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Alpha-galactosidase A (EC 3.2.1.22) (Alpha-D-galactosidase A) (Alpha-D-galactoside galactohydrolase) (Melibiase) (Agalsidase)

 AGAL_HUMAN              Reviewed;         429 AA.
P06280; Q6LER7;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
30-AUG-2017, entry version 201.
RecName: Full=Alpha-galactosidase A;
EC=3.2.1.22 {ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:27211852};
AltName: Full=Alpha-D-galactosidase A;
AltName: Full=Alpha-D-galactoside galactohydrolase;
AltName: Full=Melibiase;
AltName: INN=Agalsidase;
Flags: Precursor;
Name=GLA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=3036505; DOI=10.1111/j.1432-1033.1987.tb11438.x;
Tsuji S., Martin B.M., Kaslow D.C., Migeon B.R., Choudary P.V.,
Stubblefield B.K., Mayor J.A., Murray G.J., Barranger J.A.,
Ginns E.I.;
"Signal sequence and DNA-mediated expression of human lysosomal alpha-
galactosidase A.";
Eur. J. Biochem. 165:275-280(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lymphoblast;
PubMed=2542896; DOI=10.1093/nar/17.8.3301;
Kornreich R., Desnick R.J., Bishop D.F.;
"Nucleotide sequence of the human alpha-galactosidase A gene.";
Nucleic Acids Res. 17:3301-3302(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7626884; DOI=10.1007/BF00364796;
Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W.,
Gibbs R.A.;
"Sixty-nine kilobases of contiguous human genomic sequence containing
the alpha-galactosidase A and Bruton's tyrosine kinase loci.";
Mamm. Genome 6:334-338(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 27-429, AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Lung;
PubMed=3014515; DOI=10.1073/pnas.83.13.4859;
Bishop D.F., Calhoun D.H., Bernstein H.S., Hantzopoulos P., Quinn M.,
Desnick R.J.;
"Human alpha-galactosidase A: nucleotide sequence of a cDNA clone
encoding the mature enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 83:4859-4863(1986).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
PubMed=2892762; DOI=10.1016/0378-1119(87)90374-X;
Quinn M., Hantzopoulos P., Fidanza V., Calhoun D.H.;
"A genomic clone containing the promoter for the gene encoding the
human lysosomal enzyme, alpha-galactosidase A.";
Gene 58:177-188(1987).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
PubMed=2836863; DOI=10.1073/pnas.85.11.3903;
Bishop D.F., Kornreich R., Desnick R.J.;
"Structural organization of the human alpha-galactosidase A gene:
further evidence for the absence of a 3' untranslated region.";
Proc. Natl. Acad. Sci. U.S.A. 85:3903-3907(1988).
[9]
RNA EDITING OF POSITION 396.
PubMed=7503918; DOI=10.1093/nar/23.14.2636;
Novo F.J., Kruszewski A., McDermot K.D., Goldspink G., Gorecki D.C.;
"Editing of human alpha-galactosidase RNA resulting in a pyrimidine to
purine conversion.";
Nucleic Acids Res. 23:2636-2640(1995).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-215.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 32-422 IN COMPLEX WITH
PRODUCT, HOMODIMERIZATION, AND GLYCOSYLATION AT ASN-139; ASN-192 AND
ASN-215.
PubMed=15003450; DOI=10.1016/j.jmb.2004.01.035;
Garman S.C., Garboczi D.N.;
"The molecular defect leading to Fabry disease: structure of human
alpha-galactosidase.";
J. Mol. Biol. 337:319-335(2004).
[14]
REVIEW ON FD VARIANTS.
PubMed=7911050; DOI=10.1002/humu.1380030204;
Eng C.M., Desnick R.J.;
"Molecular basis of Fabry disease: mutations and polymorphisms in the
human alpha-galactosidase A gene.";
Hum. Mutat. 3:103-111(1994).
[15]
INVOLVEMENT IN FD, AND VARIANT FD SER-40.
PubMed=2152885; DOI=10.1016/0014-5793(90)80046-L;
Koide T., Ishiura M., Iwai K., Inoue M., Kaneda Y., Okada Y.,
Uchida T.;
"A case of Fabry's disease in a patient with no alpha-galactosidase A
activity caused by a single amino acid substitution of Pro-40 by
Ser.";
FEBS Lett. 259:353-356(1990).
[16]
VARIANT FD VAL-296.
PubMed=1846223; DOI=10.1056/NEJM199102073240607;
von Scheidt W., Eng C.M., Fitzmaurice T.F., Erdmann E., Hubner G.,
Olsen E.G.J., Christomanou H., Kandolf R., Bishop D.F., Desnick R.J.;
"An atypical variant of Fabry's disease with manifestations confined
to the myocardium.";
N. Engl. J. Med. 324:395-399(1991).
[17]
VARIANT FD GLN-301.
PubMed=2171331;
Sakuraba H., Oshima A., Fukuhara Y., Shimmoto M., Nagao Y.,
Bishop D.F., Desnick R.J., Suzuki Y.;
"Identification of point mutations in the alpha-galactosidase A gene
in classical and atypical hemizygotes with Fabry disease.";
Am. J. Hum. Genet. 47:784-789(1990).
[18]
VARIANT FD TRP-356.
PubMed=2539398; DOI=10.1172/JCI114027;
Bernstein H.S., Bishop D.F., Astrin K.H., Kornreich R., Eng C.M.,
Sakuraba H., Desnick R.J.;
"Fabry disease: six gene rearrangements and an exonic point mutation
in the alpha-galactosidase gene.";
J. Clin. Invest. 83:1390-1399(1989).
[19]
VARIANTS FD GLN-66; CYS-112; GLU-279; GLN-301 AND ARG-328.
PubMed=1315715; DOI=10.1007/BF00207037;
Ishii S., Sakuraba H., Suzuki Y.;
"Point mutations in the upstream region of the alpha-galactosidase A
gene exon 6 in an atypical variant of Fabry disease.";
Hum. Genet. 89:29-32(1992).
[20]
VARIANTS FD SER-34; GLY-56; ARG-162; GLN-227; VAL-264; VAL-266;
PHE-297; TYR-313; ALA-328 AND ARG-404 DEL.
PubMed=7504405;
Eng C.M., Resnick-Silverman L.A., Niehaus D.J., Astrin K.H.,
Desnick R.J.;
"Nature and frequency of mutations in the alpha-galactosidase A gene
that cause Fabry disease.";
Am. J. Hum. Genet. 53:1186-1197(1993).
[21]
VARIANTS FD SER-34; SER-215; ALA-269; LYS-327 AND ARG-361.
PubMed=8395937; DOI=10.1093/hmg/2.7.1051;
Davies J.P., Winchester B.G., Malcolm S.;
"Mutation analysis in patients with the typical form of Anderson-Fabry
disease.";
Hum. Mol. Genet. 2:1051-1053(1993).
[22]
VARIANTS FD ARG-35; LEU-49; VAL-165 AND GLU-316.
PubMed=8069316; DOI=10.1093/hmg/3.4.667;
Davies J.P., Christomanou H., Winchester B.G., Malcolm S.;
"Detection of 8 new mutations in the alpha-galactosidase A gene in
Fabry disease.";
Hum. Mol. Genet. 3:667-669(1994).
[23]
VARIANTS FD.
PubMed=7531540; DOI=10.1093/hmg/3.10.1795;
Eng C.M., Niehaus D.J., Enriquez A.L., Burgert T.S., Ludman M.D.,
Desnick R.J.;
"Fabry disease: twenty-three mutations including sense and antisense
CpG alterations and identification of a deletional hot-spot in the
alpha-galactosidase A gene.";
Hum. Mol. Genet. 3:1795-1799(1994).
[24]
VARIANTS FD GLN-66; CYS-112; VAL-156; VAL-166; ALA-260; GLU-279;
ILE-296; GLN-301; LYS-320; ARG-328 AND SER-373.
PubMed=7575533; DOI=10.1006/bbrc.1995.2416;
Okumiya T., Ishii S., Takenaka T., Kase R., Kamei S., Sakuraba H.,
Suzuki Y.;
"Galactose stabilizes various missense mutants of alpha-galactosidase
in Fabry disease.";
Biochem. Biophys. Res. Commun. 214:1219-1224(1995).
[25]
VARIANTS FD TYR-142; VAL-156 AND VAL-166.
PubMed=7759078; DOI=10.1007/BF00223869;
Okumiya T., Ishii S., Kase R., Kamei S., Sakuraba H., Suzuki Y.;
"Alpha-galactosidase gene mutations in Fabry disease: heterogeneous
expressions of mutant enzyme proteins.";
Hum. Genet. 95:557-561(1995).
[26]
VARIANTS FD PRO-32; SER-34; ASP-85; THR-156 AND GLN-301.
PubMed=7599642; DOI=10.1002/humu.1380050316;
Madsen K.M., Hasholt L., Soerensen S.A., Lagerstroem Fermer M.,
Dahl N.;
"Two novel mutations (L32P) and (G85N) among five different missense
mutations in six Danish families with Fabry's disease.";
Hum. Mutat. 5:277-278(1995).
[27]
VARIANTS FD PRO-20 AND ILE-296.
PubMed=7596372; DOI=10.1056/NEJM199508033330504;
Nakao S., Takenaka T., Maeda M., Kodama C., Tanaka A., Tahara M.,
Yoshida A., Kuriyama M., Hayashibe H., Sakuraba H., Tanaka H.;
"An atypical variant of Fabry's disease in men with left ventricular
hypertrophy.";
N. Engl. J. Med. 333:288-293(1995).
[28]
VARIANT FD GLN-301.
PubMed=8738659;
Sawada K., Mizoguchi K., Hishida A., Kaneko E., Koide Y.,
Nishimura K., Kimura M.;
"Point mutation in the alpha-galactosidase A gene of atypical Fabry
disease with only nephropathy.";
Clin. Nephrol. 45:289-294(1996).
[29]
VARIANTS FD VAL-42; SER-49; TYR-56; HIS-92; GLY-93; THR-205; CYS-236;
GLY-287; HIS-298 AND ARG-340.
PubMed=8875188;
Davies J.P., Eng C.M., Hill J.A., Malcolm S., MacDermot K.,
Winchester B.G., Desnick R.J.;
"Fabry disease: fourteen alpha-galactosidase A mutations in unrelated
families from the United Kingdom and other European countries.";
Eur. J. Hum. Genet. 4:219-224(1996).
[30]
VARIANT FD PHE-383 DEL.
PubMed=8834244; DOI=10.1007/BF02267068;
Cariolou M.A., Christodoulides M., Manoli P., Kokkofitou A.,
Tsambaos D.;
"Novel trinucleotide deletion in Fabry's disease.";
Hum. Genet. 97:468-470(1996).
[31]
VARIANTS FD ARG-52; CYS-162; ARG-265 AND 316-VAL--ASP-322 DEL.
PubMed=8931708; DOI=10.1007/s004390050292;
Germain D.P., Biasotto M., Tosi M., Meo T., Kahn A., Poenaru L.;
"Fluorescence-assisted mismatch analysis (FAMA) for exhaustive
screening of the alpha-galactosidase A gene and detection of carriers
in Fabry disease.";
Hum. Genet. 98:719-726(1996).
[32]
VARIANTS FD ARG-52; GLU-128; THR-205; THR-284; LYS-298 AND GLU-358
DEL.
PubMed=8807334;
DOI=10.1002/(SICI)1098-1004(1996)8:1<38::AID-HUMU5>3.0.CO;2-L;
Blanch L.C., Meaney C., Morris C.P.;
"A sensitive mutation screening strategy for Fabry disease: detection
of nine mutations in the alpha-galactosidase A gene.";
Hum. Mutat. 8:38-43(1996).
[33]
VARIANT FD ASN-231.
PubMed=8863162; DOI=10.1136/jmg.33.8.682;
Redonnet-Vernhet I., Ploos van Amstel J.K., Jansen R.P.M.,
Wevers R.A., Salvayre R., Levade T.;
"Uneven X inactivation in a female monozygotic twin pair with Fabry
disease and discordant expression of a novel mutation in the alpha-
galactosidase A gene.";
J. Med. Genet. 33:682-688(1996).
[34]
VARIANTS FD PRO-20; SER-40; GLN-66; VAL-72; CYS-112; TYR-142; VAL-156;
VAL-166; ASN-242; ALA-260; ASP-261; GLU-279; ILE-296; GLN-301;
LYS-320; ARG-328; GLU-358 DEL AND SER-373.
PubMed=9105656; DOI=10.1016/S0387-7604(96)00486-X;
Takata T., Okumiya T., Hayashibe H., Shimmoto M., Kase R., Itoh K.,
Utsumi K., Kamei S., Sakuraba H.;
"Screening and detection of gene mutations in Japanese patients with
Fabry disease by non-radioactive single-stranded conformation
polymorphism analysis.";
Brain Dev. 19:111-116(1997).
[35]
VARIANTS FD VAL-31; 45-ARG-SER-46; ARG-46; CYS-86; PRO-89; THR-91;
TYR-92; TYR-94; VAL-97; THR-100; LEU-113; SER-134; ARG-138; THR-143;
ARG-148; VAL-163; VAL-170; TYR-202; 205-PRO--TYR-207 DEL; ASP-216;
SER-263; CYS-287; SER-298 AND ARG-404 DEL.
PubMed=9100224;
Eng C.M., Ashley G.A., Burgert T.S., Enriquez A.L., D'Souza M.,
Desnick R.J.;
"Fabry disease: thirty-five mutations in the alpha-galactosidase A
gene in patients with classic and variant phenotypes.";
Mol. Med. 3:174-182(1997).
[36]
VARIANT FD THR-65.
PubMed=9554750;
DOI=10.1002/(SICI)1098-1004(1998)11:4<328::AID-HUMU11>3.0.CO;2-N;
Chen C.-H., Shyu P.-W., Wu S.-J., Sheu S.-S., Desnick R.J.,
Hsiao K.-J.;
"Identification of a novel point mutation (S65T) in alpha-
galactosidase A gene in Chinese patients with Fabry disease.";
Hum. Mutat. 11:328-330(1998).
[37]
VARIANT FD LYS-358.
PubMed=9452068;
Miyazaki T., Kajita M., Ohmori S., Mizutani N., Niwa T., Murata Y.,
Seo H.;
"A novel mutation (E358K) in the alpha-galactosidase A gene detected
in a Japanese family with Fabry disease.";
Hum. Mutat. Suppl. 1:S139-S140(1998).
[38]
VARIANT FD VAL-72.
PubMed=9452090;
Okumiya T., Kawamura O., Itoh K., Kase R., Ishii S., Kamei S.,
Sakuraba H.;
"Novel missense mutation (M72V) of alpha-galactosidase gene and its
expression product in an atypical Fabry hemizygote.";
Hum. Mutat. Suppl. 1:S213-S216(1998).
[39]
VARIANTS FD SER-40; SER-215; ASP-224; TYR-313 AND TRP-THR-SER-247 INS.
PubMed=9452111;
Guffon N., Froissart R., Chevalier-Porst F., Maire I.;
"Mutation analysis in 11 French patients with Fabry disease.";
Hum. Mutat. Suppl. 1:S288-S290(1998).
[40]
VARIANTS FD TRP-202; GLY-223; ASP-224; GLN-301 AND LYS-327.
PubMed=10208848; DOI=10.1006/bbrc.1999.0310;
Germain D.P., Poenaru L.;
"Fabry disease: identification of novel alpha-galactosidase A
mutations and molecular carrier detection by use of fluorescent
chemical cleavage of mismatches.";
Biochem. Biophys. Res. Commun. 257:708-713(1999).
[41]
VARIANT FD LYS-341.
PubMed=10090526; DOI=10.1016/S0009-8981(98)00133-8;
Beyer E.M., Karpova E.A., Udalova O.V., Ploos van Amstel J.K.,
van Diggelen O.P., Tsvetkova I.V.;
"The multiple cases of Fabry disease in a Russian family caused by an
E341K amino acid substitution in the alpha-galactosidase A.";
Clin. Chim. Acta 280:81-89(1999).
[42]
CHARACTERIZATION OF VARIANTS FD GLU-279 AND GLN-301.
PubMed=10838196; DOI=10.1016/S0925-4439(00)00024-7;
Kase R., Bierfreund U., Klein A., Kolter T., Utsumi K., Itoh K.,
Sandhoff K., Sakuraba H.;
"Characterization of two alpha-galactosidase mutants (Q279E and R301Q)
found in an atypical variant of Fabry disease.";
Biochim. Biophys. Acta 1501:227-235(2000).
[43]
VARIANTS FD VAL-42; CYS-112; ARG-142; ARG-148; VAL-165; ASP-183;
SER-215; CYS-235; LEU-236; HIS-244; LEU-259; ILE-267; PHE-289;
GLU-321; GLU-358 DEL AND TYR-378.
PubMed=10666480;
Topaloglu A.K., Ashley G.A., Tong B., Shabbeer J., Astrin K.H.,
Eng C.M., Desnick R.J.;
"Twenty novel mutations in the alpha-galactosidase A gene causing
Fabry disease.";
Mol. Med. 5:806-811(1999).
[44]
VARIANT FD ASN-266.
PubMed=11076046; DOI=10.1034/j.1399-0004.2000.580311.x;
Lee J.-K., Kim G.-H., Kim J.-S., Kim K.-K., Lee M.-C., Yoo H.-W.;
"Identification of four novel mutations in five unrelated Korean
families with Fabry disease.";
Clin. Genet. 58:228-233(2000).
[45]
VARIANTS FD LEU-40; SER-95; CYS-112; HIS-112; ASN-148; ARG-172;
VAL-187; SER-224; ARG-226; GLN-227; THR-230; HIS-266; GLN-301 AND
TYR-320.
PubMed=10916280;
Ashton-Prolla P., Tong B., Shabbeer J., Astrin K.H., Eng C.M.,
Desnick R.J.;
"Fabry disease: twenty-two novel mutations in the alpha-galactosidase
A gene and genotype/phenotype correlations in severely and mildly
affected hemizygotes and heterozygotes.";
J. Invest. Med. 48:227-235(2000).
[46]
VARIANT FD ASP-373.
PubMed=11295840; DOI=10.1002/humu.41;
Germain D.P., Salard D., Fellmann F., Azibi K., Caillaud C.,
Bernard M.-C., Poenaru L.;
"Identification of a novel de novo mutation (G373D) in the alpha-
galactosidase A gene (GLA) in a patient affected with Fabry disease.";
Hum. Mutat. 17:353-353(2001).
[47]
VARIANTS FD TYR-46; GLY-47; PRO-49; SER-94; SER-95; CYS-112; SER-113;
THR-143; SER-215; ARG-258; ARG-259; ILE-267; HIS-279; HIS-280;
HIS-298; TYR-313; HIS-363; ASP-377; ALA-409 AND THR-409.
PubMed=11668641; DOI=10.1002/humu.1219;
Blaydon D., Hill J.A., Winchester B.G.;
"Fabry disease: 20 novel GLA mutations in 35 families.";
Hum. Mutat. 18:459-459(2001).
[48]
VARIANT FD PRO-143.
PubMed=11889412; DOI=10.1097/00005792-200203000-00003;
Branton M.H., Schiffmann R., Sabnis S.G., Murray G.J., Quirk J.M.,
Altarescu G., Goldfarb L., Brady R.O., Balow J.E., Austin H.A. III,
Kopp J.B.;
"Natural history of Fabry renal disease: influence of alpha-
galactosidase A activity and genetic mutations on clinical course.";
Medicine (Baltimore) 81:122-138(2002).
[49]
VARIANT FD ALA-410.
PubMed=12694230; DOI=10.1034/j.1399-0004.2003.00050.x;
Yang C.-C., Lai L.-W., Whitehair O., Hwu W.-L., Chiang S.-C.,
Lien Y.-H.H.;
"Two novel mutations in the alpha-galactosidase A gene in Chinese
patients with Fabry disease.";
Clin. Genet. 63:205-209(2003).
[50]
CHARACTERIZATION OF VARIANT FD THR-65.
PubMed=12786754; DOI=10.1034/j.1399-0004.2003.00077.x;
Lai L.-W., Whitehair O., Wu M.-J., O'Meara M., Lien Y.-H.H.;
"Analysis of splice-site mutations of the alpha-galactosidase A gene
in Fabry disease.";
Clin. Genet. 63:476-482(2003).
[51]
VARIANT FD SER-272.
PubMed=15162124; DOI=10.1038/sj.ejhg.5201184;
Verovnik F., Benko D., Vujkovac B., Linthorst G.E.;
"Remarkable variability in renal disease in a large Slovenian family
with Fabry disease.";
Eur. J. Hum. Genet. 12:678-681(2004).
[52]
VARIANTS FD VAL-31; LEU-42; ARG-43; ASN-93; CYS-112; HIS-112; SER-112;
SER-134; VAL-135; ASP-171; PHE-201; SER-215; GLU-234; ASP-261;
TYR-264; VAL-264; GLY-276; PRO-285; PHE-300; ALA-328; VAL-328;
LYS-338; ALA-358; GLU-358 DEL; ARG-404 DEL AND SER-414.
PubMed=15712228; DOI=10.1002/humu.20144;
Shabbeer J., Robinson M., Desnick R.J.;
"Detection of alpha-galactosidase a mutations causing Fabry disease by
denaturing high performance liquid chromatography.";
Hum. Mutat. 25:299-305(2005).
[53]
VARIANT FD THR-143.
PubMed=16533976; DOI=10.1001/archneur.63.3.453;
Nance C.S., Klein C.J., Banikazemi M., Dikman S.H., Phelps R.G.,
McArthur J.C., Rodriguez M., Desnick R.J.;
"Later-onset Fabry disease: an adult variant presenting with the
cramp-fasciculation syndrome.";
Arch. Neurol. 63:453-457(2006).
[54]
VARIANTS FD 12-CYS--LEU-14 DEL; PRO-46; GLN-66; ASN-93; VAL-120;
THR-219; GLN-356 AND CYS-360, AND CHARACTERIZATION OF VARIANTS FD
12-CYS--LEU-14 DEL; PRO-46; GLN-66; ASN-93; VAL-120; THR-219; GLN-356
AND CYS-360.
PubMed=19621417; DOI=10.1002/humu.21074;
Hwu W.L., Chien Y.H., Lee N.C., Chiang S.C., Dobrovolny R.,
Huang A.C., Yeh H.Y., Chao M.C., Lin S.J., Kitagawa T., Desnick R.J.,
Hsu L.W.;
"Newborn screening for Fabry disease in Taiwan reveals a high
incidence of the later-onset GLA mutation c.936+919G>A
(IVS4+919G>A).";
Hum. Mutat. 30:1397-1405(2009).
[55]
CHARACTERIZATION OF VARIANTS FD ASP-20; PRO-20; PRO-21; GLY-33;
GLU-35; TRP-36; SER-40; THR-42; PRO-45; ASP-48; TYR-56; LEU-60;
PHE-64; ASP-80; HIS-86; ASN-91; THR-91; SER-94; TYR-94; ILE-113;
THR-121; LEU-164; GLY-164; GLN-167; PHE-180; VAL-187; SER-196;
THR-198; TYR-202; ARG-204; ARG-213; LEU-214; MET-219; PRO-227;
SER-228; VAL-242; PHE-243; PRO-247; LYS-249; THR-253; ALA-254;
ARG-259; ARG-262; GLY-269; GLY-276; VAL-309; ASN-315; ALA-316;
SER-317; TYR-320; ARG-323; ARG-327; LEU-327; ARG-328; ARG-330;
PRO-342; GLY-352; PRO-356; LYS-358; SER-360; ALA-375; SER-392; SER-399
AND ARG-404 DEL, CHARACTERIZATION OF VARIANTS PRO-3; VAL-3; GLY-71;
THR-154; VAL-289 AND ASN-313, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=26415523; DOI=10.1002/humu.22910;
Lukas J., Scalia S., Eichler S., Pockrandt A.M., Dehn N., Cozma C.,
Giese A.K., Rolfs A.;
"Functional and clinical consequences of novel alpha-galactosidase A
mutations in Fabry disease.";
Hum. Mutat. 37:43-51(2016).
[56]
VARIANT FD ARG-47, CHARACTERIZATION OF VARIANTS FD ARG-47 AND GLY-47,
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=27211852; DOI=10.1080/00207454.2016.1191483;
Ge W., Wei B., Zhu H., Miao Z., Zhang W., Leng C., Li J., Zhang D.,
Sun M., Xu X.;
"A novel mutation of alpha-galactosidase A gene causes Fabry disease
mimicking primary erythromelalgia in a Chinese family.";
Int. J. Neurosci. 2016:1-6(2016).
[57]
VARIANT FD THR-143.
PubMed=27142856; DOI=10.1186/s13023-016-0441-z;
Lenders M., Weidemann F., Kurschat C., Canaan-Kuehl S., Duning T.,
Stypmann J., Schmitz B., Reiermann S., Kraemer J., Blaschke D.,
Wanner C., Brand S.M., Brand E.;
"Alpha-Galactosidase A p.A143T, a non-Fabry disease-causing variant.";
Orphanet J. Rare Dis. 11:54-54(2016).
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing alpha-D-
galactose residues in alpha-D-galactosides, including galactose
oligosaccharides, galactomannans and galactolipids.
{ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:27211852}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15003450}.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- RNA EDITING: Modified_positions=396 {ECO:0000269|PubMed:7503918};
Note=Partially edited.;
-!- DISEASE: Fabry disease (FD) [MIM:301500]: Rare X-linked
sphingolipidosis disease where glycolipid accumulates in many
tissues. The disease consists of an inborn error of
glycosphingolipid catabolism. FD patients show systemic
accumulation of globotriaosylceramide (Gb3) and related
glycosphingolipids in the plasma and cellular lysosomes throughout
the body. Clinical recognition in males results from
characteristic skin lesions (angiokeratomas) over the lower trunk.
Patients may show ocular deposits, febrile episodes, and burning
pain in the extremities. Death results from renal failure, cardiac
or cerebral complications of hypertension or other vascular
disease. Heterozygous females may exhibit the disorder in an
attenuated form, they are more likely to show corneal opacities.
{ECO:0000269|PubMed:10090526, ECO:0000269|PubMed:10208848,
ECO:0000269|PubMed:10666480, ECO:0000269|PubMed:10838196,
ECO:0000269|PubMed:10916280, ECO:0000269|PubMed:11076046,
ECO:0000269|PubMed:11295840, ECO:0000269|PubMed:11668641,
ECO:0000269|PubMed:11889412, ECO:0000269|PubMed:12694230,
ECO:0000269|PubMed:12786754, ECO:0000269|PubMed:1315715,
ECO:0000269|PubMed:15162124, ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:16533976, ECO:0000269|PubMed:1846223,
ECO:0000269|PubMed:19621417, ECO:0000269|PubMed:2152885,
ECO:0000269|PubMed:2171331, ECO:0000269|PubMed:2539398,
ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:27142856,
ECO:0000269|PubMed:27211852, ECO:0000269|PubMed:7504405,
ECO:0000269|PubMed:7531540, ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:7596372, ECO:0000269|PubMed:7599642,
ECO:0000269|PubMed:7759078, ECO:0000269|PubMed:8069316,
ECO:0000269|PubMed:8395937, ECO:0000269|PubMed:8738659,
ECO:0000269|PubMed:8807334, ECO:0000269|PubMed:8834244,
ECO:0000269|PubMed:8863162, ECO:0000269|PubMed:8875188,
ECO:0000269|PubMed:8931708, ECO:0000269|PubMed:9100224,
ECO:0000269|PubMed:9105656, ECO:0000269|PubMed:9452068,
ECO:0000269|PubMed:9452090, ECO:0000269|PubMed:9452111,
ECO:0000269|PubMed:9554750}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- PHARMACEUTICAL: Available under the names Replagal (from Shire)
and Fabrazyme (from Genzyme). Used as a long-term enzyme
replacement therapy in patients with a confirmed diagnosis of
Fabry disease. The differences between Replagal (also known as
agalsidase alpha) and Fabrazyme (also known as agalsidase beta)
lies in the glycosylation patterns. Agalsidase beta is produced in
the hamster CHO cell line while agalsidase alpha is produced in
human cell lines.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X05790; CAA29232.1; -; mRNA.
EMBL; X14448; CAA32617.1; -; Genomic_DNA.
EMBL; U78027; AAB64203.1; -; Genomic_DNA.
EMBL; AL035422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002689; AAH02689.1; -; mRNA.
EMBL; M13571; AAA51676.1; -; Genomic_DNA.
EMBL; D00039; BAA34059.1; -; mRNA.
EMBL; M18242; AAA52514.1; -; Genomic_DNA.
EMBL; X16889; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M20317; AAA52559.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS14484.1; -.
PIR; S04081; GBHUA.
RefSeq; NP_000160.1; NM_000169.2.
UniGene; Hs.69089; -.
PDB; 1R46; X-ray; 3.25 A; A/B=32-429.
PDB; 1R47; X-ray; 3.45 A; A/B=32-429.
PDB; 3GXN; X-ray; 3.01 A; A/B=32-429.
PDB; 3GXP; X-ray; 2.20 A; A/B=32-429.
PDB; 3GXT; X-ray; 2.70 A; A/B=32-429.
PDB; 3HG2; X-ray; 2.30 A; A/B=32-429.
PDB; 3HG3; X-ray; 1.90 A; A/B=32-429.
PDB; 3HG4; X-ray; 2.30 A; A/B=32-429.
PDB; 3HG5; X-ray; 2.30 A; A/B=32-429.
PDB; 3LX9; X-ray; 2.04 A; A/B=32-429.
PDB; 3LXA; X-ray; 3.04 A; A/B=32-429.
PDB; 3LXB; X-ray; 2.85 A; A/B=32-429.
PDB; 3LXC; X-ray; 2.35 A; A/B=32-429.
PDB; 3S5Y; X-ray; 2.10 A; A/B=32-429.
PDB; 3S5Z; X-ray; 2.00 A; A/B=32-429.
PDB; 3TV8; X-ray; 2.64 A; A/B=32-429.
PDB; 4NXS; X-ray; 2.55 A; A/B=32-429.
PDBsum; 1R46; -.
PDBsum; 1R47; -.
PDBsum; 3GXN; -.
PDBsum; 3GXP; -.
PDBsum; 3GXT; -.
PDBsum; 3HG2; -.
PDBsum; 3HG3; -.
PDBsum; 3HG4; -.
PDBsum; 3HG5; -.
PDBsum; 3LX9; -.
PDBsum; 3LXA; -.
PDBsum; 3LXB; -.
PDBsum; 3LXC; -.
PDBsum; 3S5Y; -.
PDBsum; 3S5Z; -.
PDBsum; 3TV8; -.
PDBsum; 4NXS; -.
ProteinModelPortal; P06280; -.
SMR; P06280; -.
BioGrid; 108981; 15.
IntAct; P06280; 7.
STRING; 9606.ENSP00000218516; -.
BindingDB; P06280; -.
ChEMBL; CHEMBL2524; -.
DrugBank; DB05018; Migalastat.
SwissLipids; SLP:000001380; -.
Allergome; 9621; Hom s alpha-Galactosidase.
CAZy; GH27; Glycoside Hydrolase Family 27.
iPTMnet; P06280; -.
PhosphoSitePlus; P06280; -.
BioMuta; GLA; -.
EPD; P06280; -.
PaxDb; P06280; -.
PeptideAtlas; P06280; -.
PRIDE; P06280; -.
DNASU; 2717; -.
Ensembl; ENST00000218516; ENSP00000218516; ENSG00000102393.
GeneID; 2717; -.
KEGG; hsa:2717; -.
CTD; 2717; -.
DisGeNET; 2717; -.
GeneCards; GLA; -.
GeneReviews; GLA; -.
HGNC; HGNC:4296; GLA.
HPA; HPA000237; -.
HPA; HPA000966; -.
MalaCards; GLA; -.
MIM; 300644; gene.
MIM; 301500; phenotype.
neXtProt; NX_P06280; -.
OpenTargets; ENSG00000102393; -.
Orphanet; 324; Fabry disease.
PharmGKB; PA28707; -.
eggNOG; KOG2366; Eukaryota.
eggNOG; ENOG410XPF1; LUCA.
GeneTree; ENSGT00390000008751; -.
HOGENOM; HOG000161224; -.
HOVERGEN; HBG001989; -.
InParanoid; P06280; -.
KO; K01189; -.
OMA; LAMTPTM; -.
OrthoDB; EOG091G0BGV; -.
PhylomeDB; P06280; -.
TreeFam; TF312909; -.
BioCyc; MetaCyc:HS02389-MONOMER; -.
BRENDA; 3.2.1.22; 2681.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P06280; -.
EvolutionaryTrace; P06280; -.
GeneWiki; Alpha-galactosidase; -.
GenomeRNAi; 2717; -.
PRO; PR:P06280; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102393; -.
CleanEx; HS_GLA; -.
ExpressionAtlas; P06280; baseline and differential.
Genevisible; P06280; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IMP:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; IMP:UniProtKB.
GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB.
GO; GO:0003824; F:catalytic activity; IDA:UniProtKB.
GO; GO:0016936; F:galactoside binding; IEA:Ensembl.
GO; GO:0016787; F:hydrolase activity; TAS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
GO; GO:0005102; F:receptor binding; IDA:UniProtKB.
GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
GO; GO:0046479; P:glycosphingolipid catabolic process; TAS:UniProtKB.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
GO; GO:0046477; P:glycosylceramide catabolic process; ISS:UniProtKB.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0009311; P:oligosaccharide metabolic process; IDA:UniProtKB.
CDD; cd14792; GH27; 1.
Gene3D; 3.20.20.70; -; 2.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR002241; Glyco_hydro_27.
InterPro; IPR000111; Glyco_hydro_27/36_CS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR035373; Melibiase/NAGA_C.
Pfam; PF16499; Melibiase_2; 1.
Pfam; PF17450; Melibiase_2_C; 1.
PRINTS; PR00740; GLHYDRLASE27.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Glycosidase;
Hydrolase; Lysosome; Pharmaceutical; Reference proteome; RNA editing;
Signal.
SIGNAL 1 31
CHAIN 32 429 Alpha-galactosidase A.
/FTId=PRO_0000001004.
REGION 203 207 Substrate binding.
ACT_SITE 170 170 Nucleophile. {ECO:0000250}.
ACT_SITE 231 231 Proton donor. {ECO:0000250}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15003450}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15003450}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15003450,
ECO:0000269|PubMed:19159218}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 52 94
DISULFID 56 63
DISULFID 142 172
DISULFID 202 223
DISULFID 378 382
VARIANT 3 3 L -> P (polymorphism; does not affect
enzyme activity; dbSNP:rs150547672).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077365.
VARIANT 3 3 L -> V (polymorphism; does not affect
enzyme activity; dbSNP:rs869312133).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077366.
VARIANT 12 14 Missing (in FD; has 4% of wild-type
activity). {ECO:0000269|PubMed:19621417}.
/FTId=VAR_062550.
VARIANT 20 20 A -> D (in FD; loss of enzyme activity;
dbSNP:rs869312134).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077367.
VARIANT 20 20 A -> P (in FD; atypical; loss of enzyme
activity; dbSNP:rs104894847).
{ECO:0000269|PubMed:26415523,
ECO:0000269|PubMed:7596372,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_012362.
VARIANT 21 21 L -> P (in FD; loss of enzyme activity;
dbSNP:rs869312135).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077368.
VARIANT 31 31 A -> V (in FD; dbSNP:rs869312448).
{ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:9100224}.
/FTId=VAR_012363.
VARIANT 32 32 L -> P (in FD).
{ECO:0000269|PubMed:7599642}.
/FTId=VAR_000431.
VARIANT 33 33 D -> G (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312136).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077369.
VARIANT 34 34 N -> S (in FD; dbSNP:rs28935192).
{ECO:0000269|PubMed:7504405,
ECO:0000269|PubMed:7599642,
ECO:0000269|PubMed:8395937}.
/FTId=VAR_000432.
VARIANT 35 35 G -> E (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312137).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077370.
VARIANT 35 35 G -> R (in FD).
{ECO:0000269|PubMed:8069316}.
/FTId=VAR_000433.
VARIANT 36 36 L -> W (in FD; loss of enzyme activity;
dbSNP:rs869312138).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077371.
VARIANT 40 40 P -> L (in FD).
{ECO:0000269|PubMed:10916280}.
/FTId=VAR_012364.
VARIANT 40 40 P -> S (in FD; loss of enzyme activity;
dbSNP:rs104894831).
{ECO:0000269|PubMed:2152885,
ECO:0000269|PubMed:26415523,
ECO:0000269|PubMed:9105656,
ECO:0000269|PubMed:9452111}.
/FTId=VAR_000434.
VARIANT 42 42 M -> L (in FD; dbSNP:rs797044613).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062551.
VARIANT 42 42 M -> T (in FD; loss of enzyme activity;
dbSNP:rs398123201).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077372.
VARIANT 42 42 M -> V (in FD).
{ECO:0000269|PubMed:10666480,
ECO:0000269|PubMed:8875188}.
/FTId=VAR_012365.
VARIANT 43 43 G -> R (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062552.
VARIANT 45 46 LH -> RS (in FD).
/FTId=VAR_012366.
VARIANT 45 45 L -> P (in FD; loss of enzyme activity).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077373.
VARIANT 46 46 H -> P (in FD; has 36% of wild-type
activity). {ECO:0000269|PubMed:19621417}.
/FTId=VAR_062553.
VARIANT 46 46 H -> R (in FD; dbSNP:rs398123203).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012367.
VARIANT 46 46 H -> Y (in FD).
{ECO:0000269|PubMed:11668641}.
/FTId=VAR_012368.
VARIANT 47 47 W -> G (in FD; decreased alpha-
galactosidase activity).
{ECO:0000269|PubMed:11668641,
ECO:0000269|PubMed:27211852}.
/FTId=VAR_012369.
VARIANT 47 47 W -> R (in FD; decreased alpha-
galactosidase activity).
{ECO:0000269|PubMed:27211852}.
/FTId=VAR_076478.
VARIANT 48 48 E -> D (in FD; loss of enzyme activity;
dbSNP:rs869312254).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077374.
VARIANT 49 49 R -> L (in FD).
{ECO:0000269|PubMed:8069316}.
/FTId=VAR_000435.
VARIANT 49 49 R -> P (in FD; dbSNP:rs398123205).
{ECO:0000269|PubMed:11668641}.
/FTId=VAR_012370.
VARIANT 49 49 R -> S (in FD).
{ECO:0000269|PubMed:8875188}.
/FTId=VAR_012371.
VARIANT 52 52 C -> R (in FD).
{ECO:0000269|PubMed:8807334,
ECO:0000269|PubMed:8931708}.
/FTId=VAR_000436.
VARIANT 52 52 C -> S (in FD; dbSNP:rs869312256).
/FTId=VAR_000437.
VARIANT 56 56 C -> F (in FD; dbSNP:rs869312258).
/FTId=VAR_000438.
VARIANT 56 56 C -> G (in FD; dbSNP:rs28935193).
{ECO:0000269|PubMed:7504405}.
/FTId=VAR_000439.
VARIANT 56 56 C -> Y (in FD; loss of enzyme activity;
dbSNP:rs869312258).
{ECO:0000269|PubMed:26415523,
ECO:0000269|PubMed:8875188}.
/FTId=VAR_012372.
VARIANT 59 59 E -> K (in FD).
/FTId=VAR_000440.
VARIANT 60 60 P -> L (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312262).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077375.
VARIANT 64 64 I -> F (in FD; loss of enzyme activity;
dbSNP:rs869312139).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077376.
VARIANT 65 65 S -> T (in FD; does not affect enzyme
function; dbSNP:rs104894848).
{ECO:0000269|PubMed:12786754,
ECO:0000269|PubMed:9554750}.
/FTId=VAR_032290.
VARIANT 66 66 E -> Q (in FD; has 52% of wild-type
activity; dbSNP:rs28935191).
{ECO:0000269|PubMed:1315715,
ECO:0000269|PubMed:19621417,
ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_000441.
VARIANT 71 71 E -> G (polymorphism; does not affect
enzyme activity; dbSNP:rs781927744).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077377.
VARIANT 72 72 M -> V (in FD; atypical).
{ECO:0000269|PubMed:9105656,
ECO:0000269|PubMed:9452090}.
/FTId=VAR_000442.
VARIANT 80 80 G -> D (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs781838005).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077378.
VARIANT 85 85 G -> D (in FD).
{ECO:0000269|PubMed:7599642}.
/FTId=VAR_000443.
VARIANT 86 86 Y -> C (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012373.
VARIANT 86 86 Y -> H (in FD; loss of enzyme activity;
dbSNP:rs869312140).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077379.
VARIANT 89 89 L -> P (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012374.
VARIANT 89 89 L -> R (in FD).
/FTId=VAR_000444.
VARIANT 91 91 I -> N (in FD; loss of enzyme activity;
dbSNP:rs869312141).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077380.
VARIANT 91 91 I -> T (in FD; mild; loss of enzyme
activity; dbSNP:rs869312141).
{ECO:0000269|PubMed:26415523,
ECO:0000269|PubMed:9100224}.
/FTId=VAR_012375.
VARIANT 92 92 D -> H (in FD).
{ECO:0000269|PubMed:8875188}.
/FTId=VAR_012376.
VARIANT 92 92 D -> Y (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012377.
VARIANT 93 93 D -> G (in FD).
{ECO:0000269|PubMed:8875188}.
/FTId=VAR_012378.
VARIANT 93 93 D -> N (in FD; has no enzyme activity;
dbSNP:rs869312270).
{ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:19621417}.
/FTId=VAR_062554.
VARIANT 94 94 C -> S (in FD; loss of enzyme activity).
{ECO:0000269|PubMed:11668641,
ECO:0000269|PubMed:26415523}.
/FTId=VAR_012379.
VARIANT 94 94 C -> Y (in FD; loss of enzyme activity;
dbSNP:rs113173389).
{ECO:0000269|PubMed:26415523,
ECO:0000269|PubMed:9100224}.
/FTId=VAR_012380.
VARIANT 95 95 W -> S (in FD).
{ECO:0000269|PubMed:10916280,
ECO:0000269|PubMed:11668641}.
