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Galactocerebrosidase (GALCERase) (EC 3.2.1.46) (Galactocerebroside beta-galactosidase) (Galactosylceramidase) (Galactosylceramide beta-galactosidase)

 GALC_HUMAN              Reviewed;         685 AA.
P54803; B4DKE8; B4DYN1; B4DZJ8; B7Z7Z2; J3KN25; J3KPP8; Q8J030;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
08-JUN-2016, sequence version 3.
18-JUL-2018, entry version 172.
RecName: Full=Galactocerebrosidase;
Short=GALCERase;
EC=3.2.1.46;
AltName: Full=Galactocerebroside beta-galactosidase;
AltName: Full=Galactosylceramidase;
AltName: Full=Galactosylceramide beta-galactosidase;
Flags: Precursor;
Name=GALC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-562.
PubMed=7601472; DOI=10.1016/0888-7543(95)80230-J;
Luzi P., Rafi M.A., Wenger D.A.;
"Structure and organization of the human galactocerebrosidase (GALC)
gene.";
Genomics 26:407-409(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9434153; DOI=10.1016/S0167-4781(97)00140-1;
Sakai N., Fukushima H., Inui K., Fu L., Nishigaki T., Yanagihara I.,
Tatsumi N., Ozono K., Okada S.;
"Human galactocerebrosidase gene: promoter analysis of the 5'-flanking
region and structural organization.";
Biochim. Biophys. Acta 1395:62-67(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 2-685 (ISOFORM 3), AND VARIANTS CYS-184
AND THR-562.
TISSUE=Testis, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-641.
PubMed=12508121; DOI=10.1038/nature01348;
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., 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.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-685 (ISOFORM 1), PROTEIN SEQUENCE OF
43-75 AND 452-470, CATALYTIC ACTIVITY, AND FUNCTION.
TISSUE=Testis;
PubMed=8281145; DOI=10.1093/hmg/2.11.1841;
Chen Y.Q., Rafi M.A., de Gala G., Wenger D.A.;
"Cloning and expression of cDNA encoding human galactocerebrosidase,
the enzyme deficient in globoid cell leukodystrophy.";
Hum. Mol. Genet. 2:1841-1845(1993).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-685 (ISOFORM 1), AND PARTIAL PROTEIN
SEQUENCE.
TISSUE=Placenta, and Skin fibroblast;
PubMed=8297359; DOI=10.1006/bbrc.1994.1071;
Sakai N., Inui K., Fujii N., Fukushima H., Nishimoto J.,
Yanagihara I., Isegawa Y., Iwamatsu A., Okada S.;
"Krabbe disease: isolation and characterization of a full-length cDNA
for human galactocerebrosidase.";
Biochem. Biophys. Res. Commun. 198:485-491(1994).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-685 (ISOFORM 1), AND
VARIANT THR-562.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 43-61 AND 452-470, PARTIAL PROTEIN SEQUENCE,
FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
TISSUE=Urine;
PubMed=8399327; DOI=10.1016/0005-2760(93)90175-9;
Chen Y.Q., Wenger D.A.;
"Galactocerebrosidase from human urine: purification and partial
characterization.";
Biochim. Biophys. Acta 1170:53-61(1993).
[9]
REVIEW ON GLD MUTATIONS.
PubMed=9338580;
DOI=10.1002/(SICI)1098-1004(1997)10:4<268::AID-HUMU2>3.0.CO;2-D;
Wenger D.A., Rafi M.A., Luzi P.;
"Molecular genetics of Krabbe disease (globoid cell leukodystrophy):
diagnostic and clinical implications.";
Hum. Mutat. 10:268-279(1997).
[10]
REVIEW ON VARIANTS.
PubMed=10833326; DOI=10.1006/mgme.2000.2990;
Wenger D.A., Rafi M.A., Luzi P., Datto J., Costantino-Ceccarini E.;
"Krabbe disease: genetic aspects and progress toward therapy.";
Mol. Genet. Metab. 70:1-9(2000).
[11]
VARIANT CYS-184.
PubMed=7581365; DOI=10.1093/hmg/4.8.1285;
Rafi M.A., Luzi P., Chen Y.Q., Wenger D.A.;
"A large deletion together with a point mutation in the GALC gene is a
common mutant allele in patients with infantile Krabbe disease.";
Hum. Mol. Genet. 4:1285-1289(1995).
[12]
VARIANTS GLD ALA-318 AND GLY-566.
