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O43451

- MGA_HUMAN

UniProt

O43451 - MGA_HUMAN

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Protein

Maltase-glucoamylase, intestinal

Gene

MGAM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing.

Catalytic activityi

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei529 – 5291NucleophilePROSITE-ProRule annotation
Active sitei532 – 5321By similarity
Active sitei1420 – 14201NucleophilePROSITE-ProRule annotation
Active sitei1423 – 14231By similarity
Active sitei1526 – 15261Proton donorBy similarity

GO - Molecular functioni

  1. alpha-1,4-glucosidase activity Source: Reactome
  2. amylase activity Source: Ensembl
  3. carbohydrate binding Source: InterPro
  4. catalytic activity Source: ProtInc
  5. glucan 1,4-alpha-glucosidase activity Source: UniProtKB-EC
  6. maltose alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. polysaccharide digestion Source: Reactome
  3. small molecule metabolic process Source: Reactome
  4. starch catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_9472. Digestion of dietary carbohydrate.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Maltase-glucoamylase, intestinal
Including the following 2 domains:
Alternative name(s):
Alpha-glucosidase
Glucoamylase (EC:3.2.1.3)
Alternative name(s):
Glucan 1,4-alpha-glucosidase
Gene namesi
Name:MGAM
Synonyms:MGA, MGAML
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:7043. MGAM.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei14 – 3421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini35 – 18571823LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30778.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18571857Maltase-glucoamylase, intestinalPRO_0000185363Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi90 ↔ 118PROSITE-ProRule annotation
Disulfide bondi101 ↔ 1171 PublicationPROSITE-ProRule annotation
Disulfide bondi112 ↔ 1301 PublicationPROSITE-ProRule annotation
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi295 – 2951N-linked (GlcNAc...)1 Publication
Modified residuei416 – 4161SulfotyrosineSequence Analysis
Modified residuei425 – 4251SulfotyrosineSequence Analysis
Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi479 – 4791N-linked (GlcNAc...)1 Publication
Disulfide bondi659 ↔ 6701 PublicationPROSITE-ProRule annotation
Glycosylationi707 – 7071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi749 – 7491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi827 – 8271N-linked (GlcNAc...)1 Publication
Glycosylationi885 – 8851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi912 – 9121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi966 ↔ 983PROSITE-ProRule annotation
Glycosylationi977 – 9771N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi978 ↔ 996PROSITE-ProRule annotation
Glycosylationi989 – 9891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1255 – 12551N-linked (GlcNAc...)Sequence Analysis
Modified residuei1282 – 12821SulfotyrosineSequence Analysis
Glycosylationi1323 – 13231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1364 – 13641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1388 – 13881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1603 – 16031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1672 – 16721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1842 – 18421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1847 – 18471N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N- and O-glycosylated.1 Publication
Does not undergo intracellular or extracellular proteolytic cleavage.
Sulfated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PaxDbiO43451.
PRIDEiO43451.

PTM databases

PhosphoSiteiO43451.

Expressioni

Tissue specificityi

Expressed in small intestine, granulocyte, and kidney but not in salivary gland or pancreas.

Gene expression databases

BgeeiO43451.
CleanExiHS_MGA.
HS_MGAM.
ExpressionAtlasiO43451. baseline and differential.
GenevestigatoriO43451.

Organism-specific databases

HPAiHPA002270.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi114462. 2 interactions.
IntActiO43451. 2 interactions.
STRINGi9606.ENSP00000373973.

