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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. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. 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. Involved in inflammation, enhances the synthesis of proinflammatory mediators such as IL6 and IL8.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)DescriptionActionsGraphical viewLength
Metal bindingi107ZincBy similarity1
Metal bindingi112ZincBy similarity1
Metal bindingi197Iron (heme axial ligand)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi620 – 651FMNPROSITE-ProRule annotationAdd BLAST32
Nucleotide bindingi764 – 775FADBy similarityAdd BLAST12
Nucleotide bindingi900 – 910FADBy similarityAdd BLAST11
Nucleotide bindingi975 – 993NADPBy similarityAdd BLAST19
Nucleotide bindingi1073 – 1088NADPBy similarityAdd BLAST16

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
  • metal ion binding Source: UniProtKB-KW
  • NADP binding Source: RGD
  • 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 cytokine stimulus Source: MGI
  • cellular response to interleukin-1 Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to lithium ion Source: RGD
  • cellular response to organic cyclic compound Source: MGI
  • 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
  • interleukin-6 secretion Source: UniProtKB
  • interleukin-8 secretion Source: UniProtKB
  • 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
  • prostaglandin secretion Source: UniProtKB
  • regulation of blood pressure Source: RGD
  • regulation of cytokine production involved in inflammatory response Source: UniProtKB
  • regulation of heart contraction Source: RGD
  • 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
Proteomesi
  • UP000002494 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...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3051.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001709371 – 1147Nitric oxide synthase, inducibleAdd BLAST1147

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei564PhosphothreonineCombined sources1
Modified residuei572PhosphotyrosineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ06518.
PRIDEiQ06518.

PTM databases

iPTMnetiQ06518.
PhosphoSitePlusiQ06518.

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).

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

GO - Molecular functioni

  • actin binding Source: RGD
  • beta-catenin binding Source: RGD
  • cadherin binding Source: RGD
  • Hsp90 protein binding Source: RGD
  • nitric-oxide synthase binding Source: RGD
  • protein homodimerization activity Source: RGD
  • protein kinase binding Source: RGD

Protein-protein interaction databases

DIPiDIP-59942N.
STRINGi10116.ENSRNOP00000067662.

Chemistry databases

BindingDBiQ06518.

Structurei

3D structure databases

ProteinModelPortaliQ06518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini536 – 674Flavodoxin-likePROSITE-ProRule annotationAdd BLAST139
Domaini727 – 967FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST241

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni506 – 526Calmodulin-bindingSequence analysisAdd BLAST21

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

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
COG4362. LUCA.
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-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
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)DescriptionActionsGraphical viewLength
Sequence conflicti10R → K in BAA07994 (Ref. 7) Curated1
Sequence conflicti72H → Y in BAA03138 (PubMed:7680561).Curated1
Sequence conflicti107C → R in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti128D → V in BAA12035 (PubMed:8913516).Curated1
Sequence conflicti130P → H in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti171E → G in BAA12035 (PubMed:8913516).Curated1
Sequence conflicti195P → S in BAA12035 (PubMed:8913516).Curated1
Sequence conflicti248S → N in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti248S → T (PubMed:7513765).Curated1
Sequence conflicti248S → T (PubMed:7682072).Curated1
Sequence conflicti264Y → I in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti271D → A in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti277D → E in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti348A → P in BAA03138 (PubMed:7680561).Curated1
Sequence conflicti349V → A in CAA54208 (PubMed:7519448).Curated1
Sequence conflicti380F → L (PubMed:7540573).Curated1
Sequence conflicti380F → L (Ref. 7) Curated1
Sequence conflicti380F → L (PubMed:8913516).Curated1
Sequence conflicti380F → L in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti380F → L in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti395R → S in BAA02090 (PubMed:7693462).Curated1
Sequence conflicti399E → G in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti412V → A in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti477M → I (Ref. 13) Curated1
Sequence conflicti513T → R in AAB18620 (Ref. 11) Curated1
Sequence conflicti515L → W in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti545G → R in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti551A → R in AAB18620 (Ref. 11) Curated1
Sequence conflicti556A → S in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti559S → T in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti559S → T in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti564T → N in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti570E → D in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti583L → P (PubMed:7682072).Curated1
Sequence conflicti583L → P (PubMed:9535415).Curated1
Sequence conflicti591G → A in AAB31028 (PubMed:7516453).Curated1
Sequence conflicti591G → V (PubMed:7680561).Curated1
Sequence conflicti591G → V (PubMed:7519448).Curated1
Sequence conflicti619A → R in AAA85861 (PubMed:7540573).Curated1
Sequence conflicti640Q → P in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti664D → G in AAB18620 (Ref. 11) Curated1
Sequence conflicti679 – 680ET → VP in BAA03138 (PubMed:7680561).Curated2
Sequence conflicti690Q → P in AAB18620 (Ref. 11) Curated1
Sequence conflicti711S → N in AAB18620 (Ref. 11) Curated1
Sequence conflicti714 – 715SL → TR in AAB18620 (Ref. 11) Curated2
Sequence conflicti714S → P (PubMed:7540573).Curated1
Sequence conflicti714S → P (Ref. 7) Curated1
Sequence conflicti714S → P (PubMed:8913516).Curated1
Sequence conflicti714S → P in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti714S → P in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti714S → P in AAC16401 (PubMed:9535415).Curated1
Sequence conflicti719K → R in AAB18620 (Ref. 11) Curated1
Sequence conflicti721L → P (PubMed:7519448).Curated1
Sequence conflicti722S → R (PubMed:7680561).Curated1
Sequence conflicti722S → R (PubMed:7519448).Curated1
Sequence conflicti722S → R (Ref. 11) Curated1
Sequence conflicti724 – 726IHA → FLN (Ref. 11) Curated3
Sequence conflicti730F → I in AAB18620 (Ref. 11) Curated1
Sequence conflicti731T → A in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti740L → P in CAA54208 (PubMed:7519448).Curated1
Sequence conflicti779A → G in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti834P → S in BAA12035 (PubMed:8913516).Curated1
Sequence conflicti844A → G in BAA03138 (PubMed:7680561).Curated1
Sequence conflicti895S → L in BAA02090 (PubMed:7693462).Curated1
Sequence conflicti911Q → L in AAC13747 (PubMed:7513765).Curated1
Sequence conflicti925V → D in BAA12035 (PubMed:8913516).Curated1
Sequence conflicti937H → N in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti999H → R (PubMed:7540573).Curated1
Sequence conflicti999H → R (Ref. 7) Curated1
Sequence conflicti999H → R in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti999H → R in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti1008 – 1009TL → NF in AAC83554 (PubMed:9851365).Curated2
Sequence conflicti1016P → R (PubMed:7682072).Curated1
Sequence conflicti1016P → S (PubMed:8913516).Curated1
Sequence conflicti1017E → R (PubMed:7682072).Curated1
Sequence conflicti1017E → R (PubMed:8913516).Curated1
Sequence conflicti1024E → K in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti1076L → I in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti1084M → I in CAA54208 (PubMed:7519448).Curated1
Sequence conflicti1129F → V in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti1133A → V (PubMed:7540573).Curated1
Sequence conflicti1133A → V (Ref. 7) Curated1
Sequence conflicti1133A → V in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti1133A → V in AAC83554 (PubMed:9851365).Curated1
Sequence conflicti1138T → A (PubMed:7540573).Curated1
Sequence conflicti1138T → A (Ref. 7) Curated1
Sequence conflicti1138T → A in AAC83553 (PubMed:9851365).Curated1
Sequence conflicti1138T → A in AAC83554 (PubMed:9851365).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59942N.
STRINGi10116.ENSRNOP00000067662.

Chemistry databases

BindingDBiQ06518.
ChEMBLiCHEMBL3051.

PTM databases

iPTMnetiQ06518.
PhosphoSitePlusiQ06518.

Proteomic databases

PaxDbiQ06518.
PRIDEiQ06518.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24599.
KEGGirno:24599.

Organism-specific databases

CTDi4843.
RGDi3185. Nos2.

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
COG4362. LUCA.
HOVERGENiHBG000159.
InParanoidiQ06518.
KOiK13241.
PhylomeDBiQ06518.

Enzyme and pathway databases

BRENDAi1.14.13.39. 5301.

Miscellaneous databases

PROiQ06518.

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-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
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...

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: November 2, 2016
This is version 172 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

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 one 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.