Sis
entrez
69983
canonical
uniprot
B5THE3
canonical
ensembl
ENSMUSG00000027790
resolver
ensp
ENSMUSP00000091742
resolver
ensp
ENSMUSP00000129116
resolver
enst
ENSMUST00000094190
resolver
enst
ENSMUST00000167334
resolver
genesymbol
Sis
resolver
uniprot
F8VQM5
resolver
uniprot_entry
SUIS_MOUSE
resolver
uniprot_sec
F8VQM5
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:0000250|UniProtKB:P14410}.
uniprot
proteins
amino_acid_sequence
MAKKKFSGLEISLIVLFIIVTIIAIALVVVLATKVPAVEEVKSPTSTPSPGRCPPEQGEPLNERINCIPEQHPTKAKCEERGCCWRPWNNTIIPWCFFADNHGYTAASVTNDNSGLKATLSRIPSPTLFGEDIKSVLLTTQSQTRNRFRFKLTDPNNKRYEVPHQFVKDGNGIPAADTLYDVKVSENPFSIKVIRKSNNKVLFDTSIGPLVYSNQYLQISTRLPSEYIYGFGEHIHKRFRHDLYWKTWPIFTRDEIPGDNNHNLYGHQTFFMGIEDNSGKSYGVFLMNSNAMEVFIQPTPIITYRVTGGVLDFYIFLGDTPEQVVQQYQELIGRPAMPAYWNLGFQLSRWNYVSLDKVKEVVRRNREAGIPYDAQVTDIDYMEDKKDFTYDEVAFKGLPEFAQDLHNHGQKYIIILDPAISINKRANGAEYQTYVRGNEQNVWVKESDGTTSLIGEVWPGLTVYPDFTNPRTWEWWANECNLFHQQVEYDGLWIDMNEVSSFIHGSQKGCAPNLLNYPPFTPGILDKIMYSKTLCMDAVQHWGNQYDVHSLYGYSMAIATEKAVEKVFPNKRSFILTRSTFAGSGHHAAHWLGDNTASWEQMEWSITGMLEFGMFGMPLVGADICGFLANTTEELCRRWMQLGAFYPFSRNHNAEGYAEQDPAFWGADSLLVNTSRHYLTIRYTLLPFLYTLFYRAHAFGETVARPFLHEFYEDPNSWIEDTQFLWGPALLITPVLRPETKYVSAYIPDATWYDYETGEKRPWRKQRVDMYLPEDKIGLHLRGGYIIPTQQPDVTTTASRKNPLGLIVALDENQAAKGELFWDDGESKDTIEKKIYILYEFSVSNNNLIVNCTHSSYPEGNTLVFKTIKVLGLSATVTAVTVGENDQQMNPHLAFTFDAFNKILSITDLTFNLGKTFIVRWTTQSFSDNEKFTCYPDVGTATEKTCVERGCIWEPVSGLANVPPCYFPSNHNPYLLTSTQKLATGITAELQLNPASARIKLPSNPISTLRVEVKYHKNDMLQFKIYDAHHKRYEVPVPLNIPDTPTSSEENRLYDVEIKENPFGIQVRRRSTGKLIWDSCLPGFAFNDQFIQISTRLPSQYLYGFGEAEHTAFKRNLNWHTWGMFTRDQPPGYKLNSYGFHPYYMALEDEGNAHGVLLQNSNGMDVTFQPTPALTYRTIGGILDFYMFLGPTPEGATKQYHEVIGFPVMPPYWALGFQLCRYGYRNTSEIEQLYNDMKAAQIPYDVQYTDINYMERQLDFTIGERFKTLPQFVEKIRKEGMKYIVILDPAISGNETQPYPAFERGIQKDVFVKWPNTNDICWAKVWPDLPNITIDETITEDEAVNASRAHVAFPDFFRNSTSEWWTREIYDFYNEKMKFDGLWIDMNEPSSFVNGTVTNKCRNDTLNYPPYFPELTKRNEGLHFRTMCMETEHILSDGSSVLHYDVHNLYGWSQVKPTLDALRNTTGLRGIVISRSTYPTAGRWGGHWLGDNYANWENLEKSLIGMLEFNLFGIPYVGADICGFFNDSEYHLCARWMQVGAFYPYSRNHNIQFTRRQDPVSWNETFAQMSKKVLEIRYTLLPYFYTQMHEAHIHGGTVIRPLMHEFFDDKETWEIYKQFLWGPAFMVTPVIGPFQTAVNGYVPKARWFDYHTGEDIKVRGKLQTFSAPFDTINLHVRGGYILPCQEPAQNTYYSRQKYMKLIVAADDNQTAKGTLFWDDGESIDTYEKNQYTLIEFNLNQKNLTSTVLKDGYRNKSEMKLGSIYVWGKGTTSISQVNLTYGGNEQQLSFTQDEAKEILTIDLKNVTVTLDEPIQISWS
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:0000250|UniProtKB:P14410}.
uniprot
proteins
mass_dalton
208984
uniprot
proteins
pathway_participation
PATHWAY: Carbohydrate degradation. {ECO:0000250|UniProtKB:P14410}.
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:0000250|UniProtKB:P14410}.; PTM: Sulfated. {ECO:0000250|UniProtKB:P56729}.
uniprot
proteins
protein_family
Glycosyl hydrolase 31 family
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
34914943
uniprot
proteins
sequence_length
1818
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. {ECO:0000250|UniProtKB:P14410}.
uniprot
proteins
transmembrane_region
TRANSMEM 11..31; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins