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

P54803 (GALC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length685 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.5 Ref.8

Catalytic activity

D-galactosyl-N-acylsphingosine + H2O = D-galactose + N-acylsphingosine. Ref.5 Ref.8

Subcellular location

Lysosome.

Tissue specificity

Detected in urine. Detected in testis, brain and placenta (at protein level). Detected in kidney and liver. Ref.8

Polymorphism

Polymorphic amino-acid changes are responsible for the wide range of catalytic activities found in the general population.

Involvement in disease

Leukodystrophy, globoid cell (GLD) [MIM:245200]: An autosomal recessive disorder characterized by insufficient catabolism of several galactolipids that are important for normal myelin production. Four clinical forms are recognized. The infantile form accounts for 90% of cases. It manifests before six months of age with irritability, spasticity, arrest of motor and mental development, and bouts of temperature elevation without infection. This is followed by myoclonic jerks of arms and legs, oposthotonus, hypertonic fits, and mental regression, which progresses to a severe decerebrate condition with no voluntary movements and death from respiratory infections or cerebral hyperpyrexia before 2 years of age. Cases with later onset present with unexplained blindness, weakness and sensorimotor peripheral neuropathy, mental deterioration and death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Sequence similarities

Belongs to the glycosyl hydrolase 59 family.

Caution

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

Biophysicochemical properties

pH dependence:

Optimum pH is 4.0-4.4.

Temperature dependence:

Activity is lost after heating at 52 degrees Celsius for five minutes.

Sequence caution

The sequence AAA16645.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAA80975.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH36518.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA04971.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA04972.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA04972.1 differs from that shown. Reason: Probable intron retention.

The sequence BAA24902.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAG59160.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54803-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 3 (identifier: P54803-3)

The sequence of this isoform differs from the canonical sequence as follows:
     66-88: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P54803-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: MAEWLLSASW...DGIGAVSGGG → MLGKSHGRAT...HQVTPEEKPA
Isoform 5 (identifier: P54803-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: MAEWLLSASWQRRAKAMTAAAGSAGRAAVPLLLCALLAPGGAYVLDDSDGLGREFDGIGAVSGGG → MGFMVADLW
     638-685: GHFASGMLNDKSLWTDIPVNFPKNGWAAIGTHSFEFAQFDNFLVEATR → VAGRRKKT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242 Ref.5 Ref.8
Chain43 – 685643Galactocerebrosidase
PRO_0000012230

Sites

Active site1981Proton donor/acceptor By similarity
Active site2741Nucleophile By similarity
Binding site1091Substrate By similarity
Binding site1511Substrate By similarity
Binding site1971Substrate By similarity
Binding site3961Substrate By similarity

Amino acid modifications

Glycosylation1431N-linked (GlcNAc...) Potential
Glycosylation3791N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation5561N-linked (GlcNAc...) Potential
Glycosylation5591N-linked (GlcNAc...) Potential
Glycosylation6021N-linked (GlcNAc...) Potential
Disulfide bond287 ↔ 394 By similarity

Natural variations

Alternative sequence1 – 6565MAEWL…VSGGG → MLGKSHGRATHGPLPLADLG IHLPCVKVLHQVTPEEKPA in isoform 4.
VSP_036974
Alternative sequence1 – 6565MAEWL…VSGGG → MGFMVADLW in isoform 5.
VSP_036975
Alternative sequence66 – 8823Missing in isoform 3.
VSP_036976
Alternative sequence638 – 68548GHFAS…VEATR → VAGRRKKT in isoform 5.
VSP_036977
Natural variant211A → P. Ref.20
VAR_064430
Natural variant411G → S in GLD. Ref.19
VAR_064431
Natural variant591G → R in GLD; infantile; significant reduction of activity. Ref.18
VAR_013956
Natural variant681S → F in GLD; infantile; significant reduction of activity. Ref.18
VAR_013957
Natural variant791R → H in GLD. Ref.13
VAR_013958
Natural variant821I → M in GLD; adult; reduction of activity; when associated with V-2105. Ref.16
VAR_013959
Natural variant1111G → D in GLD.
VAR_003380
Natural variant1111G → S in GLD. Ref.13
VAR_003381
Natural variant1121T → A in GLD; adult.
VAR_003382
Natural variant1171M → L in GLD; adult. Ref.13
VAR_003383
Natural variant1301E → K in GLD. Ref.20
VAR_064432
Natural variant1841R → C. Ref.3 Ref.11 Ref.20
Corresponds to variant rs1805078 [ dbSNP | Ensembl ].
VAR_013960
Natural variant1871D → V in GLD.
VAR_003384
Natural variant1941G → A in GLD.
VAR_003385
Natural variant2481D → N. Ref.20
Corresponds to variant rs34362748 [ dbSNP | Ensembl ].
VAR_003386
Natural variant2501I → T in GLD; late infantile. Ref.13
VAR_003387
Natural variant2631A → T in GLD.
VAR_003388
Natural variant2781T → I in GLD; infantile; significant reduction of activity. Ref.18
VAR_013961
Natural variant2841G → S in GLD. Ref.13
VAR_003389
Natural variant2861G → D in GLD. Ref.16 Ref.17
VAR_003390
Natural variant2951N → T in GLD.
VAR_003391
Natural variant3031S → F in GLD; infantile.
VAR_003392
Natural variant3051I → V. Ref.16
Corresponds to variant rs1805079 [ dbSNP | Ensembl ].
VAR_013962
Natural variant3141Y → C in GLD. Ref.13
VAR_013963
Natural variant3181P → A in GLD. Ref.12
VAR_003393
Natural variant3181P → R in GLD. Ref.20
VAR_064433
Natural variant3231G → R in GLD. Ref.20
VAR_064434
Natural variant3351Y → C in GLD; infantile; significant reduction of activity. Ref.18
VAR_013964
Natural variant3841I → T in GLD. Ref.20
VAR_064435
Natural variant3961R → L in GLD. Ref.20
VAR_064436
Natural variant3961R → W in GLD; bilateral cherry red spots.
VAR_003394
Natural variant4001P → L in GLD.
VAR_003395
Natural variant4261W → G in GLD; infantile; significant reduction of activity. Ref.18
VAR_013965
Natural variant4681T → S in GLD.
Corresponds to variant rs34134328 [ dbSNP | Ensembl ].
VAR_003396
Natural variant4901Y → N in GLD. Ref.20
VAR_064437
Natural variant5141F → S in GLD.
VAR_003397
Natural variant5291T → M in GLD; infantile.
VAR_003398
Natural variant5311R → C in GLD.
VAR_003399
Natural variant5311R → H in GLD; infantile; significant reduction of activity. Ref.18
VAR_013966
Natural variant5441D → N in GLD; Arab patients. Ref.15
VAR_003400
Natural variant5531G → R in GLD; loss of activity. Ref.17
VAR_013967
Natural variant5621I → T Common polymorphism. Ref.1 Ref.3 Ref.7 Ref.13 Ref.16 Ref.20
Corresponds to variant rs398607 [ dbSNP | Ensembl ].
VAR_003401
Natural variant5661V → G in GLD. Ref.12
VAR_003402
Natural variant5671Y → S in GLD.
VAR_003403
Natural variant5921A → S in GLD.
VAR_003404
Natural variant5991I → S in GLD; infantile; Druze patients. Ref.15
VAR_003405
Natural variant6341L → S in GLD; adult. Ref.16
VAR_013968
Natural variant6411A → T Significant reduction of activity when associated with T-562. Ref.4 Ref.17 Ref.20
Corresponds to variant rs421262 [ dbSNP | Ensembl ].
VAR_003406
Natural variant6451L → R in GLD; adult.
VAR_003407
Natural variant6681T → R in GLD; infantile; significant reduction of activity. Ref.18
VAR_013969
Natural variant6811V → M in GLD. Ref.21
VAR_069512

Experimental info

Sequence conflict781Y → H in BAH13778. Ref.1
Sequence conflict1951I → T in BAG64110. Ref.3
Sequence conflict4221E → G in BAG64110. Ref.3
Isoform 4:
Sequence conflict171A → T in BAG64110. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 03F3D223291AD5A0

FASTA68577,033
        10         20         30         40         50         60 
MAEWLLSASW QRRAKAMTAA AGSAGRAAVP LLLCALLAPG GAYVLDDSDG LGREFDGIGA 

        70         80         90        100        110        120 
VSGGGATSRL LVNYPEPYRS QILDYLFKPN FGASLHILKV EIGGDGQTTD GTEPSHMHYA 

       130        140        150        160        170        180 
LDENYFRGYE WWLMKEAKKR NPNITLIGLP WSFPGWLGKG FDWPYVNLQL TAYYVVTWIV 

       190        200        210        220        230        240 
GAKRYHDLDI DYIGIWNERS YNANYIKILR KMLNYQGLQR VKIIASDNLW ESISASMLLD 

       250        260        270        280        290        300 
AELFKVVDVI GAHYPGTHSA KDAKLTGKKL WSSEDFSTLN SDMGAGCWGR ILNQNYINGY 

       310        320        330        340        350        360 
MTSTIAWNLV ASYYEQLPYG RCGLMTAQEP WSGHYVVESP VWVSAHTTQF TQPGWYYLKT 

       370        380        390        400        410        420 
VGHLEKGGSY VALTDGLGNL TIIIETMSHK HSKCIRPFLP YFNVSQQFAT FVLKGSFSEI 

       430        440        450        460        470        480 
PELQVWYTKL GKTSERFLFK QLDSLWLLDS DGSFTLSLHE DELFTLTTLT TGRKGSYPLP 

       490        500        510        520        530        540 
PKSQPFPSTY KDDFNVDYPF FSEAPNFADQ TGVFEYFTNI EDPGEHHFTL RQVLNQRPIT 

       550        560        570        580        590        600 
WAADASNTIS IIGDYNWTNL TIKCDVYIET PDTGGVFIAG RVNKGGILIR SARGIFFWIF 

       610        620        630        640        650        660 
ANGSYRVTGD LAGWIIYALG RVEVTAKKWY TLTLTIKGHF ASGMLNDKSL WTDIPVNFPK 

       670        680 
NGWAAIGTHS FEFAQFDNFL VEATR 

« Hide

Isoform 3 [UniParc].

Checksum: EDEF265721A257AF
Show »

FASTA66274,264
Isoform 4 [UniParc].

Checksum: A35297C54C708333
Show »

FASTA65974,734
Isoform 5 [UniParc].

Checksum: 0859D4E53CD87B64
Show »

