P23739
uniprot
P23739
canonical
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
MAKKKFSALEISLIVLFIIVTAIAIALVTVLATKVPAVEEIKSPTPTSNSTPTSTPTSTSTPTSTSTPSPGKCPPEQGEPINERINCIPEQHPTKAICEERGCCWRPWNNTVIPWCFFADNHGYNAESITNENAGLKATLNRIPSPTLFGEDIKSVILTTQTQTGNRFRFKITDPNNKRYEVPHQFVKEETGIPAADTLYDVQVSENPFSIKVIRKSNNKVLCDTSVGPLLYSNQYLQISTRLPSEYIYGFGGHIHKRFRHDLYWKTWPIFTRDEIPGDNNHNLYGHQTFFMGIGDTSGKSYGVFLMNSNAMEVFIQPTPIITYRVTGGILDFYIFLGDTPEQVVQQYQEVHWRPAMPAYWNLGFQLSRWNYGSLDTVSEVVRRNREAGIPYDAQVTDIDYMEDHKEFTYDRVKFNGLPEFAQDLHNHGKYIIILDPAISINKRANGAEYQTYVRGNEKNVWVNESDGTTPLIGEVWPGLTVYPDFTNPQTIEWWANECNLFHQQVEYDGLWIDMNEVSSFIQGSLNLKGVLLIVLNYPPFTPGILDKVMYSKTLCMDAVQHWGKQYDVHSLYGYSMAIATEQAVERVFPNKRSFILTRSTFGGSGRHANHWLGDNTASWEQMEWSITGMLEFGIFGMPLVGATSCGFLADTTEELCRRWMQLGAFYPFSRNHNAEGYMEQDPAYFGQDSSRHYLTIRYTLLPFLYTLFYRAHMFGETVARPFLYEFYDDTNSWIEDTQFLWGPALLITPVLRPGVENVSAYIPNATWYDYETGIKRPWRKERINMYLPGDKIGLHLRGGYIIPTQEPDVTTTASRKNPLGLIVALDDNQAAKGELFWDDGESKDSIEKKMYILYTFSVSNNELVLNCTHSSYAEGTSLAFKTIKVLGLREDVRSITVGENDQQMATHTNFTFDSANKILSITALNFNLAGSFIVRWCRTFSDNEKFTCYPDVGTATEGTCTQRGCLWQPVSGLSNVPPYYFPPENNPYTLTSIQPLPTGITAELQLNPPNARIKLPSNPISTLRVGVKYHPNDMLQFKIYDAQHKRYEVPVPLNIPDTPTSSNERLYDVEIKENPFGIQVRRRSSGKLIWDSRLPGFGFNDQFIQISTRLPSNYLYGFGEVEHTAFKRDLNWHTWGMFTRDQPPGYKLNSYGFHPYYMALENEGNAHGVLLLNSNGMDVTFQPTPALTYRTIGGILDFYMFLGPTPEIATRQYHEVIGFPVMPPYWALGFQLCRYGYRNTSEIEQLYNDMVAANIPYDVQYTDINYMERQLDFTIGERFKTLPEFVDRIRKDGMKYIVILAPAISGNETQPYPAFERGIQKDVFVKWPNTNDICWPKVWPDLPNVTIDETITEDEAVNASRAHVAFPDFFRNSTLEWWAREIYDFYNEKMKFDGLWIDMNEPSSFGIQMGGKVLNECRRMMTLNYPPVFSPELRVKEGEGASISEAMCMETEHILIDGSSVLQYDVHNLYGWSQVKPTLDALQNTTGLRGIVISRSTYPTTGRWGGHWLGDNYTTWDNLEKSLIGMLELNLFGIPYIGADICGVFHDSGYPSLYFVGIQVGAFYPYPRESPTINFTRSQDPVSWMKLLLQMSKKVLEIRYTLLPYFYTQMHEAHAHGGTVIRPLMHEFFDDKETWEIYKQFLWGPAFMVTPVVEPFRTSVTGYVPKARWFDYHTGADIKLKGILHTFSAPFDTINLHVRGGYILPCQEPARNTHLSRQNYMKLIVAADDNQMAQGTLFGDDGESIDTYERGQYTSIQFNLNQTTLTSTVLANGYKNKQEMRLGSIHIWGKGTLRISNANLVYGGRKHQPPFTQEEAKETLIFDLKNMNVTLDEPIQITWS
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:27480812}.
uniprot
proteins
mass_dalton
210350
uniprot
proteins
pathway_participation
PATHWAY: Carbohydrate degradation. {ECO:0000250|UniProtKB:P14410}.
uniprot
proteins
post_translational_modification
PTM: Sulfated. {ECO:0000250|UniProtKB:P56729}.; PTM: Proteolytically cleaved into 2 catalytic subunits the sucrase subunit and isomaltase subunit (PubMed:6802834). The 2 subunits remain non-covalently associated on the brush border membrane, forming a functional enzyme complex (By similarity). {ECO:0000250|UniProtKB:P14410, ECO:0000269|PubMed:6802834}.
uniprot
proteins
protein_family
Glycosyl hydrolase 31 family
uniprot
proteins
pubmed
2268340
uniprot
proteins
pubmed
2400788
uniprot
proteins
pubmed
27480812
uniprot
proteins
pubmed
6802834
uniprot
proteins
pubmed
7821806
uniprot
proteins
pubmed
8410378
uniprot
proteins
sequence_length
1841
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:8410378}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P07768}. Note=Brush border. {ECO:0000269|PubMed:8410378}.
uniprot
proteins
transmembrane_region
TRANSMEM 13..32; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000250|UniProtKB:P07768
uniprot
proteins