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Protein

Maltase-glucoamylase, intestinal

Gene

MGAM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei529NucleophilePROSITE-ProRule annotation1
Active sitei532By similarity1
Active sitei1420NucleophilePROSITE-ProRule annotation1
Active sitei1423By similarity1
Active sitei1526Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

  • polysaccharide digestion Source: Reactome
  • starch catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciZFISH:HS11348-MONOMER.
BRENDAi3.2.1.20. 2681.
3.2.1.3. 2681.
ReactomeiR-HSA-189085. Digestion of dietary carbohydrate.
R-HSA-6798695. Neutrophil degranulation.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:7043. MGAM.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 13CytoplasmicSequence analysisAdd BLAST13
Transmembranei14 – 34Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini35 – 1857LumenalSequence analysisAdd BLAST1823

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi8972.
OpenTargetsiENSG00000257335.
PharmGKBiPA30778.

Chemistry databases

ChEMBLiCHEMBL2074.
DrugBankiDB00284. Acarbose.
DB00491. Miglitol.
DB04878. Voglibose.
GuidetoPHARMACOLOGYi2627.

Polymorphism and mutation databases

BioMutaiMGAM.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001853631 – 1857Maltase-glucoamylase, intestinalAdd BLAST1857

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi90 ↔ 118PROSITE-ProRule annotation
Disulfide bondi101 ↔ 117PROSITE-ProRule annotation1 Publication
Disulfide bondi112 ↔ 130PROSITE-ProRule annotation1 Publication
Glycosylationi135N-linked (GlcNAc...)Sequence analysis1
Glycosylationi295N-linked (GlcNAc...)1 Publication1
Modified residuei416SulfotyrosineSequence analysis1
Modified residuei425SulfotyrosineSequence analysis1
Glycosylationi457N-linked (GlcNAc...)Sequence analysis1
Glycosylationi458N-linked (GlcNAc...)Sequence analysis1
Glycosylationi479N-linked (GlcNAc...)1 Publication1
Disulfide bondi659 ↔ 670PROSITE-ProRule annotation1 Publication
Glycosylationi707N-linked (GlcNAc...)Sequence analysis1
Glycosylationi749N-linked (GlcNAc...)Sequence analysis1
Glycosylationi827N-linked (GlcNAc...)1 Publication1
Glycosylationi885N-linked (GlcNAc...)Sequence analysis1
Glycosylationi912N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi966 ↔ 983PROSITE-ProRule annotation
Glycosylationi977N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi978 ↔ 996PROSITE-ProRule annotation
Glycosylationi989N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1255N-linked (GlcNAc...)Sequence analysis1
Modified residuei1282SulfotyrosineSequence analysis1
Glycosylationi1323N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1364N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1388N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1603N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1672N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1842N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1847N-linked (GlcNAc...)Sequence analysis1

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.
PeptideAtlasiO43451.
PRIDEiO43451.

PTM databases

iPTMnetiO43451.
PhosphoSitePlusiO43451.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000257335.
CleanExiHS_MGA.
HS_MGAM.
ExpressionAtlasiO43451. baseline and differential.
GenevisibleiO43451. HS.

Organism-specific databases

HPAiHPA002270.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi114462. 1 interactor.
IntActiO43451. 2 interactors.
STRINGi9606.ENSP00000447378.

Chemistry databases

BindingDBiO43451.

Structurei

Secondary structure

11857
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi95 – 97Combined sources3
Beta strandi104 – 106Combined sources3
Helixi109 – 115Combined sources7
Beta strandi129 – 131Combined sources3
Beta strandi136 – 146Combined sources11
Beta strandi148 – 157Combined sources10
Beta strandi163 – 165Combined sources3
Beta strandi169 – 179Combined sources11
Beta strandi182 – 189Combined sources8
Beta strandi214 – 220Combined sources7
Turni221 – 224Combined sources4
Beta strandi225 – 230Combined sources6
Turni231 – 233Combined sources3
Beta strandi236 – 239Combined sources4
Helixi240 – 242Combined sources3
Beta strandi246 – 248Combined sources3
Beta strandi251 – 257Combined sources7
Beta strandi263 – 269Combined sources7
Beta strandi272 – 276Combined sources5
Beta strandi279 – 285Combined sources7
Beta strandi303 – 309Combined sources7
Beta strandi316 – 321Combined sources6
Beta strandi327 – 332Combined sources6
Turni333 – 335Combined sources3
Beta strandi336 – 344Combined sources9
Beta strandi346 – 355Combined sources10
Helixi356 – 367Combined sources12
Helixi375 – 378Combined sources4
Beta strandi379 – 382Combined sources4
Helixi390 – 402Combined sources13
Beta strandi409 – 412Combined sources4
Helixi414 – 416Combined sources3
Beta strandi417 – 420Combined sources4
Turni427 – 432Combined sources6
Helixi433 – 442Combined sources10
Beta strandi446 – 451Combined sources6
Beta strandi461 – 463Combined sources3
Helixi466 – 474Combined sources9
Beta strandi483 – 486Combined sources4
Beta strandi489 – 491Combined sources3
Beta strandi494 – 497Combined sources4
Helixi504 – 518Combined sources15
Beta strandi524 – 528Combined sources5
Turni531 – 533Combined sources3
Beta strandi536 – 540Combined sources5
Turni548 – 550Combined sources3
Helixi559 – 561Combined sources3
Turni563 – 566Combined sources4
Helixi579 – 582Combined sources4
Helixi583 – 585Combined sources3
Helixi586 – 601Combined sources16
Beta strandi609 – 613Combined sources5
Helixi618 – 620Combined sources3
Beta strandi623 – 625Combined sources3
Beta strandi630 – 632Combined sources3
Helixi633 – 648Combined sources16
Beta strandi653 – 655Combined sources3
Beta strandi661 – 663Combined sources3
Helixi667 – 677Combined sources11
Beta strandi680 – 685Combined sources6
Beta strandi689 – 691Combined sources3
Helixi696 – 699Combined sources4
Helixi704 – 718Combined sources15
Helixi720 – 732Combined sources13
Beta strandi737 – 739Combined sources3
Helixi741 – 745Combined sources5
Helixi749 – 751Combined sources3
Beta strandi758 – 760Combined sources3
Turni761 – 763Combined sources3
Beta strandi764 – 767Combined sources4
Beta strandi775 – 781Combined sources7
Beta strandi786 – 788Combined sources3
Turni789 – 791Combined sources3
Beta strandi799 – 805Combined sources7
Beta strandi812 – 816Combined sources5
Beta strandi819 – 824Combined sources6
Helixi830 – 833Combined sources4
Beta strandi838 – 843Combined sources6
Beta strandi850 – 856Combined sources7
Beta strandi859 – 861Combined sources3
Turni862 – 868Combined sources7
Beta strandi871 – 877Combined sources7
Beta strandi879 – 889Combined sources11
Beta strandi898 – 906Combined sources9
Beta strandi911 – 917Combined sources7
Beta strandi927 – 931Combined sources5
Turni932 – 935Combined sources4
Beta strandi936 – 941Combined sources6
Beta strandi950 – 954Combined sources5
Helixi975 – 979Combined sources5
Turni980 – 982Combined sources3
Beta strandi983 – 985Combined sources3
Beta strandi995 – 1000Combined sources6
Beta strandi1002 – 1005Combined sources4
Beta strandi1012 – 1022Combined sources11
Helixi1024 – 1027Combined sources4
Beta strandi1030 – 1032Combined sources3
Beta strandi1036 – 1044Combined sources9
Beta strandi1046 – 1055Combined sources10
Beta strandi1057 – 1059Combined sources3
Turni1078 – 1080Combined sources3
Beta strandi1083 – 1088Combined sources6
Turni1089 – 1092Combined sources4
Beta strandi1093 – 1098Combined sources6
Beta strandi1104 – 1107Combined sources4
Beta strandi1114 – 1116Combined sources3
Beta strandi1119 – 1125Combined sources7
Beta strandi1127 – 1129Combined sources3
Beta strandi1135 – 1137Combined sources3
Beta strandi1140 – 1143Combined sources4
Beta strandi1147 – 1154Combined sources8
Beta strandi1172 – 1176Combined sources5
Beta strandi1178 – 1180Combined sources3
Beta strandi1182 – 1187Combined sources6
Beta strandi1191 – 1198Combined sources8
Turni1199 – 1201Combined sources3
Beta strandi1202 – 1210Combined sources9
Beta strandi1212 – 1217Combined sources6
Helixi1222 – 1233Combined sources12
Helixi1241 – 1244Combined sources4
Beta strandi1245 – 1248Combined sources4
Helixi1256 – 1269Combined sources14
Beta strandi1275 – 1278Combined sources4
Helixi1280 – 1282Combined sources3
Helixi1284 – 1286Combined sources3
Helixi1293 – 1295Combined sources3
Helixi1298 – 1307Combined sources10
Beta strandi1311 – 1316Combined sources6
Helixi1329 – 1337Combined sources9
Beta strandi1344 – 1346Combined sources3
Beta strandi1351 – 1357Combined sources7
Helixi1369 – 1375Combined sources7
Beta strandi1377 – 1381Combined sources5
Helixi1388 – 1402Combined sources15
Helixi1408 – 1410Combined sources3
Beta strandi1415 – 1419Combined sources5
Turni1422 – 1424Combined sources3
Beta strandi1427 – 1434Combined sources8
Turni1439 – 1441Combined sources3
Helixi1453 – 1455Combined sources3
Turni1456 – 1460Combined sources5
Beta strandi1467 – 1469Combined sources3
Beta strandi1471 – 1473Combined sources3
Beta strandi1475 – 1477Combined sources3
Helixi1478 – 1481Combined sources4
Helixi1482 – 1484Combined sources3
Helixi1485 – 1501Combined sources17
Beta strandi1507 – 1511Combined sources5
Helixi1516 – 1518Combined sources3
Beta strandi1521 – 1523Combined sources3
Beta strandi1528 – 1530Combined sources3
Helixi1532 – 1547Combined sources16
Beta strandi1551 – 1553Combined sources3
Beta strandi1559 – 1561Combined sources3
Helixi1565 – 1575Combined sources11
Beta strandi1578 – 1580Combined sources3
Beta strandi1587 – 1589Combined sources3
Helixi1594 – 1596Combined sources3
Helixi1599 – 1629Combined sources31
Beta strandi1633 – 1635Combined sources3
Helixi1637 – 1639Combined sources3
Turni1645 – 1649Combined sources5
Beta strandi1652 – 1656Combined sources5
Turni1657 – 1659Combined sources3
Beta strandi1660 – 1663Combined sources4
Beta strandi1667 – 1669Combined sources3
Beta strandi1672 – 1677Combined sources6
Beta strandi1682 – 1684Combined sources3
Turni1685 – 1687Combined sources3
Beta strandi1694 – 1701Combined sources8
Beta strandi1708 – 1712Combined sources5
Beta strandi1714 – 1720Combined sources7
Helixi1726 – 1729Combined sources4
Beta strandi1734 – 1739Combined sources6
Beta strandi1746 – 1752Combined sources7
Beta strandi1755 – 1757Combined sources3
Turni1758 – 1760Combined sources3
Helixi1761 – 1763Combined sources3
Beta strandi1767 – 1773Combined sources7
Beta strandi1778 – 1787Combined sources10
Beta strandi1790 – 1792Combined sources3
Beta strandi1795 – 1802Combined sources8
Beta strandi1815 – 1821Combined sources7
Beta strandi1829 – 1831Combined sources3
Turni1845 – 1847Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43451.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini88 – 134P-type 1PROSITE-ProRule annotationAdd BLAST47
Domaini954 – 1000P-type 2PROSITE-ProRule annotationAdd BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni198 – 915MaltaseAdd BLAST718
Regioni1067 – 1813GlucoamylaseAdd BLAST747