PubMed=8595408; DOI=10.1093/hmg/4.10.1865;
Tatsumi N., Inui K., Sakai N., Fukushima H., Nishimoto J.,
Yanagihara I., Nishigaki T., Tsukamoto H., Fu L., Taniike M.,
Okada S.;
"Molecular defects in Krabbe disease.";
Hum. Mol. Genet. 4:1865-1868(1995).
[13]
VARIANTS GLD HIS-79; SER-111; LEU-117; THR-250; SER-284 AND CYS-314,
AND VARIANT THR-562.
PubMed=8940268;
De Gasperi R., Gama Sosa M.A., Sartorato E.L., Battistini S.,
MacFarlane H., Gusella J.F., Krivit W., Kolodny E.H.;
"Molecular heterogeneity of late-onset forms of globoid-cell
leukodystrophy.";
Am. J. Hum. Genet. 59:1233-1242(1996).
[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]
VARIANTS GLD ASN-544 AND SER-599.
PubMed=8786069; DOI=10.1007/BF02185759;
Rafi M.A., Luzi P., Zlotogora J., Wenger D.A.;
"Two different mutations are responsible for Krabbe disease in the
Druze and Moslem Arab populations in Israel.";
Hum. Genet. 97:304-308(1996).
[16]
VARIANTS GLD MET-82; ASP-286 AND SER-634, AND VARIANTS VAL-305 AND
THR-562.
PubMed=9272171; DOI=10.1007/s004390050532;
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.;
"Adult onset globoid cell leukodystrophy (Krabbe disease): analysis of
galactosylceramidase cDNA from four Japanese patients.";
Hum. Genet. 100:450-456(1997).
[17]
VARIANTS GLD ASP-286 AND ARG-553, VARIANT ALA-641, AND
CHARACTERIZATION OF VARIANT GLD ASP-286.
PubMed=10477434;
DOI=10.1002/(SICI)1098-1004(1999)14:3<256::AID-HUMU9>3.0.CO;2-6;
De Gasperi R., Gama Sosa M.A., Sartorato E.L., Battistini S.,
Raghavan S., Kolodny E.H.;
"Molecular basis of late-life globoid cell leukodystrophy.";
Hum. Mutat. 14:256-262(1999).
[18]
VARIANTS GLD ARG-59; PHE-68; ILE-278; CYS-335; GLY-426; HIS-531 AND
ARG-668.
PubMed=10234611; DOI=10.1023/A:1005449919660;
Fu L., Inui K., Nishigaki T., Tatsumi N., Tsukamoto H., Kokubu C.,
Muramatsu T., Okada S.;
"Molecular heterogeneity of Krabbe disease.";
J. Inherit. Metab. Dis. 22:155-162(1999).
[19]
VARIANT GLD SER-41.
PubMed=17579360; DOI=10.1002/humu.9500;
Lissens W., Arena A., Seneca S., Rafi M., Sorge G., Liebaers I.,
Wenger D., Fiumara A.;
"A single mutation in the GALC gene is responsible for the majority of
late onset Krabbe disease patients in the Catania (Sicily, Italy)
region.";
Hum. Mutat. 28:742-742(2007).
[20]
VARIANTS GLD LYS-130; ARG-318; ARG-323; THR-384; LEU-396 AND ASN-490,
AND VARIANTS PRO-21; CYS-184; ASN-248; THR-562 AND ALA-641.
PubMed=20886637; DOI=10.1002/humu.21367;
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.;
"Identification and characterization of 15 novel GALC gene mutations
causing Krabbe disease.";
Hum. Mutat. 31:E1894-E1914(2010).
[21]
VARIANT GLD MET-681.
PubMed=23462331; DOI=10.1016/j.gene.2013.02.010;
Yang Y., Ren X., Xu Q., Wang C., Liu H., He X.;
"Four novel GALC gene mutations in two Chinese patients with Krabbe
disease.";
Gene 519:381-384(2013).
-!- 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. {ECO:0000269|PubMed:8281145,
ECO:0000269|PubMed:8399327}.
-!- CATALYTIC ACTIVITY: D-galactosyl-N-acylsphingosine + H(2)O = D-
galactose + N-acylsphingosine. {ECO:0000269|PubMed:8281145,
ECO:0000269|PubMed:8399327}.
-!- 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.;
-!- SUBCELLULAR LOCATION: Lysosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P54803-1; Sequence=Displayed;
Name=3;
IsoId=P54803-3; Sequence=VSP_036976;
Note=No experimental confirmation available.;
Name=4;
IsoId=P54803-4; Sequence=VSP_036974;
Note=Ref.3 (BAG64110) sequence is in conflict in position:
17:A->T. {ECO:0000305};
Name=5;
IsoId=P54803-5; Sequence=VSP_036975, VSP_036977;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in urine. Detected in testis, brain
and placenta (at protein level). Detected in kidney and liver.
{ECO:0000269|PubMed:8399327}.
-!- POLYMORPHISM: Polymorphic amino-acid changes are responsible for
the wide range of catalytic activities found in the general
population.
-!- 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.
{ECO:0000269|PubMed:10234611, ECO:0000269|PubMed:10477434,
ECO:0000269|PubMed:17579360, ECO:0000269|PubMed:20886637,
ECO:0000269|PubMed:23462331, ECO:0000269|PubMed:8595408,
ECO:0000269|PubMed:8786069, ECO:0000269|PubMed:8940268,
ECO:0000269|PubMed:9272171}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 59 family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA16645.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA80975.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH36518.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA04971.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA04972.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA04972.1; Type=Miscellaneous discrepancy; Note=Probable intron retention.; Evidence={ECO:0000305};
Sequence=BAA24902.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG59160.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; L38559; AAA80975.1; ALT_INIT; Genomic_DNA.
EMBL; L38544; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38545; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38546; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38547; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38548; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38549; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38550; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38551; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38552; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38553; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38555; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38556; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38557; AAA80975.1; JOINED; Genomic_DNA.
EMBL; L38558; AAA80975.1; JOINED; Genomic_DNA.
EMBL; D86181; BAA24902.1; ALT_INIT; Genomic_DNA.
EMBL; AK296530; BAG59160.1; ALT_INIT; mRNA.
EMBL; AK302519; BAG63793.1; -; mRNA.
EMBL; AK302683; BAH13778.1; -; mRNA.
EMBL; AK302956; BAG64110.1; -; mRNA.
EMBL; AL136501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL157955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L23116; AAA16645.1; ALT_INIT; mRNA.
EMBL; D25283; BAA04971.1; ALT_INIT; mRNA.
EMBL; D25284; BAA04972.1; ALT_SEQ; mRNA.
EMBL; BC036518; AAH36518.1; ALT_INIT; mRNA.
CCDS; CCDS55936.1; -. [P54803-3]
CCDS; CCDS55937.1; -. [P54803-4]
CCDS; CCDS9878.2; -. [P54803-1]
PIR; I54205; I54205.
RefSeq; NP_000144.2; NM_000153.3. [P54803-1]
RefSeq; NP_001188330.1; NM_001201401.1. [P54803-3]
RefSeq; NP_001188331.1; NM_001201402.1. [P54803-4]
UniGene; Hs.513439; -.
ProteinModelPortal; P54803; -.
SMR; P54803; -.
BioGrid; 108854; 16.
IntAct; P54803; 4.
STRING; 9606.ENSP00000261304; -.
ChEMBL; CHEMBL3713095; -.
SwissLipids; SLP:000000644; -.
CAZy; GH59; Glycoside Hydrolase Family 59.
iPTMnet; P54803; -.
PhosphoSitePlus; P54803; -.
BioMuta; GALC; -.
DMDM; 229462868; -.
EPD; P54803; -.
PaxDb; P54803; -.
PeptideAtlas; P54803; -.
PRIDE; P54803; -.
ProteomicsDB; 56722; -.
ProteomicsDB; 56723; -. [P54803-3]
ProteomicsDB; 56724; -. [P54803-4]
ProteomicsDB; 56725; -. [P54803-5]
DNASU; 2581; -.
Ensembl; ENST00000261304; ENSP00000261304; ENSG00000054983. [P54803-1]
Ensembl; ENST00000393568; ENSP00000377198; ENSG00000054983. [P54803-3]
Ensembl; ENST00000393569; ENSP00000377199; ENSG00000054983. [P54803-4]
Ensembl; ENST00000544807; ENSP00000437513; ENSG00000054983. [P54803-5]
GeneID; 2581; -.
KEGG; hsa:2581; -.
UCSC; uc010tvz.2; human. [P54803-1]
CTD; 2581; -.
DisGeNET; 2581; -.
EuPathDB; HostDB:ENSG00000054983.16; -.
GeneCards; GALC; -.
GeneReviews; GALC; -.
H-InvDB; HIX0026669; -.
HGNC; HGNC:4115; GALC.
HPA; CAB022196; -.
MalaCards; GALC; -.
MIM; 245200; phenotype.
MIM; 606890; gene.
neXtProt; NX_P54803; -.
OpenTargets; ENSG00000054983; -.
Orphanet; 206448; Adult Krabbe disease.
Orphanet; 206436; Infantile Krabbe disease.
Orphanet; 206443; Late-infantile/juvenile Krabbe disease.
PharmGKB; PA28530; -.
eggNOG; ENOG410IITE; Eukaryota.
eggNOG; ENOG410XTIS; LUCA.
GeneTree; ENSGT00390000003303; -.
HOGENOM; HOG000068033; -.
HOVERGEN; HBG005800; -.
InParanoid; P54803; -.
KO; K01202; -.
OMA; FWIFANG; -.
PhylomeDB; P54803; -.
TreeFam; TF312985; -.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
ChiTaRS; GALC; human.
GeneWiki; Galactosylceramidase; -.
GenomeRNAi; 2581; -.
PRO; PR:P54803; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000054983; -.
CleanEx; HS_GALC; -.
ExpressionAtlas; P54803; baseline and differential.
Genevisible; P54803; HS.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; TAS:ProtInc.
GO; GO:0004336; F:galactosylceramidase activity; ISS:UniProtKB.
GO; GO:0006683; P:galactosylceramide catabolic process; ISS:UniProtKB.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR001286; Glyco_hydro_59.
InterPro; IPR035394; Glyco_hydro_59_dom.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR15172; PTHR15172; 1.
Pfam; PF02057; Glyco_hydro_59; 1.
Pfam; PF17387; Glyco_hydro_59M; 1.
PRINTS; PR00850; GLHYDRLASE59.
SUPFAM; SSF51445; SSF51445; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Glycosidase;
Hydrolase; Leukodystrophy; Lipid degradation; Lipid metabolism;
Lysosome; Polymorphism; Reference proteome; Signal;
Sphingolipid metabolism.
SIGNAL 1 42 {ECO:0000269|PubMed:8281145,
ECO:0000269|PubMed:8399327}.
CHAIN 43 685 Galactocerebrosidase.
/FTId=PRO_0000012230.
ACT_SITE 198 198 Proton donor/acceptor. {ECO:0000250}.
ACT_SITE 274 274 Nucleophile. {ECO:0000250}.
BINDING 109 109 Substrate. {ECO:0000250}.
BINDING 151 151 Substrate. {ECO:0000250}.
BINDING 197 197 Substrate. {ECO:0000250}.
BINDING 396 396 Substrate. {ECO:0000250}.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 403 403 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 556 556 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 559 559 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 602 602 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 287 394 {ECO:0000250}.
VAR_SEQ 1 65 MAEWLLSASWQRRAKAMTAAAGSAGRAAVPLLLCALLAPGG
AYVLDDSDGLGREFDGIGAVSGGG -> MLGKSHGRATHGP
LPLADLGIHLPCVKVLHQVTPEEKPA (in isoform
4). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_036974.
VAR_SEQ 1 65 MAEWLLSASWQRRAKAMTAAAGSAGRAAVPLLLCALLAPGG
AYVLDDSDGLGREFDGIGAVSGGG -> MGFMVADLW (in
isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036975.
VAR_SEQ 66 88 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036976.
VAR_SEQ 638 685 GHFTSGMLNDKSLWTDIPVNFPKNGWAAIGTHSFEFAQFDN
FLVEATR -> VAGRRKKT (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036977.
VARIANT 21 21 A -> P (in dbSNP:rs111887056).
{ECO:0000269|PubMed:20886637}.
/FTId=VAR_064430.
VARIANT 41 41 G -> S (in GLD; dbSNP:rs387906955).
{ECO:0000269|PubMed:17579360}.
/FTId=VAR_064431.
VARIANT 59 59 G -> R (in GLD; infantile; significant
reduction of activity).
{ECO:0000269|PubMed:10234611}.
/FTId=VAR_013956.
VARIANT 68 68 S -> F (in GLD; infantile; significant
reduction of activity).
{ECO:0000269|PubMed:10234611}.
/FTId=VAR_013957.
VARIANT 79 79 R -> H (in GLD; dbSNP:rs370117160).
{ECO:0000269|PubMed:8940268}.
/FTId=VAR_013958.
VARIANT 82 82 I -> M (in GLD; adult; reduction of
activity; when associated with V-2105).
{ECO:0000269|PubMed:9272171}.
/FTId=VAR_013959.
VARIANT 111 111 G -> D (in GLD; dbSNP:rs746487628).
