Reviewed, UniProtKB/Swiss-Prot P06280 (AGAL_HUMAN)

Names and origin

Protein names

Recommended name:
    Alpha-galactosidase A
    EC=3.2.1.22
Alternative name(s):
    Alpha-D-galactoside galactohydrolase
    Alpha-D-galactosidase A
    Melibiase
    INN=Agalsidase

Gene names

Name:

GLA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase.
Subunit structure	Homodimer. Ref.12
Subcellular location	Lysosome.
Involvement in disease	Defects in GLA are the cause of Fabry disease (FD) [MIM:301500]. FD is a 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 globotriaoslyceramide (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. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51
Biotechnological use	Used to convert blood group antigens of type B into type O, the universal donor type.
Pharmaceutical use	Available under the names Replagal (Transkaryotic Therapies) and Fabrazyme (Genzyme). Used as a long-term enzyme replacement therapy in patients with a confirmed diagnosis of Fabry disease.
Sequence similarities	Belongs to the glycosyl hydrolase 27 family.
RNA editing	Edited at position 396. Partially edited. Ref.9

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	RNA editing
Disease	Disease mutation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing Pharmaceutical
Gene Ontology (GO)
Biological process	glycosphingolipid catabolic process Traceable author statement. Source: UniProtKB glycosylceramide catabolic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of nitric oxide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of nitric-oxide synthase activity Inferred from sequence or structural similarity. Source: UniProtKB oligosaccharide metabolic process Inferred from direct assay. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from mutant phenotype. Source: UniProtKB extracellular region Inferred from direct assay. Source: UniProtKB lysosome Inferred from mutant phenotype. Source: UniProtKB
Molecular function	alpha-galactosidase activity Inferred from direct assay. Source: UniProtKB cation binding Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from direct assay. Source: UniProtKB receptor binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Chain

32 – 429

398

Alpha-galactosidase A

PRO_0000001004

Regions

Region

203 – 207

5

Substrate binding

Sites

Active site

170

1

Nucleophile By similarity

Active site

231

1

Proton donor By similarity

Amino acid modifications

Glycosylation

139

1

N-linked (GlcNAc...) Ref.12

Glycosylation

192

1

N-linked (GlcNAc...) Ref.12

Glycosylation

215

1

N-linked (GlcNAc...) Ref.12

Glycosylation

408

1

N-linked (GlcNAc...) Potential

Disulfide bond

52 ↔ 94

Disulfide bond

56 ↔ 63

Disulfide bond

142 ↔ 172

Disulfide bond

202 ↔ 223

Disulfide bond

378 ↔ 382

Natural variations

Natural variant

20

1

A → P in FD; atypical. Ref.26 Ref.33 Ref.38

VAR_012362

Natural variant

31

1

A → V in FD. Ref.34

VAR_012363

Natural variant

32

1

L → P in FD. Ref.25

VAR_000431

Natural variant

34

1

N → S in FD. Ref.19 Ref.20 Ref.25

VAR_000432

Natural variant

35

1

G → R in FD. Ref.21

VAR_000433

Natural variant

40

1

P → L in FD. Ref.14 Ref.33 Ref.38 Ref.44

VAR_012364

Natural variant

40

1

P → S in FD. Ref.14 Ref.33 Ref.38 Ref.44

VAR_000434

Natural variant

42

1

M → V in FD. Ref.28 Ref.42

VAR_012365

Natural variant

45 – 46

2

LH → RS in FD. Ref.34 Ref.46

VAR_012366

Natural variant

46

1

H → R in FD. Ref.34 Ref.46

VAR_012367

Natural variant

46

1

H → Y in FD. Ref.34 Ref.46

VAR_012368

Natural variant

47

1

W → G in FD. Ref.46

VAR_012369

Natural variant

49

1

R → L in FD. Ref.21 Ref.28 Ref.46

VAR_000435

Natural variant

49

1

R → P in FD. Ref.21 Ref.28 Ref.46

VAR_012370

Natural variant

49

1

R → S in FD. Ref.21 Ref.28 Ref.46

VAR_012371

Natural variant

52

1

C → R in FD. Ref.30 Ref.31

VAR_000436

Natural variant

52

1

C → S in FD. Ref.30 Ref.31

VAR_000437

Natural variant

56

1

C → F in FD. Ref.19 Ref.28

VAR_000438

Natural variant

56

1

C → G in FD. Ref.19 Ref.28

VAR_000439

Natural variant

56

1

C → Y in FD. Ref.19 Ref.28

VAR_012372

Natural variant

59

1

E → K in FD.

VAR_000440

Natural variant

65

1

S → T in FD; does not affect enzyme function. Ref.35 Ref.49

VAR_032290

Natural variant

66

1

E → Q in FD. Ref.18 Ref.23 Ref.33

VAR_000441

Natural variant

72

1

M → V in FD; atypical. Ref.33 Ref.37

VAR_000442

Natural variant

85

1

G → D in FD. Ref.25

VAR_000443

Natural variant

86

1

Y → C in FD. Ref.34

VAR_012373

Natural variant

89

1

L → P in FD. Ref.34

VAR_012374

Natural variant

89

1

L → R in FD. Ref.34

VAR_000444

Natural variant

91

1

I → T in FD; mild. Ref.34

VAR_012375

Natural variant

92

1

D → H in FD. Ref.28 Ref.34

VAR_012376

Natural variant

92

1

D → Y in FD. Ref.28 Ref.34

VAR_012377

Natural variant

93

1

D → G in FD. Ref.28

VAR_012378

Natural variant

94

1

C → S in FD. Ref.34 Ref.46

VAR_012379

Natural variant

94

1

C → Y in FD. Ref.34 Ref.46

VAR_012380

Natural variant

95

1

W → S in FD. Ref.44 Ref.46

VAR_012381

Natural variant

97

1

A → V in FD. Ref.34

VAR_012382

Natural variant

100

1

R → K in FD. Ref.34 Ref.38

VAR_000445

Natural variant

100

1

R → T in FD. Ref.34 Ref.38

VAR_012383

Natural variant

112 – 117

6

Missing in FD. Ref.18 Ref.23 Ref.33 Ref.42 Ref.44 Ref.46

VAR_000446

Natural variant

112

1

R → C in FD. Ref.18 Ref.23 Ref.33 Ref.42 Ref.44 Ref.46

VAR_000447

Natural variant

112

1

R → H in FD; mild. Ref.18 Ref.23 Ref.33 Ref.42 Ref.44 Ref.46

VAR_000448

Natural variant

113

1

F → L in FD; mild. Ref.34 Ref.46

VAR_012384

Natural variant

113

1

F → S in FD. Ref.34 Ref.46

VAR_012385

Natural variant

120 – 121

2

LA → PT in FD. Ref.38

VAR_000449

Natural variant

128

1

G → E in FD. Ref.31

VAR_000450

Natural variant

131

1

L → P in FD.

VAR_000451

Natural variant

134

1

Y → S in FD. Ref.34

VAR_012386

Natural variant

138

1

G → R in FD. Ref.34

VAR_012387

Natural variant

142

1

C → R in FD. Ref.24 Ref.33 Ref.42

VAR_012388

Natural variant

142

1

C → Y in FD. Ref.24 Ref.33 Ref.42

VAR_000452

Natural variant

143

1

A → P in FD. Ref.34 Ref.46 Ref.47 Ref.51

VAR_000453

Natural variant

143

1

A → T in FD. Ref.34 Ref.46 Ref.47 Ref.51

VAR_012389

Natural variant

144

1

G → V in FD.

VAR_000454

Natural variant

146

1

P → S in FD; mild.

VAR_000455

Natural variant

148

1

S → N in FD. Ref.34 Ref.42 Ref.44

VAR_012390

Natural variant

148

1

S → R in FD. Ref.34 Ref.42 Ref.44

VAR_012391

Natural variant

156

1

A → T in FD. Ref.23 Ref.24 Ref.25 Ref.33

VAR_000456

Natural variant

156

1

A → V in FD. Ref.23 Ref.24 Ref.25 Ref.33

VAR_000457

Natural variant

162

1

W → C in FD. Ref.19 Ref.30

VAR_012392

Natural variant

162

1

W → R in FD. Ref.19 Ref.30

VAR_000458

Natural variant

163

1

G → V in FD. Ref.34

VAR_012393

Natural variant

165

1

D → V in FD. Ref.21 Ref.42

VAR_000459

Natural variant

166

1

L → V in FD. Ref.23 Ref.24 Ref.33

VAR_000460

Natural variant

170

1

D → V in FD. Ref.34 Ref.38

VAR_012394

Natural variant

172

1

C → R in FD. Ref.44

VAR_012395

Natural variant

172

1

C → Y in FD. Ref.44

VAR_000461

Natural variant

183

1

G → D in FD. Ref.42

VAR_012396

Natural variant

187

1

M → V in FD. Ref.44

VAR_012397

Natural variant

202

1

C → W in FD. Ref.34 Ref.39

VAR_000462

Natural variant

202

1

C → Y in FD. Ref.34 Ref.39

VAR_012398

Natural variant

205 – 207

3

Missing in FD. Ref.28 Ref.31 Ref.34

VAR_012399

Natural variant

205

1

P → T in FD. Ref.28 Ref.31

VAR_000463

Natural variant

215

1

N → S in FD; mild. Ref.20 Ref.38 Ref.42 Ref.46

VAR_000464

Natural variant

216

1

Y → D in FD. Ref.34

VAR_012400

Natural variant

219

1

I → N in FD.

VAR_000465

Natural variant

223

1

C → G in FD. Ref.39

VAR_012401

Natural variant

224

1

N → D in FD. Ref.38 Ref.39 Ref.44

VAR_000466

Natural variant

224

1

N → S in FD. Ref.38 Ref.39 Ref.44

VAR_012402

Natural variant

226

1

W → R in FD. Ref.44

VAR_012403

Natural variant

227

1

R → Q in FD. Ref.19 Ref.44

VAR_000467

Natural variant

230

1

A → T in FD. Ref.38 Ref.44

VAR_012404

Natural variant

231

1

D → N in FD. Ref.32

VAR_000468

Natural variant

235

1

S → C in FD. Ref.42

VAR_012405

Natural variant

236

1

W → C in FD. Ref.28 Ref.42

VAR_012406

Natural variant

236

1

W → L in FD. Ref.28 Ref.42

VAR_012407

Natural variant

242

1

I → N in FD. Ref.33

VAR_012408

Natural variant

244

1

D → H in FD. Ref.42

VAR_012409

Natural variant

244

1

D → N in FD. Ref.42

VAR_000469

Natural variant

247

1

S → SWTS in FD.

VAR_000470

Natural variant

258

1

G → R in FD. Ref.46

VAR_012410

Natural variant

259

1

P → L in FD. Ref.42 Ref.46

VAR_012411

Natural variant

259

1

P → R in FD. Ref.42 Ref.46

VAR_012412

Natural variant

260

1

G → A in FD. Ref.23 Ref.33 Ref.38

VAR_012413

Natural variant

261

1

G → D in FD. Ref.33

VAR_012414

Natural variant

263

1

N → S in FD. Ref.34

VAR_012415

Natural variant

264

1

D → V in FD. dbSNP rs28935486. Ref.19

VAR_000471

Natural variant

265

1

P → R in FD. Ref.30

VAR_012416

Natural variant

266

1

D → H in FD. Ref.19 Ref.43 Ref.44

VAR_032291

Natural variant

266

1

D → N in FD. Ref.19 Ref.43 Ref.44

VAR_012418

Natural variant

266

1

D → V in FD. dbSNP rs28935487. Ref.19 Ref.43 Ref.44

VAR_000472

Natural variant

267

1

M → I in FD. Ref.42 Ref.46

VAR_012419

Natural variant

269

1

V → A in FD. dbSNP rs28935488. Ref.20

VAR_000473

Natural variant

272

1

N → K in FD. Ref.50

VAR_000474

Natural variant

272

1

N → S in FD. dbSNP rs28935495. Ref.50

VAR_032292

Natural variant

279

1

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. Ref.18 Ref.23 Ref.33 Ref.41 Ref.46

VAR_000475

Natural variant

279

1

Q → H in FD. Ref.18 Ref.23 Ref.33 Ref.41 Ref.46

VAR_012420

Natural variant

280

1

Q → H in FD. Ref.38 Ref.46

VAR_012421

Natural variant

284

1

M → T in FD. Ref.31

VAR_000476

Natural variant

287

1

W → C in FD. Ref.28 Ref.34

VAR_012422

Natural variant

287

1

W → G in FD. Ref.28 Ref.34

VAR_012423

Natural variant

288

1

A → D in FD.

VAR_000477

Natural variant

289

1

I → F in FD. Ref.42

VAR_012424

Natural variant

296

1

M → I in FD; atypical. Ref.15 Ref.23 Ref.26 Ref.33

VAR_012425

Natural variant

296

1

M → V in FD; mild. Ref.15 Ref.23 Ref.26 Ref.33

VAR_000478

Natural variant

297

1

S → F in FD. dbSNP rs28935489. Ref.19

VAR_000479

Natural variant

298

1

N → H in FD. Ref.28 Ref.31 Ref.34 Ref.46

VAR_012426

Natural variant

298

1

N → K in FD. Ref.28 Ref.31 Ref.34 Ref.46

VAR_000480

Natural variant

298

1

N → S in FD. Ref.28 Ref.31 Ref.34 Ref.46

VAR_012427

Natural variant

301

1

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. Ref.16 Ref.18 Ref.23 Ref.25 Ref.27 Ref.33 Ref.39 Ref.41 Ref.44

VAR_000481

Natural variant

313

1

D → Y in FD. dbSNP rs28935490. Ref.19 Ref.38 Ref.46

VAR_000482

Natural variant

316 – 322

7

Missing in FD. Ref.21 Ref.30

VAR_012429

Natural variant

316

1

V → E in FD. Ref.21

VAR_000483

Natural variant

320

1

N → K in FD. Ref.23 Ref.33 Ref.38 Ref.44

VAR_012430

Natural variant

320

1

N → Y in FD. Ref.23 Ref.33 Ref.38 Ref.44

VAR_012431

Natural variant

321

1

Q → E in FD. Ref.42

VAR_012432

Natural variant

327

1

Q → K in FD. dbSNP rs28935491. Ref.20 Ref.39

VAR_000484

Natural variant

328

1

G → A in FD. Ref.18 Ref.19 Ref.23 Ref.33

VAR_000486

Natural variant

328

1

G → R in FD. Ref.18 Ref.19 Ref.23 Ref.33

VAR_000485

Natural variant

340

1

W → R in FD. Ref.28 Ref.38

VAR_012433

Natural variant

341

1

E → K in FD. Ref.40

VAR_012434

Natural variant

342

1

R → Q in FD; severe. dbSNP rs28935493.

VAR_000487

Natural variant

356

1

R → W in FD; severe. Ref.17

VAR_000488

Natural variant

358

1

E → K in FD. Ref.31 Ref.33 Ref.36 Ref.42

VAR_000489

Natural variant

358

1

Missing in FD. Ref.31 Ref.33 Ref.36 Ref.42

VAR_000490

Natural variant

361

1

G → R in FD; severe. dbSNP rs28935494. Ref.20

VAR_000491

Natural variant

363

1

R → H in FD. Ref.46

VAR_012435

Natural variant

373

1

G → D in FD. Ref.23 Ref.33 Ref.45

VAR_012436

Natural variant

373

1

G → S in FD. Ref.23 Ref.33 Ref.45

VAR_012437

Natural variant

377

1

A → D in FD. Ref.46

VAR_012438

Natural variant

378

1

C → Y in FD. Ref.42

VAR_012439

Natural variant

383

1

Missing in FD; severe; with facial telangiectasias. Ref.29

VAR_000492

Natural variant

396

1

F → Y in RNA edited version.

VAR_000493

Natural variant

404

1

Missing in FD; mild. Ref.19 Ref.34

VAR_000494

Natural variant

409

1

P → A in FD. Ref.46

VAR_012440

Natural variant

409

1

P → T in FD. Ref.46

VAR_012441

Natural variant

410

1

T → A in FD; mild. Ref.38 Ref.48

VAR_032293

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

429

Helix Strand Turn

Details...

Beta strand

42 – 46

5

Helix

47 – 50

4

Turn

56 – 58

3

Turn

60 – 62

3

Helix

66 – 78

13

Helix

81 – 84

4

Beta strand

88 – 90

3

Turn

110 – 112

3

Helix

116 – 126

11

Beta strand

130 – 140

11

Beta strand

144 – 146

3

Turn

149 – 151

3

Helix

152 – 162

11

Beta strand

166 – 170

5

Helix

177 – 194

18

Beta strand

199 – 202

4

Helix

204 – 208

5

Turn

209 – 211

3

Helix

216 – 219

4

Turn

220 – 222

3

Beta strand

224 – 227

4

Helix

236 – 247

12

Turn

248 – 252

5

Helix

253 – 256

4

Beta strand

261 – 264

4

Beta strand

272 – 274

3

Helix

277 – 289

13

Beta strand

294 – 296

3

Helix

305 – 312

8

Helix

314 – 320

7

Beta strand

329 – 332

4

Beta strand

334 – 343

10

Beta strand

345 – 355

11

Beta strand

359 – 361

3

Beta strand

363 – 369

7

Turn

370 – 372

3

Turn

374 – 376

3

Beta strand

379 – 383

5

Beta strand

385 – 390

6

Beta strand

396 – 400

5

Beta strand

402 – 407

6

Beta strand

412 – 419

8

Sequences

	Sequence		Length	Mass (Da)
	P06280-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 613F8BF21B107D7B	FASTA	429	48,767
	10 20 30 40 50 60 MQLRNPELHL GCALALRFLA LVSWDIPGAR ALDNGLARTP TMGWLHWERF MCNLDCQEEP 70 80 90 100 110 120 DSCISEKLFM EMAELMVSEG WKDAGYEYLC IDDCWMAPQR DSEGRLQADP QRFPHGIRQL 130 140 150 160 170 180 ANYVHSKGLK LGIYADVGNK TCAGFPGSFG YYDIDAQTFA DWGVDLLKFD GCYCDSLENL 190 200 210 220 230 240 ADGYKHMSLA LNRTGRSIVY SCEWPLYMWP FQKPNYTEIR QYCNHWRNFA DIDDSWKSIK 250 260 270 280 290 300 SILDWTSFNQ ERIVDVAGPG GWNDPDMLVI GNFGLSWNQQ VTQMALWAIM AAPLFMSNDL 310 320 330 340 350 360 RHISPQAKAL LQDKDVIAIN QDPLGKQGYQ LRQGDNFEVW ERPLSGLAWA VAMINRQEIG 370 380 390 400 410 420 GPRSYTIAVA SLGKGVACNP ACFITQLLPV KRKLGFYEWT SRLRSHINPT GTVLLQLENT MQMSLKDLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A." 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. Eur. J. Biochem. 165:275-280(1987) [PubMed: 3036505] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast.
[2]	"Nucleotide sequence of the human alpha-galactosidase A gene." Kornreich R., Desnick R.J., Bishop D.F. Nucleic Acids Res. 17:3301-3302(1989) [PubMed: 2542896] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Lymphoblast.
[3]	"Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci." Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W., Gibbs R.A. Mamm. Genome 6:334-338(1995) [PubMed: 7626884] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The DNA sequence of the human X chromosome." 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. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[6]	"Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme." Bishop D.F., Calhoun D.H., Bernstein H.S., Hantzopoulos P., Quinn M., Desnick R.J. Proc. Natl. Acad. Sci. U.S.A. 83:4859-4863(1986) [PubMed: 3014515] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-429, PARTIAL PROTEIN SEQUENCE. Tissue: Lung.
[7]	"A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A." Quinn M., Hantzopoulos P., Fidanza V., Calhoun D.H. Gene 58:177-188(1987) [PubMed: 2892762] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
[8]	"Structural organization of the human alpha-galactosidase A gene: further evidence for the absence of a 3' untranslated region." Bishop D.F., Kornreich R., Desnick R.J. Proc. Natl. Acad. Sci. U.S.A. 85:3903-3907(1988) [PubMed: 2836863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
[9]	"Editing of human alpha-galactosidase RNA resulting in a pyrimidine to purine conversion." Novo F.J., Kruszewski A., McDermot K.D., Goldspink G., Gorecki D.C. Nucleic Acids Res. 23:2636-2640(1995) [PubMed: 7503918] [Abstract] Cited for: RNA EDITING OF POSITION 396.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-215, MASS SPECTROMETRY. Tissue: Liver.
[12]	"The molecular defect leading to Fabry disease: structure of human alpha-galactosidase." Garman S.C., Garboczi D.N. J. Mol. Biol. 337:319-335(2004) [PubMed: 15003450] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 32-422 IN COMPLEX WITH PRODUCT, HOMODIMERIZATION, GLYCOSYLATION AT ASN-139; ASN-192 AND ASN-215.
[13]	"Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene." Eng C.M., Desnick R.J. Hum. Mutat. 3:103-111(1994) [PubMed: 7911050] [Abstract] Cited for: REVIEW ON FD VARIANTS.
[14]	"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." Koide T., Ishiura M., Iwai K., Inoue M., Kaneda Y., Okada Y., Uchida T. FEBS Lett. 259:353-356(1990) [PubMed: 2152885] [Abstract] Cited for: VARIANT FD SER-40.
[15]	"An atypical variant of Fabry's disease with manifestations confined to the myocardium." 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. N. Engl. J. Med. 324:395-399(1991) [PubMed: 1846223] [Abstract] Cited for: VARIANT FD VAL-296.
[16]	"Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease." Sakuraba H., Oshima A., Fukuhara Y., Shimmoto M., Nagao Y., Bishop D.F., Desnick R.J., Suzuki Y. Am. J. Hum. Genet. 47:784-789(1990) [PubMed: 2171331] [Abstract] Cited for: VARIANT FD GLN-301.