FASTA58967,184

References

« Hide 'large scale' references
[1]"Structure and organization of the human galactocerebrosidase (GALC) gene."
Luzi P., Rafi M.A., Wenger D.A.
Genomics 26:407-409(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-562.
[2]"Human galactocerebrosidase gene: promoter analysis of the 5'-flanking region and structural organization."
Sakai N., Fukushima H., Inui K., Fu L., Nishigaki T., Yanagihara I., Tatsumi N., Ozono K., Okada S.
Biochim. Biophys. Acta 1395:62-67(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-685 (ISOFORM 3), VARIANTS CYS-184 AND THR-562.
Tissue: Testis and Thalamus.
[4]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-641.
[5]"Cloning and expression of cDNA encoding human galactocerebrosidase, the enzyme deficient in globoid cell leukodystrophy."
Chen Y.Q., Rafi M.A., de Gala G., Wenger D.A.
Hum. Mol. Genet. 2:1841-1845(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-685 (ISOFORM 1), PROTEIN SEQUENCE OF 43-75 AND 452-470, CATALYTIC ACTIVITY, FUNCTION.
Tissue: Testis.
[6]"Krabbe disease: isolation and characterization of a full-length cDNA for human galactocerebrosidase."
Sakai N., Inui K., Fujii N., Fukushima H., Nishimoto J., Yanagihara I., Isegawa Y., Iwamatsu A., Okada S.
Biochem. Biophys. Res. Commun. 198:485-491(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-685 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
Tissue: Placenta and Skin fibroblast.
[7]"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] OF 15-685 (ISOFORM 1), VARIANT THR-562.
Tissue: Testis.
[8]"Galactocerebrosidase from human urine: purification and partial characterization."
Chen Y.Q., Wenger D.A.
Biochim. Biophys. Acta 1170:53-61(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 43-61 AND 452-470, PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
Tissue: Urine.
[9]"Molecular genetics of Krabbe disease (globoid cell leukodystrophy): diagnostic and clinical implications."
Wenger D.A., Rafi M.A., Luzi P.
Hum. Mutat. 10:268-279(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON GLD MUTATIONS.
[10]"Krabbe disease: genetic aspects and progress toward therapy."
Wenger D.A., Rafi M.A., Luzi P., Datto J., Costantino-Ceccarini E.
Mol. Genet. Metab. 70:1-9(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[11]"A large deletion together with a point mutation in the GALC gene is a common mutant allele in patients with infantile Krabbe disease."
Rafi M.A., Luzi P., Chen Y.Q., Wenger D.A.
Hum. Mol. Genet. 4:1285-1289(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-184.
[12]"Molecular defects in Krabbe disease."
Tatsumi N., Inui K., Sakai N., Fukushima H., Nishimoto J., Yanagihara I., Nishigaki T., Tsukamoto H., Fu L., Taniike M., Okada S.
Hum. Mol. Genet. 4:1865-1868(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLD ALA-318 AND GLY-566.
[13]"Molecular heterogeneity of late-onset forms of globoid-cell leukodystrophy."
De Gasperi R., Gama Sosa M.A., Sartorato E.L., Battistini S., MacFarlane H., Gusella J.F., Krivit W., Kolodny E.H.
Am. J. Hum. Genet. 59:1233-1242(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLD HIS-79; SER-111; LEU-117; THR-250; SER-284 AND CYS-314, VARIANT THR-562.
[14]Erratum
De Gasperi R., Gama Sosa M.A., Sartorato E.L., Battistini S., MacFarlane H., Gusella J.F., Krivit W., Kolodny E.H.
Am. J. Hum. Genet. 60:1264-1264(1997)
[15]"Two different mutations are responsible for Krabbe disease in the Druze and Moslem Arab populations in Israel."
Rafi M.A., Luzi P., Zlotogora J., Wenger D.A.
Hum. Genet. 97:304-308(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLD ASN-544 AND SER-599.
[16]"Adult onset globoid cell leukodystrophy (Krabbe disease): analysis of galactosylceramidase cDNA from four Japanese patients."
Furuya H., Kukita Y.-J., Nagano S., Sakai Y., Yamashita Y., Fukuyama H., Inatomi Y., Saito Y., Koike R., Tsuji S., Fukumaki Y., Hayashi K., Kobayashi T.
Hum. Genet. 100:450-456(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLD MET-82; ASP-286 AND SER-634, VARIANTS VAL-305 AND THR-562.
[17]"Molecular basis of late-life globoid cell leukodystrophy."
De Gasperi R., Gama Sosa M.A., Sartorato E.L., Battistini S., Raghavan S., Kolodny E.H.
Hum. Mutat. 14:256-262(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLD ASP-286 AND ARG-553, VARIANT THR-641.
[18]"Molecular heterogeneity of Krabbe disease."
Fu L., Inui K., Nishigaki T., Tatsumi N., Tsukamoto H., Kokubu C., Muramatsu T., Okada S.
J. Inherit. Metab. Dis. 22:155-162(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLD ARG-59; PHE-68; ILE-278; CYS-335; GLY-426; HIS-531 AND ARG-668.
[19]"A single mutation in the GALC gene is responsible for the majority of late onset Krabbe disease patients in the Catania (Sicily, Italy) region."
Lissens W., Arena A., Seneca S., Rafi M., Sorge G., Liebaers I., Wenger D., Fiumara A.
Hum. Mutat. 28:742-742(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLD SER-41.
[20]"Identification and characterization of 15 novel GALC gene mutations causing Krabbe disease."
Tappino B., Biancheri R., Mort M., Regis S., Corsolini F., Rossi A., Stroppiano M., Lualdi S., Fiumara A., Bembi B., Di Rocco M., Cooper D.N., Filocamo M.
Hum. Mutat. 31:E1894-E1914(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLD LYS-130; ARG-318; ARG-323; THR-384; LEU-396 AND ASN-490, VARIANTS PRO-21; CYS-184; ASN-248; THR-562 AND THR-641.
[21]"Four novel GALC gene mutations in two Chinese patients with Krabbe disease."
Yang Y., Ren X., Xu Q., Wang C., Liu H., He X.
Gene 519:381-384(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLD MET-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L38559 expand/collapse EMBL AC list , L38544, L38545, L38546, L38547, L38548, L38549, L38550, L38551, L38552, L38553, L38555, L38556, L38557, L38558 Genomic DNA. Translation: AAA80975.1. Different initiation.
D86181 Genomic DNA. Translation: BAA24902.1. Different initiation.
AK296530 mRNA. Translation: BAG59160.1. Different initiation.
AK302519 mRNA. Translation: BAG63793.1.
AK302683 mRNA. Translation: BAH13778.1.
AK302956 mRNA. Translation: BAG64110.1.
AL136501 Genomic DNA. No translation available.
AL157955 Genomic DNA. No translation available.
L23116 mRNA. Translation: AAA16645.1. Different initiation.
D25283 mRNA. Translation: BAA04971.1. Different initiation.
D25284 mRNA. Translation: BAA04972.1. Sequence problems.
BC036518 mRNA. Translation: AAH36518.1. Different initiation.
CCDSCCDS55936.1. [P54803-3]
CCDS55937.1. [P54803-4]
CCDS9878.2. [P54803-1]
PIRI54205.
RefSeqNP_000144.2. NM_000153.3.
NP_001188330.1. NM_001201401.1.
NP_001188331.1. NM_001201402.1.
UniGeneHs.513439.