Structurei

Secondary structure

1
1857
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi95 – 973Combined sources
Beta strandi104 – 1063Combined sources
Helixi109 – 1157Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi136 – 14611Combined sources
Beta strandi148 – 15710Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi169 – 17911Combined sources
Beta strandi182 – 1898Combined sources
Beta strandi214 – 2207Combined sources
Turni221 – 2244Combined sources
Beta strandi225 – 2306Combined sources
Turni231 – 2333Combined sources
Beta strandi236 – 2394Combined sources
Helixi240 – 2423Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi251 – 2577Combined sources
Beta strandi263 – 2697Combined sources
Beta strandi272 – 2765Combined sources
Beta strandi279 – 2857Combined sources
Beta strandi303 – 3097Combined sources
Beta strandi316 – 3216Combined sources
Beta strandi327 – 3326Combined sources
Turni333 – 3353Combined sources
Beta strandi336 – 3449Combined sources
Beta strandi346 – 35510Combined sources
Helixi356 – 36712Combined sources
Helixi375 – 3784Combined sources
Beta strandi379 – 3824Combined sources
Helixi390 – 40213Combined sources
Beta strandi409 – 4124Combined sources
Helixi414 – 4163Combined sources
Beta strandi417 – 4204Combined sources
Turni427 – 4326Combined sources
Helixi433 – 44210Combined sources
Beta strandi446 – 4516Combined sources
Beta strandi461 – 4633Combined sources
Helixi466 – 4749Combined sources
Beta strandi483 – 4864Combined sources
Beta strandi489 – 4913Combined sources
Beta strandi494 – 4974Combined sources
Helixi504 – 51815Combined sources
Beta strandi524 – 5285Combined sources
Turni531 – 5333Combined sources
Beta strandi536 – 5405Combined sources
Turni548 – 5503Combined sources
Helixi559 – 5613Combined sources
Turni563 – 5664Combined sources
Helixi579 – 5824Combined sources
Helixi583 – 5853Combined sources
Helixi586 – 60116Combined sources
Beta strandi609 – 6135Combined sources
Helixi618 – 6203Combined sources
Beta strandi623 – 6253Combined sources
Beta strandi630 – 6323Combined sources
Helixi633 – 64816Combined sources
Beta strandi653 – 6553Combined sources
Beta strandi661 – 6633Combined sources
Helixi667 – 67711Combined sources
Beta strandi680 – 6856Combined sources
Beta strandi689 – 6913Combined sources
Helixi696 – 6994Combined sources
Helixi704 – 71815Combined sources
Helixi720 – 73213Combined sources
Beta strandi737 – 7393Combined sources
Helixi741 – 7455Combined sources
Helixi749 – 7513Combined sources
Beta strandi758 – 7603Combined sources
Turni761 – 7633Combined sources
Beta strandi764 – 7674Combined sources
Beta strandi775 – 7817Combined sources
Beta strandi786 – 7883Combined sources
Turni789 – 7913Combined sources
Beta strandi799 – 8057Combined sources
Beta strandi812 – 8165Combined sources
Beta strandi819 – 8246Combined sources
Helixi830 – 8334Combined sources
Beta strandi838 – 8436Combined sources
Beta strandi850 – 8567Combined sources
Beta strandi859 – 8613Combined sources
Turni862 – 8687Combined sources
Beta strandi871 – 8777Combined sources
Beta strandi879 – 88911Combined sources
Beta strandi898 – 9069Combined sources
Beta strandi911 – 9177Combined sources
Beta strandi927 – 9315Combined sources
Turni932 – 9354Combined sources
Beta strandi936 – 9416Combined sources
Beta strandi950 – 9545Combined sources
Helixi975 – 9795Combined sources
Turni980 – 9823Combined sources
Beta strandi983 – 9853Combined sources
Beta strandi995 – 10006Combined sources
Beta strandi1002 – 10054Combined sources
Beta strandi1012 – 102211Combined sources
Helixi1024 – 10274Combined sources
Beta strandi1030 – 10323Combined sources
Beta strandi1036 – 10449Combined sources
Beta strandi1046 – 105510Combined sources
Beta strandi1057 – 10593Combined sources
Turni1078 – 10803Combined sources
Beta strandi1083 – 10886Combined sources
Turni1089 – 10924Combined sources
Beta strandi1093 – 10986Combined sources
Beta strandi1104 – 11074Combined sources
Beta strandi1114 – 11163Combined sources
Beta strandi1119 – 11257Combined sources
Beta strandi1127 – 11293Combined sources