/FTId=VAR_012381.
VARIANT 97 97 A -> V (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012382.
VARIANT 100 100 R -> K (in FD; dbSNP:rs869312273).
/FTId=VAR_000445.
VARIANT 100 100 R -> T (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012383.
VARIANT 112 117 Missing (in FD).
/FTId=VAR_000446.
VARIANT 112 112 R -> C (in FD; dbSNP:rs104894834).
{ECO:0000269|PubMed:10666480,
ECO:0000269|PubMed:10916280,
ECO:0000269|PubMed:11668641,
ECO:0000269|PubMed:1315715,
ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_000447.
VARIANT 112 112 R -> H (in FD; mild; dbSNP:rs372966991).
{ECO:0000269|PubMed:10916280,
ECO:0000269|PubMed:15712228}.
/FTId=VAR_000448.
VARIANT 112 112 R -> S (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062555.
VARIANT 113 113 F -> I (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312142).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077381.
VARIANT 113 113 F -> L (in FD; mild; dbSNP:rs869312142).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012384.
VARIANT 113 113 F -> S (in FD).
{ECO:0000269|PubMed:11668641}.
/FTId=VAR_012385.
VARIANT 120 121 LA -> PT (in FD).
/FTId=VAR_000449.
VARIANT 120 120 L -> V (in FD; has 42% of wild-type
activity). {ECO:0000269|PubMed:19621417}.
/FTId=VAR_062556.
VARIANT 121 121 A -> T (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs782197638).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077382.
VARIANT 128 128 G -> E (in FD).
{ECO:0000269|PubMed:8807334}.
/FTId=VAR_000450.
VARIANT 131 131 L -> P (in FD; dbSNP:rs869312298).
/FTId=VAR_000451.
VARIANT 134 134 Y -> S (in FD).
{ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:9100224}.
/FTId=VAR_012386.
VARIANT 135 135 A -> V (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062557.
VARIANT 138 138 G -> R (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012387.
VARIANT 142 142 C -> R (in FD).
{ECO:0000269|PubMed:10666480}.
/FTId=VAR_012388.
VARIANT 142 142 C -> Y (in FD).
{ECO:0000269|PubMed:7759078,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_000452.
VARIANT 143 143 A -> P (in FD; dbSNP:rs104894845).
{ECO:0000269|PubMed:11889412}.
/FTId=VAR_000453.
VARIANT 143 143 A -> T (in FD; unknown pathological
significance; dbSNP:rs104894845).
{ECO:0000269|PubMed:11668641,
ECO:0000269|PubMed:16533976,
ECO:0000269|PubMed:27142856,
ECO:0000269|PubMed:9100224}.
/FTId=VAR_012389.
VARIANT 144 144 G -> V (in FD).
/FTId=VAR_000454.
VARIANT 146 146 P -> S (in FD; mild; dbSNP:rs28935194).
/FTId=VAR_000455.
VARIANT 148 148 S -> N (in FD).
{ECO:0000269|PubMed:10916280}.
/FTId=VAR_012390.
VARIANT 148 148 S -> R (in FD).
{ECO:0000269|PubMed:10666480,
ECO:0000269|PubMed:9100224}.
/FTId=VAR_012391.
VARIANT 154 154 I -> T (polymorphism; does not affect
enzyme activity; dbSNP:rs869312143).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077383.
VARIANT 156 156 A -> T (in FD; dbSNP:rs28935195).
{ECO:0000269|PubMed:7599642}.
/FTId=VAR_000456.
VARIANT 156 156 A -> V (in FD; dbSNP:rs869312307).
{ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:7759078,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_000457.
VARIANT 162 162 W -> C (in FD; dbSNP:rs869312311).
{ECO:0000269|PubMed:8931708}.
/FTId=VAR_012392.
VARIANT 162 162 W -> R (in FD; dbSNP:rs28935196).
{ECO:0000269|PubMed:7504405}.
/FTId=VAR_000458.
VARIANT 163 163 G -> V (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012393.
VARIANT 164 164 V -> G (in FD; loss of enzyme activity).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077384.
VARIANT 164 164 V -> L (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312144).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077385.
VARIANT 165 165 D -> V (in FD).
{ECO:0000269|PubMed:10666480,
ECO:0000269|PubMed:8069316}.
/FTId=VAR_000459.
VARIANT 166 166 L -> V (in FD).
{ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:7759078,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_000460.
VARIANT 167 167 L -> Q (in FD; loss of enzyme activity).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077386.
VARIANT 170 170 D -> V (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012394.
VARIANT 171 171 G -> D (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062558.
VARIANT 172 172 C -> R (in FD).
{ECO:0000269|PubMed:10916280}.
/FTId=VAR_012395.
VARIANT 172 172 C -> Y (in FD; dbSNP:rs869312318).
/FTId=VAR_000461.
VARIANT 180 180 L -> F (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312145).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077387.
VARIANT 183 183 G -> D (in FD).
{ECO:0000269|PubMed:10666480}.
/FTId=VAR_012396.
VARIANT 187 187 M -> I (in FD; loss of enzyme activity;
dbSNP:rs869312146).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077388.
VARIANT 187 187 M -> V (in FD; decreased enzyme activity;
dbSNP:rs869312340).
{ECO:0000269|PubMed:10916280,
ECO:0000269|PubMed:26415523}.
/FTId=VAR_012397.
VARIANT 196 196 R -> S (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312147).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077389.
VARIANT 198 198 I -> T (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs727503950).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077390.
VARIANT 201 201 S -> F (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062559.
VARIANT 202 202 C -> W (in FD; dbSNP:rs28936082).
{ECO:0000269|PubMed:10208848}.
/FTId=VAR_000462.
VARIANT 202 202 C -> Y (in FD; loss of enzyme activity;
dbSNP:rs869312344).
{ECO:0000269|PubMed:26415523,
ECO:0000269|PubMed:9100224}.
/FTId=VAR_012398.
VARIANT 204 204 W -> R (in FD; loss of enzyme activity;
dbSNP:rs869312148).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077391.
VARIANT 205 207 Missing (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012399.
VARIANT 205 205 P -> T (in FD; dbSNP:rs397515870).
{ECO:0000269|PubMed:8807334,
ECO:0000269|PubMed:8875188}.
/FTId=VAR_000463.
VARIANT 213 213 K -> R (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312149).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077392.
VARIANT 214 214 P -> L (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312150).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077393.
VARIANT 215 215 N -> S (in FD; mild; dbSNP:rs28935197).
{ECO:0000269|PubMed:10666480,
ECO:0000269|PubMed:11668641,
ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:8395937,
ECO:0000269|PubMed:9452111}.
/FTId=VAR_000464.
VARIANT 216 216 Y -> D (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012400.
VARIANT 219 219 I -> M (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312151).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077394.
VARIANT 219 219 I -> N (in FD).
/FTId=VAR_000465.
VARIANT 219 219 I -> T (in FD; has 46% of wild-type
activity). {ECO:0000269|PubMed:19621417}.
/FTId=VAR_062560.
VARIANT 223 223 C -> G (in FD; dbSNP:rs869312381).
{ECO:0000269|PubMed:10208848}.
/FTId=VAR_012401.
VARIANT 224 224 N -> D (in FD).
{ECO:0000269|PubMed:10208848,
ECO:0000269|PubMed:9452111}.
/FTId=VAR_000466.
VARIANT 224 224 N -> S (in FD; dbSNP:rs869312383).
{ECO:0000269|PubMed:10916280}.
/FTId=VAR_012402.
VARIANT 226 226 W -> R (in FD).
{ECO:0000269|PubMed:10916280}.
/FTId=VAR_012403.
VARIANT 227 227 R -> P (in FD; loss of enzyme activity).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077395.
VARIANT 227 227 R -> Q (in FD; dbSNP:rs28935198).
{ECO:0000269|PubMed:10916280,
ECO:0000269|PubMed:7504405}.
/FTId=VAR_000467.
VARIANT 228 228 N -> S (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312152).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077396.
VARIANT 230 230 A -> T (in FD).
{ECO:0000269|PubMed:10916280}.
/FTId=VAR_012404.
VARIANT 231 231 D -> N (in FD).
{ECO:0000269|PubMed:8863162}.
/FTId=VAR_000468.
VARIANT 234 234 D -> E (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062561.
VARIANT 235 235 S -> C (in FD; dbSNP:rs797044746).
{ECO:0000269|PubMed:10666480}.
/FTId=VAR_012405.
VARIANT 236 236 W -> C (in FD; dbSNP:rs869312386).
{ECO:0000269|PubMed:8875188}.
/FTId=VAR_012406.
VARIANT 236 236 W -> L (in FD).
