ID A0A3B3IUC4_HUMAN Unreviewed; 470 AA. AC A0A3B3IUC4; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 13-FEB-2019, entry version 3. DE RecName: Full=Alpha-galactosidase {ECO:0000256|RuleBase:RU361168}; DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361168}; GN Name=GLA {ECO:0000313|Ensembl:ENSP00000498186}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000498186, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000498186, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000213|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [4] {ECO:0000313|Ensembl:ENSP00000498186} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2018) to UniProtKB. CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU361168}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. CC {ECO:0000256|RuleBase:RU361168, ECO:0000256|SAAS:SAAS01073723}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL035422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENST00000649178; ENSP00000498186; ENSG00000102393. DR HGNC; HGNC:4296; GLA. DR OpenTargets; ENSG00000102393; -. DR GeneTree; ENSGT00390000008751; -. DR Proteomes; UP000005640; Chromosome X. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd14792; GH27; 1. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.20.20.70; -; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR002241; Glyco_hydro_27. DR InterPro; IPR000111; Glyco_hydro_27/36_CS. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR035373; Melibiase/NAGA_C. DR PANTHER; PTHR11452; PTHR11452; 2. DR Pfam; PF16499; Melibiase_2; 2. DR Pfam; PF17450; Melibiase_2_C; 1. DR PRINTS; PR00740; GLHYDRLASE27. DR SUPFAM; SSF51445; SSF51445; 1. DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|RuleBase:RU361168}; KW Glycosidase {ECO:0000256|RuleBase:RU361168, KW ECO:0000256|SAAS:SAAS01073727}; KW Hydrolase {ECO:0000256|RuleBase:RU361168, KW ECO:0000256|SAAS:SAAS01073727}; KW Proteomics identification {ECO:0000213|EPD:A0A3B3IUC4, KW ECO:0000213|MaxQB:A0A3B3IUC4, ECO:0000213|PeptideAtlas:A0A3B3IUC4}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 470 Alpha-galactosidase. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5017251743. FT DOMAIN 366 452 Melibiase_2_C. FT {ECO:0000259|Pfam:PF17450}. SQ SEQUENCE 470 AA; 53284 MW; D1BD6EC730677AAE CRC64; MQLRNPELHL GCALALRFLA LVSWDIPGAR ALDNGLARTP TMGWLHWERF MCNLDCQEEP DSCISWSFAL VAQAGVQCHD LGSPQPPPPR FKQFSCLILA SSWNYSEKLF MEMAELMVSE GWKDAGYEYL CIDDCWMAPQ RDSEGRLQAD PQRFPHGIRQ LANYVHSKGL KLGIYADVGN KTCAGFPGSF GYYDIDAQTF ADWGVDLLKF DGCYCDSLEN LADGYKHMSL ALNRTGRSIV YSCEWPLYMW PFQKPNYTEI RQYCNHWRNF ADIDDSWKSI KSILDWTSFN QERIVDVAGP GGWNDPDMLV IGNFGLSWNQ QVTQMALWAI MAAPLFMSND LRHISPQAKA LLQDKDVIAI NQDPLGKQGY QLRQGDNFEV WERPLSGLAW AVAMINRQEI GGPRSYTIAV ASLGKGVACN PACFITQLLP VKRKLGFYEW TSRLRSHINP TGTVLLQLEN TMQMSLKDLL //