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P56729 (SUIS_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sucrase-isomaltase, intestinal

Cleaved into the following 2 chains:

  1. Sucrase
    EC=3.2.1.48
  2. Isomaltase
    EC=3.2.1.10
Gene names
Name:SI
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length62 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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.

Subunit structure

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

Subcellular location

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

Post-translational modification

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

Sulfated.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – ›38›37Isomaltase
PRO_0000018554
Chain39 – ›62›24Sucrase
PRO_0000018555

Regions

Topological domain2 – 1211Cytoplasmic Potential
Transmembrane13 – 3220Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – ›38›6Lumenal Potential

Amino acid modifications

Modified residue71Phosphoserine; by PKA By similarity
Modified residue591Sulfotyrosine Potential

Experimental info

Sequence uncertainty331
Sequence uncertainty341
Sequence uncertainty511M or V
Sequence uncertainty531M or V
Sequence uncertainty541T or K
Sequence uncertainty571T or K
Sequence uncertainty601M or V
Non-adjacent residues38 – 392
Non-terminal residue621

Sequences

Sequence LengthMass (Da)Tools
P56729 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7D4E3C6AFC5AFB8B

FASTA626,893
        10         20         30         40         50         60 
MARKKFSGLE IXLIVLFAIV LSIAIALVVV XASKXPAVIK LPSDPIPTLR MEMTYHTDYM 


LE 

« Hide

References

[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.

Cross-references

Sequence databases

PIRA25987.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameSUIS_PIG
AccessionPrimary (citable) accession number: P56729
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries