Version 5.4
Mus musculus Protein: Slc26a5
Summary
InnateDB Protein IDBP-250197.5
Last Modified 2012-02-14 [Report errors or provide feedback]
Gene Symbol Slc26a5
Protein Name solute carrier family 26, member 5
Synonyms Pres; prestin;
Species Mus musculus
Ensembl Protein ENSMUSP00000110830
InnateDB Gene IDBG-138604 (Slc26a5)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0008271 secondary active sulfate transmembrane transporter activity
GO:0015116 sulfate transmembrane transporter activity
GO:0030507 spectrin binding
Biological Process
GO:0008272 sulfate transport
GO:0042391 regulation of membrane potential
GO:0055085 transmembrane transport
GO:1902358 sulfate transmembrane transport
Cellular Component
GO:0016020 membrane
GO:0016021 integral component of membrane
GO:0016323 basolateral plasma membrane
GO:0016328 lateral plasma membrane
Protein Structure and Domains
PDB ID MGI:1933154
InterPro IPR001902 Sulphate anion transporter
IPR002645 STAS domain
IPR011547 Sulphate transporter
PFAM PF01740
PF13466
PF00916
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL Q32MT7
UniProt Splice Variant
Entrez Gene 80979
UniGene Mm.160370
RefSeq NP_001276717
MGI ID
MGI Symbol Slc26a5
OMIM
CCDS CCDS71547
HPRD
IMGT
EMBL AC113028 AC125313 BC108986 BC108987
GenPept AAI08987 AAI08988

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca