ID MGA_HUMAN Reviewed; 2753 AA. AC O43451; E7ER45; Q0VAX6; Q75ME7; Q86UM5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 6. DT 27-MAR-2024, entry version 196. DE RecName: Full=Maltase-glucoamylase {ECO:0000303|PubMed:22058037}; DE AltName: Full=Alpha-1,4-glucosidase; DE EC=3.2.1.20 {ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037, ECO:0000269|PubMed:27480812}; GN Name=MGAM {ECO:0000303|PubMed:27480812, ECO:0000312|HGNC:HGNC:7043}; GN Synonyms=MGA, MGAML; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT RP ASP-858, AND TISSUE SPECIFICITY. RC TISSUE=Small intestine; RX PubMed=9446624; DOI=10.1074/jbc.273.5.3076; RA Nichols B.L., Eldering J.A., Avery S.E., Hahn D., Quaroni A., Sterchi E.E.; RT "Human small intestinal maltase-glucoamylase cDNA cloning. Homology to RT sucrase-isomaltase."; RL J. Biol. Chem. 273:3076-3081(1998). RN [2] RP SEQUENCE REVISION TO 777; 1050; 1101; 1542; 2509 AND 2708. RA Nichols B.L., Eldering J.A., Avery S.E., Hahn D., Quaroni A., Sterchi E.E.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2). RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-858. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Kidney, and Stomach; RX PubMed=24309898; DOI=10.1074/mcp.m113.035600; RA Fagerberg L., Hallstroem B.M., Oksvold P., Kampf C., Djureinovic D., RA Odeberg J., Habuka M., Tahmasebpoor S., Danielsson A., Edlund K., RA Asplund A., Sjoestedt E., Lundberg E., Szigyarto C.A., Skogs M., RA Takanen J.O., Berling H., Tegel H., Mulder J., Nilsson P., Schwenk J.M., RA Lindskog C., Danielsson F., Mardinoglu A., Sivertsson A., von Feilitzen K., RA Forsberg M., Zwahlen M., Olsson I., Navani S., Huss M., Nielsen J., RA Ponten F., Uhlen M.; RT "Analysis of the human tissue-specific expression by genome-wide RT integration of transcriptomics and antibody-based proteomics."; RL Mol. Cell. Proteomics 13:397-406(2014). RN [6] RP SULFATION. RX PubMed=3121301; DOI=10.1002/j.1460-2075.1987.tb02592.x; RA Danielsen E.M.; RT "Tyrosine sulfation, a post-translational modification of microvillar RT enzymes in the small intestinal enterocyte."; RL EMBO J. 6:2891-2896(1987). RN [7] RP CHARACTERIZATION, SUBUNIT, SUBCELLULAR LOCATION, AND PTM. RC TISSUE=Small intestine mucosa; RX PubMed=3143729; DOI=10.1016/s0021-9258(19)77693-5; RA Naim H.Y., Sterchi E.E., Lentze M.J.; RT "Structure, biosynthesis, and glycosylation of human small intestinal RT maltase-glucoamylase."; RL J. Biol. Chem. 263:19709-19717(1988). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF ASP-529. RX PubMed=12547908; DOI=10.1073/pnas.0237170100; RA Nichols B.L., Avery S., Sen P., Swallow D.M., Hahn D., Sterchi E.; RT "The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with RT complementary starch digestion activities."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1432-1437(2003). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND DOMAIN. RX PubMed=18356321; DOI=10.1093/jn/138.4.685; RA Quezada-Calvillo R., Sim L., Ao Z., Hamaker B.R., Quaroni A., Brayer G.D., RA Sterchi E.E., Robayo-Torres C.C., Rose D.R., Nichols B.L.; RT "Luminal starch substrate brake on maltase-glucoamylase activity is located RT within the glucoamylase subunit."; RL J. Nutr. 138:685-692(2008). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, PATHWAY, DOMAIN, AND MUTAGENESIS OF TYR-385; TYR-1251 AND RP 1357-ASP--ARG-1377. RX PubMed=22058037; DOI=10.1007/s13238-011-1105-3; RA Ren L., Qin X., Cao X., Wang L., Bai F., Bai G., Shen Y.; RT "Structural insight into substrate specificity of human intestinal maltase- RT glucoamylase."; RL Protein Cell 2:827-836(2011). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RX PubMed=27480812; DOI=10.1021/acs.jafc.6b01816; RA Lee B.H., Rose D.R., Lin A.H., Quezada-Calvillo R., Nichols B.L., RA Hamaker B.R.; RT "Contribution of the Individual Small Intestinal alpha-Glucosidases to RT Digestion of Unusual alpha-Linked Glycemic Disaccharides."; RL J. Agric. Food Chem. 64:6487-6494(2016). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 87-954 IN COMPLEX WITH ACARBOSE, RP GLYCOSYLATION AT ASN-295; ASN-479 AND ASN-827, DISULFIDE BOND, FUNCTION, RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, RP DOMAIN, AND PATHWAY. RX PubMed=18036614; DOI=10.1016/j.jmb.2007.10.069; RA Sim L., Quezada-Calvillo R., Sterchi E.E., Nichols B.L., Rose D.R.; RT "Human intestinal maltase-glucoamylase: crystal structure of the N-terminal RT catalytic subunit and basis of inhibition and substrate specificity."; RL J. Mol. Biol. 375:782-792(2008). CC -!- FUNCTION: Alpha-(1,4) exo-glucosidase involved in breakdown of dietary CC starch oligosaccharides in small intestine. Cleaves the non-reducing CC alpha-(1,4)-linked glucose residue in linear dextrins with retention of CC anomeric center stereochemistry (PubMed:12547908, PubMed:18356321, CC PubMed:27480812, PubMed:18036614, PubMed:22058037). Mainly hydrolyzes CC short length oligomaltoses having two to seven glucose residues CC (PubMed:12547908, PubMed:18356321, PubMed:27480812, PubMed:18036614, CC PubMed:22058037). Can cleave alpha-(1,2), alpha-(1,3) and alpha-(1,6) CC glycosidic linkages with lower efficiency, whereas beta glycosidic CC linkages are usually not hydrolyzed (PubMed:27480812). CC {ECO:0000269|PubMed:12547908, ECO:0000269|PubMed:18036614, CC ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037, CC ECO:0000269|PubMed:27480812}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D- CC glucose residues with release of alpha-D-glucose.; EC=3.2.1.20; CC Evidence={ECO:0000269|PubMed:12547908, ECO:0000269|PubMed:18036614, CC ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037, CC ECO:0000269|PubMed:27480812}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-maltoheptaose + H2O = alpha-D-glucose + D-maltohexaose; CC Xref=Rhea:RHEA:29643, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925, CC ChEBI:CHEBI:143182, ChEBI:CHEBI:143183; CC Evidence={ECO:0000269|PubMed:22058037}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29644; CC Evidence={ECO:0000305|PubMed:22058037}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-maltohexaose + H2O = alpha-D-glucose + D-maltopentaose; CC Xref=Rhea:RHEA:29639, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925, CC ChEBI:CHEBI:143181, ChEBI:CHEBI:143182; CC Evidence={ECO:0000269|PubMed:22058037}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29640; CC Evidence={ECO:0000305|PubMed:22058037}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-maltopentaose + H2O = alpha-D-glucose + D-maltotetraose; CC Xref=Rhea:RHEA:29635, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925, CC ChEBI:CHEBI:143180, ChEBI:CHEBI:143181; CC Evidence={ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, CC ECO:0000269|PubMed:22058037}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29636; CC Evidence={ECO:0000305|PubMed:22058037}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-maltotetraose + H2O = alpha-D-glucose + D-maltotriose; CC Xref=Rhea:RHEA:29631, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925, CC ChEBI:CHEBI:140999, ChEBI:CHEBI:143180; CC Evidence={ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, CC ECO:0000269|PubMed:22058037}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29632; CC Evidence={ECO:0000305|PubMed:18036614, ECO:0000305|PubMed:18356321, CC ECO:0000305|PubMed:22058037}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-maltotriose + H2O = alpha-D-glucose + D-maltose; CC Xref=Rhea:RHEA:27970, ChEBI:CHEBI:15377, ChEBI:CHEBI:17306, CC ChEBI:CHEBI:17925, ChEBI:CHEBI:140999; CC Evidence={ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, CC ECO:0000269|PubMed:22058037}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27971; CC Evidence={ECO:0000305|PubMed:18036614, ECO:0000305|PubMed:18356321, CC ECO:0000305|PubMed:22058037}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-maltose + H2O = alpha-D-glucose + D-glucose; CC Xref=Rhea:RHEA:68796, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17306, ChEBI:CHEBI:17925; CC Evidence={ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, CC ECO:0000269|PubMed:22058037, ECO:0000269|PubMed:27480812}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68797; CC Evidence={ECO:0000305|PubMed:18036614, ECO:0000305|PubMed:18356321, CC ECO:0000305|PubMed:22058037, ECO:0000305|PubMed:27480812}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + nigerose = alpha-D-glucose + D-glucose; CC Xref=Rhea:RHEA:68800, ChEBI:CHEBI:4167, ChEBI:CHEBI:7570, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17925; CC Evidence={ECO:0000269|PubMed:27480812}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68801; CC Evidence={ECO:0000305|PubMed:27480812}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + kojibiose = alpha-D-glucose + D-glucose; CC Xref=Rhea:RHEA:68804, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17925, ChEBI:CHEBI:142460; CC Evidence={ECO:0000269|PubMed:27480812}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68805; CC Evidence={ECO:0000305|PubMed:27480812}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + isomaltose = alpha-D-glucose + D-glucose; CC Xref=Rhea:RHEA:68864, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17925, ChEBI:CHEBI:28189; CC Evidence={ECO:0000269|PubMed:27480812}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68865; CC Evidence={ECO:0000305|PubMed:27480812}; CC -!- CATALYTIC ACTIVITY: CC Reaction=6-O-alpha-D-glucopyranosyl-D-fructose + H2O = alpha-D-glucose CC + D-fructose; Xref=Rhea:RHEA:68808, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17925, ChEBI:CHEBI:18394, ChEBI:CHEBI:37721; CC Evidence={ECO:0000269|PubMed:27480812}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68809; CC Evidence={ECO:0000305|PubMed:27480812}; CC -!- ACTIVITY REGULATION: Down-regulated at high oligomaltose concentration CC as it occurs during the mealtime (PubMed:18356321). Down-regulated by CC anti-diabetic drug acarbose (PubMed:18036614, PubMed:22058037). CC {ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, CC ECO:0000269|PubMed:22058037}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.27 mM for maltoheptaose (with ctMGAM) CC {ECO:0000269|PubMed:22058037}; CC KM=1.05 mM for maltohexaose (with ctMGAM) CC {ECO:0000269|PubMed:22058037}; CC KM=0.61 mM for maltopentaose (with ctMGAM) CC {ECO:0000269|PubMed:22058037}; CC KM=0.96 mM for maltotetraose (with ctMGAM) CC {ECO:0000269|PubMed:22058037}; CC KM=0.91 mM for maltotriose (with ctMGAM) CC {ECO:0000269|PubMed:22058037}; CC KM=5.67 mM for maltose (with ctMGAM) {ECO:0000269|PubMed:22058037}; CC KM=13.12 mM for maltoheptaose (with ntMGAM) CC {ECO:0000269|PubMed:22058037}; CC KM=9.76 mM for maltohexaose (with ntMGAM) CC {ECO:0000269|PubMed:22058037}; CC KM=9.14 mM for maltopentaose (with ntMGAM) CC {ECO:0000269|PubMed:22058037}; CC KM=3.39 mM for maltotetraose (with ntMGAM) CC {ECO:0000269|PubMed:22058037}; CC KM=4.44 mM for maltotriose (with ntMGAM) CC {ECO:0000269|PubMed:22058037}; CC KM=6.4 mM for maltose (with ntMGAM) {ECO:0000269|PubMed:22058037}; CC KM=6.7 mM for maltopentaose (with ntMGAM) CC {ECO:0000269|PubMed:18036614}; CC KM=3 mM for maltotetraose (with ntMGAM) {ECO:0000269|PubMed:18036614, CC ECO:0000269|PubMed:18356321}; CC KM=4.6 mM for maltotriose (with ntMGAM) {ECO:0000269|PubMed:18036614, CC ECO:0000269|PubMed:18356321}; CC KM=7.7 mM for maltose (with ntMGAM) {ECO:0000269|PubMed:18036614}; CC KM=8.7 mM for maltose (with ntMGAM) {ECO:0000269|PubMed:27480812}; CC KM=27.1 mM for nigerose (with ntMGAM) {ECO:0000269|PubMed:27480812}; CC KM=11.6 mM for kojibiose (with ntMGAM) {ECO:0000269|PubMed:27480812}; CC KM=128 mM for isomaltose (with ntMGAM) {ECO:0000269|PubMed:27480812}; CC KM=6.66 mM for maltopentaose (with ntMGAM) CC {ECO:0000269|PubMed:18356321}; CC KM=7.71 mM for maltose (with ntMGAM) {ECO:0000269|PubMed:18356321}; CC KM=4.34 mM for maltodextrin (with ntMGAM) CC {ECO:0000269|PubMed:18356321}; CC KM=7 mM for alpha-limit dextrin (with ntMGAM) CC {ECO:0000269|PubMed:18356321}; CC Vmax=6.97 umol/min/mg enzyme toward maltopentaose (with ntMGAM) CC {ECO:0000269|PubMed:18356321}; CC Vmax=7.65 umol/min/mg enzyme toward maltotetraose (with ntMGAM) CC {ECO:0000269|PubMed:18356321}; CC Vmax=9.58 umol/min/mg enzyme toward maltotriose (with ntMGAM) CC {ECO:0000269|PubMed:18356321}; CC Vmax=8.26 umol/min/mg enzyme toward maltose (with ntMGAM) CC {ECO:0000269|PubMed:18356321}; CC Vmax=7.51 umol/min/mg enzyme toward maltodextrin (with ntMGAM) CC {ECO:0000269|PubMed:18356321}; CC Vmax=11 umol/min/mg enzyme toward alpha-limit dextrin (with ntMGAM) CC {ECO:0000269|PubMed:18356321}; CC pH dependence: CC Optimum pH is 7. Has substantial activity at acidic pH. CC {ECO:0000269|PubMed:18356321}; CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000305|PubMed:18036614, CC ECO:0000305|PubMed:22058037, ECO:0000305|PubMed:27480812}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3143729}. CC -!- INTERACTION: CC O43451; Q13520: AQP6; NbExp=3; IntAct=EBI-2829774, EBI-13059134; CC O43451; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-2829774, EBI-18013275; CC O43451; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2829774, EBI-6942903; CC O43451; O15529: GPR42; NbExp=3; IntAct=EBI-2829774, EBI-18076404; CC O43451; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-2829774, EBI-17595455; CC O43451; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2829774, EBI-8638294; CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II CC membrane protein. Note=Brush border. {ECO:0000269|PubMed:3143729}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; CC IsoId=O43451-2; Sequence=Displayed; CC Name=1; CC IsoId=O43451-1; Sequence=VSP_061364; CC -!- TISSUE SPECIFICITY: Broadly expressed. Highly expressed in small CC intestine. Expressed in granulocytes. {ECO:0000269|PubMed:24309898, CC ECO:0000269|PubMed:9446624}. CC -!- DOMAIN: The N-terminal maltase domain (ntMGAM) mainly hydrolyzes short CC length oligomaltoses having two to four glucose residues. CC {ECO:0000269|PubMed:12547908, ECO:0000269|PubMed:18036614, CC ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037}. CC -!- DOMAIN: The C-terminal glucoamylase domain (ctMGAM) acts on longer CC maltoside substrates having four to seven glucose residues. CC {ECO:0000269|PubMed:22058037}. CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:18036614, CC ECO:0000269|PubMed:3143729}. CC -!- PTM: Does not undergo intracellular or extracellular proteolytic CC cleavage. {ECO:0000269|PubMed:3143729}. CC -!- PTM: Sulfated. {ECO:0000250}. CC -!- MISCELLANEOUS: The displayed isoform 2 sequence is inferred based on CC alignments, homology, conservation, expression and longest protein. CC RNA-seq transcriptomic analysis supports all introns in a single CC sample. No single full-size mRNA sequence supports this isoform yet, CC however it is clearly identified by mass spectrometry analysis. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}. 