Q8IWF2 (FXRD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FAD-dependent oxidoreductase domain-containing protein 2

Alternative name(s):
Endoplasmic reticulum flavoprotein associated with degradation

Gene names

Name:	FOXRED2
Synonyms:	ERFAD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	684 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. Ref.7
Cofactor	FAD.
Subunit structure	Interacts with SEL1L. May interact with OS9 and DNAJC10. Ref.7
Subcellular location	Endoplasmic reticulum lumen Ref.7.
Post-translational modification	N-glycosylated. Ref.7
Sequence similarities	Belongs to the FOXRED2 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype Ref.7. Source: UniProtKB
Cellular_component	endoplasmic reticulum lumen Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	flavin adenine dinucleotide binding Inferred from direct assay Ref.7. Source: UniProtKB oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8IWF2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8IWF2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-327: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Potential
	Chain	27 – 684	658	FAD-dependent oxidoreductase domain-containing protein 2		PRO_0000337692
Regions
	Motif	681 – 684	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	143	1	N-linked (GlcNAc...) Ref.6
Natural variations
	Alternative sequence	1 – 327	327	Missing in isoform 2.		VSP_033997
	Natural variant	71	1	R → C. Corresponds to variant rs56767103 [ dbSNP | Ensembl ].		VAR_062247
	Natural variant	179	1	F → L. Ref.1 Ref.5 Corresponds to variant rs760718 [ dbSNP | Ensembl ].		VAR_043704
	Natural variant	308	1	N → S. Ref.1 Ref.4 Ref.5 Corresponds to variant rs2277841 [ dbSNP | Ensembl ].		VAR_043705
	Natural variant	374	1	K → R. Corresponds to variant rs35813894 [ dbSNP | Ensembl ].		VAR_043706
	Natural variant	637	1	E → D. Corresponds to variant rs35748020 [ dbSNP | Ensembl ].		VAR_043707
Experimental info
	Sequence conflict	345	1	F → S in BAB15610. Ref.2
	Sequence conflict	607	1	T → A in BAB15227. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 8209FFAF6289DDAF	FASTA	684	77,791
	10 20 30 40 50 60 MGLSAAAPLW GPPGLLLAIA LHPALSVPPR RDYCVLGAGP AGLQMAYFLQ RAGRDYAVFE 70 80 90 100 110 120 RAPRPGSFFT RYPRHRKLIS INKRYTGKAN AEFNLRHDWN SLLSHDPRLL FRHYSRAYFP 130 140 150 160 170 180 DARDMVRYLG DFADTLGLRV QYNTTIAHVT LDKDRQAWNG HYFILTDQKG QVHQCSVLFV 190 200 210 220 230 240 ATGLSVPNQV DFPGSEYAEG YESVSVDPED FVGQNVLILG RGNSAFETAE NILGVTNFIH 250 260 270 280 290 300 MLSRSRVRLS WATHYVGDLR AINNGLLDTY QLKSLDGLLE SDLTDLAILK DSKGKFHVTP 310 320 330 340 350 360 KFFLEEANTN QSADSITLPQ DDNDNFAMRV PYDRVIRCLG WNFDFSIFNK SLRLNSGNAF 370 380 390 400 410 420 GKKYPLIRAS YESKGSRGLF ILGTASHSVD YRKSAGGFIH GFRYTVRAVH RLLEHRHHSV 430 440 450 460 470 480 TWPATELPIT QLTSSIVRRV NEASGLYQMF GVLADVILLK ENSTAFEYLE EFPIQMLAQL 490 500 510 520 530 540 ETLTGRKAKH GLFVINMEYG RNFSGPDKDV FFDDRSVGHT EDAWQSNFLH PVIYYYRYLP 550 560 570 580 590 600 TEQEVRFRPA HWPLPRPTAI HHIVEDFLTD WTAPIGHILP LRRFLENCLD TDLRSFYAES 610 620 630 640 650 660 CFLFALTRQK LPPFCQQGYL RMQGLVSTES LWQHRVESRL LRDYAPTGRR LEDSSQQLGD 670 680 QEPLGSPLAP GPLAQSVDSN KEEL
	Isoform 2 [UniParc]. Checksum: 14C82B1E14D54A0A	FASTA	357	41,157
