ID   A0A8M1RH12_DANRE        Unreviewed;       956 AA.
AC   A0A8M1RH12; A0AC58JG41; E7FCP7;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   28-JAN-2026, sequence version 2.
DT   02-SEP-2026, entry version 21.
DE   RecName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000256|PROSITE-ProRule:PRU10066};
DE            EC=3.2.1.3 {ECO:0000256|PROSITE-ProRule:PRU10066};
GN   Name=gaa2 {ECO:0000313|RefSeq:XP_002660410.2,
GN   ECO:0000313|RefSeq:XP_005170936.2, ECO:0000313|RefSeq:XP_073805452.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-130530-749};
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_002660410.2};
RN   [1] {ECO:0000313|RefSeq:XP_002660410.2, ECO:0000313|RefSeq:XP_005170936.2}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_002660410.2,
RC   ECO:0000313|RefSeq:XP_005170936.2};
RC   TISSUE=Fibroblasts and whole tissue
RC   {ECO:0000313|RefSeq:XP_002660410.2,
RC   ECO:0000313|RefSeq:XP_005170936.2};
RG   RefSeq;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC         successively from non-reducing ends of the chains with release of
CC         beta-D-glucose.; EC=3.2.1.3; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU10066};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
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}.
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DR   RefSeq; XP_002660410.2; XM_002660364.7.
DR   RefSeq; XP_005170936.2; XM_005170879.6.
DR   RefSeq; XP_073805452.1; XM_073949351.1.
DR   AlphaFoldDB; A0A8M1RH12; -.
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   OMA; PYVINHD; -.
DR   OrthoDB; 5839090at2759; -.
DR   Proteomes; UP000000437; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProtKB-ARBA.
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   FunFam; 3.20.20.80:FF:000072; lysosomal alpha-glucosidase isoform X2; 1.
DR   FunFam; 2.60.40.1180:FF:000001; Maltase-glucoamylase, intestinal; 1.
DR   FunFam; 2.60.40.1760:FF:000001; Maltase-glucoamylase, intestinal; 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; IPR017853; GH_hydrolase_sf.
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; 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|ARBA:ARBA00023295, 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        89..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        540
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10066"
SQ   SEQUENCE   956 AA;  107973 MW;  8986DEBCD400451D 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 LSMEADGNAH 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 SGRTVATPLL FQFPTDEKTY GIDKQFLWGK SLLVTPVLDA
     GRDYVVGYFP KGLWYDFHTG NSLISSGEEI KLEAPADKIN LHLREGSVIP TQRPNTTLWV
     SSGQPLHLIV SLSEDGRAKG DLYWDDGETI DSYESNQYAY IYFTVEQNTM MSEVLHNHEE
     ATYITVETAS FYGVKAKPEN VTVNSQEAAF TYLDNQVLTV TDLGLNLSHN FTISWM
//