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; AF016833; AAC39568.2; -; mRNA. DR EMBL; AC091684; AAP21875.1; -; Genomic_DNA. DR EMBL; AC073647; AAS07445.1; -; Genomic_DNA. DR EMBL; AC091742; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC120872; AAI20873.1; -; mRNA. DR CCDS; CCDS47727.1; -. [O43451-1] DR CCDS; CCDS94221.1; -. [O43451-2] DR RefSeq; NP_004659.2; NM_004668.2. [O43451-1] DR RefSeq; XP_006716231.1; XM_006716168.2. DR RefSeq; XP_011514972.1; XM_011516670.2. [O43451-2] DR RefSeq; XP_011514973.1; XM_011516671.2. [O43451-2] DR RefSeq; XP_011514974.1; XM_011516672.2. [O43451-2] DR RefSeq; XP_011514975.1; XM_011516673.2. [O43451-2] DR RefSeq; XP_016868261.1; XM_017012772.1. [O43451-2] DR PDB; 2QLY; X-ray; 2.00 A; A=87-954. DR PDB; 2QMJ; X-ray; 1.90 A; A=87-954. DR PDB; 3CTT; X-ray; 2.10 A; A=87-954. DR PDB; 3L4T; X-ray; 1.90 A; A=87-954. DR PDB; 3L4U; X-ray; 1.90 A; A=87-954. DR PDB; 3L4V; X-ray; 2.10 A; A=87-954. DR PDB; 3L4W; X-ray; 2.00 A; A=87-954. DR PDB; 3L4X; X-ray; 1.90 A; A=87-954. DR PDB; 3L4Y; X-ray; 1.80 A; A=87-954. DR PDB; 3L4Z; X-ray; 2.00 A; A=87-954. DR PDB; 3TON; X-ray; 2.95 A; A/B=960-1853. DR PDB; 3TOP; X-ray; 2.88 A; A/B=960-1853. DR PDBsum; 2QLY; -. DR PDBsum; 2QMJ; -. DR PDBsum; 3CTT; -. DR PDBsum; 3L4T; -. DR PDBsum; 3L4U; -. DR PDBsum; 3L4V; -. DR PDBsum; 3L4W; -. DR PDBsum; 3L4X; -. DR PDBsum; 3L4Y; -. DR PDBsum; 3L4Z; -. DR PDBsum; 3TON; -. DR PDBsum; 3TOP; -. DR AlphaFoldDB; O43451; -. DR SMR; O43451; -. DR BioGRID; 114462; 10. DR CORUM; O43451; -. DR IntAct; O43451; 11. DR MINT; O43451; -. DR STRING; 9606.ENSP00000447378; -. DR BindingDB; O43451; -. DR ChEMBL; CHEMBL2074; -. DR DrugBank; DB00284; Acarbose. DR DrugBank; DB00491; Miglitol. DR DrugBank; DB04878; Voglibose. DR DrugCentral; O43451; -. DR GuidetoPHARMACOLOGY; 2627; -. DR CAZy; GH31; Glycoside Hydrolase Family 31. DR UniLectin; O43451; -. DR GlyConnect; 1958; 24 N-Linked glycans (6 sites). DR GlyCosmos; O43451; 26 sites, 28 glycans. DR GlyGen; O43451; 26 sites, 24 N-linked glycans (6 sites), 4 O-linked glycans (4 sites). DR iPTMnet; O43451; -. DR PhosphoSitePlus; O43451; -. DR BioMuta; MGAM; -. DR jPOST; O43451; -. DR MassIVE; O43451; -. DR PaxDb; 9606-ENSP00000447378; -. DR PeptideAtlas; O43451; -. DR ProteomicsDB; 17714; -. DR ProteomicsDB; 48955; -. DR Pumba; O43451; -. DR Antibodypedia; 50132; 44 antibodies from 15 providers. DR DNASU; 8972; -. DR Ensembl; ENST00000475668.6; ENSP00000417515.2; ENSG00000257335.8. [O43451-2] DR Ensembl; ENST00000549489.6; ENSP00000447378.2; ENSG00000257335.8. [O43451-1] DR Ensembl; ENST00000620571.1; ENSP00000482292.1; ENSG00000257335.8. [O43451-1] DR GeneID; 8972; -. DR KEGG; hsa:8972; -. DR MANE-Select; ENST00000475668.6; ENSP00000417515.2; NM_001365693.1; NP_001352622.1. DR UCSC; uc003vwy.4; human. [O43451-2] DR AGR; HGNC:7043; -. DR CTD; 8972; -. DR DisGeNET; 8972; -. DR GeneCards; MGAM; -. DR HGNC; HGNC:7043; MGAM. DR HPA; ENSG00000257335; Tissue enhanced (epididymis, intestine). DR MIM; 154360; gene. DR neXtProt; NX_O43451; -. DR OpenTargets; ENSG00000257335; -. DR PharmGKB; PA30778; -. DR VEuPathDB; HostDB:ENSG00000257335; -. DR eggNOG; KOG1065; Eukaryota. DR GeneTree; ENSGT00940000161540; -. DR HOGENOM; CLU_000631_3_0_1; -. DR InParanoid; O43451; -. DR OMA; LFYHAHS; -. DR OrthoDB; 5480935at2759; -. DR PhylomeDB; O43451; -. DR TreeFam; TF314577; -. DR BRENDA; 3.2.1.20; 2681. DR BRENDA; 3.2.1.3; 2681. DR PathwayCommons; O43451; -. DR Reactome; R-HSA-189085; Digestion of dietary carbohydrate. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; O43451; -. DR SIGNOR; O43451; -. DR BioGRID-ORCS; 8972; 12 hits in 1159 CRISPR screens. DR EvolutionaryTrace; O43451; -. DR GeneWiki; Maltase-glucoamylase; -. DR GenomeRNAi; 8972; -. DR Pharos; O43451; Tclin. DR PRO; PR:O43451; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; O43451; Protein. DR Bgee; ENSG00000257335; Expressed in duodenum and 97 other cell types or tissues. DR ExpressionAtlas; O43451; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome. DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:UniProtKB. DR GO; GO:0016160; F:amylase activity; IEA:Ensembl. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0003824; F:catalytic activity; TAS:ProtInc. DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:1901027; P:dextrin catabolic process; IDA:UniProtKB. DR GO; GO:0000025; P:maltose catabolic process; IDA:UniProtKB. DR GO; GO:0005983; P:starch catabolic process; TAS:ProtInc. DR CDD; cd06602; GH31_MGAM_SI_GAA; 3. DR CDD; cd14752; GH31_N; 3. DR CDD; cd00111; Trefoil; 3. DR Gene3D; 3.20.20.80; Glycosidases; 3. DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 3. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 6. DR Gene3D; 4.10.110.10; Spasmolytic Protein, domain 1; 3. 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; IPR017957; P_trefoil_CS. DR InterPro; IPR000519; P_trefoil_dom. DR InterPro; IPR044913; P_trefoil_dom_sf. DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1. DR PANTHER; PTHR22762:SF168; P-TYPE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF13802; Gal_mutarotas_2; 3. DR Pfam; PF01055; Glyco_hydro_31_2nd; 3. DR Pfam; PF21365; Glyco_hydro_31_3rd; 3. DR Pfam; PF00088; Trefoil; 3. DR SMART; SM00018; PD; 3. DR SUPFAM; SSF51445; (Trans)glycosidases; 3. DR SUPFAM; SSF74650; Galactose mutarotase-like; 3. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 3. DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 3. DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1. DR PROSITE; PS00025; P_TREFOIL_1; 1. DR PROSITE; PS51448; P_TREFOIL_2; 3. DR Genevisible; O43451; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Membrane; Multifunctional enzyme; Reference proteome; Repeat; KW Signal-anchor; Sulfation; Transmembrane; Transmembrane helix. FT CHAIN 1..2753 FT /note="Maltase-glucoamylase" FT /id="PRO_0000185363" FT TOPO_DOM 1..13 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 14..34 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 35..2753 FT /note="Lumenal" FT /evidence="ECO:0000255" FT DOMAIN 88..134 FT /note="P-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779" FT DOMAIN 954..1000 FT /note="P-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779" FT DOMAIN 1850..1896 FT /note="P-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779" FT REGION 41..87 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 356..737 FT /note="Maltase" FT /evidence="ECO:0000305|PubMed:18036614" FT REGION 1221..1632 FT /note="Glucoamylase" FT /evidence="ECO:0000305|PubMed:22058037" FT COMPBIAS 42..87 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 529 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066" FT ACT_SITE 532 FT /evidence="ECO:0000250" FT ACT_SITE 1420 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066" FT ACT_SITE 1423 FT /evidence="ECO:0000250" FT ACT_SITE 1526 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 289 FT /ligand="acarbose" FT /ligand_id="ChEBI:CHEBI:84363" FT /evidence="ECO:0000269|PubMed:18036614" FT BINDING 413 FT /ligand="acarbose" FT /ligand_id="ChEBI:CHEBI:84363" FT /evidence="ECO:0000269|PubMed:18036614" FT BINDING 612 FT /ligand="acarbose" FT /ligand_id="ChEBI:CHEBI:84363" FT /evidence="ECO:0000269|PubMed:18036614" FT BINDING 628 FT /ligand="acarbose" FT /ligand_id="ChEBI:CHEBI:84363" FT /evidence="ECO:0000269|PubMed:18036614" FT BINDING 686 FT /ligand="acarbose" FT /ligand_id="ChEBI:CHEBI:84363" FT /evidence="ECO:0000269|PubMed:18036614" FT MOD_RES 416 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 425 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 1282 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT CARBOHYD 135 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 295 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18036614" FT CARBOHYD 457 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 458 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 479 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18036614" FT CARBOHYD 707 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 749 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 827 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18036614" FT CARBOHYD 885 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 912 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 977 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 989 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1255 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1323 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1364 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1388 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2499 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2568 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2738 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2743 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 90..118 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779" FT DISULFID 101..117 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779, FT ECO:0000269|PubMed:18036614" FT DISULFID 112..130 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779, FT ECO:0000269|PubMed:18036614" FT DISULFID 659..670 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779, FT ECO:0000269|PubMed:18036614" FT DISULFID 966..983 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779" FT DISULFID 978..996 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779" FT DISULFID 1862..1879 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779" FT DISULFID 1874..1892 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779" FT VAR_SEQ 1594..2489 FT /note="Missing (in isoform 1)" FT /evidence="ECO:0000305|PubMed:9446624" FT /id="VSP_061364" FT VARIANT 404 FT /note="Q -> H (in dbSNP:rs2272330)" FT /id="VAR_047350" FT VARIANT 542 FT /note="S -> L (in dbSNP:rs10266732)" FT /id="VAR_047351" FT VARIANT 858 FT /note="N -> D (in dbSNP:rs2960746)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9446624" FT /id="VAR_047352" FT VARIANT 2534 FT /note="L -> I (in dbSNP:rs9655651)" FT /id="VAR_047353" FT MUTAGEN 385 FT /note="Y->W: Decreases alpha-1,4-glucosidase activity FT toward maltose." FT /evidence="ECO:0000269|PubMed:22058037" FT MUTAGEN 529 FT /note="D->A: Loss of alpha-1,4-glucosidase activity toward FT maltose." FT /evidence="ECO:0000269|PubMed:12547908" FT MUTAGEN 1251 FT /note="Y->W: Decreases alpha-1,4-glucosidase activity FT toward maltose." FT /evidence="ECO:0000269|PubMed:22058037" FT MUTAGEN 1357..1377 FT /note="Missing: Decreases alpha-1,4-glucosidase activity FT toward long oligomaltose substrates having four to seven FT D-glucose residues." FT /evidence="ECO:0000269|PubMed:22058037" FT CONFLICT 854 FT /note="L -> P (in Ref. 4; AAI20873)" FT /evidence="ECO:0000305" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 109..115 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 136..146 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 148..157 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 169..179 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 182..189 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 214..220 FT /evidence="ECO:0007829|PDB:3L4Y" FT TURN 221..224 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 225..230 FT /evidence="ECO:0007829|PDB:3L4Y" FT TURN 231..233 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 236..239 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 251..257 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 263..269 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 272..276 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 279..285 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 303..309 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 316..321 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 327..332 FT /evidence="ECO:0007829|PDB:3L4Y" FT TURN 333..335 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 336..344 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 346..355 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 356..367 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 375..378 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 379..382 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 390..402 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 409..412 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 414..416 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 417..420 FT /evidence="ECO:0007829|PDB:2QLY" FT TURN 427..432 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 433..442 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 446..451 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 466..474 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 483..486 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 489..491 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 494..497 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 504..518 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 524..528 FT /evidence="ECO:0007829|PDB:3L4Y" FT TURN 531..533 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 536..540 FT /evidence="ECO:0007829|PDB:3L4Y" FT TURN 548..550 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 559..561 FT /evidence="ECO:0007829|PDB:3L4Y" FT TURN 563..566 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 579..582 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 583..585 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 586..601 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 609..613 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 618..620 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 623..625 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 630..632 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 633..648 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 653..655 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 661..663 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 667..677 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 680..685 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 689..691 FT /evidence="ECO:0007829|PDB:2QMJ" FT HELIX 696..699 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 704..718 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 720..732 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 737..739 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 741..745 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 749..751 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 758..760 FT /evidence="ECO:0007829|PDB:3L4Y" FT TURN 761..763 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 764..767 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 775..781 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 786..788 FT /evidence="ECO:0007829|PDB:3L4Y" FT TURN 789..791 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 799..805 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 812..816 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 819..824 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 830..833 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 838..843 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 850..856 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 859..861 FT /evidence="ECO:0007829|PDB:3L4Y" FT TURN 862..868 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 871..877 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 879..889 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 898..906 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 911..917 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 927..931 FT /evidence="ECO:0007829|PDB:3L4Y" FT TURN 932..935 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 936..941 FT /evidence="ECO:0007829|PDB:3L4Y" FT STRAND 950..954 FT /evidence="ECO:0007829|PDB:3L4Y" FT HELIX 1871..1875 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 1876..1878 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 1879..1881 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 1891..1896 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 1898..1901 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 1908..1918 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 1920..1923 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 1926..1928 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 1932..1940 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 1942..1951 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 1953..1955 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 1974..1976 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 1979..1984 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 1985..1988 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 1989..1994 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2000..2003 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2010..2012 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2015..2021 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2023..2025 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2031..2033 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2036..2039 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2043..2050 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2068..2072 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2074..2076 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2078..2083 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2087..2094 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 2095..2097 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2098..2106 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2108..2113 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2118..2129 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2137..2140 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2141..2144 FT /evidence="ECO:0007829|PDB:3TON" FT HELIX 2152..2165 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2171..2174 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2176..2178 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2180..2182 FT /evidence="ECO:0007829|PDB:3TON" FT HELIX 2189..2191 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2194..2203 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2207..2212 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2225..2233 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2240..2242 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2247..2253 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2265..2271 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2273..2277 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2284..2298 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2304..2306 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2311..2315 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 2318..2320 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2323..2330 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 2335..2337 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2349..2351 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 2352..2356 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2363..2365 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2367..2369 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2371..2373 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2374..2377 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2378..2380 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2381..2397 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2403..2407 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2412..2414 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2417..2419 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2424..2426 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2428..2443 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2447..2449 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2455..2457 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2461..2471 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2474..2476 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2483..2485 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2490..2492 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2495..2525 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2529..2531 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2533..2535 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 2541..2545 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2548..2552 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 2553..2555 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2556..2559 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2563..2565 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2568..2573 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2578..2580 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 2581..2583 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2590..2597 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2604..2608 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2610..2616 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2622..2625 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2630..2635 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2642..2648 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2651..2653 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 2654..2656 FT /evidence="ECO:0007829|PDB:3TOP" FT HELIX 2657..2659 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2663..2669 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2674..2683 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2686..2688 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2691..2698 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2711..2717 FT /evidence="ECO:0007829|PDB:3TOP" FT STRAND 2725..2727 FT /evidence="ECO:0007829|PDB:3TOP" FT TURN 2741..2743 FT /evidence="ECO:0007829|PDB:3TOP" SQ SEQUENCE 2753 AA; 312022 MW; 148327B7C5E264EF CRC64; MARKKLKKFT TLEIVLSVLL LVLFIISIVL IVLLAKESLK STAPDPGTTG TPDPGTTGTP DPGTTGTTHA RTTGPPDPGT TGTTPVSAEC PVVNELERIN CIPDQPPTKA TCDQRGCCWN PQGAVSVPWC YYSKNHSYHV EGNLVNTNAG FTARLKNLPS SPVFGSNVDN VLLTAEYQTS NRFHFKLTDQ TNNRFEVPHE HVQSFSGNAA ASLTYQVEIS RQPFSIKVTR RSNNRVLFDS SIGPLLFADQ FLQLSTRLPS TNVYGLGEHV HQQYRHDMNW KTWPIFNRDT TPNGNGTNLY GAQTFFLCLE DASGLSFGVF LMNSNAMEVV LQPAPAITYR TIGGILDFYV FLGNTPEQVV QEYLELIGRP ALPSYWALGF HLSRYEYGTL DNMREVVERN RAAQLPYDVQ HADIDYMDER RDFTYDSVDF KGFPEFVNEL HNNGQKLVII VDPAISNNSS SSKPYGPYDR GSDMKIWVNS SDGVTPLIGE VWPGQTVFPD YTNPNCAVWW TKEFELFHNQ VEFDGIWIDM NEVSNFVDGS VSGCSTNNLN NPPFTPRILD GYLFCKTLCM DAVQHWGKQY DIHNLYGYSM AVATAEAAKT VFPNKRSFIL TRSTFAGSGK FAAHWLGDNT ATWDDLRWSI PGVLEFNLFG IPMVGPDICG FALDTPEELC RRWMQLGAFY PFSRNHNGQG YKDQDPASFG ADSLLLNSSR HYLNIRYTLL PYLYTLFFRA HSRGDTVARP LLHEFYEDNS TWDVHQQFLW GPGLLITPVL DEGAEKVMAY VPDAVWYDYE TGSQVRWRKQ KVEMELPGDK IGLHLRGGYI FPTQQPNTTT LASRKNPLGL IIALDENKEA KGELFWDNGE TKDTVANKVY LLCEFSVTQN RLEVNISQST YKDPNNLAFN EIKILGTEEP SNVTVKHNGV PSQTSPTVTY DSNLKVAIIT DIDLLLGEAY TVEWSIKIRD EEKIDCYPDE NGASAENCTA RGCIWEASNS SGVPFCYFVN DLYSVSDVQY NSHGATADIS LKSSVYANAF PSTPVNPLRL DVTYHKNEML QFKIYDPNKN RYEVPVPLNI PSMPSSTPEG QLYDVLIKKN PFGIEIRRKS TGTIIWDSQL LGFTFSDMFI RISTRLPSKY LYGFGETEHR SYRRDLEWHT WGMFSRDQPP GYKKNSYGVH PYYMGLEEDG SAHGVLLLNS NAMDVTFQPL PALTYRTTGG VLDFYVFLGP TPELVTQQYT ELIGRPVMVP YWSLGFQLCR YGYQNDSEIA SLYDEMVAAQ IPYDVQYSDI DYMERQLDFT LSPKFAGFPA LINRMKADGM RVILILDPAI SGNETQPYPA FTRGVEDDVF IKYPNDGDIV WGKVWPDFPD VVVNGSLDWD SQVELYRAYV AFPDFFRNST AKWWKREIEE LYNNPQNPER SLKFDGMWID MNEPSSFVNG AVSPGCRDAS LNHPPYMPHL ESRDRGLSSK TLCMESQQIL PDGSLVQHYN VHNLYGWSQT RPTYEAVQEV TGQRGVVITR STFPSSGRWA GHWLGDNTAA WDQLKKSIIG MMEFSLFGIS YTGADICGFF QDAEYEMCVR WMQLGAFYPF SRNHNTIGTR RQDPVSWDAA FVNISRNVLQ TRYTLLPYLY TLMQKAHTEG VTVVRPLLHE FVSDQVTWDI DSQFLLGPAF LVSPVLERNA RNVTAYFPRA RWYDYYTGVD INARGEWKTL PAPLDHINLH VRGGYILPWQ EPALNTHLSR KNPLGLIIAL DENKEAKGEL FWDDGQTKDT VAKKVYLLCE FSVTQNHLEV TISQSTYKDP NNLAFNEIKI LGMEEPSNVT VKHNGVPSQT SPTVTYDSNL KVAIITDINL FLGEAYTVEW SIKIRDEEKI DCYPDENGDS AENCTARGCI WEASNSSGVP FCYFVNDLYS VSDVQYNSHG ATADISLKSS VHANAFPSTP VNPLRLDVTY HKNEMLQFKI YDPNNNRYEV PVPLNIPSVP SSTPEGQLYD VLIKKNPFGI EIRRKSTGTI IWDSQLLGFT FNDMFIRIST RLPSKYLYGF GETEHTSYRR DLEWHTWGMF SRDQPPGYKK NSYGVHPYYM GLEEDGSAHG VLLLNSNAMD VTFQPLPALT YRTTGGVLDF YVFLGPTPEL VTQQYTELIG RPVMVPYWSL GFQLCRYGYQ NDSEISSLYD EMVAAQIPYD VQYSDIDYME RQLDFTLSPK FAGFPALINR MKADGMRVIL ILDPAISGNE TQPYPAFTRG VEDDVFIKYP NDGDIVWGKV WPDFPDVVVN GSLDWDSQVE LYRAYVAFPD FFRNSTAKWW KREIEELYNN PQNPERSLKF DGMWIDMNEP SSFVNGAVSP GCRDASLNHP PYMPYLESRD RGLSSKTLCM ESQQILPDGS PVQHYNVHNL YGWSQTRPTY EAVQEVTGQR GVVITRSTFP SSGRWAGHWL GDNTAAWDQL KKSIIGMMEF SLFGISYTGA DICGFFQDAE YEMCVRWMQL GAFYPFSRNH NTIGTRRQDP VSWDVAFVNI SRTVLQTRYT LLPYLYTLMH KAHTEGVTVV RPLLHEFVSD QVTWDIDSQF LLGPAFLVSP VLERNARNVT AYFPRARWYD YYTGVDINAR GEWKTLPAPL DHINLHVRGG YILPWQEPAL NTHLSRQKFM GFKIALDDEG TAGGWLFWDD GQSIDTYGKG LYYLASFSAS QNTMQSHIIF NNYITGTNPL KLGYIEIWGV GSVPVTSVSI SVSGMVITPS FNNDPTTQVL SIDVTDRNIS LHNFTSLTWI STL //