Beta strandi1135 – 11373Combined sources
Beta strandi1140 – 11434Combined sources
Beta strandi1147 – 11548Combined sources
Beta strandi1172 – 11765Combined sources
Beta strandi1178 – 11803Combined sources
Beta strandi1182 – 11876Combined sources
Beta strandi1191 – 11988Combined sources
Turni1199 – 12013Combined sources
Beta strandi1202 – 12109Combined sources
Beta strandi1212 – 12176Combined sources
Helixi1222 – 123312Combined sources
Helixi1241 – 12444Combined sources
Beta strandi1245 – 12484Combined sources
Helixi1256 – 126914Combined sources
Beta strandi1275 – 12784Combined sources
Helixi1280 – 12823Combined sources
Helixi1284 – 12863Combined sources
Helixi1293 – 12953Combined sources
Helixi1298 – 130710Combined sources
Beta strandi1311 – 13166Combined sources
Helixi1329 – 13379Combined sources
Beta strandi1344 – 13463Combined sources
Beta strandi1351 – 13577Combined sources
Helixi1369 – 13757Combined sources
Beta strandi1377 – 13815Combined sources
Helixi1388 – 140215Combined sources
Helixi1408 – 14103Combined sources
Beta strandi1415 – 14195Combined sources
Turni1422 – 14243Combined sources
Beta strandi1427 – 14348Combined sources
Turni1439 – 14413Combined sources
Helixi1453 – 14553Combined sources
Turni1456 – 14605Combined sources
Beta strandi1467 – 14693Combined sources
Beta strandi1471 – 14733Combined sources
Beta strandi1475 – 14773Combined sources
Helixi1478 – 14814Combined sources
Helixi1482 – 14843Combined sources
Helixi1485 – 150117Combined sources
Beta strandi1507 – 15115Combined sources
Helixi1516 – 15183Combined sources
Beta strandi1521 – 15233Combined sources
Beta strandi1528 – 15303Combined sources
Helixi1532 – 154716Combined sources
Beta strandi1551 – 15533Combined sources
Beta strandi1559 – 15613Combined sources
Helixi1565 – 157511Combined sources
Beta strandi1578 – 15803Combined sources
Beta strandi1587 – 15893Combined sources
Helixi1594 – 15963Combined sources
Helixi1599 – 162931Combined sources
Beta strandi1633 – 16353Combined sources
Helixi1637 – 16393Combined sources
Turni1645 – 16495Combined sources
Beta strandi1652 – 16565Combined sources
Turni1657 – 16593Combined sources
Beta strandi1660 – 16634Combined sources
Beta strandi1667 – 16693Combined sources
Beta strandi1672 – 16776Combined sources
Beta strandi1682 – 16843Combined sources
Turni1685 – 16873Combined sources
Beta strandi1694 – 17018Combined sources
Beta strandi1708 – 17125Combined sources
Beta strandi1714 – 17207Combined sources
Helixi1726 – 17294Combined sources
Beta strandi1734 – 17396Combined sources
Beta strandi1746 – 17527Combined sources
Beta strandi1755 – 17573Combined sources
Turni1758 – 17603Combined sources
Helixi1761 – 17633Combined sources
Beta strandi1767 – 17737Combined sources
Beta strandi1778 – 178710Combined sources
Beta strandi1790 – 17923Combined sources
Beta strandi1795 – 18028Combined sources
Beta strandi1815 – 18217Combined sources
Beta strandi1829 – 18313Combined sources
Turni1845 – 18473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QLYX-ray2.00A87-954[»]
2QMJX-ray1.90A87-954[»]
3CTTX-ray2.10A87-954[»]
3L4TX-ray1.90A87-954[»]
3L4UX-ray1.90A87-954[»]
3L4VX-ray2.10A87-954[»]
3L4WX-ray2.00A87-954[»]
3L4XX-ray1.90A87-954[»]
3L4YX-ray1.80A87-954[»]
3L4ZX-ray2.00A87-954[»]
3TONX-ray2.95A/B960-1853[»]
3TOPX-ray2.88A/B960-1853[»]
ProteinModelPortaliO43451.
SMRiO43451. Positions 93-955, 960-1849.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43451.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 13447P-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini954 – 100047P-type 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 915718MaltaseAdd
BLAST
Regioni1067 – 1813747GlucoamylaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi38 – 8447Ser/Thr-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated
Contains 2 P-type (trefoil) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1501.
GeneTreeiENSGT00760000119229.
HOGENOMiHOG000067936.
HOVERGENiHBG080721.
InParanoidiO43451.
KOiK12047.
PhylomeDBiO43451.
TreeFamiTF314577.

Family and domain databases

Gene3Di4.10.110.10. 2 hits.
InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view]
SMARTiSM00018. PD. 2 hits.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 4 hits.
SSF74650. SSF74650. 2 hits.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 2 hits.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
PS00025. P_TREFOIL_1. 1 hit.
PS51448. P_TREFOIL_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43451-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARKKLKKFT TLEIVLSVLL LVLFIISIVL IVLLAKESLK STAPDPGTTG
60 70 80 90 100
TPDPGTTGTP DPGTTGTTHA RTTGPPDPGT TGTTPVSAEC PVVNELERIN
110 120 130 140 150
CIPDQPPTKA TCDQRGCCWN PQGAVSVPWC YYSKNHSYHV EGNLVNTNAG
160 170 180 190 200
FTARLKNLPS SPVFGSNVDN VLLTAEYQTS NRFHFKLTDQ TNNRFEVPHE
210 220 230 240 250
HVQSFSGNAA ASLTYQVEIS RQPFSIKVTR RSNNRVLFDS SIGPLLFADQ
260 270 280 290 300
FLQLSTRLPS TNVYGLGEHV HQQYRHDMNW KTWPIFNRDT TPNGNGTNLY
310 320 330 340 350
GAQTFFLCLE DASGLSFGVF LMNSNAMEVV LQPAPAITYR TIGGILDFYV
360 370 380 390 400
FLGNTPEQVV QEYLELIGRP ALPSYWALGF HLSRYEYGTL DNMREVVERN
410 420 430 440 450
RAAQLPYDVQ HADIDYMDER RDFTYDSVDF KGFPEFVNEL HNNGQKLVII
460 470 480 490 500
VDPAISNNSS SSKPYGPYDR GSDMKIWVNS SDGVTPLIGE VWPGQTVFPD
510 520 530 540 550
YTNPNCAVWW TKEFELFHNQ VEFDGIWIDM NEVSNFVDGS VSGCSTNNLN
560 570 580 590 600
NPPFTPRILD GYLFCKTLCM DAVQHWGKQY DIHNLYGYSM AVATAEAAKT
610 620 630 640 650
VFPNKRSFIL TRSTFAGSGK FAAHWLGDNT ATWDDLRWSI PGVLEFNLFG
660 670 680 690 700
IPMVGPDICG FALDTPEELC RRWMQLGAFY PFSRNHNGQG YKDQDPASFG
710 720 730 740 750
ADSLLLNSSR HYLNIRYTLL PYLYTLFFRA HSRGDTVARP LLHEFYEDNS
760 770 780 790 800
TWDVHQQFLW GPGLLITPVL DEGAEKVMAY VPDAVWYDYE TGSQVRWRKQ
810 820 830 840 850
KVEMELPGDK IGLHLRGGYI FPTQQPNTTT LASRKNPLGL IIALDENKEA
860 870 880 890 900
KGELFWDNGE TKDTVANKVY LLCEFSVTQN RLEVNISQST YKDPNNLAFN
910 920 930 940 950
EIKILGTEEP SNVTVKHNGV PSQTSPTVTY DSNLKVAIIT DIDLLLGEAY
960 970 980 990 1000
TVEWSIKIRD EEKIDCYPDE NGASAENCTA RGCIWEASNS SGVPFCYFVN
1010 1020 1030 1040 1050
DLYSVSDVQY NSHGATADIS LKSSVYANAF PSTPVNPLRL DVTYHKNEML
1060 1070 1080 1090 1100
QFKIYDPNKN RYEVPVPLNI PSMPSSTPEG QLYDVLIKKN PFGIEIRRKS
1110 1120 1130 1140 1150
TGTIIWDSQL LGFTFSDMFI RISTRLPSKY LYGFGETEHR SYRRDLEWHT
1160 1170 1180 1190 1200
WGMFSRDQPP GYKKNSYGVH PYYMGLEEDG SAHGVLLLNS NAMDVTFQPL
1210 1220 1230 1240 1250
PALTYRTTGG VLDFYVFLGP TPELVTQQYT ELIGRPVMVP YWSLGFQLCR
1260 1270 1280 1290 1300
YGYQNDSEIA SLYDEMVAAQ IPYDVQYSDI DYMERQLDFT LSPKFAGFPA
1310 1320 1330 1340 1350
LINRMKADGM RVILILDPAI SGNETQPYPA FTRGVEDDVF IKYPNDGDIV
1360 1370 1380 1390 1400
WGKVWPDFPD VVVNGSLDWD SQVELYRAYV AFPDFFRNST AKWWKREIEE
1410 1420 1430 1440 1450
LYNNPQNPER SLKFDGMWID MNEPSSFVNG AVSPGCRDAS LNHPPYMPHL
1460 1470 1480 1490 1500
ESRDRGLSSK TLCMESQQIL PDGSLVQHYN VHNLYGWSQT RPTYEAVQEV
1510 1520 1530 1540 1550
TGQRGVVITR STFPSSGRWA GHWLGDNTAA WDQLKKSIIG MMEFSLFGIS
1560 1570 1580 1590 1600
YTGADICGFF QDAEYEMCVR WMQLGAFYPF SRNHNTIGTR RQDPVSWDVA
1610 1620 1630 1640 1650
FVNISRTVLQ TRYTLLPYLY TLMHKAHTEG VTVVRPLLHE FVSDQVTWDI
1660 1670 1680 1690 1700
DSQFLLGPAF LVSPVLERNA RNVTAYFPRA RWYDYYTGVD INARGEWKTL
1710 1720 1730 1740 1750
PAPLDHINLH VRGGYILPWQ EPALNTHLSR QKFMGFKIAL DDEGTAGGWL
1760 1770 1780 1790 1800
FWDDGQSIDT YGKGLYYLAS FSASQNTMQS HIIFNNYITG TNPLKLGYIE
1810 1820 1830 1840 1850
IWGVGSVPVT SVSISVSGMV ITPSFNNDPT TQVLSIDVTD RNISLHNFTS

LTWISTL
Length:1,857
Mass (Da):209,852
Last modified:November 25, 2008 - v5
Checksum:i166EEC045C2031F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti854 – 8541L → P in AAI20873. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti404 – 4041Q → H.
Corresponds to variant rs2272330 [ dbSNP | Ensembl ].
VAR_047350
Natural varianti542 – 5421S → L.
Corresponds to variant rs10266732 [ dbSNP | Ensembl ].
VAR_047351
Natural varianti858 – 8581N → D.2 Publications
Corresponds to variant rs2960746 [ dbSNP | Ensembl ].
VAR_047352
Natural varianti1638 – 16381L → I.
Corresponds to variant rs9655651 [ dbSNP | Ensembl ].
VAR_047353

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016833 mRNA. Translation: AAC39568.2.
AC091684 Genomic DNA. Translation: AAP21875.1.
AC073647 Genomic DNA. Translation: AAS07445.1.
AC091742 Genomic DNA. No translation available.
BC120872 mRNA. Translation: AAI20873.1.
CCDSiCCDS47727.1.
RefSeqiNP_004659.2. NM_004668.2.
UniGeneiHs.122785.

Genome annotation databases

EnsembliENST00000549489; ENSP00000447378; ENSG00000257335.
ENST00000620571; ENSP00000482292; ENSG00000257335.
GeneIDi8972.
KEGGihsa:8972.
UCSCiuc003vwy.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016833 mRNA. Translation: AAC39568.2 .
AC091684 Genomic DNA. Translation: AAP21875.1 .
AC073647 Genomic DNA. Translation: AAS07445.1 .
AC091742 Genomic DNA. No translation available.
BC120872 mRNA. Translation: AAI20873.1 .
CCDSi CCDS47727.1.
RefSeqi NP_004659.2. NM_004668.2.
UniGenei Hs.122785.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QLY X-ray 2.00 A 87-954 [» ]
2QMJ X-ray 1.90 A 87-954 [» ]
3CTT X-ray 2.10 A 87-954 [» ]
3L4T X-ray 1.90 A 87-954 [» ]
3L4U X-ray 1.90 A 87-954 [» ]
3L4V X-ray 2.10 A 87-954 [» ]
3L4W X-ray 2.00 A 87-954 [» ]
3L4X X-ray 1.90 A 87-954 [» ]
3L4Y X-ray 1.80 A 87-954 [» ]
3L4Z X-ray 2.00 A 87-954 [» ]
3TON X-ray 2.95 A/B 960-1853 [» ]
3TOP X-ray 2.88 A/B 960-1853 [» ]
ProteinModelPortali O43451.
SMRi O43451. Positions 93-955, 960-1849.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114462. 2 interactions.
IntActi O43451. 2 interactions.
STRINGi 9606.ENSP00000373973.

Chemistry

BindingDBi O43451.
ChEMBLi CHEMBL2074.
DrugBanki DB00284. Acarbose.
DB00491. Miglitol.
DB04878. Voglibose.
GuidetoPHARMACOLOGYi 2627.

Protein family/group databases

CAZyi GH31. Glycoside Hydrolase Family 31.

PTM databases

PhosphoSitei O43451.

Proteomic databases

PaxDbi O43451.
PRIDEi O43451.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000549489 ; ENSP00000447378 ; ENSG00000257335 .
ENST00000620571 ; ENSP00000482292 ; ENSG00000257335 .
GeneIDi 8972.
KEGGi hsa:8972.
UCSCi uc003vwy.3. human.

Organism-specific databases

CTDi 8972.
GeneCardsi GC07P141607.
H-InvDB HIX0025263.
HGNCi HGNC:7043. MGAM.
HPAi HPA002270.
MIMi 154360. gene.
neXtProti NX_O43451.
PharmGKBi PA30778.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1501.
GeneTreei ENSGT00760000119229.
HOGENOMi HOG000067936.
HOVERGENi HBG080721.
InParanoidi O43451.
KOi K12047.
PhylomeDBi O43451.
TreeFami TF314577.

Enzyme and pathway databases

Reactomei REACT_9472. Digestion of dietary carbohydrate.

Miscellaneous databases

EvolutionaryTracei O43451.
GeneWikii Maltase-glucoamylase.
GenomeRNAii 8972.
NextBioi 33667.
PROi O43451.
SOURCEi Search...

Gene expression databases

Bgeei O43451.
CleanExi HS_MGA.
HS_MGAM.
ExpressionAtlasi O43451. baseline and differential.
Genevestigatori O43451.

Family and domain databases

Gene3Di 4.10.110.10. 2 hits.
InterProi IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view ]
Pfami PF01055. Glyco_hydro_31. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view ]
SMARTi SM00018. PD. 2 hits.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 4 hits.
SSF74650. SSF74650. 2 hits.
PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 2 hits.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
PS00025. P_TREFOIL_1. 1 hit.
PS51448. P_TREFOIL_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase."
    Nichols B.L., Eldering J.A., Avery S.E., Hahn D., Quaroni A., Sterchi E.E.
    J. Biol. Chem. 273:3076-3081(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT ASP-858.
    Tissue: Small intestine.
  2. Nichols B.L., Eldering J.A., Avery S.E., Hahn D., Quaroni A., Sterchi E.E.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 777; 1050; 1101; 1542; 1613 AND 1812.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-858.
  5. "Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase."
    Naim H.Y., Sterchi E.E., Lentze M.J.
    J. Biol. Chem. 263:19709-19717(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Tissue: Small intestine mucosa.
  6. "Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte."
    Danielsen E.M.
    EMBO J. 6:2891-2896(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: SULFATION.
  7. "Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity."
    Sim L., Quezada-Calvillo R., Sterchi E.E., Nichols B.L., Rose D.R.
    J. Mol. Biol. 375:782-792(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 87-954, GLYCOSYLATION, DISULFIDE BONDS.

Entry informationi

Entry nameiMGA_HUMAN
AccessioniPrimary (citable) accession number: O43451
Secondary accession number(s): Q0VAX6, Q75ME7, Q86UM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 25, 2008
Last modified: November 26, 2014
This is version 135 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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