/FTId=VAR_003380.
VARIANT 111 111 G -> S (in GLD; dbSNP:rs756690487).
{ECO:0000269|PubMed:8940268}.
/FTId=VAR_003381.
VARIANT 112 112 T -> A (in GLD; adult;
dbSNP:rs147313927).
/FTId=VAR_003382.
VARIANT 117 117 M -> L (in GLD; adult).
{ECO:0000269|PubMed:8940268}.
/FTId=VAR_003383.
VARIANT 130 130 E -> K (in GLD; dbSNP:rs374635469).
{ECO:0000269|PubMed:20886637}.
/FTId=VAR_064432.
VARIANT 184 184 R -> C (in dbSNP:rs1805078).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:20886637,
ECO:0000269|PubMed:7581365}.
/FTId=VAR_013960.
VARIANT 187 187 D -> V (in GLD; dbSNP:rs997021099).
/FTId=VAR_003384.
VARIANT 194 194 G -> A (in GLD; dbSNP:rs963756824).
/FTId=VAR_003385.
VARIANT 248 248 D -> N (in dbSNP:rs34362748).
{ECO:0000269|PubMed:20886637}.
/FTId=VAR_003386.
VARIANT 250 250 I -> T (in GLD; late infantile;
dbSNP:rs886039569).
{ECO:0000269|PubMed:8940268}.
/FTId=VAR_003387.
VARIANT 263 263 A -> T (in GLD).
/FTId=VAR_003388.
VARIANT 278 278 T -> I (in GLD; infantile; significant
reduction of activity).
{ECO:0000269|PubMed:10234611}.
/FTId=VAR_013961.
VARIANT 284 284 G -> S (in GLD; dbSNP:rs377274761).
{ECO:0000269|PubMed:8940268}.
/FTId=VAR_003389.
VARIANT 286 286 G -> D (in GLD; significant reduction of
activity; dbSNP:rs199847983).
{ECO:0000269|PubMed:10477434,
ECO:0000269|PubMed:9272171}.
/FTId=VAR_003390.
VARIANT 295 295 N -> T (in GLD; dbSNP:rs746922378).
/FTId=VAR_003391.
VARIANT 303 303 S -> F (in GLD; infantile;
dbSNP:rs756352952).
/FTId=VAR_003392.
VARIANT 305 305 I -> V (in dbSNP:rs74887188).
{ECO:0000269|PubMed:9272171}.
/FTId=VAR_013962.
VARIANT 314 314 Y -> C (in GLD).
{ECO:0000269|PubMed:8940268}.
/FTId=VAR_013963.
VARIANT 318 318 P -> A (in GLD; dbSNP:rs1057516642).
{ECO:0000269|PubMed:8595408}.
/FTId=VAR_003393.
VARIANT 318 318 P -> R (in GLD; dbSNP:rs387906954).
{ECO:0000269|PubMed:20886637}.
/FTId=VAR_064433.
VARIANT 323 323 G -> R (in GLD).
{ECO:0000269|PubMed:20886637}.
/FTId=VAR_064434.
VARIANT 335 335 Y -> C (in GLD; infantile; significant
reduction of activity;
dbSNP:rs757407613).
{ECO:0000269|PubMed:10234611}.
/FTId=VAR_013964.
VARIANT 384 384 I -> T (in GLD).
{ECO:0000269|PubMed:20886637}.
/FTId=VAR_064435.
VARIANT 396 396 R -> L (in GLD).
{ECO:0000269|PubMed:20886637}.
/FTId=VAR_064436.
VARIANT 396 396 R -> W (in GLD; bilateral cherry red
spots; dbSNP:rs770485731).
/FTId=VAR_003394.
VARIANT 400 400 P -> L (in GLD).
/FTId=VAR_003395.
VARIANT 426 426 W -> G (in GLD; infantile; significant
reduction of activity).
{ECO:0000269|PubMed:10234611}.
/FTId=VAR_013965.
VARIANT 468 468 T -> S (in GLD; unknown pathological
significance; dbSNP:rs34134328).
{ECO:0000269|PubMed:9338580}.
/FTId=VAR_003396.
VARIANT 490 490 Y -> N (in GLD; dbSNP:rs202135871).
{ECO:0000269|PubMed:20886637}.
/FTId=VAR_064437.
VARIANT 514 514 F -> S (in GLD; dbSNP:rs375867319).
/FTId=VAR_003397.
VARIANT 529 529 T -> M (in GLD; infantile;
dbSNP:rs200960659).
