Version 5.4
Mus musculus Protein: Slc38a5
Summary
InnateDB Protein IDBP-249293.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Slc38a5
Protein Name solute carrier family 38, member 5
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000111253
InnateDB Gene IDBG-130505 (Slc38a5)
Protein Structure
UniProt Annotation
Function Functions as a sodium-dependent amino acid transporter which countertransport protons. Mediates the saturable, pH- sensitive, and electrogenic cotransport of several neutral amino acids including glycine, asparagine, alanine, serine, glutamine and histidine with sodium (By similarity). {ECO:0000250}.
Subcellular Localization Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
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.
They are also associated with 2 interaction(s) predicted by orthology.
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0015187 glycine transmembrane transporter activity
Biological Process
GO:0003333 amino acid transmembrane transport
GO:0015816 glycine transport
Cellular Component
GO:0005886 plasma membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:2148066
InterPro IPR013057 Amino acid transporter, transmembrane
PFAM PF01490
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3U1J0
PhosphoSite PhosphoSite-Q3U1J0
TrEMBL A2ALH6
UniProt Splice Variant
Entrez Gene 209837
UniGene Mm.6055
RefSeq
MGI ID
MGI Symbol Slc38a5
OMIM
CCDS
HPRD
IMGT
EMBL AK054485 AK077667 AK155928 AK158125 AL805902 BC152401
GenPept AAI52402 BAC35799 BAC36941 BAE33507 BAE34371 CAM17938 CAM17940

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