Version 5.4
Mus musculus Protein: AI317395
Summary
InnateDB Protein IDBP-621974.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol AI317395
Protein Name expressed sequence AI317395
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000128324
InnateDB Gene IDBG-145115 (AI317395)
Protein Structure
UniProt Annotation
Function May function as a sodium-dependent glucose transporter. {ECO:0000250}.
Subcellular Localization Apical 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.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0015293 symporter activity
Biological Process
GO:0006814 sodium ion transport
GO:0008150 biological_process
GO:0008643 carbohydrate transport
GO:0055085 transmembrane transport
Cellular Component
GO:0005575 cellular_component
GO:0016021 integral component of membrane
GO:0016324 apical plasma membrane
Protein Structure and Domains
PDB ID MGI:2143575
InterPro IPR011701 Major facilitator superfamily
IPR016196 Major facilitator superfamily domain, general substrate transporter
PFAM PF07690
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8VCV9
PhosphoSite PhosphoSite-Q8VCV9
TrEMBL
UniProt Splice Variant
Entrez Gene 215929
UniGene Mm.55513
RefSeq NP_659070
MGI ID
MGI Symbol AI317395
OMIM
CCDS CCDS35884
HPRD
IMGT
EMBL AK089961 BC018406
GenPept AAH18406 BAC41015

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