{ECO:0000269|PubMed:10666480}.
/FTId=VAR_012407.
VARIANT 242 242 I -> N (in FD).
{ECO:0000269|PubMed:9105656}.
/FTId=VAR_012408.
VARIANT 242 242 I -> V (in FD; unknown pathological
significance; decreased enzyme activity).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077397.
VARIANT 243 243 L -> F (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs397515874).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077398.
VARIANT 244 244 D -> H (in FD).
{ECO:0000269|PubMed:10666480}.
/FTId=VAR_012409.
VARIANT 244 244 D -> N (in FD; dbSNP:rs727503948).
/FTId=VAR_000469.
VARIANT 247 247 S -> P (in FD; loss of enzyme activity;
dbSNP:rs869312393).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077399.
VARIANT 247 247 S -> SWTS (in FD).
/FTId=VAR_000470.
VARIANT 249 249 N -> K (in FD; unknown pathological
significance; decreased enzyme activity).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077400.
VARIANT 253 253 I -> T (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs727505292).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077401.
VARIANT 254 254 V -> A (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312153).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077402.
VARIANT 258 258 G -> R (in FD).
{ECO:0000269|PubMed:11668641}.
/FTId=VAR_012410.
VARIANT 259 259 P -> L (in FD; dbSNP:rs869312399).
{ECO:0000269|PubMed:10666480}.
/FTId=VAR_012411.
VARIANT 259 259 P -> R (in FD; decreased enzyme activity;
dbSNP:rs869312399).
{ECO:0000269|PubMed:11668641,
ECO:0000269|PubMed:26415523}.
/FTId=VAR_012412.
VARIANT 260 260 G -> A (in FD).
{ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_012413.
VARIANT 261 261 G -> D (in FD).
{ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_012414.
VARIANT 262 262 W -> R (in FD; loss of enzyme activity;
dbSNP:rs869312154).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077403.
VARIANT 263 263 N -> S (in FD; dbSNP:rs869312404).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012415.
VARIANT 264 264 D -> V (in FD; dbSNP:rs28935486).
{ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:7504405}.
/FTId=VAR_000471.
VARIANT 264 264 D -> Y (in FD; dbSNP:rs190347120).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062562.
VARIANT 265 265 P -> R (in FD).
{ECO:0000269|PubMed:8931708}.
/FTId=VAR_012416.
VARIANT 266 266 D -> H (in FD).
{ECO:0000269|PubMed:10916280}.
/FTId=VAR_032291.
VARIANT 266 266 D -> N (in FD; dbSNP:rs869312407).
{ECO:0000269|PubMed:11076046}.
/FTId=VAR_012418.
VARIANT 266 266 D -> V (in FD; dbSNP:rs28935487).
{ECO:0000269|PubMed:7504405}.
/FTId=VAR_000472.
VARIANT 267 267 M -> I (in FD; dbSNP:rs730880451).
{ECO:0000269|PubMed:10666480,
ECO:0000269|PubMed:11668641}.
/FTId=VAR_012419.
VARIANT 269 269 V -> A (in FD; dbSNP:rs28935488).
{ECO:0000269|PubMed:8395937}.
/FTId=VAR_000473.
VARIANT 269 269 V -> G (in FD; loss of enzyme activity).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077404.
VARIANT 272 272 N -> K (in FD).
/FTId=VAR_000474.
VARIANT 272 272 N -> S (in FD; dbSNP:rs28935495).
{ECO:0000269|PubMed:15162124}.
/FTId=VAR_032292.
VARIANT 276 276 S -> G (in FD; loss of enzyme activity;
dbSNP:rs869312432).
{ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:26415523}.
/FTId=VAR_062563.
VARIANT 279 279 Q -> E (in FD; mild; does not
significantly affect the enzyme activity
but the mutant protein levels are
decreased presumably in the ER of the
cells; dbSNP:rs28935485).
{ECO:0000269|PubMed:10838196,
ECO:0000269|PubMed:1315715,
ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_000475.
VARIANT 279 279 Q -> H (in FD).
{ECO:0000269|PubMed:11668641}.
/FTId=VAR_012420.
VARIANT 280 280 Q -> H (in FD).
{ECO:0000269|PubMed:11668641}.
/FTId=VAR_012421.
VARIANT 284 284 M -> T (in FD).
{ECO:0000269|PubMed:8807334}.
/FTId=VAR_000476.
VARIANT 285 285 A -> P (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062564.
VARIANT 287 287 W -> C (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012422.
VARIANT 287 287 W -> G (in FD).
{ECO:0000269|PubMed:8875188}.
/FTId=VAR_012423.
VARIANT 288 288 A -> D (in FD; dbSNP:rs869312437).
/FTId=VAR_000477.
VARIANT 289 289 I -> F (in FD).
{ECO:0000269|PubMed:10666480}.
/FTId=VAR_012424.
VARIANT 289 289 I -> V (polymorphism; decreased enzyme
activity; dbSNP:rs140329381).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077405.
VARIANT 296 296 M -> I (in FD; atypical;
dbSNP:rs104894846).
{ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:7596372,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_012425.
VARIANT 296 296 M -> V (in FD; mild; dbSNP:rs104894830).
{ECO:0000269|PubMed:1846223}.
/FTId=VAR_000478.
VARIANT 297 297 S -> F (in FD; dbSNP:rs28935489).
{ECO:0000269|PubMed:7504405}.
/FTId=VAR_000479.
VARIANT 298 298 N -> H (in FD).
{ECO:0000269|PubMed:11668641,
ECO:0000269|PubMed:8875188}.
/FTId=VAR_012426.
VARIANT 298 298 N -> K (in FD).
{ECO:0000269|PubMed:8807334}.
/FTId=VAR_000480.
VARIANT 298 298 N -> S (in FD).
{ECO:0000269|PubMed:9100224}.
/FTId=VAR_012427.
VARIANT 300 300 L -> F (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062565.
VARIANT 301 301 R -> Q (in FD; mild; does not
significantly affect the enzyme activity
but the mutant protein levels are
decreased presumably in the ER of the
cells; dbSNP:rs104894828).
{ECO:0000269|PubMed:10208848,
ECO:0000269|PubMed:10838196,
ECO:0000269|PubMed:10916280,
ECO:0000269|PubMed:1315715,
ECO:0000269|PubMed:2171331,
ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:7599642,
ECO:0000269|PubMed:8738659,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_000481.
VARIANT 309 309 A -> V (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312155).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077406.
VARIANT 313 313 D -> N (polymorphism; does not affect
enzyme activity).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077407.
VARIANT 313 313 D -> Y (in FD; dbSNP:rs28935490).
{ECO:0000269|PubMed:11668641,
ECO:0000269|PubMed:7504405,
ECO:0000269|PubMed:9452111}.
/FTId=VAR_000482.
VARIANT 315 315 D -> N (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312156).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077408.
VARIANT 316 322 Missing (in FD).
{ECO:0000269|PubMed:8931708}.
/FTId=VAR_012429.
VARIANT 316 316 V -> A (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312157).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077409.
VARIANT 316 316 V -> E (in FD).
{ECO:0000269|PubMed:8069316}.
/FTId=VAR_000483.
VARIANT 317 317 I -> S (in FD; loss of enzyme activity;
dbSNP:rs869312158).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077410.
VARIANT 320 320 N -> K (in FD).
{ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_012430.
VARIANT 320 320 N -> Y (in FD; loss of enzyme activity).
{ECO:0000269|PubMed:10916280,
ECO:0000269|PubMed:26415523}.
/FTId=VAR_012431.
VARIANT 321 321 Q -> E (in FD; dbSNP:rs730880439).
{ECO:0000269|PubMed:10666480}.
/FTId=VAR_012432.
VARIANT 323 323 P -> R (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312159).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077411.
VARIANT 327 327 Q -> K (in FD; dbSNP:rs28935491).
{ECO:0000269|PubMed:10208848,
ECO:0000269|PubMed:8395937}.
/FTId=VAR_000484.
VARIANT 327 327 Q -> L (in FD; loss of enzyme activity;
dbSNP:rs869312160).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077412.
VARIANT 327 327 Q -> R (in FD; loss of enzyme activity;
dbSNP:rs869312160).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077413.
VARIANT 328 328 G -> A (in FD; dbSNP:rs28935492).
{ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:7504405}.
/FTId=VAR_000486.
VARIANT 328 328 G -> R (in FD; loss of enzyme activity;
dbSNP:rs104894832).
{ECO:0000269|PubMed:1315715,
ECO:0000269|PubMed:26415523,
ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_000485.
VARIANT 328 328 G -> V (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062566.
VARIANT 330 330 Q -> R (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312161).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077414.
