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Protein

Nitric oxide synthase, inducible

Gene

Nos2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM (By similarity).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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).By similarity

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi620 – 65132FMNPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi764 – 77512FADBy similarityAdd
BLAST
Nucleotide bindingi900 – 91011FADBy similarityAdd
BLAST
Nucleotide bindingi975 – 99319NADPBy similarityAdd
BLAST
Nucleotide bindingi1073 – 108816NADPBy similarityAdd
BLAST

GO - Molecular functioni

  • actin binding Source: RGD
  • amino acid binding Source: RGD
  • beta-catenin binding Source: RGD
  • cadherin binding Source: RGD
  • cAMP-dependent protein kinase regulator activity Source: RGD
  • flavin adenine dinucleotide binding Source: RGD
  • FMN binding Source: RGD
  • heme binding Source: RGD
  • Hsp90 protein binding Source: RGD
  • iron ion binding Source: InterPro
  • NADP binding Source: RGD
  • NADPH-hemoprotein reductase activity Source: GO_Central
  • nitric-oxide synthase activity Source: UniProtKB
  • nitric-oxide synthase binding Source: RGD
  • protein homodimerization activity Source: RGD
  • protein kinase binding Source: RGD

GO - Biological processi

  • aging Source: RGD
  • blood vessel remodeling Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to lithium ion Source: RGD
  • cellular response to redox state Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • cellular response to vitamin D Source: RGD
  • cGMP-mediated signaling Source: RGD
  • defense response to bacterium Source: UniProtKB
  • defense response to Gram-negative bacterium Source: RGD
  • endothelial cell proliferation Source: RGD
  • glycoside metabolic process Source: RGD
  • G-protein coupled receptor signaling pathway coupled to cGMP nucleotide second messenger Source: RGD
  • inflammatory response Source: GO_Central
  • intracellular signal transduction Source: RGD
  • negative regulation of blood pressure Source: GO_Central
  • nitric oxide biosynthetic process Source: UniProtKB
  • nitric oxide mediated signal transduction Source: GO_Central
  • peptidyl-cysteine S-nitrosylation Source: UniProtKB
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of guanylate cyclase activity Source: GO_Central
  • positive regulation of vasodilation Source: GO_Central
  • regulation of blood pressure Source: RGD
  • regulation of heart contraction Source: RGD
  • regulation of protein kinase activity Source: GOC
  • response to activity Source: RGD
  • response to dexamethasone Source: RGD
  • response to estradiol Source: RGD
  • response to hormone Source: RGD
  • response to immobilization stress Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to tumor necrosis factor Source: RGD
  • retinoic acid receptor signaling pathway Source: RGD
  • signal transduction Source: RGD
  • superoxide metabolic process Source: UniProtKB
  • wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi1.14.13.39. 5301.

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 Componenti: Unplaced

Organism-specific databases

RGDi3185. Nos2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular space Source: RGD
  • nucleus Source: BHF-UCL
  • perinuclear region of cytoplasm Source: RGD
  • peroxisome Source: UniProtKB
  • vesicle membrane Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11471147Nitric oxide synthase, induciblePRO_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

GenevisibleiQ06518. RN.

Interactioni

Subunit structurei

Homodimer. Binds SLC9A3R1 (By similarity). Interacts with GAPDH. Interacts with S100A8 and S100A9 to form the iNOS-S100A8/9 transnitrosylase complex (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-59942N.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini536 – 674139Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini727 – 967241FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni506 – 52621Calmodulin-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.
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.
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]
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

        10         20         30         40         50
MACPWKFLFR VKSYQGDLKE EKDINNNVEK TPGAIPSPTT QDDPKSHKHQ
60 70 80 90 100
NGFPQFLTGT AQNVPESLDK LHVTPSTRPQ HVRIKNWGNG EIFHDTLHHK
110 120 130 140 150
ATSDISCKSK LCMGSIMNSK SLTRGPRDKP TPVEELLPQA IEFINQYYGS
160 170 180 190 200
FKEAKIEEHL ARLEAVTKEI ETTGTYQLTL DELIFATKMA WRNAPRCIGR
210 220 230 240 250
IQWSNLQVFD ARSCSTASEM FQHICRHILY ATNSGNIRSA ITVFPQRSDG
260 270 280 290 300
KHDFRIWNSQ LIRYAGYQMP DGTIRGDPAT LEFTQLCIDL GWKPRYGRFD
310 320 330 340 350
VLPLVLQAHG QDPEVFEIPP DLVLEVTMEH PKYEWFQELG LKWYALPAVA
360 370 380 390 400
NMLLEVGGLE FPACPFNGWY MGTEIGVRDF CDTQRYNILE EVGRRMGLET
410 420 430 440 450
HTLASLWKDR AVTEINAAVL HSFQKQNVTI MDHHTASESF MKHMQNEYRA
460 470 480 490 500
RGGCPADWIW LVPPVSGSIT PVFHQEMLNY VLSPFYYYQI EPWKTHIWQD
510 520 530 540 550
EKLRPRRREI RFTVLVKAVF FASVLMRKVM ASRVRATVLF ATETGKSEAL
560 570 580 590 600
ARDLAALFSY AFNTKVVCME QYKANTLEEE QLLLVVTSTF GNGDCPSNGQ
610 620 630 640 650
TLKKSLFMMK ELGHTFRYAV FGLGSSMYPQ FCAFAHDIDQ KLSHLGASQL
660 670 680 690 700
APTGEGDELS GQEDAFRSWA VQTFRAACET FDVRSKHCIQ IPKRYTSNAT
710 720 730 740 750
WEPEQYKLTQ SPESLDLNKA LSSIHAKNVF TMRLKSLQNL QSEKSSRTTL
760 770 780 790 800
LVQLTFEGSR GPSYLPGEHL GIFPGNQTAL VQGILERVVD CSSPDQTVCL
810 820 830 840 850
EVLDESGSYW VKDKRLPPCS LRQALTYFLD ITTPPTQLQL HKLARFATEE
860 870 880 890 900
THRQRLEALC QPSEYNDWKF SNNPTFLEVL EEFPSLRVPA AFLLSQLPIL
910 920 930 940 950
KPRYYSISSS QDHTPSEVHL TVAVVTYRTR DGQGPLHHGV CSTWINNLKP
960 970 980 990 1000
EDPVPCFVRS VSGFQLPEDP SQPCILIGPG TGIAPFRSFW QQRLHDSQHR
1010 1020 1030 1040 1050
GLKGGRMTLV FGCRHPEEDH LYQEEMQEMV RKGVLFQVHT GYSRLPGKPK
1060 1070 1080 1090 1100
VYVQDILQKE LADEVFSVLH GEQGHLYVCG DVRMARDVAT TLKKLVAAKL
1110 1120 1130 1140
NLSEEQVEDY FFQLKSQKRY HEDIFGAVFS YGAKKGNTLE EPKGTRL
Length:1,147
Mass (Da):130,628
Last modified:October 1, 1996 - v2
Checksum:i77C77432DD8AB0A9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101R → K in BAA07994 (Ref. 7) Curated
Sequence conflicti72 – 721H → Y in BAA03138 (PubMed:7680561).Curated
Sequence conflicti107 – 1071C → R in AAC13747 (PubMed:7513765).Curated
Sequence conflicti128 – 1281D → V in BAA12035 (PubMed:8913516).Curated
Sequence conflicti130 – 1301P → H in AAC13747 (PubMed:7513765).Curated
Sequence conflicti171 – 1711E → G in BAA12035 (PubMed:8913516).Curated
Sequence conflicti195 – 1951P → S in BAA12035 (PubMed:8913516).Curated
Sequence conflicti248 – 2481S → N in AAC83553 (PubMed:9851365).Curated
Sequence conflicti248 – 2481S → T (PubMed:7513765).Curated
Sequence conflicti248 – 2481S → T (PubMed:7682072).Curated
Sequence conflicti264 – 2641Y → I in AAC13747 (PubMed:7513765).Curated
Sequence conflicti271 – 2711D → A in AAC83554 (PubMed:9851365).Curated
Sequence conflicti277 – 2771D → E in AAC13747 (PubMed:7513765).Curated
Sequence conflicti348 – 3481A → P in BAA03138 (PubMed:7680561).Curated
Sequence conflicti349 – 3491V → A in CAA54208 (PubMed:7519448).Curated
Sequence conflicti380 – 3801F → L (PubMed:7540573).Curated
Sequence conflicti380 – 3801F → L (Ref. 7) Curated
Sequence conflicti380 – 3801F → L (PubMed:8913516).Curated
Sequence conflicti380 – 3801F → L in AAC83553 (PubMed:9851365).Curated
Sequence conflicti380 – 3801F → L in AAC83554 (PubMed:9851365).Curated
Sequence conflicti395 – 3951R → S in BAA02090 (PubMed:7693462).Curated
Sequence conflicti399 – 3991E → G in AAC83553 (PubMed:9851365).Curated
Sequence conflicti412 – 4121V → A in AAC13747 (PubMed:7513765).Curated
Sequence conflicti477 – 4771M → I (Ref. 13) Curated
Sequence conflicti513 – 5131T → R in AAB18620 (Ref. 11) Curated
Sequence conflicti515 – 5151L → W in AAB31028 (PubMed:7516453).Curated
Sequence conflicti545 – 5451G → R in AAB31028 (PubMed:7516453).Curated
Sequence conflicti551 – 5511A → R in AAB18620 (Ref. 11) Curated
Sequence conflicti556 – 5561A → S in AAB31028 (PubMed:7516453).Curated
Sequence conflicti559 – 5591S → T in AAC83553 (PubMed:9851365).Curated
Sequence conflicti559 – 5591S → T in AAC83554 (PubMed:9851365).Curated
Sequence conflicti564 – 5641T → N in AAB31028 (PubMed:7516453).Curated
Sequence conflicti570 – 5701E → D in AAB31028 (PubMed:7516453).Curated
Sequence conflicti583 – 5831L → P (PubMed:7682072).Curated
Sequence conflicti583 – 5831L → P (PubMed:9535415).Curated
Sequence conflicti591 – 5911G → A in AAB31028 (PubMed:7516453).Curated
Sequence conflicti591 – 5911G → V (PubMed:7680561).Curated
Sequence conflicti591 – 5911G → V (PubMed:7519448).Curated
Sequence conflicti619 – 6191A → R in AAA85861 (PubMed:7540573).Curated
Sequence conflicti640 – 6401Q → P in AAC83553 (PubMed:9851365).Curated
Sequence conflicti664 – 6641D → G in AAB18620 (Ref. 11) Curated
Sequence conflicti679 – 6802ET → VP in BAA03138 (PubMed:7680561).Curated
Sequence conflicti690 – 6901Q → P in AAB18620 (Ref. 11) Curated
Sequence conflicti711 – 7111S → N in AAB18620 (Ref. 11) Curated
Sequence conflicti714 – 7152SL → TR in AAB18620 (Ref. 11) Curated
Sequence conflicti714 – 7141S → P (PubMed:7540573).Curated
Sequence conflicti714 – 7141S → P (Ref. 7) Curated
Sequence conflicti714 – 7141S → P (PubMed:8913516).Curated
Sequence conflicti714 – 7141S → P in AAC83553 (PubMed:9851365).Curated
Sequence conflicti714 – 7141S → P in AAC83554 (PubMed:9851365).Curated
Sequence conflicti714 – 7141S → P in AAC16401 (PubMed:9535415).Curated
Sequence conflicti719 – 7191K → R in AAB18620 (Ref. 11) Curated
Sequence conflicti721 – 7211L → P (PubMed:7519448).Curated
Sequence conflicti722 – 7221S → R (PubMed:7680561).Curated
Sequence conflicti722 – 7221S → R (PubMed:7519448).Curated
Sequence conflicti722 – 7221S → R (Ref. 11) Curated
Sequence conflicti724 – 7263IHA → FLN (Ref. 11) Curated
Sequence conflicti730 – 7301F → I in AAB18620 (Ref. 11) Curated
Sequence conflicti731 – 7311T → A in AAC83553 (PubMed:9851365).Curated
Sequence conflicti740 – 7401L → P in CAA54208 (PubMed:7519448).Curated
Sequence conflicti779 – 7791A → G in AAC13747 (PubMed:7513765).Curated
Sequence conflicti834 – 8341P → S in BAA12035 (PubMed:8913516).Curated
Sequence conflicti844 – 8441A → G in BAA03138 (PubMed:7680561).Curated
Sequence conflicti895 – 8951S → L in BAA02090 (PubMed:7693462).Curated
Sequence conflicti911 – 9111Q → L in AAC13747 (PubMed:7513765).Curated
Sequence conflicti925 – 9251V → D in BAA12035 (PubMed:8913516).Curated
Sequence conflicti937 – 9371H → N in AAC83554 (PubMed:9851365).Curated
Sequence conflicti999 – 9991H → R (PubMed:7540573).Curated
Sequence conflicti999 – 9991H → R (Ref. 7) Curated
Sequence conflicti999 – 9991H → R in AAC83553 (PubMed:9851365).Curated
Sequence conflicti999 – 9991H → R in AAC83554 (PubMed:9851365).Curated
Sequence conflicti1008 – 10092TL → NF in AAC83554 (PubMed:9851365).Curated
Sequence conflicti1016 – 10161P → R (PubMed:7682072).Curated
Sequence conflicti1016 – 10161P → S (PubMed:8913516).Curated
Sequence conflicti1017 – 10171E → R (PubMed:7682072).Curated
Sequence conflicti1017 – 10171E → R (PubMed:8913516).Curated
Sequence conflicti1024 – 10241E → K in AAC83554 (PubMed:9851365).Curated
Sequence conflicti1076 – 10761L → I in AAC83553 (PubMed:9851365).Curated
Sequence conflicti1084 – 10841M → I in CAA54208 (PubMed:7519448).Curated
Sequence conflicti1129 – 11291F → V in AAC83554 (PubMed:9851365).Curated
Sequence conflicti1133 – 11331A → V (PubMed:7540573).Curated
Sequence conflicti1133 – 11331A → V (Ref. 7) Curated
Sequence conflicti1133 – 11331A → V in AAC83553 (PubMed:9851365).Curated
Sequence conflicti1133 – 11331A → V in AAC83554 (PubMed:9851365).Curated
Sequence conflicti1138 – 11381T → A (PubMed:7540573).Curated
Sequence conflicti1138 – 11381T → A (Ref. 7) Curated
Sequence conflicti1138 – 11381T → A in AAC83553 (PubMed:9851365).Curated
Sequence conflicti1138 – 11381T → A in AAC83554 (PubMed:9851365).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

DIPiDIP-59942N.

Chemistry

BindingDBiQ06518.
ChEMBLiCHEMBL3051.

PTM databases

PhosphoSiteiQ06518.

Proteomic databases

PRIDEiQ06518.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24599.
KEGGirno:24599.

Organism-specific databases

CTDi4843.
RGDi3185. Nos2.

Phylogenomic databases

eggNOGiCOG4362.
HOVERGENiHBG000159.
InParanoidiQ06518.
KOiK13241.
PhylomeDBiQ06518.

Enzyme and pathway databases

BRENDAi1.14.13.39. 5301.

Miscellaneous databases

NextBioi603804.
PROiQ06518.

Gene expression databases

GenevisibleiQ06518. RN.

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.
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]
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]
ProtoNetiSearch...

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: June 24, 2015
This is version 158 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 thought to originate from human but appears to be from rat.1 Publication

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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.