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi38 – 84Ser/Thr-richAdd BLAST47

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

eggNOGiKOG1065. Eukaryota.
COG1501. LUCA.
GeneTreeiENSGT00760000119229.
HOGENOMiHOG000067936.
HOVERGENiHBG080721.
InParanoidiO43451.
KOiK12047.
PhylomeDBiO43451.
TreeFamiTF314577.

Family and domain databases

CDDicd00111. Trefoil. 2 hits.
Gene3Di4.10.110.10. 2 hits.
InterProiIPR031727. Gal_mutarotase_N.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR030459. Glyco_hydro_31_CS.
IPR017853. Glycoside_hydrolase_SF.
IPR017957. P_trefoil_CS.
IPR000519. P_trefoil_dom.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 2 hits.
PF16863. NtCtMGAM_N. 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)DescriptionActionsGraphical viewLength
Sequence conflicti854L → P in AAI20873 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_047350404Q → H.Corresponds to variant rs2272330dbSNPEnsembl.1
Natural variantiVAR_047351542S → L.Corresponds to variant rs10266732dbSNPEnsembl.1
Natural variantiVAR_047352858N → D.2 PublicationsCorresponds to variant rs2960746dbSNPEnsembl.1
Natural variantiVAR_0473531638L → I.Corresponds to variant rs9655651dbSNPEnsembl.1

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.4. 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.
CCDSiCCDS47727.1.
RefSeqiNP_004659.2. NM_004668.2.
UniGeneiHs.122785.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114462. 1 interactor.
IntActiO43451. 2 interactors.
STRINGi9606.ENSP00000447378.

Chemistry databases

BindingDBiO43451.
ChEMBLiCHEMBL2074.
DrugBankiDB00284. Acarbose.
DB00491. Miglitol.
DB04878. Voglibose.
GuidetoPHARMACOLOGYi2627.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

PTM databases

iPTMnetiO43451.
PhosphoSitePlusiO43451.

Polymorphism and mutation databases

BioMutaiMGAM.

Proteomic databases

PaxDbiO43451.
PeptideAtlasiO43451.
PRIDEiO43451.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000549489; ENSP00000447378; ENSG00000257335.
ENST00000620571; ENSP00000482292; ENSG00000257335.
GeneIDi8972.
KEGGihsa:8972.
UCSCiuc003vwy.4. human.

Organism-specific databases

CTDi8972.
DisGeNETi8972.
GeneCardsiMGAM.
H-InvDBHIX0025263.
HGNCiHGNC:7043. MGAM.
HPAiHPA002270.
MIMi154360. gene.
neXtProtiNX_O43451.
OpenTargetsiENSG00000257335.
PharmGKBiPA30778.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1065. Eukaryota.
COG1501. LUCA.
GeneTreeiENSGT00760000119229.
HOGENOMiHOG000067936.
HOVERGENiHBG080721.
InParanoidiO43451.
KOiK12047.
PhylomeDBiO43451.
TreeFamiTF314577.

Enzyme and pathway databases

BioCyciZFISH:HS11348-MONOMER.
BRENDAi3.2.1.20. 2681.
3.2.1.3. 2681.
ReactomeiR-HSA-189085. Digestion of dietary carbohydrate.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiO43451.
GeneWikiiMaltase-glucoamylase.
GenomeRNAii8972.
PROiO43451.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000257335.
CleanExiHS_MGA.
HS_MGAM.
ExpressionAtlasiO43451. baseline and differential.
GenevisibleiO43451. HS.

Family and domain databases

CDDicd00111. Trefoil. 2 hits.
Gene3Di4.10.110.10. 2 hits.
InterProiIPR031727. Gal_mutarotase_N.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR030459. Glyco_hydro_31_CS.
IPR017853. Glycoside_hydrolase_SF.
IPR017957. P_trefoil_CS.
IPR000519. P_trefoil_dom.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 2 hits.
PF16863. NtCtMGAM_N. 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]
ProtoNetiSearch...

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 30, 2016
This is version 153 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.