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P54818

- GALC_MOUSE

UniProt

P54818 - GALC_MOUSE

Protein

Galactocerebrosidase

Gene

Galc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    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

    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

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

    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.
    InParanoidiQ3U3H7.
    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

    MANSQPKASQ QRQAKVMTAA AGSASRVAVP LLLCALLVPG GAYVLDDSDG    50
    LGREFDGIGA VSGGGATSRL LVNYPEPYRS EILDYLFKPN FGASLHILKV 100
    EIGGDGQTTD GTEPSHMHYE LDENYFRGYE WWLMKEAKKR NPDIILMGLP 150
    WSFPGWLGKG FSWPYVNLQL TAYYVVRWIL GAKHYHDLDI DYIGIWNERP 200
    FDANYIKELR KMLDYQGLQR VRIIASDNLW EPISSSLLLD QELWKVVDVI 250
    GAHYPGTYTV WNAKMSGKKL WSSEDFSTIN SNVGAGCWSR ILNQNYINGN 300
    MTSTIAWNLV ASYYEELPYG RSGLMTAQEP WSGHYVVASP IWVSAHTTQF 350
    TQPGWYYLKT VGHLEKGGSY VALTDGLGNL TIIIETMSHQ HSMCIRPYLP 400
    YYNVSHQLAT FTLKGSLREI QELQVWYTKL GTPQQRLHFK QLDTLWLLDG 450
    SGSFTLELEE DEIFTLTTLT TGRKGSYPPP PSSKPFPTNY KDDFNVEYPL 500
    FSEAPNFADQ TGVFEYYMNN EDREHRFTLR QVLNQRPITW AADASSTISV 550
    IGDHHWTNMT VQCDVYIETP RSGGVFIAGR VNKGGILIRS ATGVFFWIFA 600
    NGSYRVTADL GGWITYASGH ADVTAKRWYT LTLGIKGYFA FGMLNGTILW 650
    KNVRVKYPGH GWAAIGTHTF EFAQFDNFRV EAAR 684
    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 Q3U3H7.
    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

    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 1, 2014
    This is version 105 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