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P56729

- SUIS_PIG

UniProt

P56729 - SUIS_PIG

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Protein

Sucrase-isomaltase, intestinal

Gene

SI

Organism
Sus scrofa (Pig)
Status
Reviewed - 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

  1. oligo-1,6-glucosidase activity Source: UniProtKB-EC
  2. sucrose alpha-glucosidase activity Source: UniProtKB-EC
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
ProteomesiUP000008227: Unplaced

Subcellular locationi

Apical cell membrane By similarity; Single-pass type II membrane protein By similarity
Note: Brush border.By similarity

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – ›38›37IsomaltasePRO_0000018554Add
BLAST
Chaini39 – ›62›24SucrasePRO_0000018555Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine; by PKABy similarity
Modified residuei59 – 591SulfotyrosineSequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Sulfation

Interactioni

Subunit structurei

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

Structurei

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1211CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini33 – ›38›6LumenalSequence Analysis

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei13 – 3220Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

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

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        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence uncertaintyi33 – 331
Sequence uncertaintyi34 – 341
Non-adjacent residuesi38 – 392Curated
Sequence uncertaintyi51 – 511M or V
Sequence uncertaintyi53 – 531M or V
Sequence uncertaintyi54 – 541T or K
Sequence uncertaintyi57 – 571T or K
Sequence uncertaintyi60 – 601M or V
Non-terminal residuei62 – 621

Sequence databases

PIRiA25987.

Cross-referencesi

Sequence databases

PIRi A25987.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

Publicationsi

  1. "N-terminal sequences of pig intestinal sucrase-isomaltase and pro-sucrase-isomaltase. Implications for the biosynthesis and membrane insertion of pro-sucrase-isomaltase."
    Sjoestroem H., Noren O., Christiansen L.A., Wacker H., Spiess M., Bigler-Meier B., Rickli E.E., Semenza G.
    FEBS Lett. 148:321-325(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-62.
  2. "Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte."
    Danielsen E.M.
    EMBO J. 6:2891-2896(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: SULFATION.

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 29, 2014
This is version 63 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

External Data

Dasty 3