Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P54818 (GALC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Galactocerebrosidase

Short name=GALCERase
EC=3.2.1.46
Alternative name(s):
Galactocerebroside beta-galactosidase
Galactosylceramidase
Galactosylceramide beta-galactosidase
Gene names
Name:Galc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length684 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon. Ref.1

Catalytic activity

D-galactosyl-N-acylsphingosine + H2O = D-galactose + N-acylsphingosine. Ref.1

Subcellular location

Lysosome By similarity.

Tissue specificity

Detected in brain and kidney. Ref.1

Involvement in disease

Defects in Galc are the cause of the 'twitcher' phenotype; an autosomal recessive leukodystrophy similar to the human disease (Krabbe disease). This deficiency results in the insufficient catabolism of several galactolipids that are important in the production of normal myelin. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 59 family.

Caution

It is uncertain whether Met-1 or Met-17 is the initiator.

Sequence caution

The sequence AAB71823.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH86671.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA07560.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242 By similarity
Chain43 – 684642Galactocerebrosidase
PRO_0000012232

Sites

Active site1981Proton donor/acceptor Ref.6
Active site2741Nucleophile Ref.6
Binding site1091Substrate
Binding site1511Substrate
Binding site1971Substrate
Binding site3961Substrate

Amino acid modifications

Glycosylation3001N-linked (GlcNAc...) Ref.6
Glycosylation3791N-linked (GlcNAc...) Ref.6
Glycosylation4031N-linked (GlcNAc...) Ref.6
Glycosylation5581N-linked (GlcNAc...) Ref.6
Glycosylation6011N-linked (GlcNAc...) Potential
Glycosylation6451N-linked (GlcNAc...) Potential
Disulfide bond287 ↔ 394 Ref.6

Experimental info

Sequence conflict3761G → A in AAB71823. Ref.2

Secondary structure

...................................................................................................................... 684
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54818 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: DD4BD45AE898C524

FASTA68477,256
        10         20         30         40         50         60 
MANSQPKASQ QRQAKVMTAA AGSASRVAVP LLLCALLVPG GAYVLDDSDG LGREFDGIGA 

        70         80         90        100        110        120 
VSGGGATSRL LVNYPEPYRS EILDYLFKPN FGASLHILKV EIGGDGQTTD GTEPSHMHYE 

       130        140        150        160        170        180 
LDENYFRGYE WWLMKEAKKR NPDIILMGLP WSFPGWLGKG FSWPYVNLQL TAYYVVRWIL 

       190        200        210        220        230        240 
GAKHYHDLDI DYIGIWNERP FDANYIKELR KMLDYQGLQR VRIIASDNLW EPISSSLLLD 

       250        260        270        280        290        300 
QELWKVVDVI GAHYPGTYTV WNAKMSGKKL WSSEDFSTIN SNVGAGCWSR ILNQNYINGN 

       310        320        330        340        350        360 
MTSTIAWNLV ASYYEELPYG RSGLMTAQEP WSGHYVVASP IWVSAHTTQF TQPGWYYLKT 

       370        380        390        400        410        420 
VGHLEKGGSY VALTDGLGNL TIIIETMSHQ HSMCIRPYLP YYNVSHQLAT FTLKGSLREI 

       430        440        450        460        470        480 
QELQVWYTKL GTPQQRLHFK QLDTLWLLDG SGSFTLELEE DEIFTLTTLT TGRKGSYPPP 

       490        500        510        520        530        540 
PSSKPFPTNY KDDFNVEYPL FSEAPNFADQ TGVFEYYMNN EDREHRFTLR QVLNQRPITW 

       550        560        570        580        590        600 
AADASSTISV IGDHHWTNMT VQCDVYIETP RSGGVFIAGR VNKGGILIRS ATGVFFWIFA 

       610        620        630        640        650        660 
NGSYRVTADL GGWITYASGH ADVTAKRWYT LTLGIKGYFA FGMLNGTILW KNVRVKYPGH 

       670        680 
GWAAIGTHTF EFAQFDNFRV EAAR 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of cDNA for murine galactocerebrosidase and mutation analysis of the twitcher mouse, a model of Krabbe's disease."
Sakai N., Inui K., Tatsumi N., Fukushima H., Nishigaki T., Taniike M., Nishimoto J., Tsukamoto H., Yanagihara I., Ozono K., Okada S.
J. Neurochem. 66:1118-1124(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, ROLE IN DISEASE.
Strain: C57BL/6J.
Tissue: Testis.
[2]"Genomic organization of the mouse galactocerebrosidase (GALC) gene."
Luzi P., Victoria T., Wenger D.A.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
[6]"Insights into Krabbe disease from structures of galactocerebrosidase."
Deane J.E., Graham S.C., Kim N.N., Stein P.E., McNair R., Cachon-Gonzalez M.B., Cox T.M., Read R.J.
Proc. Natl. Acad. Sci. U.S.A. 108:15169-15173(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 40-684 IN COMPLEX WITH GALACTOSE, ACTIVE SITE, GLYCOSYLATION AT ASN-300; ASN-379; ASN-403 AND ASN-558, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38557 mRNA. Translation: BAA07560.1. Different initiation.
AF003886 expand/collapse EMBL AC list , AF003870, AF003871, AF003872, AF003873, AF003874, AF003875, AF003876, AF003877, AF003878, AF003879, AF003880, AF003881, AF003882, AF003883, AF003884, AF003885 Genomic DNA. Translation: AAB71823.1. Different initiation.
AK154760 mRNA. Translation: BAE32809.1.
CH466549 Genomic DNA. Translation: EDL18937.1.
BC086671 mRNA. Translation: AAH86671.1. Different initiation.
RefSeqNP_032105.2. NM_008079.3.
UniGeneMm.5120.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZR5X-ray2.10A40-684[»]
3ZR6X-ray2.44A40-684[»]
4CCCX-ray2.09A41-684[»]
4CCDX-ray1.97A41-684[»]
4CCEX-ray2.06A41-684[»]
ProteinModelPortalP54818.
SMRP54818. Positions 41-684.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2218.

Protein family/group databases

CAZyGH59. Glycoside Hydrolase Family 59.

PTM databases

PhosphoSiteP54818.

Proteomic databases

PaxDbP54818.
PRIDEP54818.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021390; ENSMUSP00000021390; ENSMUSG00000021003.
GeneID14420.
KEGGmmu:14420.
UCSCuc007olf.1. mouse.

Organism-specific databases

CTD2581.
MGIMGI:95636. Galc.

Phylogenomic databases

eggNOGNOG76999.
GeneTreeENSGT00390000003303.
HOGENOMHOG000068033.
HOVERGENHBG005800.
InParanoidQ3U3H7.
KOK01202.
OMAAGWIIYA.
OrthoDBEOG77WWCH.
PhylomeDBP54818.
TreeFamTF312985.

Gene expression databases

BgeeP54818.
CleanExMM_GALC.
GenevestigatorP54818.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001286. Glyco_hydro_59.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR15172. PTHR15172. 1 hit.
PfamPF02057. Glyco_hydro_59. 1 hit.
[Graphical view]
PRINTSPR00850. GLHYDRLASE59.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

NextBio286009.
PROP54818.
SOURCESearch...

Entry information

Entry nameGALC_MOUSE
AccessionPrimary (citable) accession number: P54818
Secondary accession number(s): O35151, Q3U3H7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries