Reviewed, UniProtKB/Swiss-Prot Q93WJ8 (MDAR4_ARATH)

Names and origin

Protein names

Recommended name:
    Probable monodehydroascorbate reductase, cytoplasmic isoform 4
      Short name=MDAR 4
    EC=1.6.5.4

Gene names

Ordered Locus Names:	At5g03630
ORF Names:	F17C15_50

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	435 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process By similarity.
Catalytic activity	NADH + 2 monodehydroascorbate = NAD+ + 2 ascorbate.
Cofactor	FAD By similarity.
Subcellular location	Cytoplasm Potential.
Sequence similarities	Belongs to the FAD-dependent oxidoreductase family.
Sequence caution	The sequence CAB82928.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Inferred from expression pattern. Source: TAIR response to salt stress Inferred from expression pattern. Source: TAIR
Cellular component	cytosol Inferred from direct assay. Source: TAIR
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro monodehydroascorbate reductase (NADH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 435	435	Probable monodehydroascorbate reductase, cytoplasmic isoform 4		PRO_0000209139
Amino acid modifications
	Modified residue	417	1	Phosphoserine Ref.4
Experimental info
	Sequence conflict	390	1	R → G in AAM64868. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q93WJ8-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 1724F290D1EC43F7	FASTA	435	47,480
	10 20 30 40 50 60 MAEEKSFKYV IVGGGVAAGY AAREFFNQGV KPGELAIISR EQVPPYERPA LSKGYIHLEN 70 80 90 100 110 120 KATLPNFYVA AGIGGERQFP QWYKEKGIEL ILGTEIVKAD LAAKTLVSGT GQVFKYQTLL 130 140 150 160 170 180 AATGSSVIRL SDFGVPGADA KNIFYLRELE DADYLAYAME TKEKGKAVVV GGGYIGLELG 190 200 210 220 230 240 AALKANNLDV TMVYPEPWCM PRLFTAGIAS FYEGYYANKG INIVKGTVAS GFTTNSNGEV 250 260 270 280 290 300 TEVKLKDGRT LEADIVIVGV GGRPIISLFK DQVEEEKGGL KTDGFFKTSL PDVYAIGDVA 310 320 330 340 350 360 TFPMKLYNEM RRVEHVDHAR KSAEQAVKAI KAAEEGNSIP EYDYLPYFYS RAFDLSWQFY 370 380 390 400 410 420 GDNVGESVLF GDNDPESPKP KFGSYWIKER KVVGAFLEGG SPEENNAIAK LARAQPSVES 430 LEVLSKEGLS FATNI

References

[1]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, MASS SPECTROMETRY. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL162506 Genomic DNA. Translation: CAB82928.1. Sequence problems. AF428317 mRNA. Translation: AAL16247.1. AY057628 mRNA. Translation: AAL15259.1. AY142000 mRNA. Translation: AAM98264.1. AY087318 mRNA. Translation: AAM64868.1.
IPI	IPI00529861.
PIR	T48390.
RefSeq	NP_568125.1.
UniGene	At.4763
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q93WJ8.
Proteomic databases
PRIDE	Q93WJ8.
Genome annotation databases
GeneID	831774.
GenomeReviews	Gene locus AT5G03630 in contig BA000015_GR.
KEGG	ath:AT5G03630.
NMPDR	fig|3702.1.peg.22451.
Organism-specific databases
TAIR	At5g03630.
Phylogenomic databases
OMA	VTMVYPE.
Enzyme and pathway databases
BRENDA	1.6.5.4. 302.
Gene expression databases
ArrayExpress	Q93WJ8.
Genevestigator	Q93WJ8.
GermOnline	AT5G03630. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

MDAR4_ARATH

Accession

Primary (citable) accession number: Q93WJ8
Secondary accession number(s): Q8LBB1, Q9LZS5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)