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Protein

FAD-dependent oxidoreductase domain-containing protein 2

Gene

Foxred2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Cofactori

FADBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: UniProtKB
  2. glycoprotein binding Source: MGI
  3. oxidoreductase activity Source: UniProtKB-KW

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
FAD-dependent oxidoreductase domain-containing protein 2
Gene namesi
Name:Foxred2
Synonyms:D15Bwg0759e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:106315. Foxred2.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 665648FAD-dependent oxidoreductase domain-containing protein 2PRO_0000337693Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ3USW5.

PTM databases

PhosphoSiteiQ3USW5.

Expressioni

Gene expression databases

BgeeiQ3USW5.
ExpressionAtlasiQ3USW5. baseline and differential.
GenevestigatoriQ3USW5.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000016696.

Structurei

3D structure databases

ProteinModelPortaliQ3USW5.
SMRiQ3USW5. Positions 23-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi662 – 6654Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the FOXRED2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG303889.
GeneTreeiENSGT00640000091519.
HOGENOMiHOG000031485.
HOVERGENiHBG100868.
InParanoidiQ3USW5.
OMAiQAWNGHY.
OrthoDBiEOG7M6D70.
PhylomeDBiQ3USW5.
TreeFamiTF324712.

Family and domain databases

PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3USW5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPSGLLVAL ALHLAVCSRP HRDYCVLGAG PAGLQMAAFL HRAGRDYEVF
60 70 80 90 100
ERESAPGSFF TRYPRHRKLI SINKRHTGKA NAEFNLRHDW NSLLSDDPHL
110 120 130 140 150
LFRHYSQAYF PDASDMVRYL GDFARRLGLH VLYNTNITHV TLDKDPQAWN
160 170 180 190 200
GHYFILTDQK GQVYQCSVLL VATGLAVPKL VDFPGSEYVE GYESVSVDPE
210 220 230 240 250
DFVGQNVLIL GHGNSAFETA ENILGVTNFV HMLSRSRVRL SWATHYVGDV
260 270 280 290 300
RAINNGLLDT YQLKSLDGLL ESDLEYLALV KDSKGKFHVT LKFLLENNSS
310 320 330 340 350
QSADSIPLPE DDNDNFAMRV AYDRVIRCLG WTFDFSIFDQ SLRLSSGTEF
360 370 380 390 400
SKKYPLIKAS YESKGSRGLF ILGTASHSVD YRKSAGGFIH GFRYTVRAVH
410 420 430 440 450
RLLEHRHHGI PWPSTEYPIT QLTSSIIRRV NEASGLYQMF SVLADIILLK
460 470 480 490 500
ENATAFEYLE EFPMQMLAQL EMLTGRTARH GLFVINMEYG KNFSGPEKDV
510 520 530 540 550
FYYDRSVAHI EDAWMSNFLH PVIYYYRHLP TEQDMRFRPA QWPLPRPTAI
560 570 580 590 600
HHIVEDFLTD WTAPVGHILP LRRFLENCLD TDLRSFYAES CFLFTLTRQR
610 620 630 640 650
LPPFCQQGYL RMQGLSSTKS LWQHGVESRL LQDYTAMENS NRWLGDHSTA
660
PEPLTQSLDS NKEEL
Length:665
Mass (Da):76,004
Last modified:October 11, 2005 - v1
Checksum:i077E8266EB031C24
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti298 – 2981N → S in BAE42033 (PubMed:16141072).Curated
Sequence conflicti329 – 3291L → P in AAH86662 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK140027 mRNA. Translation: BAE24215.1.
AK170795 mRNA. Translation: BAE42033.1. Frameshift.
AL589650 Genomic DNA. Translation: CAP19080.1.
BC086662 mRNA. Translation: AAH86662.1.
CCDSiCCDS27607.1.
RefSeqiNP_001017983.2. NM_001017983.2.
NP_001161732.1. NM_001168260.1.
UniGeneiMm.295605.

Genome annotation databases

EnsembliENSMUST00000016696; ENSMUSP00000016696; ENSMUSG00000016552.
ENSMUST00000117725; ENSMUSP00000113403; ENSMUSG00000016552.
GeneIDi239554.
KEGGimmu:239554.
UCSCiuc007woj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK140027 mRNA. Translation: BAE24215.1.
AK170795 mRNA. Translation: BAE42033.1. Frameshift.
AL589650 Genomic DNA. Translation: CAP19080.1.
BC086662 mRNA. Translation: AAH86662.1.
CCDSiCCDS27607.1.
RefSeqiNP_001017983.2. NM_001017983.2.
NP_001161732.1. NM_001168260.1.
UniGeneiMm.295605.

3D structure databases

ProteinModelPortaliQ3USW5.
SMRiQ3USW5. Positions 23-223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000016696.

PTM databases

PhosphoSiteiQ3USW5.

Proteomic databases

PRIDEiQ3USW5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000016696; ENSMUSP00000016696; ENSMUSG00000016552.
ENSMUST00000117725; ENSMUSP00000113403; ENSMUSG00000016552.
GeneIDi239554.
KEGGimmu:239554.
UCSCiuc007woj.2. mouse.

Organism-specific databases

CTDi80020.
MGIiMGI:106315. Foxred2.

Phylogenomic databases

eggNOGiNOG303889.
GeneTreeiENSGT00640000091519.
HOGENOMiHOG000031485.
HOVERGENiHBG100868.
InParanoidiQ3USW5.
OMAiQAWNGHY.
OrthoDBiEOG7M6D70.
PhylomeDBiQ3USW5.
TreeFamiTF324712.

Miscellaneous databases

NextBioi384169.
PROiQ3USW5.
SOURCEiSearch...

Gene expression databases

BgeeiQ3USW5.
ExpressionAtlasiQ3USW5. baseline and differential.
GenevestigatoriQ3USW5.

Family and domain databases

PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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. 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.

Entry informationi

Entry nameiFXRD2_MOUSE
AccessioniPrimary (citable) accession number: Q3USW5
Secondary accession number(s): Q3TCC4, Q5RJH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 11, 2005
Last modified: February 4, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.