Version 5.4
Mus musculus Protein: Rft1
Summary
InnateDB Protein IDBP-142977.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Rft1
Protein Name RFT1 homolog (S. cerevisiae)
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000064153
InnateDB Gene IDBG-142975 (Rft1)
Protein Structure
UniProt Annotation
Function May be involved in N-linked oligosaccharide assembly. May participate in the translocation of oligosaccharide from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane (By similarity). {ECO:0000250}.
Subcellular Localization Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
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:0003674 molecular_function
GO:0005319 lipid transporter activity
Biological Process
GO:0006869 lipid transport
GO:0008643 carbohydrate transport
Cellular Component
GO:0005575 cellular_component
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:3607791
InterPro IPR007594 RFT1
PFAM PF04506
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8C3B8
PhosphoSite PhosphoSite-Q8C3B8
TrEMBL
UniProt Splice Variant
Entrez Gene 328370
UniGene Mm.259657
RefSeq NP_808483
MGI ID
MGI Symbol Rft1
OMIM
CCDS CCDS26896
HPRD
IMGT
EMBL AC154436 AC154646 AK086390 BC116368 BC116369 BC141275
GenPept AAI16369 AAI16370 AAI41276 BAC39658

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