SI
entrez
6476
canonical
uniprot
P14410
canonical
ensembl
ENSG00000090402
resolver
ensp
ENSP00000264382
resolver
enst
ENST00000264382
resolver
genesymbol
SI
resolver
hgnc
HGNC:10856
resolver
uniprot
A2RUC3
resolver
uniprot
Q1JQ80
resolver
uniprot
Q1RMC2
resolver
uniprot_entry
SUIS_HUMAN
resolver
uniprot_sec
A2RUC3
resolver
uniprot_sec
Q1JQ80
resolver
uniprot_sec
Q1RMC2
resolver
activity_regulation
ACTIVITY REGULATION: The glucose produced is able to inhibit SI activity both competitively, at the active site, and uncompetitively, via allosteric interactions. {ECO:0000269|PubMed:28522605}.
uniprot
proteins
amino_acid_sequence
MARKKFSGLEISLIVLFVIVTIIAIALIVVLATKTPAVDEISDSTSTPATTRVTTNPSDSGKCPNVLNDPVNVRINCIPEQFPTEGICAQRGCCWRPWNDSLIPWCFFVDNHGYNVQDMTTTSIGVEAKLNRIPSPTLFGNDINSVLFTTQNQTPNRFRFKITDPNNRRYEVPHQYVKEFTGPTVSDTLYDVKVAQNPFSIQVIRKSNGKTLFDTSIGPLVYSDQYLQISTRLPSDYIYGIGEQVHKRFRHDLSWKTWPIFTRDQLPGDNNNNLYGHQTFFMCIEDTSGKSFGVFLMNSNAMEIFIQPTPIVTYRVTGGILDFYILLGDTPEQVVQQYQQLVGLPAMPAYWNLGFQLSRWNYKSLDVVKEVVRRNREAGIPFDTQVTDIDYMEDKKDFTYDQVAFNGLPQFVQDLHDHGQKYVIILDPAISIGRRANGTTYATYERGNTQHVWINESDGSTPIIGEVWPGLTVYPDFTNPNCIDWWANECSIFHQEVQYDGLWIDMNEVSSFIQGSTKGCNVNKLNYPPFTPDILDKLMYSKTICMDAVQNWGKQYDVHSLYGYSMAIATEQAVQKVFPNKRSFILTRSTFAGSGRHAAHWLGDNTASWEQMEWSITGMLEFSLFGIPLVGADICGFVAETTEELCRRWMQLGAFYPFSRNHNSDGYEHQDPAFFGQNSLLVKSSRQYLTIRYTLLPFLYTLFYKAHVFGETVARPVLHEFYEDTNSWIEDTEFLWGPALLITPVLKQGADTVSAYIPDAIWYDYESGAKRPWRKQRVDMYLPADKIGLHLRGGYIIPIQEPDVTTTASRKNPLGLIVALGENNTAKGDFFWDDGETKDTIQNGNYILYTFSVSNNTLDIVCTHSSYQEGTTLAFQTVKILGLTDSVTEVRVAENNQPMNAHSNFTYDASNQVLLIADLKLNLGRNFSVQWNQIFSENERFNCYPDADLATEQKCTQRGCVWRTGSSLSKAPECYFPRQDNSYSVNSARYSSMGITADLQLNTANARIKLPSDPISTLRVEVKYHKNDMLQFKIYDPQKKRYEVPVPLNIPTTPISTYEDRLYDVEIKENPFGIQIRRRSSGRVIWDSWLPGFAFNDQFIQISTRLPSEYIYGFGEVEHTAFKRDLNWNTWGMFTRDQPPGYKLNSYGFHPYYMALEEEGNAHGVFLLNSNAMDVTFQPTPALTYRTVGGILDFYMFLGPTPEVATKQYHEVIGHPVMPAYWALGFQLCRYGYANTSEVRELYDAMVAANIPYDVQYTDIDYMERQLDFTIGEAFQDLPQFVDKIRGEGMRYIIILDPAISGNETKTYPAFERGQQNDVFVKWPNTNDICWAKVWPDLPNITIDKTLTEDEAVNASRAHVAFPDFFRTSTAEWWAREIVDFYNEKMKFDGLWIDMNEPSSFVNGTTTNQCRNDELNYPPYFPELTKRTDGLHFRTICMEAEQILSDGTSVLHYDVHNLYGWSQMKPTHDALQKTTGKRGIVISRSTYPTSGRWGGHWLGDNYARWDNMDKSIIGMMEFSLFGMSYTGADICGFFNNSEYHLCTRWMQLGAFYPYSRNHNIANTRRQDPASWNETFAEMSRNILNIRYTLLPYFYTQMHEIHANGGTVIRPLLHEFFDEKPTWDIFKQFLWGPAFMVTPVLEPYVQTVNAYVPNARWFDYHTGKDIGVRGQFQTFNASYDTINLHVRGGHILPCQEPAQNTFYSRQKHMKLIVAADDNQMAQGSLFWDDGESIDTYERDLYLSVQFNLNQTTLTSTILKRGYINKSETRLGSLHVWGKGTTPVNAVTLTYNGNKNSLPFNEDTTNMILRIDLTTHNVTLEEPIEINWS
uniprot
proteins
disease_involvement
DISEASE: Congenital sucrase-isomaltase deficiency (CSID) [MIM:222900]: Autosomal recessive intestinal disorder that is clinically characterized by fermentative diarrhea, abdominal pain, and cramps upon ingestion of sugar. The symptoms are the consequence of absent or drastically reduced enzymatic activities of sucrase and isomaltase. The prevalence of CSID is 0.02 % in individuals of European descent and appears to be much higher in Greenland, Alaskan, and Canadian native people. CSID arises due to post-translational perturbations in the intracellular transport, polarized sorting, aberrant processing, and defective function of SI. {ECO:0000269|PubMed:10903344, ECO:0000269|PubMed:11340066, ECO:0000269|PubMed:14724820, ECO:0000269|PubMed:16329100, ECO:0000269|PubMed:8609217}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.2.1.10
uniprot
proteins
ec_number
3.2.1.48
uniprot
proteins
function
FUNCTION: Bifunctional enzyme with both sucrase and isomaltase activities involved in breakdown of dietary starch oligosaccharides in small intestine. The isomaltase domain hydrolazes alpha-1,6-glycosidic linkages in isomaltose. The sucrase domain cleaves the alpha-1,2-glycosidic linkages in sucrose to form glucose and fructose, and contributes to the cleavage of the alpha-1,4-glycosidic linkage in maltose to form two glucose monosaccharides. {ECO:0000269|PubMed:20356844, ECO:0000269|PubMed:28522605}.
uniprot
proteins
mass_dalton
209453
uniprot
proteins
mutagenesis
MUTAGEN 265; /note="Q->A: Does not affect sucrase activity. Increases isomaltase activity."; /evidence="ECO:0000269|PubMed:31254546"; MUTAGEN 266; /note="L->A,V: Decreases sucrase activity. Reduces maltose hydrolysis. Reduces isomaltase activity."; /evidence="ECO:0000269|PubMed:31254546"; MUTAGEN 505; /note="D->E: Abolishes the isomaltase activity. Reduces maltose hydrolysis, but do not affect sucrase activity."; /evidence="ECO:0000269|PubMed:28522605"; MUTAGEN 604; /note="D->E,N,Y: Abolishes the isomaltase activity. Reduces maltose hydrolysis. Does not affect sucrase activity."; /evidence="ECO:0000269|PubMed:28522605"; MUTAGEN 638; /note="V->A,L: Decreases sucrase activity. Reduces maltose hydrolysis."; /evidence="ECO:0000269|PubMed:31254546"; MUTAGEN 1394; /note="D->E: Abolishes sucrase activity."; /evidence="ECO:0000269|PubMed:28522605"; MUTAGEN 1500; /note="D->E,N,S,Y: Abolishes sucrase activity."; /evidence="ECO:0000269|PubMed:28522605
uniprot
proteins
pathway_participation
PATHWAY: Carbohydrate degradation. {ECO:0000305|PubMed:20356844}.
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved into 2 catalytic subunits the sucrase subunit and isomaltase subunit. The 2 subunits remain non-covalently associated on the brush border membrane, forming a functional enzyme complex. {ECO:0000269|PubMed:3366777}.; PTM: Sulfated. {ECO:0000250|UniProtKB:P56729}.
uniprot
proteins
protein_family
Glycosyl hydrolase 31 family
uniprot
proteins
pubmed
10903344
uniprot
proteins
pubmed
11340066
uniprot
proteins
pubmed
1353958
uniprot
proteins
pubmed
14724820
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16329100
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
1677636
uniprot
proteins
pubmed
20356844
uniprot
proteins
pubmed
28522605
uniprot
proteins
pubmed
2962903
uniprot
proteins
pubmed
31254546
uniprot
proteins
pubmed
3366777
uniprot
proteins
pubmed
8521865
uniprot
proteins
pubmed
8609217
uniprot
proteins
sequence_length
1827
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P23739}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P07768}. Note=Brush border.
uniprot
proteins
transmembrane_region
TRANSMEM 13..32; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000250|UniProtKB:P07768
uniprot
proteins