ID   B5THE2_MOUSE            Unreviewed;      1827 AA.
AC   B5THE2;
DT   04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Maltase-glucoamylase {ECO:0000313|EMBL:ACH86011.1, ECO:0000313|Ensembl:ENSMUSP00000071466.7};
DE            EC=3.2.1.20 {ECO:0000313|EMBL:ACH86011.1};
GN   Name=Mgam {ECO:0000313|EMBL:ACH86011.1,
GN   ECO:0000313|Ensembl:ENSMUSP00000071466.7,
GN   ECO:0000313|MGI:MGI:1203495};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:ACH86011.1};
RN   [1] {ECO:0000313|EMBL:ACH86011.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/Sv {ECO:0000313|EMBL:ACH86011.1};
RC   TISSUE=Small intestine {ECO:0000313|EMBL:ACH86011.1};
RA   Nichols B.L.Jr., Avery S.E., Quezada-Calvillo R., Sen P.;
RT   "Mouse intestinal maltase-glucoamylase.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000071466.7, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000071466.7,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000071466.7}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000071466.7};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00779}.
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DR   EMBL; EU937529; ACH86011.1; -; mRNA.
DR   RefSeq; NP_001164474.1; NM_001171003.1.
DR   STRING; 10090.ENSMUSP00000071466; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   PaxDb; 10090-ENSMUSP00000071466; -.
DR   ProteomicsDB; 328915; -.
DR   Antibodypedia; 50132; 44 antibodies from 15 providers.
DR   Ensembl; ENSMUST00000071535.10; ENSMUSP00000071466.7; ENSMUSG00000068587.11.
DR   Ensembl; ENSMUST00000201148.4; ENSMUSP00000143946.2; ENSMUSG00000068587.11.
DR   GeneID; 232714; -.
DR   KEGG; mmu:232714; -.
DR   UCSC; uc009bnf.2; mouse.
DR   AGR; MGI:1203495; -.
DR   CTD; 8972; -.
DR   MGI; MGI:1203495; Mgam.
DR   VEuPathDB; HostDB:ENSMUSG00000068587; -.
DR   eggNOG; KOG1065; Eukaryota.
DR   GeneTree; ENSGT00940000161540; -.
DR   OrthoDB; 5480935at2759; -.
DR   TreeFam; TF314577; -.
DR   BioGRID-ORCS; 232714; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Mgam; mouse.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000068587; Expressed in small intestine Peyer's patch and 75 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:MGI.
DR   GO; GO:0016160; F:amylase activity; IDA:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:1901027; P:dextrin catabolic process; ISO:MGI.
DR   GO; GO:0000025; P:maltose catabolic process; ISO:MGI.
DR   CDD; cd06602; GH31_MGAM_SI_GAA; 2.
DR   CDD; cd14752; GH31_N; 2.
DR   CDD; cd00111; Trefoil; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 4.
DR   Gene3D; 4.10.110.10; Spasmolytic Protein, domain 1; 2.
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:SF168; P-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 2.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 2.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 2.
DR   Pfam; PF00088; Trefoil; 2.
DR   SMART; SM00018; PD; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 2.
DR   SUPFAM; SSF57492; Trefoil; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 2.
DR   PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
DR   PROSITE; PS51448; P_TREFOIL_2; 2.
