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Q06518

- NOS2_RAT

UniProt

Q06518 - NOS2_RAT

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Protein
Nitric oxide synthase, inducible
Gene
Nos2
Organism
Rattus norvegicus (Rat)
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. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2 By similarity.

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi107 – 1071Zinc By similarity
Metal bindingi112 – 1121Zinc By similarity
Metal bindingi197 – 1971Iron (heme axial ligand) By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi620 – 65132FMN By similarity
Add
BLAST
Nucleotide bindingi764 – 77512FAD By similarity
Add
BLAST
Nucleotide bindingi900 – 91011FAD By similarity
Add
BLAST
Nucleotide bindingi975 – 99319NADP By similarity
Add
BLAST
Nucleotide bindingi1073 – 108816NADP By similarity
Add
BLAST

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. NADP binding Source: InterPro
  3. flavin adenine dinucleotide binding Source: InterPro
  4. heme binding Source: InterPro
  5. iron ion binding Source: InterPro
  6. nitric-oxide synthase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. defense response to bacterium Source: UniProtKB
  2. nitric oxide biosynthetic process Source: UniProtKB
  3. peptidyl-cysteine S-nitrosylation Source: UniProtKB
  4. superoxide metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

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
NOS type II
Peptidyl-cysteine S-nitrosylase NOS2
Gene namesi
Name:Nos2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3185. Nos2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. nucleus Source: BHF-UCL
  4. peroxisome Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11471147Nitric oxide synthase, inducible
PRO_0000170937Add
BLAST

Proteomic databases

PRIDEiQ06518.

PTM databases

PhosphoSiteiQ06518.

Expressioni

Tissue specificityi

In normal kidney, expressed primarily in the medullary thick ascending limb, with minor amounts in the medullary collecting duct and vasa recta bundle.

Inductioni

By interferon gamma and lipopolysaccharides (LPS).

Gene expression databases

GenevestigatoriQ06518.

Interactioni

Subunit structurei

Homodimer. Binds SLC9A3R1 By similarity.

Protein-protein interaction databases

DIPiDIP-59942N.

Structurei

3D structure databases

ProteinModelPortaliQ06518.
SMRiQ06518. Positions 80-499, 700-1127.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini536 – 674139Flavodoxin-like
Add
BLAST
Domaini727 – 967241FAD-binding FR-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni506 – 52621Calmodulin-binding Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the NOS family.

Phylogenomic databases

eggNOGiCOG4362.
HOVERGENiHBG000159.
InParanoidiQ06518.
KOiK13241.
PhylomeDBiQ06518.

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.

Q06518-1 [UniParc]FASTAAdd to Basket

« Hide

MACPWKFLFR VKSYQGDLKE EKDINNNVEK TPGAIPSPTT QDDPKSHKHQ     50
NGFPQFLTGT AQNVPESLDK LHVTPSTRPQ HVRIKNWGNG EIFHDTLHHK 100
ATSDISCKSK LCMGSIMNSK SLTRGPRDKP TPVEELLPQA IEFINQYYGS 150
FKEAKIEEHL ARLEAVTKEI ETTGTYQLTL DELIFATKMA WRNAPRCIGR 200
IQWSNLQVFD ARSCSTASEM FQHICRHILY ATNSGNIRSA ITVFPQRSDG 250
KHDFRIWNSQ LIRYAGYQMP DGTIRGDPAT LEFTQLCIDL GWKPRYGRFD 300
VLPLVLQAHG QDPEVFEIPP DLVLEVTMEH PKYEWFQELG LKWYALPAVA 350
NMLLEVGGLE FPACPFNGWY MGTEIGVRDF CDTQRYNILE EVGRRMGLET 400
HTLASLWKDR AVTEINAAVL HSFQKQNVTI MDHHTASESF MKHMQNEYRA 450
RGGCPADWIW LVPPVSGSIT PVFHQEMLNY VLSPFYYYQI EPWKTHIWQD 500
EKLRPRRREI RFTVLVKAVF FASVLMRKVM ASRVRATVLF ATETGKSEAL 550
ARDLAALFSY AFNTKVVCME QYKANTLEEE QLLLVVTSTF GNGDCPSNGQ 600
TLKKSLFMMK ELGHTFRYAV FGLGSSMYPQ FCAFAHDIDQ KLSHLGASQL 650
APTGEGDELS GQEDAFRSWA VQTFRAACET FDVRSKHCIQ IPKRYTSNAT 700
WEPEQYKLTQ SPESLDLNKA LSSIHAKNVF TMRLKSLQNL QSEKSSRTTL 750
LVQLTFEGSR GPSYLPGEHL GIFPGNQTAL VQGILERVVD CSSPDQTVCL 800
EVLDESGSYW VKDKRLPPCS LRQALTYFLD ITTPPTQLQL HKLARFATEE 850
THRQRLEALC QPSEYNDWKF SNNPTFLEVL EEFPSLRVPA AFLLSQLPIL 900
KPRYYSISSS QDHTPSEVHL TVAVVTYRTR DGQGPLHHGV CSTWINNLKP 950
EDPVPCFVRS VSGFQLPEDP SQPCILIGPG TGIAPFRSFW QQRLHDSQHR 1000
GLKGGRMTLV FGCRHPEEDH LYQEEMQEMV RKGVLFQVHT GYSRLPGKPK 1050
VYVQDILQKE LADEVFSVLH GEQGHLYVCG DVRMARDVAT TLKKLVAAKL 1100
NLSEEQVEDY FFQLKSQKRY HEDIFGAVFS YGAKKGNTLE EPKGTRL 1147
Length:1,147
Mass (Da):130,628
Last modified:October 1, 1996 - v2
Checksum:i77C77432DD8AB0A9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101R → K in BAA07994. 1 Publication
Sequence conflicti72 – 721H → Y in BAA03138. 1 Publication
Sequence conflicti107 – 1071C → R in AAC13747. 1 Publication
Sequence conflicti128 – 1281D → V in BAA12035. 1 Publication
Sequence conflicti130 – 1301P → H in AAC13747. 1 Publication
Sequence conflicti171 – 1711E → G in BAA12035. 1 Publication
Sequence conflicti195 – 1951P → S in BAA12035. 1 Publication
Sequence conflicti248 – 2481S → N in AAC83553. 1 Publication
Sequence conflicti248 – 2481S → T1 Publication
Sequence conflicti248 – 2481S → T1 Publication
Sequence conflicti264 – 2641Y → I in AAC13747. 1 Publication
Sequence conflicti271 – 2711D → A in AAC83554. 1 Publication
Sequence conflicti277 – 2771D → E in AAC13747. 1 Publication
Sequence conflicti348 – 3481A → P in BAA03138. 1 Publication
Sequence conflicti349 – 3491V → A in CAA54208. 1 Publication
Sequence conflicti380 – 3801F → L1 Publication
Sequence conflicti380 – 3801F → L1 Publication
Sequence conflicti380 – 3801F → L1 Publication
Sequence conflicti380 – 3801F → L in AAC83553. 1 Publication
Sequence conflicti380 – 3801F → L in AAC83554. 1 Publication
Sequence conflicti395 – 3951R → S in BAA02090. 1 Publication
Sequence conflicti399 – 3991E → G in AAC83553. 1 Publication
Sequence conflicti412 – 4121V → A in AAC13747. 1 Publication
Sequence conflicti477 – 4771M → I1 Publication
Sequence conflicti513 – 5131T → R in AAB18620. 1 Publication
Sequence conflicti515 – 5151L → W in AAB31028. 1 Publication
Sequence conflicti545 – 5451G → R in AAB31028. 1 Publication
Sequence conflicti551 – 5511A → R in AAB18620. 1 Publication
Sequence conflicti556 – 5561A → S in AAB31028. 1 Publication
Sequence conflicti559 – 5591S → T in AAC83553. 1 Publication
Sequence conflicti559 – 5591S → T in AAC83554. 1 Publication
Sequence conflicti564 – 5641T → N in AAB31028. 1 Publication
Sequence conflicti570 – 5701E → D in AAB31028. 1 Publication
Sequence conflicti583 – 5831L → P1 Publication
Sequence conflicti583 – 5831L → P1 Publication
Sequence conflicti591 – 5911G → A in AAB31028. 1 Publication
Sequence conflicti591 – 5911G → V1 Publication
Sequence conflicti591 – 5911G → V1 Publication
Sequence conflicti619 – 6191A → R in AAA85861. 1 Publication
Sequence conflicti640 – 6401Q → P in AAC83553. 1 Publication
Sequence conflicti664 – 6641D → G in AAB18620. 1 Publication
Sequence conflicti679 – 6802ET → VP in BAA03138. 1 Publication
Sequence conflicti690 – 6901Q → P in AAB18620. 1 Publication
Sequence conflicti711 – 7111S → N in AAB18620. 1 Publication
Sequence conflicti714 – 7152SL → TR in AAB18620. 1 Publication
Sequence conflicti714 – 7141S → P1 Publication
Sequence conflicti714 – 7141S → P1 Publication
Sequence conflicti714 – 7141S → P1 Publication
Sequence conflicti714 – 7141S → P in AAC83553. 1 Publication
Sequence conflicti714 – 7141S → P in AAC83554. 1 Publication
Sequence conflicti714 – 7141S → P in AAC16401. 1 Publication
Sequence conflicti719 – 7191K → R in AAB18620. 1 Publication
Sequence conflicti721 – 7211L → P1 Publication
Sequence conflicti722 – 7221S → R1 Publication
Sequence conflicti722 – 7221S → R1 Publication
Sequence conflicti722 – 7221S → R1 Publication
Sequence conflicti724 – 7263IHA → FLN1 Publication
Sequence conflicti730 – 7301F → I in AAB18620. 1 Publication
Sequence conflicti731 – 7311T → A in AAC83553. 1 Publication
Sequence conflicti740 – 7401L → P in CAA54208. 1 Publication
Sequence conflicti779 – 7791A → G in AAC13747. 1 Publication
Sequence conflicti834 – 8341P → S in BAA12035. 1 Publication
Sequence conflicti844 – 8441A → G in BAA03138. 1 Publication
Sequence conflicti895 – 8951S → L in BAA02090. 1 Publication
Sequence conflicti911 – 9111Q → L in AAC13747. 1 Publication
Sequence conflicti925 – 9251V → D in BAA12035. 1 Publication
Sequence conflicti937 – 9371H → N in AAC83554. 1 Publication
Sequence conflicti999 – 9991H → R1 Publication
Sequence conflicti999 – 9991H → R1 Publication
Sequence conflicti999 – 9991H → R in AAC83553. 1 Publication
Sequence conflicti999 – 9991H → R in AAC83554. 1 Publication
Sequence conflicti1008 – 10092TL → NF in AAC83554. 1 Publication
Sequence conflicti1016 – 10161P → R1 Publication
Sequence conflicti1016 – 10161P → S1 Publication
Sequence conflicti1017 – 10171E → R1 Publication
Sequence conflicti1017 – 10171E → R1 Publication
Sequence conflicti1024 – 10241E → K in AAC83554. 1 Publication
Sequence conflicti1076 – 10761L → I in AAC83553. 1 Publication
Sequence conflicti1084 – 10841M → I in CAA54208. 1 Publication
Sequence conflicti1129 – 11291F → V in AAC83554. 1 Publication
Sequence conflicti1133 – 11331A → V1 Publication
Sequence conflicti1133 – 11331A → V1 Publication
Sequence conflicti1133 – 11331A → V in AAC83553. 1 Publication
Sequence conflicti1133 – 11331A → V in AAC83554. 1 Publication
Sequence conflicti1138 – 11381T → A1 Publication
Sequence conflicti1138 – 11381T → A1 Publication
Sequence conflicti1138 – 11381T → A in AAC83553. 1 Publication
Sequence conflicti1138 – 11381T → A in AAC83554. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14051 mRNA. Translation: BAA03138.1.
U26686 mRNA. Translation: AAA85861.1.
U03699 mRNA. Translation: AAC13747.1.
D12520 mRNA. Translation: BAA02090.1.
L12562 mRNA. Translation: AAA41720.1.
X76881 mRNA. Translation: CAA54208.1.
D44591 mRNA. Translation: BAA07994.1.
D83661 mRNA. Translation: BAA12035.1.
AF049656 mRNA. Translation: AAC83553.1.
AF051164 mRNA. Translation: AAC83554.1.
AF006619 mRNA. Translation: AAC16401.1.
AF006620 mRNA. Translation: AAC16402.1.
U48829 mRNA. Translation: AAB18620.1.
S71597 mRNA. Translation: AAB31028.2.
L36063 mRNA. Translation: AAC02242.1.
PIRiI53165.
I56575.
JC5027.
S38253.
S47647.
RefSeqiNP_036743.3. NM_012611.3.
UniGeneiRn.10400.

Genome annotation databases

GeneIDi24599.
KEGGirno:24599.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14051 mRNA. Translation: BAA03138.1 .
U26686 mRNA. Translation: AAA85861.1 .
U03699 mRNA. Translation: AAC13747.1 .
D12520 mRNA. Translation: BAA02090.1 .
L12562 mRNA. Translation: AAA41720.1 .
X76881 mRNA. Translation: CAA54208.1 .
D44591 mRNA. Translation: BAA07994.1 .
D83661 mRNA. Translation: BAA12035.1 .
AF049656 mRNA. Translation: AAC83553.1 .
AF051164 mRNA. Translation: AAC83554.1 .
AF006619 mRNA. Translation: AAC16401.1 .
AF006620 mRNA. Translation: AAC16402.1 .
U48829 mRNA. Translation: AAB18620.1 .
S71597 mRNA. Translation: AAB31028.2 .
L36063 mRNA. Translation: AAC02242.1 .
PIRi I53165.
I56575.
JC5027.
S38253.
S47647.
RefSeqi NP_036743.3. NM_012611.3.
UniGenei Rn.10400.

3D structure databases

ProteinModelPortali Q06518.
SMRi Q06518. Positions 80-499, 700-1127.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-59942N.

Chemistry

BindingDBi Q06518.
ChEMBLi CHEMBL3051.

PTM databases

PhosphoSitei Q06518.

Proteomic databases

PRIDEi Q06518.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24599.
KEGGi rno:24599.

Organism-specific databases

CTDi 4843.
RGDi 3185. Nos2.

Phylogenomic databases

eggNOGi COG4362.
HOVERGENi HBG000159.
InParanoidi Q06518.
KOi K13241.
PhylomeDBi Q06518.

Miscellaneous databases

NextBioi 603804.

Gene expression databases

Genevestigatori Q06518.

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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning of inducible nitric oxide synthase in rat vascular smooth muscle cells."
    Nunokawa Y., Ishida N., Tanaka S.
    Biochem. Biophys. Res. Commun. 191:89-94(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Vascular smooth muscle.
  2. "Cloning and expression of cytokine-inducible nitric oxide synthase cDNA from rat islets of Langerhans."
    Karlsen A.E., Andersen H.U., Vissing H., Larsen P.M., Fey S.J., Cuartero B.G., Madsen O.D., Petersen J.S., Mortensen S.B., Mandrup-Poulsen T., Boel E., Nerup J.
    Diabetes 44:753-758(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Pancreatic islet.
  3. "Cloning and expression of inducible nitric oxide synthase from rat astrocytes."
    Galea E., Reis D.J., Feinstein D.L.
    J. Neurosci. Res. 37:406-414(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Astrocyte.
  4. "Molecular cloning of a cDNA encoding an inducible calmodulin-dependent nitric-oxide synthase from rat liver and its expression in COS 1 cells."
    Adachi H., Iida S., Oguchi S., Ohshima H., Suzuki H., Nagasaki K., Kawasaki H., Sugimura T., Esumi H.
    Eur. J. Biochem. 217:37-43(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  5. "Hepatocytes and macrophages express an identical cytokine inducible nitric oxide synthase gene."
    Wood E.R., Berger H. Jr., Sherman P.A., Lapetina E.G.
    Biochem. Biophys. Res. Commun. 191:767-774(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Hepatocyte.
  6. "cDNA cloning and expression of inducible nitric oxide synthase from rat vascular smooth muscle cells."
    Geng Y.J., Almquist M., Hansson G.K.
    Biochim. Biophys. Acta 1218:421-424(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Aorta.
  7. "Cloning of an inducible nitric oxide synthase from rat polymorphonuclear neutrophils."
    Kosuga K., Yui Y., Hattori R., Sase K., Eizawa H., Aoyama T., Inoue R., Sasayama S.
    Endothelium 2:217-221(1994)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  8. "Sequence analysis of inducible nitric oxide synthase in rat kidney, lung, and uterus."
    Tsutsumishita Y., Kawai Y., Takahara H., Onda T., Miyoshi J., Futaki S., Niwa M.
    Biol. Pharm. Bull. 19:1374-1376(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  9. "Complete coding sequence of inducible nitric oxide synthase from human heart and skeletal muscle of patients with chronic heart failure."
    Adams V., Krabbes S., Jiang H., Yu J., Rahmel A., Gielen S., Schuler G., Hambrecht R.
    Nitric Oxide 2:242-249(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  10. "Vascular smooth muscle nitric oxide synthase anomalies in Dahl/Rapp salt-sensitive rats."
    Chen P.Y., Gladish R.D., Sanders P.W.
    Hypertension 31:918-924(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 426-788.
    Strain: Dahl/Rapp salt sensitive strain.
    Tissue: Vascular smooth muscle.
  11. "Advances in the studies of NO synthesis regulation in mesanglial cells."
    Saura M., Zaragoza C., Martinez-Dalmau R., Perez-Sala D., Lamas S.
    Nefrologia 16:35-39(1996)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 509-740.
    Strain: Wistar.
    Tissue: Renal glomerulus.
  12. "Location of an inducible nitric oxide synthase mRNA in the normal kidney."
    Morrissey J.J., McCracken R., Kaneto H., Vehaskari M., Montani D., Klahr S.
    Kidney Int. 45:998-1005(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 479-655.
    Strain: Sprague-Dawley.
    Tissue: Renal glomerulus.
  13. "Isolation and characterization of iNOS from rat cardiocytes."
    Michel T., Balligand J.-L.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 420-479.
    Tissue: Myocardium.

Entry informationi

Entry nameiNOS2_RAT
AccessioniPrimary (citable) accession number: Q06518
Secondary accession number(s): O35765
, O35766, O60591, O60604, P97774, Q63267, Q64005, Q64558
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

sequence Was originally (1 Publication) thought to originate from human but appears to be from rat.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi