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UniProtKB/Swiss-Prot entry P92947


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MDARP_ARATH
Primary accession number P92947
Secondary accession numbers Q94CE2 Q9CAK5
Integrated into Swiss-Prot on July 19, 2004
Sequence was last modified on July 19, 2004 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 57)
Name and origin of the protein
Protein name Monodehydroascorbate reductase, chloroplastic [Precursor]
Synonyms MDAR
EC 1.6.5.4
Gene name
OrderedLocusNames: At1g63940
ORFNames: T12P18.4
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Hossain A., Miyake C., Aoki H., Matsuo M., Yamaguchi T., Nishimura M., Ida S., Asada K.;
"cDNA of chloroplastic monodehydroascorbate radical reductase from Arabidopsis thaliana.";
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D84417; BAA12349.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC010852; AAG52455.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY034934; AAK59441.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY142572; AAN13141.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000667; AAN31814.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E96664; E96664.
RefSeq NP_849839.1; -.
UniGene At.24374
3D structure databases
HSSP O95831; 1M6I. [HSSP ENTRY / PDB]
ModBase P92947.
Organism-specific databases
TAIR At1g63940; -.
Gene expression databases
ArrayExpress P92947; -.
Ontologies
GO
GO:0016656; Molecular function: monodehydroascorbate reductase (NADH) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS P92947.
Genome annotation databases
GeneID 842697; -.
GenomeReviews CT485782_GR; AT1G63940.
Other
ProtoNet P92947.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Chloroplast; Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase; Plastid; Redox-active center; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    53  53     Chloroplast (Potential). 
CHAIN   54   493  440     Monodehydroascorbate reductase, chloroplastic. PRO_0000018621
VAR_SEQ   1     7        Missing (in isoform 2). VSP_011360
CONFLICT   109   109        Y -> H (in Ref. 1; BAA12349). 
Sequence information
Length: 493 AA [This is the length of the unprocessed precursor] Molecular weight: 53302 Da [This is the MW of the unprocessed precursor] CRC64: 44FBF0DE65DA89D7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAVRRVMAL ASTTLPTKSG LSLWCPSSPS LARRFPARFS PIGSRIASRS LVTASFANEN 

        70         80         90        100        110        120 
REFVIVGGGN AAGYAARTFV ENGMADGRLC IVTKEAYAPY ERPALTKAYL FPPEKKPARL 

       130        140        150        160        170        180 
PGFHTCVGGG GERQTPDWYK EKGIEVIYED PVAGADFEKQ TLTTDAGKQL KYGSLIIATG 

       190        200        210        220        230        240 
CTASRFPDKI GGHLPGVHYI REVADADSLI ASLGKAKKIV IVGGGYIGME VAAAAVAWNL 

       250        260        270        280        290        300 
DTTIVFPEDQ LLQRLFTPSL AQKYEELYRQ NGVKFVKGAS INNLEAGSDG RVSAVKLADG 

       310        320        330        340        350        360 
STIEADTVVI GIGAKPAIGP FETLAMNKSI GGIQVDGLFR TSTPGIFAIG DVAAFPLKIY 

       370        380        390        400        410        420 
DRMTRVEHVD HARRSAQHCV KSLLTAHTDT YDYLPYFYSR VFEYEGSPRK VWWQFFGDNV 

       430        440        450        460        470        480 
GETVEVGNFD PKIATFWIES GRLKGVLVES GSPEEFQLLP KLARSQPLVD KAKLASASSV 

       490 
EEALEIAQAA LQS 

P92947 in FASTA format

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