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Protein

Sucrase-isomaltase, intestinal

Gene

SI

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides (By similarity).By similarity

Catalytic activityi

Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Sucrase-isomaltase, intestinal
Cleaved into the following 2 chains:
Gene namesi
Name:SI
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 12CytoplasmicSequence analysisAdd BLAST11
Transmembranei13 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini33 – ›38LumenalSequence analysis›6

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000185542 – ›38IsomaltaseAdd BLAST›37
ChainiPRO_000001855539 – ›62SucraseAdd BLAST›24

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7Phosphoserine; by PKABy similarity1
Modified residuei59SulfotyrosineSequence analysis1

Post-translational modificationi

The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.
Sulfated.1 Publication

Keywords - PTMi

Phosphoprotein, Sulfation

Proteomic databases

PeptideAtlasiP56729.
PRIDEiP56729.

Interactioni

Subunit structurei

The resulting sucrase and isomaltase subunits stay associated with one another in a complex by non-covalent linkages.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Sequencei

Sequence statusi: Fragments.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56729-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKKFSGLE IXLIVLFAIV LSIAIALVVV XASKXPAVIK LPSDPIPTLR
60
MEMTYHTDYM LE
Length:62
Mass (Da):6,893
Last modified:January 23, 2007 - v2
Checksum:i7D4E3C6AFC5AFB8B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence uncertaintyi331
Sequence uncertaintyi341
Non-adjacent residuesi38 – 39Curated2
Sequence uncertaintyi51M or V1
Sequence uncertaintyi53M or V1
Sequence uncertaintyi54T or K1
Sequence uncertaintyi57T or K1
Sequence uncertaintyi60M or V1
Non-terminal residuei621

Sequence databases

PIRiA25987.

Cross-referencesi

Sequence databases

PIRiA25987.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PeptideAtlasiP56729.
PRIDEiP56729.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiSUIS_PIG
AccessioniPrimary (citable) accession number: P56729
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.