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P54818

- GALC_MOUSE

UniProt

P54818 - GALC_MOUSE

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Protein

Galactocerebrosidase

Gene

Galc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091Substrate
Binding sitei151 – 1511Substrate
Binding sitei197 – 1971Substrate
Active sitei198 – 1981Proton donor/acceptor1 Publication
Active sitei274 – 2741Nucleophile1 Publication
Binding sitei396 – 3961Substrate

GO - Molecular functioni

  1. galactosylceramidase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. galactosylceramide catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

ReactomeiREACT_199008. 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):
Galactocerebroside beta-galactosidase
Galactosylceramidase
Galactosylceramide beta-galactosidase
Gene namesi
Name:Galc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:95636. Galc.

Subcellular locationi

Lysosome By similarity

GO - Cellular componenti

  1. lysosome Source: MGI
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242By similarityAdd
BLAST
Chaini43 – 684642GalactocerebrosidasePRO_0000012232Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi287 ↔ 3941 Publication
Glycosylationi300 – 3001N-linked (GlcNAc...)1 Publication
Glycosylationi379 – 3791N-linked (GlcNAc...)1 Publication
Glycosylationi403 – 4031N-linked (GlcNAc...)1 Publication
Glycosylationi558 – 5581N-linked (GlcNAc...)1 Publication
Glycosylationi601 – 6011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi645 – 6451N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP54818.
PaxDbiP54818.
PRIDEiP54818.

PTM databases

PhosphoSiteiP54818.

Expressioni

Tissue specificityi

Detected in brain and kidney.1 Publication

Gene expression databases

BgeeiP54818.
CleanExiMM_GALC.
GenevestigatoriP54818.

Structurei

Secondary structure

1
684
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 454Combined sources
Beta strandi51 – 544Combined sources
Beta strandi57 – 626Combined sources
Turni67 – 737Combined sources
Helixi78 – 8710Combined sources
Turni89 – 913Combined sources
Beta strandi96 – 1027Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi109 – 1124Combined sources
Beta strandi127 – 1293Combined sources
Helixi130 – 14011Combined sources
Beta strandi145 – 1517Combined sources
Helixi155 – 1584Combined sources
Helixi168 – 18619Combined sources
Helixi203 – 21513Combined sources
Beta strandi222 – 2287Combined sources
Helixi233 – 2397Combined sources
Helixi241 – 2466Combined sources
Beta strandi249 – 2546Combined sources
Helixi261 – 2666Combined sources
Beta strandi269 – 2768Combined sources
Helixi282 – 29918Combined sources
Beta strandi303 – 3075Combined sources
Beta strandi309 – 3113Combined sources
Turni318 – 3214Combined sources
Beta strandi323 – 3264Combined sources
Turni330 – 3323Combined sources
Helixi340 – 3489Combined sources
Beta strandi356 – 3594Combined sources
Beta strandi369 – 3746Combined sources
Beta strandi376 – 3783Combined sources
Beta strandi380 – 3856Combined sources
Helixi389 – 3913Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi407 – 4137Combined sources
Helixi415 – 4173Combined sources
Beta strandi422 – 4298Combined sources
Beta strandi437 – 44610Combined sources
Beta strandi449 – 4513Combined sources
Beta strandi453 – 4586Combined sources
Beta strandi460 – 4689Combined sources
Beta strandi488 – 4925Combined sources
Beta strandi500 – 5034Combined sources
Beta strandi508 – 5125Combined sources
Beta strandi514 – 5185Combined sources
Beta strandi526 – 5316Combined sources
Beta strandi545 – 5528Combined sources
Beta strandi558 – 56710Combined sources
Turni570 – 5723Combined sources
Beta strandi574 – 5818Combined sources
Helixi585 – 5906Combined sources
Beta strandi592 – 5998Combined sources
Turni600 – 6023Combined sources
Beta strandi603 – 6097Combined sources
Beta strandi614 – 6207Combined sources
Beta strandi628 – 6369Combined sources
Beta strandi639 – 6446Combined sources
Beta strandi647 – 6548Combined sources
Beta strandi662 – 6709Combined sources
Beta strandi673 – 68311Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZR5X-ray2.10A40-684[»]
3ZR6X-ray2.44A40-684[»]
4CCCX-ray2.09A41-684[»]
4CCDX-ray1.97A41-684[»]
4CCEX-ray2.06A41-684[»]
ProteinModelPortaliP54818.
SMRiP54818. Positions 41-684.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 59 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG76999.
GeneTreeiENSGT00390000003303.
HOGENOMiHOG000068033.
HOVERGENiHBG005800.
InParanoidiP54818.
KOiK01202.
OMAiPVWVSAH.
OrthoDBiEOG77WWCH.
PhylomeDBiP54818.
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.

P54818-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANSQPKASQ QRQAKVMTAA AGSASRVAVP LLLCALLVPG GAYVLDDSDG
60 70 80 90 100
LGREFDGIGA VSGGGATSRL LVNYPEPYRS EILDYLFKPN FGASLHILKV
110 120 130 140 150
EIGGDGQTTD GTEPSHMHYE LDENYFRGYE WWLMKEAKKR NPDIILMGLP
160 170 180 190 200
WSFPGWLGKG FSWPYVNLQL TAYYVVRWIL GAKHYHDLDI DYIGIWNERP
210 220 230 240 250
FDANYIKELR KMLDYQGLQR VRIIASDNLW EPISSSLLLD QELWKVVDVI
260 270 280 290 300
GAHYPGTYTV WNAKMSGKKL WSSEDFSTIN SNVGAGCWSR ILNQNYINGN
310 320 330 340 350
MTSTIAWNLV ASYYEELPYG RSGLMTAQEP WSGHYVVASP IWVSAHTTQF
360 370 380 390 400
TQPGWYYLKT VGHLEKGGSY VALTDGLGNL TIIIETMSHQ HSMCIRPYLP
410 420 430 440 450
YYNVSHQLAT FTLKGSLREI QELQVWYTKL GTPQQRLHFK QLDTLWLLDG
460 470 480 490 500
SGSFTLELEE DEIFTLTTLT TGRKGSYPPP PSSKPFPTNY KDDFNVEYPL
510 520 530 540 550
FSEAPNFADQ TGVFEYYMNN EDREHRFTLR QVLNQRPITW AADASSTISV
560 570 580 590 600
IGDHHWTNMT VQCDVYIETP RSGGVFIAGR VNKGGILIRS ATGVFFWIFA
610 620 630 640 650
NGSYRVTADL GGWITYASGH ADVTAKRWYT LTLGIKGYFA FGMLNGTILW
660 670 680
KNVRVKYPGH GWAAIGTHTF EFAQFDNFRV EAAR
Length:684
Mass (Da):77,256
Last modified:May 5, 2009 - v2
Checksum:iDD4BD45AE898C524
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti376 – 3761G → A in AAB71823. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38557 mRNA. Translation: BAA07560.1. Different initiation.
AF003886
, 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.
CCDSiCCDS36517.1.
RefSeqiNP_032105.2. NM_008079.3.
UniGeneiMm.5120.

Genome annotation databases

EnsembliENSMUST00000021390; ENSMUSP00000021390; ENSMUSG00000021003.
GeneIDi14420.
KEGGimmu:14420.
UCSCiuc007olf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38557 mRNA. Translation: BAA07560.1 . Different initiation.
AF003886
, 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.
CCDSi CCDS36517.1.
RefSeqi NP_032105.2. NM_008079.3.
UniGenei Mm.5120.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ZR5 X-ray 2.10 A 40-684 [» ]
3ZR6 X-ray 2.44 A 40-684 [» ]
4CCC X-ray 2.09 A 41-684 [» ]
4CCD X-ray 1.97 A 41-684 [» ]
4CCE X-ray 2.06 A 41-684 [» ]
ProteinModelPortali P54818.
SMRi P54818. Positions 41-684.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2218.

Protein family/group databases

CAZyi GH59. Glycoside Hydrolase Family 59.

PTM databases

PhosphoSitei P54818.

Proteomic databases

MaxQBi P54818.
PaxDbi P54818.
PRIDEi P54818.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021390 ; ENSMUSP00000021390 ; ENSMUSG00000021003 .
GeneIDi 14420.
KEGGi mmu:14420.
UCSCi uc007olf.1. mouse.

Organism-specific databases

CTDi 2581.
MGIi MGI:95636. Galc.

Phylogenomic databases

eggNOGi NOG76999.
GeneTreei ENSGT00390000003303.
HOGENOMi HOG000068033.
HOVERGENi HBG005800.
InParanoidi P54818.
KOi K01202.
OMAi PVWVSAH.
OrthoDBi EOG77WWCH.
PhylomeDBi P54818.
TreeFami TF312985.

Enzyme and pathway databases

Reactomei REACT_199008. Glycosphingolipid metabolism.

Miscellaneous databases

NextBioi 286009.
PROi P54818.
SOURCEi Search...

Gene expression databases

Bgeei P54818.
CleanExi MM_GALC.
Genevestigatori P54818.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001286. Glyco_hydro_59.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR15172. PTHR15172. 1 hit.
Pfami PF02057. Glyco_hydro_59. 1 hit.
[Graphical view ]
PRINTSi PR00850. GLHYDRLASE59.
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiGALC_MOUSE
AccessioniPrimary (citable) accession number: P54818
Secondary accession number(s): O35151, Q3U3H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 5, 2009
Last modified: October 29, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3