033.
InParanoidiQ5SNX7.
KOiK01202.
OMAiCIRPALP.
OrthoDBiEOG77WWCH.
PhylomeDBiQ5SNX7.
TreeFamiTF312985.

Enzyme and pathway databases

ReactomeiR-DRE-1660662. Glycosphingolipid metabolism.

Miscellaneous databases

PROiQ5SNX7.

Gene expression databases

BgeeiQ5SNX7.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001286. Glyco_hydro_59.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR15172. PTHR15172. 1 hit.
PfamiPF02057. Glyco_hydro_59. 1 hit.
[Graphical view]
PRINTSiPR00850. GLHYDRLASE59.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.
  2. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: AB.

Entry informationi

Entry nameiGALC_DANRE
AccessioniPrimary (citable) accession number: Q5SNX7
Secondary accession number(s): Q5XJ01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: December 21, 2004
Last modified: June 8, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.