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Q3USW5 (FXRD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FAD-dependent oxidoreductase domain-containing protein 2
Gene names
Name:Foxred2
Synonyms:D15Bwg0759e
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probable flavoprotein which may function in endoplasmic reticulum associated degradation (ERAD). May bind non-native proteins in the endoplasmic reticulum and target them to the ubiquitination machinery for subsequent degradation By similarity.

Cofactor

FAD By similarity.

Subunit structure

Interacts with SEL1L. May interact with OS9 and DNAJC10 By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the FOXRED2 family.

Sequence caution

The sequence BAE42033.1 differs from that shown. Reason: Frameshift at position 535.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentendoplasmic reticulum lumen

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionflavin adenine dinucleotide binding

Inferred from sequence or structural similarity. Source: UniProtKB

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 665648FAD-dependent oxidoreductase domain-containing protein 2
PRO_0000337693

Regions

Motif662 – 6654Prevents secretion from ER Potential

Amino acid modifications

Glycosylation1361N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2981N → S in BAE42033. Ref.1
Sequence conflict3291L → P in AAH86662. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q3USW5 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 077E8266EB031C24

FASTA66576,004
        10         20         30         40         50         60 
MGPSGLLVAL ALHLAVCSRP HRDYCVLGAG PAGLQMAAFL HRAGRDYEVF ERESAPGSFF 

        70         80         90        100        110        120 
TRYPRHRKLI SINKRHTGKA NAEFNLRHDW NSLLSDDPHL LFRHYSQAYF PDASDMVRYL 

       130        140        150        160        170        180 
GDFARRLGLH VLYNTNITHV TLDKDPQAWN GHYFILTDQK GQVYQCSVLL VATGLAVPKL 

       190        200        210        220        230        240 
VDFPGSEYVE GYESVSVDPE DFVGQNVLIL GHGNSAFETA ENILGVTNFV HMLSRSRVRL 

       250        260        270        280        290        300 
SWATHYVGDV RAINNGLLDT YQLKSLDGLL ESDLEYLALV KDSKGKFHVT LKFLLENNSS 

       310        320        330        340        350        360 
QSADSIPLPE DDNDNFAMRV AYDRVIRCLG WTFDFSIFDQ SLRLSSGTEF SKKYPLIKAS 

       370        380        390        400        410        420 
YESKGSRGLF ILGTASHSVD YRKSAGGFIH GFRYTVRAVH RLLEHRHHGI PWPSTEYPIT 

       430        440        450        460        470        480 
QLTSSIIRRV NEASGLYQMF SVLADIILLK ENATAFEYLE EFPMQMLAQL EMLTGRTARH 

       490        500        510        520        530        540 
GLFVINMEYG KNFSGPEKDV FYYDRSVAHI EDAWMSNFLH PVIYYYRHLP TEQDMRFRPA 

       550        560        570        580        590        600 
QWPLPRPTAI HHIVEDFLTD WTAPVGHILP LRRFLENCLD TDLRSFYAES CFLFTLTRQR 

       610        620        630        640        650        660 
LPPFCQQGYL RMQGLSSTKS LWQHGVESRL LQDYTAMENS NRWLGDHSTA PEPLTQSLDS 


NKEEL

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Corpora quadrigemina.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK140027 mRNA. Translation: BAE24215.1.
AK170795 mRNA. Translation: BAE42033.1. Frameshift.
AL589650 Genomic DNA. Translation: CAP19080.1.
BC086662 mRNA. Translation: AAH86662.1.
IPIIPI00132825.
RefSeqNP_001017983.2. NM_001017983.2.
NP_001161732.1. NM_001168260.1.
UniGeneMm.295605.

3D structure databases

ProteinModelPortalQ3USW5.
SMRQ3USW5. Positions 22-238.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000016696.

PTM databases

PhosphoSiteQ3USW5.

Proteomic databases

PRIDEQ3USW5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016696; ENSMUSP00000016696; ENSMUSG00000016552.
ENSMUST00000117725; ENSMUSP00000113403; ENSMUSG00000016552.
GeneID239554.
KEGGmmu:239554.
UCSCuc007woj.2. mouse.

Organism-specific databases

CTD80020.
MGIMGI:106315. Foxred2.

Phylogenomic databases

eggNOGNOG303889.
GeneTreeENSGT00640000091519.
HOGENOMHOG000031485.
HOVERGENHBG100868.
InParanoidQ3USW5.
OMAQAWNGHY.
OrthoDBEOG4NKBV6.

Gene expression databases

ArrayExpressQ3USW5.
BgeeQ3USW5.
GenevestigatorQ3USW5.

Family and domain databases

PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio384169.
SOURCESearch...

Entry information

Entry nameFXRD2_MOUSE
AccessionPrimary (citable) accession number: Q3USW5
Secondary accession number(s): Q3TCC4, Q5RJH0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 11, 2005
Last modified: May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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