P29477 (NOS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Nos2
Synonyms:	Inosl

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1144 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.12
Catalytic activity	2 L-arginine + 3 NADPH + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O.
Cofactor	Heme group. Binds 1 FAD. Binds 1 FMN. Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.
Enzyme regulation	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.
Subunit structure	Homodimer. Binds SLC9A3R1 By similarity.
Tissue specificity	Macrophages.
Induction	By treatment with endotoxins or cytokines.
Sequence similarities	Belongs to the NOS family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP Zinc
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	arginine catabolic process Inferred from direct assay PubMed 1383204. Source: BHF-UCL cellular response to interferon-gamma Inferred from direct assay PubMed 18025219. Source: MGI cellular response to lipopolysaccharide Inferred from direct assay PubMed 18025219PubMed 18791161. Source: MGI defense response to bacterium Inferred from mutant phenotype PubMed 12933833. Source: MGI inflammatory response Traceable author statement PubMed 12855682. Source: UniProtKB negative regulation of blood pressure Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of gene expression Inferred from genetic interaction PubMed 12085352. Source: UniProtKB negative regulation of protein catabolic process Inferred from direct assay PubMed 18003616. Source: BHF-UCL nitric oxide biosynthetic process Inferred from direct assay PubMed 1383204PubMed 9271491. Source: BHF-UCL nitric oxide mediated signal transduction Inferred from Biological aspect of Ancestor. Source: RefGenome peptidyl-cysteine S-nitrosylation Inferred from direct assay Ref.12. Source: UniProtKB positive regulation of guanylate cyclase activity Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of killing of cells of other organism Inferred from electronic annotation. Source: Compara positive regulation of vasodilation Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of cell proliferation Inferred from genetic interaction PubMed 11606502PubMed 11731407. Source: MGI regulation of insulin secretion Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from direct assay PubMed 12960352. Source: MGI superoxide metabolic process Inferred from mutant phenotype PubMed 12933833. Source: MGI
Cellular_component	cortical cytoskeleton Inferred from direct assay PubMed 12960352. Source: MGI cytosol Traceable author statement PubMed 12855682. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay PubMed 12960352. Source: MGI peroxisome Inferred from electronic annotation. Source: Compara
Molecular_function	FMN binding Inferred from direct assay PubMed 1383204. Source: BHF-UCL NADP binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activity Inferred from Biological aspect of Ancestor. Source: RefGenome arginine binding Inferred from direct assay PubMed 9271491. Source: BHF-UCL calmodulin binding Traceable author statement PubMed 12855682. Source: UniProtKB flavin adenine dinucleotide binding Inferred from direct assay PubMed 1383204. Source: BHF-UCL heme binding Inferred from direct assay PubMed 1383204PubMed 9271491. Source: BHF-UCL iron ion binding Inferred from electronic annotation. Source: InterPro nitric-oxide synthase activity Inferred from direct assay PubMed 1383204PubMed 9271491. Source: BHF-UCL protein homodimerization activity Inferred from direct assay PubMed 9271491. Source: BHF-UCL tetrahydrobiopterin binding Inferred from direct assay PubMed 9271491. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1144

1144

Nitric oxide synthase, inducible

PRO_0000170934

Regions

Domain

533 – 671

139

Flavodoxin-like

Domain

724 – 964

241

FAD-binding FR-type

Nucleotide binding

617 – 648

32

FMN By similarity

Nucleotide binding

761 – 772

12

FAD By similarity

Nucleotide binding

897 – 907

11

FAD By similarity

Nucleotide binding

972 – 990

19

NADP By similarity

Nucleotide binding

1070 – 1085

16

NADP By similarity

Region

503 – 523

21

Calmodulin-binding Potential

Sites

Metal binding

104

1

Zinc

Metal binding

109

1

Zinc

Metal binding

194

1

Iron (heme axial ligand)

Amino acid modifications

Modified residue

708

1

Phosphoserine Ref.13

Natural variations

Natural variant

211

1

C → R in strain: NOD/LtJ. Ref.5

Natural variant

967

1

P → L in strain: SJL/J. Ref.5

Natural variant

968

1

S → F in strain: BALB/CBYJ. Ref.5

Experimental info

Sequence conflict

19

1

K → T in AAC52356. Ref.4

Sequence conflict

72

1

T → TP in AAM11887. Ref.7

Sequence conflict

72

1

T → TP in AAH62378. Ref.9

Sequence conflict

191

1

A → V in M92649. Ref.2

Sequence conflict

245

1

S → T in AAM11887. Ref.7

Sequence conflict

245

1

S → T in AAH62378. Ref.9

Sequence conflict

844

1

A → G in M92649. Ref.2

Sequence conflict

1075

1

I → V in AAH62378. Ref.9

Secondary structure

1

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1144

Helix Strand Turn

Details...

Beta strand

79 – 83

5

Turn

84 – 86

3

Beta strand

89 – 92

4

Helix

94 – 97

4

Beta strand

103 – 107

5

Helix

117 – 119

3

Helix

130 – 146

17

Turn

147 – 150

4

Helix

153 – 170

18

Helix

177 – 189

13

Helix

195 – 199

5

Beta strand

204 – 207

4

Helix

208 – 210

3

Helix

214 – 229

16

Helix

230 – 232

3

Beta strand

237 – 240

4

Beta strand

245 – 249

5

Beta strand

255 – 259

5

Beta strand

263 – 265

3

Beta strand

267 – 269

3

Beta strand

271 – 273

3

Helix

275 – 277

3

Helix

278 – 286

9

Beta strand

294 – 296

3

Beta strand

301 – 304

4

Beta strand

311 – 313

3

Helix

317 – 319

3

Beta strand

322 – 324

3

Helix

332 – 334

3

Turn

335 – 337

3

Beta strand

339 – 342

4

Beta strand

350 – 353

4

Beta strand

356 – 359

4

Helix

369 – 373

5

Helix

375 – 378

4

Turn

380 – 383

4

Helix

386 – 392

7

Helix

400 – 402

3

Helix

415 – 422

8

Helix

430 – 442

13

Helix

455 – 458

4

Beta strand

461 – 463

3

Helix

464 – 466

3

Helix

468 – 471

4

Beta strand

480 – 485

6

Helix

489 – 492

4

Helix

509 – 517

9

Sequences

	Sequence		Length	Mass (Da)
	P29477 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 0735BE676113457F	FASTA	1,144	130,575
	10 20 30 40 50 60 MACPWKFLFK VKSYQSDLKE EKDINNNVKK TPCAVLSPTI QDDPKSHQNG SPQLLTGTAQ 70 80 90 100 110 120 NVPESLDKLH VTSTRPQYVR IKNWGSGEIL HDTLHHKATS DFTCKSKSCL GSIMNPKSLT 130 140 150 160 170 180 RGPRDKPTPL EELLPHAIEF INQYYGSFKE AKIEEHLARL EAVTKEIETT GTYQLTLDEL 190 200 210 220 230 240 IFATKMAWRN APRCIGRIQW SNLQVFDARN CSTAQEMFQH ICRHILYATN NGNIRSAITV 250 260 270 280 290 300 FPQRSDGKHD FRLWNSQLIR YAGYQMPDGT IRGDAATLEF TQLCIDLGWK PRYGRFDVLP 310 320 330 340 350 360 LVLQADGQDP EVFEIPPDLV LEVTMEHPKY EWFQELGLKW YALPAVANML LEVGGLEFPA 370 380 390 400 410 420 CPFNGWYMGT EIGVRDFCDT QRYNILEEVG RRMGLETHTL ASLWKDRAVT EINVAVLHSF 430 440 450 460 470 480 QKQNVTIMDH HTASESFMKH MQNEYRARGG CPADWIWLVP PVSGSITPVF HQEMLNYVLS 490 500 510 520 530 540 PFYYYQIEPW KTHIWQNEKL RPRRREIRFR VLVKVVFFAS MLMRKVMASR VRATVLFATE 550 560 570 580 590 600 TGKSEALARD LATLFSYAFN TKVVCMDQYK ASTLEEEQLL LVVTSTFGNG DCPSNGQTLK 610 620 630 640 650 660 KSLFMLRELN HTFRYAVFGL GSSMYPQFCA FAHDIDQKLS HLGASQLAPT GEGDELSGQE 670 680 690 700 710 720 DAFRSWAVQT FRAACETFDV RSKHHIQIPK RFTSNATWEP QQYRLIQSPE PLDLNRALSS 730 740 750 760 770 780 IHAKNVFTMR LKSQQNLQSE KSSRTTLLVQ LTFEGSRGPS YLPGEHLGIF PGNQTALVQG 790 800 810 820 830 840 ILERVVDCPT PHQTVCLEVL DESGSYWVKD KRLPPCSLSQ ALTYFLDITT PPTQLQLHKL 850 860 870 880 890 900 ARFATDETDR QRLEALCQPS EYNDWKFSNN PTFLEVLEEF PSLHVPAAFL LSQLPILKPR 910 920 930 940 950 960 YYSISSSQDH TPSEVHLTVA VVTYRTRDGQ GPLHHGVCST WIRNLKPQDP VPCFVRSVSG 970 980 990 1000 1010 1020 FQLPEDPSQP CILIGPGTGI APFRSFWQQR LHDSQHKGLK GGRMSLVFGC RHPEEDHLYQ 1030 1040 1050 1060 1070 1080 EEMQEMVRKR VLFQVHTGYS RLPGKPKVYV QDILQKQLAN EVLSVLHGEQ GHLYICGDVR 1090 1100 1110 1120 1130 1140 MARDVATTLK KLVATKLNLS EEQVEDYFFQ LKSQKRYHED IFGAVFSYGA KKGSALEEPK ATRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-708, MASS SPECTROMETRY. Tissue: Macrophage.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00125726.

PIR

A43271.

RefSeq

NP_035057.1. NM_010927.3.

UniGene

Mm.2893.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P29477.

SMR

P29477. Positions 77-497, 505-1126.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31080N.

IntAct

P29477. 1 interaction.

MINT

MINT-202500.

PTM databases

PhosphoSite

P29477.

Proteomic databases

PRIDE

P29477.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000018610; ENSMUSP00000018610; ENSMUSG00000020826.

GeneID

18126.

KEGG

mmu:18126.

UCSC

uc007kkc.1. mouse.

Organism-specific databases

CTD

4843.

MGI

MGI:97361. Nos2.

Phylogenomic databases

eggNOG

COG4362.

GeneTree

ENSGT00620000087711.

HOGENOM

HOG000220884.

HOVERGEN

HBG000159.

InParanoid

P29477.

KO

K13241.

OMA

KFTNSPT.

OrthoDB

EOG4D26P1.

Gene expression databases

Bgee

P29477.

CleanEx

MM_NOS2.

Genevestigator

P29477.

GermOnline

ENSMUSG00000020826. Mus musculus.

Family and domain databases

Gene3D

1.20.990.10. 1 hit.
3.90.340.10. 1 hit.

InterPro

IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR004030. NO_synthase_oxygenase_dom.
IPR026009. NOS.
IPR012144. NOS_met.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]

PANTHER

PTHR19384:SF5. PTHR19384:SF5. 1 hit.

Pfam

PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view]

PIRSF

PIRSF000333. NOS. 1 hit.

PRINTS

PR00369. FLAVODOXIN.
PR00371. FPNCR.

SUPFAM

SSF56512. NO_synthase_oxygenase_reg. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.

PROSITE

PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P29477.

ChEMBL

CHEMBL3464.

EvolutionaryTrace

P29477.

NextBio

293348.

SOURCE

Search...

Entry information

Entry name

NOS2_MOUSE

Accession

Primary (citable) accession number: P29477
Secondary accession number(s): O70515 , O70516, Q5SXT3, Q6P6A0, Q8R410

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 149 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program