ID A0A8M1RH12_DANRE Unreviewed; 956 AA. AC A0A8M1RH12; E7FCP7; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 27-MAR-2024, entry version 10. DE SubName: Full=Lysosomal alpha-glucosidase isoform X2 {ECO:0000313|RefSeq:XP_002660410.1, ECO:0000313|RefSeq:XP_005170936.1}; DE SubName: Full=Si:ch73-12o23.1 {ECO:0000313|Ensembl:ENSDARP00000101564}; GN Name=gaa2 {ECO:0000313|ZFIN:ZDB-GENE-130530-749}; GN Synonyms=si:ch73-12o23.1 {ECO:0000313|RefSeq:XP_002660410.1, GN ECO:0000313|RefSeq:XP_005170936.1, ECO:0000313|RefSeq:XP_021331622.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_002660410.1}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000101564} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000101564}; RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000101564, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000101564}; RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [3] {ECO:0000313|RefSeq:XP_002660410.1, ECO:0000313|RefSeq:XP_005170936.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_002660410.1, RC ECO:0000313|RefSeq:XP_005170936.1}; RG RefSeq; RL Submitted (NOV-2023) to UniProtKB. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00779}. 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; CU104756; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU914772; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002660410.1; XM_002660364.5. DR RefSeq; XP_005170936.1; XM_005170879.4. DR RefSeq; XP_021331622.1; XM_021475947.1. DR STRING; 7955.ENSDARP00000101564; -. DR PaxDb; 7955-ENSDARP00000101564; -. DR Ensembl; ENSDART00000110790; ENSDARP00000101564; ENSDARG00000074282. DR Ensembl; ENSDART00000110790.4; ENSDARP00000101564.2; ENSDARG00000074282.4. DR GeneID; 100332784; -. DR KEGG; dre:100332784; -. DR AGR; ZFIN:ZDB-GENE-130530-749; -. DR CTD; 100332784; -. DR ZFIN; ZDB-GENE-130530-749; gaa2. DR eggNOG; KOG1065; Eukaryota. DR HOGENOM; CLU_000631_11_2_1; -. DR OMA; YKGAVWP; -. DR OrthoDB; 5480935at2759; -. DR TreeFam; TF314577; -. DR Proteomes; UP000000437; Chromosome 1. DR Bgee; ENSDARG00000074282; Expressed in blastula and 21 other cell types or tissues. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd06602; GH31_MGAM_SI_GAA; 1. DR CDD; cd14752; GH31_N; 1. DR CDD; cd00111; Trefoil; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2. DR Gene3D; 4.10.110.10; Spasmolytic Protein, domain 1; 1. DR InterPro; IPR011013; Gal_mutarotase_sf_dom. DR InterPro; IPR030458; Glyco_hydro_31_AS. DR InterPro; IPR048395; Glyco_hydro_31_C. DR InterPro; IPR030459; Glyco_hydro_31_CS. DR InterPro; IPR025887; Glyco_hydro_31_N_dom. DR InterPro; IPR000322; Glyco_hydro_31_TIM. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR000519; P_trefoil_dom. DR InterPro; IPR044913; P_trefoil_dom_sf. DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1. DR PANTHER; PTHR22762:SF104; P-TYPE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF13802; Gal_mutarotas_2; 1. DR Pfam; PF01055; Glyco_hydro_31_2nd; 1. DR Pfam; PF21365; Glyco_hydro_31_3rd; 1. DR Pfam; PF00088; Trefoil; 1. DR SMART; SM00018; PD; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. DR SUPFAM; SSF57492; Trefoil; 1. DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1. DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1. DR PROSITE; PS51448; P_TREFOIL_2; 1. PE 1: Evidence at protein level; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Glycosidase {ECO:0000256|RuleBase:RU361185}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361185}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A8M1RH12}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 50..74 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 99..153 FT /note="P-type" FT /evidence="ECO:0000259|PROSITE:PS51448" FT REGION 79..103 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 85..101 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 956 AA; 107970 MW; D5BE50DE95ADD4C6 CRC64; MVSYERLTPE EVHFSGAALL DNDESTDADL KEGDPELPLL PQSPRCSITA ALLTLGGLIV VLSAVWLLGT LFWIHNPPST ESHRPPSPKS QNGTGLQPES CSQVPEGWRF DCYPERNVVV TEDMCHARNC CFIQSSRGNV SAQNGVPWCF YTPDYPSYEL MSIVDTEMGK VGKLLRNKKT YYPKDIDALQ LEVLFEEDHR LRVKITDPTE KRYEVPIDVP VVHKRASNPS YTVDFIKEPF GLIVKRTQTG AVLLNTSIAP LFYADQFLQM SSSLPTRFIY GLGEHRSNFL HDVQWNTLTM WARDVPPMEL TNLYGVHPFY LSMESDGNAH GFFMLNSNAM DVVLQPAPAV TWRMIGGILD FYIFLGPDPS SVIGQYLDVV GKPAMPIYWA LGYHLCRWGY KTSNKTWSVV KEMRNYGIPQ DVQWNDIDYM DRSLDFTYDP SGFSTLPDLV KDLQRHDQHY VMILDPGISN SQPPGSYWPF DEGKKKGIFI NDSNGDILIG KVWPGLTAFP DFSNPDTHEW WYQNLQRFHN KVPFDGVWID MNEPSNFFDG SLNGCPDNEL ENPPYTPGIL GGTLKGKTVC ASARQKISVH YNIHSLYGLM EAQATESALR RITKKRPFII SRSTFPSQGK YSGHWLGDNR SQWKDLATSI PGMLTFNILG IPLIGADICG FGGSTTEELC VRWTQLGAFY PFTRNHNSID EQDQEPTAFS PAARTAMKEA ILLRYSLFPH LYTLFHHAHV SGHTVATPLL FQFPTDEKTY GIDKQFLWGK SLLVTPVLDA GRDYVVGYFP KGLWYDFHTG NSLISSGEEI KLEAPADKIN LHLREGSVIP TQRPNTTLWV SSGQPLHLIV SLSEDGRAKG DLYWDDGETI DSYESNQYAY IYFTVEQNTM MSEVLHNHEE ATYITVETAS FYGVKAKPEN VTVNSQEAAF TYLDNQVLTV TDLGLNLSHN FTISWM //