MGA_HUMAN
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 03-AUG-2022, entry version 187.
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=6.40 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}.
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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 RefSeq; NP_004659.2; NM_004668.2.
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 GlyConnect; 1958; 24 N-Linked glycans (6 sites).
DR GlyGen; O43451; 24 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; O43451; -.
DR PeptideAtlas; O43451; -.
DR PRIDE; O43451; -.
DR ProteomicsDB; 17714; -.
DR ProteomicsDB; 48955; -.
DR Antibodypedia; 50132; 39 antibodies from 14 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 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; LTWDIDS; -.
DR OrthoDB; 151244at2759; -.
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 BioGRID-ORCS; 8972; 12 hits in 1073 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 96 other tissues.
DR ExpressionAtlas; O43451; baseline and differential.
DR Genevisible; O43451; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
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; cd00111; Trefoil; 3.
DR Gene3D; 2.60.40.1180; -; 6.
DR Gene3D; 4.10.110.10; -; 3.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
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 Pfam; PF01055; Glyco_hydro_31; 3.
DR Pfam; PF16863; NtCtMGAM_N; 3.
DR Pfam; PF00088; Trefoil; 3.
DR SMART; SM00018; PD; 3.
DR SUPFAM; SSF51445; SSF51445; 3.
DR SUPFAM; SSF74650; SSF74650; 3.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 2.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
DR PROSITE; PS00025; P_TREFOIL_1; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 2.
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 D-
FT 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
