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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.

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1211Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei13 – 3220Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini33 – ›38›6Lumenal Reviewed prediction

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB-SubCell
  2. integral component of 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›37Isomaltase
PRO_0000018554Add
BLAST
Chaini39 – ›62›24Sucrase
PRO_0000018555Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine; by PKA By similarity
Modified residuei59 – 591Sulfotyrosine Reviewed prediction

Post-translational modificationi

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

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.

Family & Domainsi

Sequence similaritiesi

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

Sequence uncertainty

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence uncertaintyi33 – 331
Sequence uncertaintyi34 – 341
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-adjacent residues

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi38 – 392

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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: February 19, 2014
This is version 61 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