[17]	"Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene." Bernstein H.S., Bishop D.F., Astrin K.H., Kornreich R., Eng C.M., Sakuraba H., Desnick R.J. J. Clin. Invest. 83:1390-1399(1989) [PubMed: 2539398] [Abstract] Cited for: VARIANT FD TRP-356.
[18]	"Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease." Ishii S., Sakuraba H., Suzuki Y. Hum. Genet. 89:29-32(1992) [PubMed: 1315715] [Abstract] Cited for: VARIANTS FD GLN-66; CYS-112; GLU-279; GLN-301 AND ARG-328.
[19]	"Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease." Eng C.M., Resnick-Silverman L.A., Niehaus D.J., Astrin K.H., Desnick R.J. Am. J. Hum. Genet. 53:1186-1197(1993) [PubMed: 7504405] [Abstract] Cited for: VARIANTS FD SER-34; GLY-56; ARG-162; GLN-227; VAL-264; VAL-266; PHE-297; TYR-313; ALA-328 AND ARG-404 DEL.
[20]	"Mutation analysis in patients with the typical form of Anderson-Fabry disease." Davies J.P., Winchester B.G., Malcolm S. Hum. Mol. Genet. 2:1051-1053(1993) [PubMed: 8395937] [Abstract] Cited for: VARIANTS FD SER-34; SER-215; ALA-269; LYS-327 AND ARG-361.
[21]	"Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry disease." Davies J.P., Christomanou H., Winchester B.G., Malcolm S. Hum. Mol. Genet. 3:667-669(1994) [PubMed: 8069316] [Abstract] Cited for: VARIANTS FD ARG-35; LEU-49; VAL-165 AND GLU-316.
[22]	"Fabry disease: twenty-three mutations including sense and antisense CpG alterations and identification of a deletional hot-spot in the alpha-galactosidase A gene." Eng C.M., Niehaus D.J., Enriquez A.L., Burgert T.S., Ludman M.D., Desnick R.J. Hum. Mol. Genet. 3:1795-1799(1994) [PubMed: 7531540] [Abstract] Cited for: VARIANTS FD.
[23]	"Galactose stabilizes various missense mutants of alpha-galactosidase in Fabry disease." Okumiya T., Ishii S., Takenaka T., Kase R., Kamei S., Sakuraba H., Suzuki Y. Biochem. Biophys. Res. Commun. 214:1219-1224(1995) [PubMed: 7575533] [Abstract] Cited for: 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.
[24]	"Alpha-galactosidase gene mutations in Fabry disease: heterogeneous expressions of mutant enzyme proteins." Okumiya T., Ishii S., Kase R., Kamei S., Sakuraba H., Suzuki Y. Hum. Genet. 95:557-561(1995) [PubMed: 7759078] [Abstract] Cited for: VARIANTS FD TYR-142; VAL-156 AND VAL-166.
[25]	"Two novel mutations (L32P) and (G85N) among five different missense mutations in six Danish families with Fabry's disease." Madsen K.M., Hasholt L., Soerensen S.A., Lagerstroem Fermer M., Dahl N. Hum. Mutat. 5:277-278(1995) [PubMed: 7599642] [Abstract] Cited for: VARIANTS FD PRO-32; SER-34; ASP-85; THR-156 AND GLN-301.
[26]	"An atypical variant of Fabry's disease in men with left ventricular hypertrophy." Nakao S., Takenaka T., Maeda M., Kodama C., Tanaka A., Tahara M., Yoshida A., Kuriyama M., Hayashibe H., Sakuraba H., Tanaka H. N. Engl. J. Med. 333:288-293(1995) [PubMed: 7596372] [Abstract] Cited for: VARIANTS FD PRO-20 AND ILE-296.
[27]	"Point mutation in the alpha-galactosidase A gene of atypical Fabry disease with only nephropathy." Sawada K., Mizoguchi K., Hishida A., Kaneko E., Koide Y., Nishimura K., Kimura M. Clin. Nephrol. 45:289-294(1996) [PubMed: 8738659] [Abstract] Cited for: VARIANT FD GLN-301.
[28]	"Fabry disease: fourteen alpha-galactosidase A mutations in unrelated families from the United Kingdom and other European countries." Davies J.P., Eng C.M., Hill J.A., Malcolm S., MacDermot K., Winchester B.G., Desnick R.J. Eur. J. Hum. Genet. 4:219-224(1996) [PubMed: 8875188] [Abstract] Cited for: VARIANTS FD VAL-42; SER-49; TYR-56; HIS-92; GLY-93; THR-205; CYS-236; GLY-287; HIS-298 AND ARG-340.
[29]	"Novel trinucleotide deletion in Fabry's disease." Cariolou M.A., Christodoulides M., Manoli P., Kokkofitou A., Tsambaos D. Hum. Genet. 97:468-470(1996) [PubMed: 8834244] [Abstract] Cited for: VARIANT FD PHE-383 DEL.
[30]	"Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of the alpha-galactosidase A gene and detection of carriers in Fabry disease." Germain D.P., Biasotto M., Tosi M., Meo T., Kahn A., Poenaru L. Hum. Genet. 98:719-726(1996) [PubMed: 8931708] [Abstract] Cited for: VARIANTS FD ARG-52; CYS-162; ARG-265 AND 316-VAL--ASP-322 DEL.
[31]	"A sensitive mutation screening strategy for Fabry disease: detection of nine mutations in the alpha-galactosidase A gene." Blanch L.C., Meaney C., Morris C.P. Hum. Mutat. 8:38-43(1996) [PubMed: 8807334] [Abstract] Cited for: VARIANTS FD ARG-52; GLU-128; THR-205; THR-284; LYS-298 AND GLU-358 DEL.
[32]	"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." Redonnet-Vernhet I., Ploos van Amstel J.K., Jansen R.P.M., Wevers R.A., Salvayre R., Levade T. J. Med. Genet. 33:682-688(1996) [PubMed: 8863162] [Abstract] Cited for: VARIANT FD ASN-231.
[33]	"Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis." Takata T., Okumiya T., Hayashibe H., Shimmoto M., Kase R., Itoh K., Utsumi K., Kamei S., Sakuraba H. Brain Dev. 19:111-116(1997) [PubMed: 9105656] [Abstract] Cited for: 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.
[34]	"Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in patients with classic and variant phenotypes." Eng C.M., Ashley G.A., Burgert T.S., Enriquez A.L., D'Souza M., Desnick R.J. Mol. Med. 3:174-182(1997) [PubMed: 9100224] [Abstract] Cited for: 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.