/FTId=VAR_003398.
VARIANT 531 531 R -> C (in GLD; dbSNP:rs749893889).
/FTId=VAR_003399.
VARIANT 531 531 R -> H (in GLD; infantile; significant
reduction of activity;
dbSNP:rs200378205).
{ECO:0000269|PubMed:10234611}.
/FTId=VAR_013966.
VARIANT 544 544 D -> N (in GLD; Arab patients;
dbSNP:rs387906952).
{ECO:0000269|PubMed:8786069}.
/FTId=VAR_003400.
VARIANT 553 553 G -> R (in GLD; loss of activity;
dbSNP:rs748573754).
{ECO:0000269|PubMed:10477434}.
/FTId=VAR_013967.
VARIANT 562 562 I -> T (common polymorphism;
dbSNP:rs398607).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:20886637,
ECO:0000269|PubMed:7601472,
ECO:0000269|PubMed:8940268,
ECO:0000269|PubMed:9272171}.
/FTId=VAR_003401.
VARIANT 566 566 V -> G (in GLD).
{ECO:0000269|PubMed:8595408}.
/FTId=VAR_003402.
VARIANT 567 567 Y -> S (in GLD; dbSNP:rs752537626).
/FTId=VAR_003403.
VARIANT 592 592 A -> S (in GLD).
/FTId=VAR_003404.
VARIANT 599 599 I -> S (in GLD; infantile; Druze
patients; dbSNP:rs387906953).
{ECO:0000269|PubMed:8786069}.
/FTId=VAR_003405.
VARIANT 634 634 L -> S (in GLD; adult;
dbSNP:rs138577661).
{ECO:0000269|PubMed:9272171}.
/FTId=VAR_013968.
VARIANT 641 641 T -> A (in dbSNP:rs421262).
{ECO:0000269|PubMed:10477434,
ECO:0000269|PubMed:12508121,
ECO:0000269|PubMed:20886637}.
/FTId=VAR_003406.
VARIANT 645 645 L -> R (in GLD; adult;
dbSNP:rs780593419).
/FTId=VAR_003407.
VARIANT 668 668 T -> R (in GLD; infantile; significant
reduction of activity).
{ECO:0000269|PubMed:10234611}.
/FTId=VAR_013969.
VARIANT 681 681 V -> M (in GLD; dbSNP:rs200607029).
{ECO:0000269|PubMed:23462331}.
/FTId=VAR_069512.
CONFLICT 78 78 Y -> H (in Ref. 1; BAH13778).
{ECO:0000305}.
CONFLICT 195 195 I -> T (in Ref. 3; BAG64110).
{ECO:0000305}.
CONFLICT 422 422 E -> G (in Ref. 3; BAG64110).
{ECO:0000305}.
SEQUENCE 685 AA; 77063 MW; 03F3D223381AD5B1 CRC64;
MAEWLLSASW QRRAKAMTAA AGSAGRAAVP LLLCALLAPG GAYVLDDSDG LGREFDGIGA
VSGGGATSRL LVNYPEPYRS QILDYLFKPN FGASLHILKV EIGGDGQTTD GTEPSHMHYA
LDENYFRGYE WWLMKEAKKR NPNITLIGLP WSFPGWLGKG FDWPYVNLQL TAYYVVTWIV
GAKRYHDLDI DYIGIWNERS YNANYIKILR KMLNYQGLQR VKIIASDNLW ESISASMLLD
AELFKVVDVI GAHYPGTHSA KDAKLTGKKL WSSEDFSTLN SDMGAGCWGR ILNQNYINGY
MTSTIAWNLV ASYYEQLPYG RCGLMTAQEP WSGHYVVESP VWVSAHTTQF TQPGWYYLKT
VGHLEKGGSY VALTDGLGNL TIIIETMSHK HSKCIRPFLP YFNVSQQFAT FVLKGSFSEI
PELQVWYTKL GKTSERFLFK QLDSLWLLDS DGSFTLSLHE DELFTLTTLT TGRKGSYPLP
PKSQPFPSTY KDDFNVDYPF FSEAPNFADQ TGVFEYFTNI EDPGEHHFTL RQVLNQRPIT
WAADASNTIS IIGDYNWTNL TIKCDVYIET PDTGGVFIAG RVNKGGILIR SARGIFFWIF
ANGSYRVTGD LAGWIIYALG RVEVTAKKWY TLTLTIKGHF TSGMLNDKSL WTDIPVNFPK
NGWAAIGTHS FEFAQFDNFL VEATR


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