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UniProtKB/Swiss-Prot entry P11035


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

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Entry information
Entry name NIA2_ARATH
Primary accession number P11035
Secondary accession number Q7Y260
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 96)
Name and origin of the protein
Protein name Nitrate reductase [NADH] 2
Synonyms NR2
EC 1.7.1.1
Gene name
Name: NIA2
Synonyms: CHL3
OrderedLocusNames: At1g37130
ORFNames: F28L22.2
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=3393528 [NCBI, ExPASy, EBI, Israel, Japan]
Crawford N.M., Smith M., Bellissimo D.B., Davis R.W.;
"Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding nitrate reductase, a metalloflavoprotein with three functional domains.";
Proc. Natl. Acad. Sci. U.S.A. 85:5006-5010(1988).
[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].
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 350-422.
DOI=10.1105/tpc.3.5.461; PubMed=1840922 [NCBI, ExPASy, EBI, Israel, Japan]
Wilkinson J.Q., Crawford N.M.;
"Identification of the Arabidopsis CHL3 gene as the nitrate reductase structural gene NIA2.";
Plant Cell 3:461-471(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 522-917.
PubMed=2905260 [NCBI, ExPASy, EBI, Israel, Japan]
Cheng C., Dewdney J., Nam H., den Boer B.G.W., Goodman H.M.;
"A new locus (NIA 1) in Arabidopsis thaliana encoding nitrate reductase.";
EMBO J. 7:3309-3314(1988).
[6]
HERBICIDE RESISTANCE.
PubMed=8510658 [NCBI, ExPASy, EBI, Israel, Japan]
Wilkinson J.Q., Crawford N.M.;
"Identification and characterization of a chlorate-resistant mutant of Arabidopsis thaliana with mutations in both nitrate reductase structural genes NIA1 and NIA2.";
Mol. Gen. Genet. 239:289-297(1993).
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
J03240; AAA32830.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007505; AAF19225.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF367272; AAK56261.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF436835; AAL32017.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY037183; AAK59768.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY039914; AAK64018.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY133530; AAM91360.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY142568; AAN13137.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S45385; AAL32273.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13435; CAA31787.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A31821; RDMUNH.
RefSeq NP_174901.1; -.
UniGene At.23731
3D structure databases
HSSP P17571; 2CND. [HSSP ENTRY / PDB]
ModBase P11035.
Organism-specific databases
TAIR At1g37130; -.
Gene expression databases
GermOnline AT1G37130; Arabidopsis thaliana.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from TAIR).
GO:0005773; Cellular component: vacuole (inferred from direct assay from TAIR).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0030151; Molecular function: molybdenum ion binding (inferred from electronic annotation from InterPro).
GO:0009703; Molecular function: nitrate reductase (NADH) activity (inferred from electronic annotation from EC).
GO:0042128; Biological process: nitrate assimilation (inferred from electronic annotation from InterPro).
GO:0006809; Biological process: nitric oxide biosynthetic process (inferred from mutant phenotype from TAIR).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009635; Biological process: response to herbicide (inferred from electronic annotation from UniProtKB-KW).
GO:0009416; Biological process: response to light stimulus (inferred from mutant phenotype from TAIR).
GO:0009610; Biological process: response to symbiotic fungus (inferred from expression pattern from TAIR).
QuickGo view.
Family and domain databases
InterPro IPR001199; Cyt_B5.
IPR001834; Cyt_B5_reductase.
IPR001709; FPN_cyt_redctse.
IPR005066; MoCF_OxRdtse_dimer.
IPR008335; Mopterin_OxRdtase_euk.
IPR012137; Nitr_rd_NADH.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR000572; OxRdtase_Mopterin-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.10.120.10; Cyt_B5; 1.
G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
G3DSA:3.90.420.10; Oxred_molyb_bd; 1.
Pfam PF00173; Cyt-b5; 1.
PF00970; FAD_binding_6; 1.
PF03404; Mo-co_dimer; 1.
PF00175; NAD_binding_1; 1.
PF00174; Oxidored_molyb; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000233; Nitr_rd_NADH; 1.
PRINTS PR00406; CYTB5RDTASE.
PR00363; CYTOCHROMEB5.
PR00407; EUMOPTERIN.
PR00371; FPNCR.
ProDom PD000612; Cyt_B5; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00191; CYTOCHROME_B5_1; 1.
PS50255; CYTOCHROME_B5_2; 1.
PS51384; FAD_FR; 1.
PS00559; MOLYBDOPTERIN_EUK; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE P11035; -.
Proteomic databases
ProMEX P11035; -.
Genome annotation databases
GeneID 840630; -.
GenomeReviews CT485782_GR; AT1G37130.
KEGG ath:AT1G37130; -.
Other
ProtoNet P11035.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; Heme; Herbicide resistance; Iron; Metal-binding; Molybdenum; NAD; Nitrate assimilation; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   917  917     Nitrate reductase [NADH] 2. PRO_0000166050
DOMAIN   542   617  76     Cytochrome b5 heme-binding. 
DOMAIN   660   772  113     FAD-binding FR-type. 
METAL   191   191        Molybdenum-pterin (Potential). 
METAL   245   245        Molybdenum-pterin (Potential). 
METAL   577   577        Iron (heme axial ligand) (By similarity). 
METAL   600   600        Iron (heme axial ligand) (By similarity). 
DISULFID   433   433        Interchain (Potential). 
Sequence information
Length: 917 AA [This is the length of the unprocessed precursor] Molecular weight: 102844 Da [This is the MW of the unprocessed precursor] CRC64: B8909A318C04C39A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAASVDNRQY ARLEPGLNGV VRSYKPPVPG RSDSPKAHQN QTTNQTVFLK PAKVHDDDED 

        70         80         90        100        110        120 
VSSEDENETH NSNAVYYKEM IRKSNAELEP SVLDPRDEYT ADSWIERNPS MVRLTGKHPF 

       130        140        150        160        170        180 
NSEAPLNRLM HHGFITPVPL HYVRNHGHVP KAQWAEWTVE VTGFVKRPMK FTMDQLVSEF 

       190        200        210        220        230        240 
AYREFAATLV CAGNRRKEQN MVKKSKGFNW GSAGVSTSVW RGVPLCDVLR RCGIFSRKGG 

       250        260        270        280        290        300 
ALNVCFEGSE DLPGGAGTAG SKYGTSIKKE YAMDPSRDII LAYMQNGEYL TPDHGFPVRI 

       310        320        330        340        350        360 
IIPGFIGGRM VKWLKRIIVT TKESDNFYHF KDNRVLPSLV DAELADEEGW WYKPEYIINE 

       370        380        390        400        410        420 
LNINSVITTP CHEEILPINA FTTQRPYTLK GYAYSGGGKK VTRVEVTVDG GETWNVCALD 

       430        440        450        460        470        480 
HQEKPNKYGK FWCWCFWSLE VEVLDLLSAK EIAVRAWDET LNTQPEKMIW NLMGMMNNCW 

       490        500        510        520        530        540 
FRVKTNVCKP HKGEIGIVFE HPTLPGNESG GWMAKERHLE KSADAPPSLK KSVSTPFMNT 

       550        560        570        580        590        600 
TAKMYSMSEV KKHNSADSCW IIVHGHIYDC TRFLMDHPGG SDSILINAGT DCTEEFEAIH 

       610        620        630        640        650        660 
SDKAKKMLED YRIGELITTG YSSDSSSPNN SVHGSSAVFS LLAPIGEATP VRNLALVNPR 

       670        680        690        700        710        720 
AKVPVQLVEK TSISHDVRKF RFALPVEDMV LGLPVGKHIF LCATINDKLC LRAYTPSSTV 

       730        740        750        760        770        780 
DVVGYFELVV KIYFGGVHPR FPNGGLMSQY LDSLPIGSTL EIKGPLGHVE YLGKGSFTVH 

       790        800        810        820        830        840 
GKPKFADKLA MLAGGTGITP VYQIIQAILK DPEDETEMYV IYANRTEEDI LLREELDGWA 

       850        860        870        880        890        900 
EQYPDRLKVW YVVESAKEGW AYSTGFISEA IMREHIPDGL DGSALAMACG PPPMIQFAVQ 

       910 
PNLEKMQYNI KEDFLIF 

P11035 in FASTA format

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