[35]	"Identification of a novel point mutation (S65T) in alpha-galactosidase A gene in Chinese patients with Fabry disease." Chen C.-H., Shyu P.-W., Wu S.-J., Sheu S.-S., Desnick R.J., Hsiao K.-J. Hum. Mutat. 11:328-330(1998) [PubMed: 9554750] [Abstract] Cited for: VARIANT FD THR-65.
[36]	"A novel mutation (E358K) in the alpha-galactosidase A gene detected in a Japanese family with Fabry disease." Miyazaki T., Kajita M., Ohmori S., Mizutani N., Niwa T., Murata Y., Seo H. Hum. Mutat. Suppl. 1:S139-S140(1998) [PubMed: 9452068] [Abstract] Cited for: VARIANT FD LYS-358.
[37]	"Novel missense mutation (M72V) of alpha-galactosidase gene and its expression product in an atypical Fabry hemizygote." Okumiya T., Kawamura O., Itoh K., Kase R., Ishii S., Kamei S., Sakuraba H. Hum. Mutat. Suppl. 1:S213-S216(1998) [PubMed: 9452090] [Abstract] Cited for: VARIANT FD VAL-72.
[38]	"Mutation analysis in 11 French patients with Fabry disease." Guffon N., Froissart R., Chevalier-Porst F., Maire I. Hum. Mutat. Suppl. 1:S288-S290(1998) [PubMed: 9452111] [Abstract] Cited for: VARIANTS FD SER-40; SER-215; ASP-224; TYR-313 AND TRP-THR-SER-247 INS.
[39]	"Fabry disease: identification of novel alpha-galactosidase A mutations and molecular carrier detection by use of fluorescent chemical cleavage of mismatches." Germain D.P., Poenaru L. Biochem. Biophys. Res. Commun. 257:708-713(1999) [PubMed: 10208848] [Abstract] Cited for: VARIANTS FD TRP-202; GLY-223; ASP-224; GLN-301 AND LYS-327.
[40]	"The multiple cases of Fabry disease in a Russian family caused by an E341K amino acid substitution in the alpha-galactosidase A." Beyer E.M., Karpova E.A., Udalova O.V., Ploos van Amstel J.K., van Diggelen O.P., Tsvetkova I.V. Clin. Chim. Acta 280:81-89(1999) [PubMed: 10090526] [Abstract] Cited for: VARIANT FD LYS-341.
[41]	"Characterization of two alpha-galactosidase mutants (Q279E and R301Q) found in an atypical variant of Fabry disease." Kase R., Bierfreund U., Klein A., Kolter T., Utsumi K., Itoh K., Sandhoff K., Sakuraba H. Biochim. Biophys. Acta 1501:227-235(2000) [PubMed: 10838196] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS FD GLU-279 AND GLN-301.
[42]	"Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease." Topaloglu A.K., Ashley G.A., Tong B., Shabbeer J., Astrin K.H., Eng C.M., Desnick R.J. Mol. Med. 5:806-811(1999) [PubMed: 10666480] [Abstract] Cited for: 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.
[43]	"Identification of four novel mutations in five unrelated Korean families with Fabry disease." Lee J.-K., Kim G.-H., Kim J.-S., Kim K.-K., Lee M.-C., Yoo H.-W. Clin. Genet. 58:228-233(2000) [PubMed: 11076046] [Abstract] Cited for: VARIANT FD ASN-266.
[44]	"Fabry disease: twenty-two novel mutations in the alpha-galactosidase A gene and genotype/phenotype correlations in severely and mildly affected hemizygotes and heterozygotes." Ashton-Prolla P., Tong B., Shabbeer J., Astrin K.H., Eng C.M., Desnick R.J. J. Invest. Med. 48:227-235(2000) [PubMed: 10916280] [Abstract] Cited for: 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.
[45]	"Identification of a novel de novo mutation (G373D) in the alpha-galactosidase A gene (GLA) in a patient affected with Fabry disease." Germain D.P., Salard D., Fellmann F., Azibi K., Caillaud C., Bernard M.-C., Poenaru L. Hum. Mutat. 17:353-353(2001) [PubMed: 11295840] [Abstract] Cited for: VARIANT FD ASP-373.
[46]	"Fabry disease: 20 novel GLA mutations in 35 families." Blaydon D., Hill J.A., Winchester B.G. Hum. Mutat. 18:459-459(2001) [PubMed: 11668641] [Abstract] Cited for: 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.
[47]	"Natural history of Fabry renal disease: influence of alpha-galactosidase A activity and genetic mutations on clinical course." 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. Medicine (Baltimore) 81:122-138(2002) [PubMed: 11889412] [Abstract] Cited for: VARIANT FD PRO-143.
[48]	"Two novel mutations in the alpha-galactosidase A gene in Chinese patients with Fabry disease." Yang C.-C., Lai L.-W., Whitehair O., Hwu W.-L., Chiang S.-C., Lien Y.-H.H. Clin. Genet. 63:205-209(2003) [PubMed: 12694230] [Abstract] Cited for: VARIANT FD ALA-410.
[49]	"Analysis of splice-site mutations of the alpha-galactosidase A gene in Fabry disease." Lai L.-W., Whitehair O., Wu M.-J., O'Meara M., Lien Y.-H.H. Clin. Genet. 63:476-482(2003) [PubMed: 12786754] [Abstract] Cited for: CHARACTERIZATION OF VARIANT FD THR-65.
[50]	"Remarkable variability in renal disease in a large Slovenian family with Fabry disease." Verovnik F., Benko D., Vujkovac B., Linthorst G.E. Eur. J. Hum. Genet. 12:678-681(2004) [PubMed: 15162124] [Abstract] Cited for: VARIANT FD SER-272.
[51]	"Later-onset Fabry disease: an adult variant presenting with the cramp-fasciculation syndrome." Nance C.S., Klein C.J., Banikazemi M., Dikman S.H., Phelps R.G., McArthur J.C., Rodriguez M., Desnick R.J. Arch. Neurol. 63:453-457(2006) [PubMed: 16533976] [Abstract] Cited for: VARIANT FD THR-143.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

X05790 mRNA. Translation: CAA29232.1.
X14448 Genomic DNA. Translation: CAA32617.1.
U78027 Genomic DNA. Translation: AAB64203.1.
AL035422 Genomic DNA. Translation: CAB55878.1.
BC002689 mRNA. Translation: AAH02689.1.
M13571 Genomic DNA. Translation: AAA51676.1.
D00039 mRNA. No translation available.
M18242 Genomic DNA. Translation: AAA52514.1.
X16889 mRNA. No translation available.
M20317 Genomic DNA. Translation: AAA52559.1. Sequence problems.

IPI

IPI00025869.

PIR

GBHUA. S04081.

RefSeq

NP_000160.1.

UniGene

Hs.69089

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R46	X-ray	3.25	A/B	32-429	[»]
1R47	X-ray	3.45	A/B	32-429	[»]
3GXN	X-ray	3.01	A/B	32-429	[»]
3GXP	X-ray	2.20	A/B	32-429	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH27. Glycoside Hydrolase Family 27.

PTM databases

PhosphoSite

P06280.

Proteomic databases

PeptideAtlas

P06280.

PRIDE

P06280.

Genome annotation databases

Ensembl

ENSG00000102393. Homo sapiens. [Contig view]

GeneID

2717.

KEGG

hsa:2717.

Organism-specific databases

GeneCards

GC0XM100539.

H-InvDB

HIX0016928.

HGNC

HGNC:4296. GLA.

HPA

HPA000237.
HPA000966.

MIM

300644. gene.
301500. phenotype.

Orphanet

324. Fabry disease.

PharmGKB

PA28707.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P06280.

HOVERGEN

P06280.

OMA

P06280. CWMAPQR.

Enzyme and pathway databases

BRENDA

3.2.1.22. 247.

Gene expression databases

ArrayExpress

P06280.

Bgee

P06280.

CleanEx

HS_GLA.

GermOnline

ENSG00000102393. Homo sapiens.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.

Pfam

PF02065. Melibiase. 1 hit.
[Graphical view]

PRINTS

PR00740. GLHYDRLASE27.

ProDom

PD002572. Glyco_hydro_GHD. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00103. Agalsidase beta.

NextBio

10728.

SOURCE

Search...

Entry information

Entry name

AGAL_HUMAN

Accession

Primary (citable) accession number: P06280

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	August 1, 1988
Last modified:	June 16, 2009
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)