	10 20 30 40 50 60 MRVPYDRVIR CLGWNFDFSI FNKSLRLNSG NAFGKKYPLI RASYESKGSR GLFILGTASH 70 80 90 100 110 120 SVDYRKSAGG FIHGFRYTVR AVHRLLEHRH HSVTWPATEL PITQLTSSIV RRVNEASGLY 130 140 150 160 170 180 QMFGVLADVI LLKENSTAFE YLEEFPIQML AQLETLTGRK AKHGLFVINM EYGRNFSGPD 190 200 210 220 230 240 KDVFFDDRSV GHTEDAWQSN FLHPVIYYYR YLPTEQEVRF RPAHWPLPRP TAIHHIVEDF 250 260 270 280 290 300 LTDWTAPIGH ILPLRRFLEN CLDTDLRSFY AESCFLFALT RQKLPPFCQQ GYLRMQGLVS 310 320 330 340 350 TESLWQHRVE SRLLRDYAPT GRRLEDSSQQ LGDQEPLGSP LAPGPLAQSV DSNKEEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS LEU-179 AND SER-308.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Placenta.
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-308.
[5]	"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] (ISOFORM 1), VARIANTS LEU-179 AND SER-308. Tissue: Brain, Colon and Eye.
[6]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-143, MASS SPECTROMETRY. Tissue: Liver.
[7]	"A luminal flavoprotein in endoplasmic reticulum-associated degradation." Riemer J., Appenzeller-Herzog C., Johansson L., Bodenmiller B., Hartmann-Petersen R., Ellgaard L. Proc. Natl. Acad. Sci. U.S.A. 106:14831-14836(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, FAD-BINDING, GLYCOSYLATION, SUBCELLULAR LOCATION, INTERACTION WITH DNAJC10; OS9 AND SEL1L.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR456444 mRNA. Translation: CAG30330.1. AK025714 mRNA. Translation: BAB15227.1. AK026975 mRNA. Translation: BAB15610.1. AK315555 mRNA. Translation: BAG37931.1. AL022313 Genomic DNA. Translation: CAI19228.1. CH471095 Genomic DNA. Translation: EAW60106.1. BC015726 mRNA. Translation: AAH15726.1. BC027716 mRNA. Translation: AAH27716.1. BC040351 mRNA. Translation: AAH40351.1.
IPI	IPI00647558. IPI00893305.
RefSeq	NP_001095841.1. NM_001102371.1. NP_079231.4. NM_024955.5.
UniGene	Hs.387601.
3D structure databases
ProteinModelPortal	Q8IWF2.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48946N.
STRING	9606.ENSP00000216187.
PTM databases
PhosphoSite	Q8IWF2.
Polymorphism databases
DMDM	74759632.
Proteomic databases
PaxDb	Q8IWF2.
PRIDE	Q8IWF2.
Protocols and materials databases
DNASU	80020.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000216187; ENSP00000216187; ENSG00000100350. ENST00000397223; ENSP00000380400; ENSG00000100350. ENST00000397224; ENSP00000380401; ENSG00000100350.
GeneID	80020.
KEGG	hsa:80020.
UCSC	uc003apn.4. human.
Organism-specific databases
CTD	80020.
GeneCards	GC22M036883.
H-InvDB	HIX0203159.
HGNC	HGNC:26264. FOXRED2.
HPA	HPA031611. HPA031612.
MIM	613777. gene.
neXtProt	NX_Q8IWF2.
PharmGKB	PA145148808.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG303889.
HOGENOM	HOG000031485.
HOVERGEN	HBG100868.
InParanoid	Q8IWF2.
OMA	QAWNGHY.
OrthoDB	EOG4NKBV6.
PhylomeDB	Q8IWF2.
Gene expression databases
ArrayExpress	Q8IWF2.
Bgee	Q8IWF2.
CleanEx	HS_FOXRED2.
Genevestigator	Q8IWF2.
Family and domain databases
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	80020.
NextBio	70142.
SOURCE	Search...

Entry information

Entry name

FXRD2_HUMAN

Accession

Primary (citable) accession number: Q8IWF2
Secondary accession number(s): B2RDI4 , Q8N378, Q96BD1, Q9H5L5, Q9H6M8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.