PE   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00779}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000313|EMBL:ACH86011.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACH86011.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0007829|MaxQB:B5THE2,
KW   ECO:0007829|PeptideAtlas:B5THE2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          63..108
FT                   /note="P-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51448"
FT   DOMAIN          924..974
FT                   /note="P-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51448"
FT   DISULFID        87..104
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00779"
SQ   SEQUENCE   1827 AA;  208549 MW;  00FD29494C846ACE CRC64;
     MAGRRFKKFS KLELVLIVLL LVLFIIAVVL IVLLANSTPE NAIGAETTGT PDTTVTRTTL
     NSPNCPVLSE LERINCIPDQ SSNKGTCDER GCCWDPQGSI SVPCYYSRNH GYKMESDVVN
     TNAGFTATLK NLPSAPVFGN SIENILLTAE YQTSNRFHFK LTDQTKKRYE VPHEHVQPFS
     GNAPSSLNYK VEVSKEPFSI KVTRKSNNRV LFDSSIGPLL FSDQFLQFST HLPSANVYGL
     GEHVHQQYRH NMNWKTWPMF SRDTTPNEDG TNLYGVQTFF LCLEDNSGLS FGVFLMNSNA
     MEVTLQPTPA ITYRTTGGIL DFYVFLGNTP EQVVQEYLEL IGRPALPSYW TLGFQLSRYD
     YKSLDNMKAV VERNRAAQLP YDVQHADIDY MDQKKDFTYD PVNFKGFPEF VKELHNNGQK
     LVIILDPAIS NNSFSSNPYG PYDRGSAMKI WVNSSDGISP VIGKVWPGTT VFPDYTSPNC
     AVWWTKEFEL FHKEVEFDGI WIDMNEVSNF IDGSFSGCSQ NNLNYPPFTP KVLDGYLFSK
     TLCMDAVQHW GKQYDVHNLY GYSMAIATAK AVKDVFPDKR SFIITRSTFA GSGKFAAHWL
     GDNTATWKDL QWSIPGMLEF NLFGIPMVGA DICGFAQDTY EELCRRWMQL GAFYPFSRNH
     NGQGYKDQDP ASFGNNSLLL NSSRHYLNIR YTLLPYLYTL FYRAHSRGDT VARPLLHEFY
     DDNNTWGIDR QFLWGPGLLI TPVLDQGAEK VKAYVPNATW YDYETGEELG WRKQSIEMQL
     PGDKIGLHLR GGYIFPTQQP ATTTEASRKN PLGLIVALDE NKEARGELFW DDGESKDTVA
     QNIYLFSEFS VTQNHLDVTI SSPNYKDPNN LEFQEIKIFG TREFRNVRVK QNGNLLQMSP
     QVTYNPNLKV ATITNIHLRL GEAYTVEWDF FTREEERIDC YPDEHGASEA NCSARGCIWE
     ASNTTRGPPC YFAHELYSVS NVQYDSHGAT ADISLKASTY SNAFPSTPVN KLKLQVTYHK
     NEMLQFKIYD PNHSRYEVPV PLNIPSAPLS TPEGRLYDVL IKENPFGIQI RRKTTGTVIW
     DSQLLGFTFN DMFIRISTRL PSTYIYGFGE TEHTTFKIDM NWHTWGMFSR DEPPGYKKNS
     YGVHPYYMGL EEDGNAHGVL LMNSNAMDVT FQPMPALTYR TIGGILDFYV FLGPTPEIVT
     QQYTELIGRP VMVPYWSLGF QLCRYGYEND TEIANLYDEM VAKQIPYDVQ YSDIDYMERQ
     LDFKLSPKFS GFPALINRMK ANGMRVILIL DPAISGNETE PYPAFTRGVE NDVFIRYPNN
     GSIVWGKVWP DYPNITVDPS LGWDHQVEQY RAYVAFPDFF RNSTATWWKK EIKELHSNTQ
     DPAKSLKFDG LWIDMNEPSS FVNGAVPSGC SDATLNHPPY MPYLEARDRG LSSKTLCMES
     EQILPDGSRV RHYDVHNLYG WSQTRPTYEA VQEVTGERGI VITRSTFPSS GRWGGHWLGD
     NTAAWDQLGK SIIGMMDFSL FGISYTGSDI CGFFQDAEYE MCVRWMQLGA FYPFSRNHNT
     IGTRRQDPVS WNKTFEDISR SVLETRYTLL PYLYTLMYKA HTEGSTVVRP LLHEFVSDRE
     TWNIDKQFLL GPAFLVSPVL EPNARKVEAY FPRARWYDYY KGVDINATGE WKTLEAPLEY
     INLHIRGGYI LPWQEPAMNT HLSRQKFMGL RAALNAEGRA EGWLFWDDGK RINTDQYYLA
     RFSVNQTTLL THEKFNNYLT GTAPLYLGYI DIWGLSSSSI TNVSISWNTN NEEVFANYNS
     TTKILSVNMT DKKISLHTFN SLTWSSS
//