VARIANT 338 338 E -> K (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062567.
VARIANT 340 340 W -> R (in FD).
{ECO:0000269|PubMed:8875188}.
/FTId=VAR_012433.
VARIANT 341 341 E -> K (in FD; dbSNP:rs869312214).
{ECO:0000269|PubMed:10090526}.
/FTId=VAR_012434.
VARIANT 342 342 R -> P (in FD; loss of enzyme activity).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077415.
VARIANT 342 342 R -> Q (in FD; severe; dbSNP:rs28935493).
/FTId=VAR_000487.
VARIANT 352 352 A -> G (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312162).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077416.
VARIANT 356 356 R -> P (in FD; loss of enzyme activity;
dbSNP:rs869312163).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077417.
VARIANT 356 356 R -> Q (in FD; has 15% of wild-type
activity; dbSNP:rs869312163).
{ECO:0000269|PubMed:19621417}.
/FTId=VAR_062568.
VARIANT 356 356 R -> W (in FD; severe;
dbSNP:rs104894827).
{ECO:0000269|PubMed:2539398}.
/FTId=VAR_000488.
VARIANT 358 358 E -> A (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062569.
VARIANT 358 358 E -> K (in FD; loss of enzyme activity;
dbSNP:rs797044774).
{ECO:0000269|PubMed:26415523,
ECO:0000269|PubMed:9452068}.
/FTId=VAR_000489.
VARIANT 358 358 Missing (in FD).
{ECO:0000269|PubMed:10666480,
ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:8807334,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_000490.
VARIANT 360 360 G -> C (in FD; has 6% of wild-type
activity; dbSNP:rs782598150).
{ECO:0000269|PubMed:19621417}.
/FTId=VAR_062570.
VARIANT 360 360 G -> S (in FD; loss of enzyme activity).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077418.
VARIANT 361 361 G -> R (in FD; severe; dbSNP:rs28935494).
{ECO:0000269|PubMed:8395937}.
/FTId=VAR_000491.
VARIANT 363 363 R -> H (in FD; dbSNP:rs111422676).
{ECO:0000269|PubMed:11668641}.
/FTId=VAR_012435.
VARIANT 373 373 G -> D (in FD; dbSNP:rs869312227).
{ECO:0000269|PubMed:11295840}.
/FTId=VAR_012436.
VARIANT 373 373 G -> S (in FD; dbSNP:rs727504348).
{ECO:0000269|PubMed:7575533,
ECO:0000269|PubMed:9105656}.
/FTId=VAR_012437.
VARIANT 375 375 G -> A (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312164).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077419.
VARIANT 377 377 A -> D (in FD).
{ECO:0000269|PubMed:11668641}.
/FTId=VAR_012438.
VARIANT 378 378 C -> Y (in FD).
{ECO:0000269|PubMed:10666480}.
/FTId=VAR_012439.
VARIANT 383 383 Missing (in FD; severe; with facial
telangiectasias).
{ECO:0000269|PubMed:8834244}.
/FTId=VAR_000492.
VARIANT 392 392 R -> S (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs869312165).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077420.
VARIANT 396 396 F -> Y (in RNA edited version).
/FTId=VAR_000493.
VARIANT 399 399 W -> S (in FD; unknown pathological
significance; decreased enzyme activity;
dbSNP:rs782449839).
{ECO:0000269|PubMed:26415523}.
/FTId=VAR_077421.
VARIANT 404 404 Missing (in FD; mild; loss of enzyme
activity). {ECO:0000269|PubMed:15712228,
ECO:0000269|PubMed:26415523,
ECO:0000269|PubMed:7504405,
ECO:0000269|PubMed:9100224}.
/FTId=VAR_000494.
VARIANT 409 409 P -> A (in FD).
{ECO:0000269|PubMed:11668641}.
/FTId=VAR_012440.
VARIANT 409 409 P -> T (in FD).
{ECO:0000269|PubMed:11668641}.
/FTId=VAR_012441.
VARIANT 410 410 T -> A (in FD; mild; dbSNP:rs104894852).
{ECO:0000269|PubMed:12694230}.
/FTId=VAR_032293.
VARIANT 414 414 L -> S (in FD).
{ECO:0000269|PubMed:15712228}.
/FTId=VAR_062571.
STRAND 42 46 {ECO:0000244|PDB:3HG3}.
HELIX 47 50 {ECO:0000244|PDB:3HG3}.
TURN 56 58 {ECO:0000244|PDB:3HG3}.
TURN 60 62 {ECO:0000244|PDB:3HG3}.
STRAND 63 65 {ECO:0000244|PDB:3HG3}.
HELIX 66 78 {ECO:0000244|PDB:3HG3}.
HELIX 81 84 {ECO:0000244|PDB:3HG3}.
STRAND 88 90 {ECO:0000244|PDB:3HG3}.
STRAND 102 104 {ECO:0000244|PDB:3GXT}.
TURN 110 112 {ECO:0000244|PDB:3HG3}.
STRAND 113 115 {ECO:0000244|PDB:1R47}.
HELIX 116 126 {ECO:0000244|PDB:3HG3}.
STRAND 130 140 {ECO:0000244|PDB:3HG3}.
STRAND 144 146 {ECO:0000244|PDB:3HG3}.
TURN 149 151 {ECO:0000244|PDB:3GXN}.
HELIX 152 162 {ECO:0000244|PDB:3HG3}.
STRAND 166 170 {ECO:0000244|PDB:3HG3}.
HELIX 177 193 {ECO:0000244|PDB:3HG3}.
STRAND 199 202 {ECO:0000244|PDB:3HG3}.
HELIX 205 208 {ECO:0000244|PDB:3HG3}.
TURN 209 211 {ECO:0000244|PDB:3HG3}.
HELIX 216 222 {ECO:0000244|PDB:3HG3}.
STRAND 224 227 {ECO:0000244|PDB:3HG3}.
HELIX 236 248 {ECO:0000244|PDB:3HG3}.
HELIX 250 253 {ECO:0000244|PDB:3HG3}.
TURN 254 256 {ECO:0000244|PDB:3HG3}.
STRAND 261 264 {ECO:0000244|PDB:3HG3}.
STRAND 272 274 {ECO:0000244|PDB:3HG3}.
HELIX 277 289 {ECO:0000244|PDB:3HG3}.
STRAND 294 296 {ECO:0000244|PDB:3HG3}.
HELIX 305 311 {ECO:0000244|PDB:3HG3}.
HELIX 314 320 {ECO:0000244|PDB:3HG3}.
STRAND 329 334 {ECO:0000244|PDB:3HG3}.
STRAND 337 343 {ECO:0000244|PDB:3HG3}.
HELIX 345 347 {ECO:0000244|PDB:3S5Z}.
STRAND 349 355 {ECO:0000244|PDB:3HG3}.
STRAND 359 361 {ECO:0000244|PDB:3HG3}.
STRAND 363 368 {ECO:0000244|PDB:3HG3}.
HELIX 369 371 {ECO:0000244|PDB:3HG3}.
HELIX 373 375 {ECO:0000244|PDB:3HG3}.
TURN 376 378 {ECO:0000244|PDB:3HG3}.
STRAND 379 390 {ECO:0000244|PDB:3HG3}.
STRAND 392 398 {ECO:0000244|PDB:3HG3}.
STRAND 402 407 {ECO:0000244|PDB:3HG3}.
STRAND 412 419 {ECO:0000244|PDB:3HG3}.
HELIX 420 424 {ECO:0000244|PDB:3HG3}.
SEQUENCE 429 AA; 48767 MW; 613F8BF21B107D7B CRC64;
MQLRNPELHL GCALALRFLA LVSWDIPGAR ALDNGLARTP TMGWLHWERF MCNLDCQEEP
DSCISEKLFM EMAELMVSEG WKDAGYEYLC IDDCWMAPQR DSEGRLQADP QRFPHGIRQL
ANYVHSKGLK LGIYADVGNK TCAGFPGSFG YYDIDAQTFA DWGVDLLKFD GCYCDSLENL
ADGYKHMSLA LNRTGRSIVY SCEWPLYMWP FQKPNYTEIR QYCNHWRNFA DIDDSWKSIK
SILDWTSFNQ ERIVDVAGPG GWNDPDMLVI GNFGLSWNQQ VTQMALWAIM AAPLFMSNDL
RHISPQAKAL LQDKDVIAIN QDPLGKQGYQ LRQGDNFEVW ERPLSGLAWA VAMINRQEIG
GPRSYTIAVA SLGKGVACNP ACFITQLLPV KRKLGFYEWT SRLRSHINPT GTVLLQLENT
MQMSLKDLL


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