3D structure databases

ProteinModelPortalP54803.
SMRP54803. Positions 41-685.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108854. 1 interaction.
STRING9606.ENSP00000261304.

Protein family/group databases

CAZyGH59. Glycoside Hydrolase Family 59.

PTM databases

PhosphoSiteP54803.

Polymorphism databases

DMDM229462868.

Proteomic databases

MaxQBP54803.
PaxDbP54803.
PRIDEP54803.

Protocols and materials databases

DNASU2581.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000544807; ENSP00000437513; ENSG00000054983. [P54803-5]
GeneID2581.
KEGGhsa:2581.
UCSCuc001xvu.2. human. [P54803-1]
uc010tvx.2. human. [P54803-4]
uc010tvz.1. human. [P54803-5]

Organism-specific databases

CTD2581.
GeneCardsGC14M088399.
GeneReviewsGALC.
H-InvDBHIX0026669.
HGNCHGNC:4115. GALC.
HPACAB022196.
MIM245200. phenotype.
606890. gene.
neXtProtNX_P54803.
Orphanet206448. Adult Krabbe disease.
206436. Infantile Krabbe disease.
206443. Late-infantile/juvenile Krabbe disease.
PharmGKBPA28530.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG76999.
HOGENOMHOG000068033.
HOVERGENHBG005800.
InParanoidP54803.
KOK01202.
PhylomeDBP54803.
TreeFamTF312985.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP54803.
BgeeP54803.
CleanExHS_GALC.
GenevestigatorP54803.

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

ChiTaRSGALC. human.
GeneWikiGalactosylceramidase.
GenomeRNAi2581.
NextBio10207.
PROP54803.
SOURCESearch...

Entry information

Entry nameGALC_HUMAN
AccessionPrimary (citable) accession number: P54803
Secondary accession number(s): B4DKE8 expand/collapse secondary AC list , B4DYN1, B4DZJ8, B7Z7Z2, J3KN25, J3KPP8, Q8J030
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries