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P29477

- NOS2_MOUSE

UniProt

P29477 - NOS2_MOUSE

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Protein

Nitric oxide synthase, inducible

Gene

Nos2

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

Functioni

Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.1 Publication

Catalytic activityi

2 L-arginine + 3 NADPH + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O.

Cofactori

Heme group.
Binds 1 FAD.
Binds 1 FMN.
Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.

Enzyme regulationi

Not stimulated by calcium/calmodulin. Aspirin inhibits expression and function of this enzyme and effects may be exerted at the level of translational/post-translational modification and directly on the catalytic activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi104 – 1041Zinc
Metal bindingi109 – 1091Zinc
Metal bindingi194 – 1941Iron (heme axial ligand)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi617 – 64832FMNPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi761 – 77212FADBy similarityAdd
BLAST
Nucleotide bindingi897 – 90711FADBy similarityAdd
BLAST
Nucleotide bindingi972 – 99019NADPBy similarityAdd
BLAST
Nucleotide bindingi1070 – 108516NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. arginine binding Source: BHF-UCL
  2. calmodulin binding Source: UniProtKB
  3. flavin adenine dinucleotide binding Source: BHF-UCL
  4. FMN binding Source: BHF-UCL
  5. heme binding Source: BHF-UCL
  6. iron ion binding Source: InterPro
  7. NADP binding Source: InterPro
  8. NADPH-hemoprotein reductase activity Source: RefGenome
  9. nitric-oxide synthase activity Source: BHF-UCL
  10. protein homodimerization activity Source: BHF-UCL
  11. tetrahydrobiopterin binding Source: BHF-UCL

GO - Biological processi

  1. arginine catabolic process Source: BHF-UCL
  2. cellular response to interferon-gamma Source: MGI
  3. cellular response to lipopolysaccharide Source: MGI
  4. circadian rhythm Source: UniProtKB
  5. defense response to bacterium Source: MGI
  6. inflammatory response Source: UniProtKB
  7. negative regulation of blood pressure Source: RefGenome
  8. negative regulation of gene expression Source: UniProtKB
  9. negative regulation of protein catabolic process Source: BHF-UCL
  10. nitric oxide biosynthetic process Source: BHF-UCL
  11. nitric oxide mediated signal transduction Source: RefGenome
  12. peptidyl-cysteine S-nitrosylation Source: UniProtKB
  13. positive regulation of guanylate cyclase activity Source: RefGenome
  14. positive regulation of killing of cells of other organism Source: Ensembl
  15. positive regulation of vasodilation Source: RefGenome
  16. regulation of cell proliferation Source: MGI
  17. regulation of insulin secretion Source: Ensembl
  18. response to hypoxia Source: MGI
  19. response to lipopolysaccharide Source: UniProtKB
  20. superoxide metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calmodulin-binding, FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP, Zinc

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).

Names & Taxonomyi

Protein namesi
Recommended name:
Nitric oxide synthase, inducible (EC:1.14.13.39)
Alternative name(s):
Inducible NO synthase
Short name:
Inducible NOS
Short name:
iNOS
Macrophage NOS
Short name:
MAC-NOS
NOS type II
Peptidyl-cysteine S-nitrosylase NOS2
Gene namesi
Name:Nos2
Synonyms:Inosl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:97361. Nos2.

Subcellular locationi

GO - Cellular componenti

  1. cortical cytoskeleton Source: MGI
  2. cytoplasm Source: MGI
  3. cytosol Source: UniProtKB
  4. perinuclear region of cytoplasm Source: MGI
  5. peroxisome Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11441144Nitric oxide synthase, induciblePRO_0000170934Add
BLAST

Proteomic databases

MaxQBiP29477.
PRIDEiP29477.

PTM databases

PhosphoSiteiP29477.

Expressioni

Tissue specificityi

Macrophages.

Inductioni

By treatment with endotoxins or cytokines. By lipopolysaccharides (LPS) (in vitro). Expression in the liver oscillates in a circadian manner with peak levels occurring during the late night.1 Publication

Gene expression databases

BgeeiP29477.
CleanExiMM_NOS2.
GenevestigatoriP29477.

Interactioni

Subunit structurei

Homodimer. Binds SLC9A3R1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi201806. 6 interactions.
DIPiDIP-31080N.
IntActiP29477. 1 interaction.
MINTiMINT-202500.

Structurei

Secondary structure

1
1144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi79 – 835
Turni84 – 863
Beta strandi89 – 924
Helixi94 – 974
Beta strandi103 – 1075
Helixi117 – 1193
Helixi130 – 14617
Turni147 – 1504
Helixi153 – 17018
Helixi177 – 18913
Helixi195 – 1995
Beta strandi204 – 2074
Helixi208 – 2103
Helixi214 – 22916
Helixi230 – 2323
Beta strandi237 – 2404
Beta strandi245 – 2495
Beta strandi255 – 2595
Beta strandi263 – 2653
Beta strandi267 – 2693
Beta strandi271 – 2733
Helixi275 – 2773
Helixi278 – 2869
Beta strandi294 – 2963
Beta strandi301 – 3044
Beta strandi311 – 3133
Helixi317 – 3193
Beta strandi322 – 3243
Helixi332 – 3343
Turni335 – 3373
Beta strandi339 – 3424
Beta strandi350 – 3534
Beta strandi356 – 3594
Helixi369 – 3735
Helixi375 – 3784
Turni380 – 3834
Helixi386 – 3927
Helixi400 – 4023
Helixi415 – 4228
Helixi430 – 44213
Helixi455 – 4584
Beta strandi461 – 4633
Helixi464 – 4663
Helixi468 – 4714
Beta strandi480 – 4856
Helixi489 – 4924
Helixi509 – 5179

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DD7X-ray2.25A114-498[»]
1DF1X-ray2.35A/B77-499[»]
1DWVX-ray2.35A/B77-496[»]
1DWWX-ray2.35A/B77-496[»]
1DWXX-ray2.60A/B77-496[»]
1JWJX-ray2.60A/B66-498[»]
1JWKX-ray2.30A/B66-498[»]
1M8DX-ray2.35A/B65-498[»]
1M8EX-ray2.90A/B65-498[»]
1M8HX-ray2.85A/B65-498[»]
1M8IX-ray2.70A/B65-498[»]
1M9TX-ray2.40A/B65-498[»]
1N2NX-ray2.40A/B77-495[»]
1NOCX-ray2.60A115-498[»]
1NODX-ray2.60A/B77-499[»]
1NOSX-ray2.10A115-498[»]
1QOMX-ray2.70A/B65-498[»]
1QW4X-ray2.40A/B77-495[»]
1QW5X-ray2.70A/B77-495[»]
1R35X-ray2.30A/B66-498[»]
1VAFX-ray2.90A/B77-495[»]
2BHJX-ray3.20A77-498[»]
2NODX-ray2.60A/B77-499[»]
2NOSX-ray2.30A115-498[»]
2OROX-ray2.00A114-498[»]
2ORPX-ray1.97A114-498[»]
2ORQX-ray2.10A114-498[»]
2ORRX-ray2.00A114-498[»]
2ORSX-ray2.00A114-498[»]
2ORTX-ray1.87A114-498[»]
2Y37X-ray2.60A/B66-498[»]
3DWJX-ray2.75A/B66-496[»]
3E65X-ray2.05A/B66-498[»]
3E67X-ray2.60A/B66-498[»]
3E68X-ray2.20A/B66-498[»]
3E6LX-ray2.30A/B66-498[»]
3E6NX-ray2.40A/B66-498[»]
3E6OX-ray2.60A/B66-498[»]
3E6TX-ray2.50A/B66-498[»]
3E7IX-ray2.90A/B66-498[»]
3E7MX-ray2.00A/B66-498[»]
3E7TX-ray2.60A/B66-498[»]
3EAIX-ray2.20A/B66-498[»]
3EBDX-ray2.40A/B66-498[»]
3EBFX-ray2.29A/B66-498[»]
3GOFX-ray1.45C/D503-518[»]
3NODX-ray2.70A/B77-499[»]
3NQSX-ray2.20A/B66-498[»]
3NW2X-ray2.80A/B77-499[»]
4JS9X-ray2.78A/B66-496[»]
ProteinModelPortaliP29477.
SMRiP29477. Positions 77-497, 505-1126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29477.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini533 – 671139Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini724 – 964241FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni503 – 52321Calmodulin-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the NOS family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG4362.
GeneTreeiENSGT00620000087711.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
InParanoidiP29477.
KOiK13241.
OMAiKFTNSPT.
OrthoDBiEOG79SDW7.
PhylomeDBiP29477.
TreeFamiTF324410.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
3.90.340.10. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR012144. NOS_euk.
IPR004030. NOS_N.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF000333. NOS. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29477-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MACPWKFLFK VKSYQSDLKE EKDINNNVKK TPCAVLSPTI QDDPKSHQNG
60 70 80 90 100
SPQLLTGTAQ NVPESLDKLH VTSTRPQYVR IKNWGSGEIL HDTLHHKATS
110 120 130 140 150
DFTCKSKSCL GSIMNPKSLT RGPRDKPTPL EELLPHAIEF INQYYGSFKE
160 170 180 190 200
AKIEEHLARL EAVTKEIETT GTYQLTLDEL IFATKMAWRN APRCIGRIQW
210 220 230 240 250
SNLQVFDARN CSTAQEMFQH ICRHILYATN NGNIRSAITV FPQRSDGKHD
260 270 280 290 300
FRLWNSQLIR YAGYQMPDGT IRGDAATLEF TQLCIDLGWK PRYGRFDVLP
310 320 330 340 350
LVLQADGQDP EVFEIPPDLV LEVTMEHPKY EWFQELGLKW YALPAVANML
360 370 380 390 400
LEVGGLEFPA CPFNGWYMGT EIGVRDFCDT QRYNILEEVG RRMGLETHTL
410 420 430 440 450
ASLWKDRAVT EINVAVLHSF QKQNVTIMDH HTASESFMKH MQNEYRARGG
460 470 480 490 500
CPADWIWLVP PVSGSITPVF HQEMLNYVLS PFYYYQIEPW KTHIWQNEKL
510 520 530 540 550
RPRRREIRFR VLVKVVFFAS MLMRKVMASR VRATVLFATE TGKSEALARD
560 570 580 590 600
LATLFSYAFN TKVVCMDQYK ASTLEEEQLL LVVTSTFGNG DCPSNGQTLK
610 620 630 640 650
KSLFMLRELN HTFRYAVFGL GSSMYPQFCA FAHDIDQKLS HLGASQLAPT
660 670 680 690 700
GEGDELSGQE DAFRSWAVQT FRAACETFDV RSKHHIQIPK RFTSNATWEP
710 720 730 740 750
QQYRLIQSPE PLDLNRALSS IHAKNVFTMR LKSQQNLQSE KSSRTTLLVQ
760 770 780 790 800
LTFEGSRGPS YLPGEHLGIF PGNQTALVQG ILERVVDCPT PHQTVCLEVL
810 820 830 840 850
DESGSYWVKD KRLPPCSLSQ ALTYFLDITT PPTQLQLHKL ARFATDETDR
860 870 880 890 900
QRLEALCQPS EYNDWKFSNN PTFLEVLEEF PSLHVPAAFL LSQLPILKPR
910 920 930 940 950
YYSISSSQDH TPSEVHLTVA VVTYRTRDGQ GPLHHGVCST WIRNLKPQDP
960 970 980 990 1000
VPCFVRSVSG FQLPEDPSQP CILIGPGTGI APFRSFWQQR LHDSQHKGLK
1010 1020 1030 1040 1050
GGRMSLVFGC RHPEEDHLYQ EEMQEMVRKR VLFQVHTGYS RLPGKPKVYV
1060 1070 1080 1090 1100
QDILQKQLAN EVLSVLHGEQ GHLYICGDVR MARDVATTLK KLVATKLNLS
1110 1120 1130 1140
EEQVEDYFFQ LKSQKRYHED IFGAVFSYGA KKGSALEEPK ATRL
Length:1,144
Mass (Da):130,575
Last modified:April 1, 1993 - v1
Checksum:i0735BE676113457F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191K → T in AAC52356. (PubMed:7503239)Curated
Sequence conflicti72 – 721T → TP in AAM11887. 1 PublicationCurated
Sequence conflicti72 – 721T → TP in AAH62378. (PubMed:15489334)Curated
Sequence conflicti191 – 1911A → V in M92649. (PubMed:1379716)Curated
Sequence conflicti245 – 2451S → T in AAM11887. 1 PublicationCurated
Sequence conflicti245 – 2451S → T in AAH62378. (PubMed:15489334)Curated
Sequence conflicti844 – 8441A → G in M92649. (PubMed:1379716)Curated
Sequence conflicti1075 – 10751I → V in AAH62378. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti211 – 2111C → R in strain: NOD/LtJ. 1 Publication
Natural varianti967 – 9671P → L in strain: SJL/J. 1 Publication
Natural varianti968 – 9681S → F in strain: BALB/CBYJ. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87039 mRNA. Translation: AAA39315.1.
M92649 mRNA. No translation available.
M84373 mRNA. Translation: AAA39834.1.
U43428 mRNA. Translation: AAC52356.1.
AF065919 mRNA. Translation: AAC17914.1.
AF065920 mRNA. Translation: AAC17915.1.
AF065921 mRNA. Translation: AAC17916.2.
AF065922 mRNA. Translation: AAC17917.2.
AF065923 mRNA. Translation: AAC17918.2.
AF427516 Genomic DNA. Translation: AAL24076.1.
AY090567 mRNA. Translation: AAM11887.1.
AL592185 Genomic DNA. Translation: CAI25275.1.
BC062378 mRNA. Translation: AAH62378.1.
CCDSiCCDS25115.1.
PIRiA43271.
RefSeqiNP_035057.1. NM_010927.3.
UniGeneiMm.2893.

Genome annotation databases

EnsembliENSMUST00000018610; ENSMUSP00000018610; ENSMUSG00000020826.
GeneIDi18126.
KEGGimmu:18126.
UCSCiuc007kkc.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87039 mRNA. Translation: AAA39315.1 .
M92649 mRNA. No translation available.
M84373 mRNA. Translation: AAA39834.1 .
U43428 mRNA. Translation: AAC52356.1 .
AF065919 mRNA. Translation: AAC17914.1 .
AF065920 mRNA. Translation: AAC17915.1 .
AF065921 mRNA. Translation: AAC17916.2 .
AF065922 mRNA. Translation: AAC17917.2 .
AF065923 mRNA. Translation: AAC17918.2 .
AF427516 Genomic DNA. Translation: AAL24076.1 .
AY090567 mRNA. Translation: AAM11887.1 .
AL592185 Genomic DNA. Translation: CAI25275.1 .
BC062378 mRNA. Translation: AAH62378.1 .
CCDSi CCDS25115.1.
PIRi A43271.
RefSeqi NP_035057.1. NM_010927.3.
UniGenei Mm.2893.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DD7 X-ray 2.25 A 114-498 [» ]
1DF1 X-ray 2.35 A/B 77-499 [» ]
1DWV X-ray 2.35 A/B 77-496 [» ]
1DWW X-ray 2.35 A/B 77-496 [» ]
1DWX X-ray 2.60 A/B 77-496 [» ]
1JWJ X-ray 2.60 A/B 66-498 [» ]
1JWK X-ray 2.30 A/B 66-498 [» ]
1M8D X-ray 2.35 A/B 65-498 [» ]
1M8E X-ray 2.90 A/B 65-498 [» ]
1M8H X-ray 2.85 A/B 65-498 [» ]
1M8I X-ray 2.70 A/B 65-498 [» ]
1M9T X-ray 2.40 A/B 65-498 [» ]
1N2N X-ray 2.40 A/B 77-495 [» ]
1NOC X-ray 2.60 A 115-498 [» ]
1NOD X-ray 2.60 A/B 77-499 [» ]
1NOS X-ray 2.10 A 115-498 [» ]
1QOM X-ray 2.70 A/B 65-498 [» ]
1QW4 X-ray 2.40 A/B 77-495 [» ]
1QW5 X-ray 2.70 A/B 77-495 [» ]
1R35 X-ray 2.30 A/B 66-498 [» ]
1VAF X-ray 2.90 A/B 77-495 [» ]
2BHJ X-ray 3.20 A 77-498 [» ]
2NOD X-ray 2.60 A/B 77-499 [» ]
2NOS X-ray 2.30 A 115-498 [» ]
2ORO X-ray 2.00 A 114-498 [» ]
2ORP X-ray 1.97 A 114-498 [» ]
2ORQ X-ray 2.10 A 114-498 [» ]
2ORR X-ray 2.00 A 114-498 [» ]
2ORS X-ray 2.00 A 114-498 [» ]
2ORT X-ray 1.87 A 114-498 [» ]
2Y37 X-ray 2.60 A/B 66-498 [» ]
3DWJ X-ray 2.75 A/B 66-496 [» ]
3E65 X-ray 2.05 A/B 66-498 [» ]
3E67 X-ray 2.60 A/B 66-498 [» ]
3E68 X-ray 2.20 A/B 66-498 [» ]
3E6L X-ray 2.30 A/B 66-498 [» ]
3E6N X-ray 2.40 A/B 66-498 [» ]
3E6O X-ray 2.60 A/B 66-498 [» ]
3E6T X-ray 2.50 A/B 66-498 [» ]
3E7I X-ray 2.90 A/B 66-498 [» ]
3E7M X-ray 2.00 A/B 66-498 [» ]
3E7T X-ray 2.60 A/B 66-498 [» ]
3EAI X-ray 2.20 A/B 66-498 [» ]
3EBD X-ray 2.40 A/B 66-498 [» ]
3EBF X-ray 2.29 A/B 66-498 [» ]
3GOF X-ray 1.45 C/D 503-518 [» ]
3NOD X-ray 2.70 A/B 77-499 [» ]
3NQS X-ray 2.20 A/B 66-498 [» ]
3NW2 X-ray 2.80 A/B 77-499 [» ]
4JS9 X-ray 2.78 A/B 66-496 [» ]
ProteinModelPortali P29477.
SMRi P29477. Positions 77-497, 505-1126.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201806. 6 interactions.
DIPi DIP-31080N.
IntActi P29477. 1 interaction.
MINTi MINT-202500.

Chemistry

BindingDBi P29477.
ChEMBLi CHEMBL3464.

PTM databases

PhosphoSitei P29477.

Proteomic databases

MaxQBi P29477.
PRIDEi P29477.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018610 ; ENSMUSP00000018610 ; ENSMUSG00000020826 .
GeneIDi 18126.
KEGGi mmu:18126.
UCSCi uc007kkc.1. mouse.

Organism-specific databases

CTDi 4843.
MGIi MGI:97361. Nos2.

Phylogenomic databases

eggNOGi COG4362.
GeneTreei ENSGT00620000087711.
HOGENOMi HOG000220884.
HOVERGENi HBG000159.
InParanoidi P29477.
KOi K13241.
OMAi KFTNSPT.
OrthoDBi EOG79SDW7.
PhylomeDBi P29477.
TreeFami TF324410.

Enzyme and pathway databases

Reactomei REACT_198345. Phagosomal maturation (early endosomal stage).

Miscellaneous databases

EvolutionaryTracei P29477.
NextBioi 293348.
PROi P29477.
SOURCEi Search...

Gene expression databases

Bgeei P29477.
CleanExi MM_NOS2.
Genevestigatori P29477.

Family and domain databases

Gene3Di 1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
3.90.340.10. 1 hit.
InterProi IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR012144. NOS_euk.
IPR004030. NOS_N.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000333. NOS. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMi SSF52218. SSF52218. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
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Publicationsi

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  1. "Cloning and characterization of inducible nitric oxide synthase from mouse macrophages."
    Xie Q.-W., Cho H.J., Calaycay J., Mumford R.A., Swiderek K.M., Lee T.D., Ding A., Troso T., Nathan C.
    Science 256:225-228(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme."
    Lowenstein C.J., Glatt C.S., Bredt D.S., Snyder S.H.
    Proc. Natl. Acad. Sci. U.S.A. 89:6711-6715(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Molecular cloning and functional expression of an inducible nitric oxide synthase from a murine macrophage cell line."
    Lyons C.R., Orloff G.J., Cunningham J.M.
    J. Biol. Chem. 267:6370-6374(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Role of NF-kappa B in the regulation of inducible nitric oxide synthase in an MTAL cell line."
    Kone B.C., Schwoebel J., Turner P., Mohaupt M.G., Cangro C.B.
    Am. J. Physiol. 269:F718-F729(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Sequence polymorphisms in the chemokines Scya1 (TCA-3), Scya2 (monocyte chemoattractant protein (MCP)-1), and Scya12 (MCP-5) are candidates for eae7, a locus controlling susceptibility to monophasic remitting/nonrelapsing experimental allergic encephalomyelitis."
    Teuscher C., Butterfield R.J., Ma R.Z., Zachary J.F., Doerge R.W., Blankenhorn E.P.
    J. Immunol. 163:2262-2266(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-211; LEU-967 AND PHE-968.
    Strain: B10.S/J, BALB/cByJ, DBA/2J, NOD/LtJ and SJL/J.
    Tissue: Spleen.
  6. "Genomic structure of the murine inducible nitric oxide synthase (i-NOS) gene."
    Coge F., Levacher B., Rique H., Leopold O., Boutin J.A., Galizzi J.-P.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CD-1.
  7. "Mouse inducible nitric oxide synthase mRNA."
    Hagiwara K., Endo Y., Xin H., Takahashi M., Huqun X., Nukiwa T.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  9. "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: NMRI.
    Tissue: Mammary tumor.
  10. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 733-744, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  11. "The mode of action of aspirin-like drugs: effect on inducible nitric oxide synthase."
    Amin A.R., Vyas P., Attur M., Leszczynska-Piziak J., Patel I.R., Weissmann G., Abramson S.B.
    Proc. Natl. Acad. Sci. U.S.A. 92:7926-7930(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: EFFECT OF ASPIRIN.
    Tissue: Macrophage.
  12. "Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2."
    Kim S.F., Huri D.A., Snyder S.H.
    Science 310:1966-1970(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS NITROSYLASE.
  13. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The circadian deadenylase Nocturnin is necessary for stabilization of the iNOS mRNA in mice."
    Niu S., Shingle D.L., Garbarino-Pico E., Kojima S., Gilbert M., Green C.B.
    PLoS ONE 6:E26954-E26954(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  15. "The structure of nitric oxide synthase oxygenase domain and inhibitor complexes."
    Crane B.R., Arvai A.S., Gachhui R., Wu C., Ghosh D.K., Getzoff E.D., Stuehr D.J., Tainer J.A.
    Science 278:425-431(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 116-496.
  16. "Structure of nitric oxide synthase oxygenase dimer with pterin and substrate."
    Crane B.R., Arvai A.S., Ghosh D.K., Wu C., Getzoff E.D., Stuehr D.J., Tainer J.A.
    Science 279:2121-2126(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 77-496.
  17. "Inducible nitric oxide synthase: role of the N-terminal beta-hairpin hook and pterin-binding segment in dimerization and tetrahydrobiopterin interaction."
    Ghosh D.K., Crane B.R., Ghosh S., Wolan D., Gachhui R., Crooks C., Presta A., Tainer J.A., Getzoff E.D., Stuehr D.J.
    EMBO J. 18:6260-6270(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
  18. "N-terminal domain swapping and metal ion binding in nitric oxide synthase dimerization."
    Crane B.R., Rosenfeld R.J., Arvai A.S., Ghosh D.K., Ghosh S., Tainer J.A., Stuehr D.J., Getzoff E.D.
    EMBO J. 18:6271-6281(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-499.
  19. "Structures of the N(omega)-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins."
    Crane B.R., Arvai A.S., Ghosh S., Getzoff E.D., Stuehr D.J., Tainer J.A.
    Biochemistry 39:4608-4621(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
  20. "Structures of tetrahydrobiopterin binding-site mutants of inducible nitric oxide synthase oxygenase dimer and implicated roles of Trp457."
    Aoyagi M., Arvai A.S., Ghosh S., Stuehr D.J., Tainer J.A., Getzoff E.D.
    Biochemistry 40:12826-12832(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF TRP-457 MUTANTS.
  21. "Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: crystallographic and computational analyses of inhibitor potency."
    Rosenfeld R.J., Garcin E.D., Panda K., Andersson G., Aberg A., Wallace A.V., Morris G.M., Olson A.J., Stuehr D.J., Tainer J.A., Getzoff E.D.
    Biochemistry 41:13915-13925(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
  22. "Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase -- structural models of the short-lived oxygen complexes."
    Fedorov R., Ghosh D.K., Schlichting I.
    Arch. Biochem. Biophys. 409:25-31(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 77-495.

Entry informationi

Entry nameiNOS2_MOUSE
AccessioniPrimary (citable) accession number: P29477
Secondary accession number(s): O70515
, O70516, Q5SXT3, Q6P6A0, Q8R410
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 29, 2014
This is version 162 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3