Nitric oxide synthase, inducible - Bos taurus (Bovine)

Preferred order of sections

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
NOS type II
Short name=NOSII
Peptidyl-cysteine S-nitrosylase NOS2

Gene names

Name:

NOS2

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	1156 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity.
Catalytic activity	2 L-arginine + 3 NADPH + 4 O₂ = 2 L-citrulline + 2 nitric oxide + 3 NADP⁺ + 4 H₂O.
Cofactor	Heme group By similarity. Binds 1 FAD By similarity. Binds 1 FMN By similarity. Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme By similarity.
Enzyme regulation	Regulated by calcium/calmodulin By similarity.
Subunit structure	Homodimer. Binds SLC9A3R1 By similarity.
Sequence similarities	Belongs to the NOS family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Ligand	Calcium Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nitric oxide biosynthetic process Inferred from electronic annotation. Source: InterPro peptidyl-cysteine S-nitrosylation Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	FMN binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro nitric-oxide synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1156

1156

Nitric oxide synthase, inducible

PRO_0000170926

Regions

Domain

539 – 677

139

Flavodoxin-like

Domain

730 – 970

241

FAD-binding FR-type

Nucleotide binding

623 – 654

32

FMN By similarity

Nucleotide binding

767 – 778

12

FAD By similarity

Nucleotide binding

903 – 913

11

FAD By similarity

Nucleotide binding

978 – 996

19

NADP By similarity

Nucleotide binding

1076 – 1091

16

NADP By similarity

Region

509 – 529

21

Calmodulin-binding Potential

Sites

Metal binding

200

1

Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict

236

1

N → S in AAC48470. Ref.2

Sequence conflict

1068 – 1069

2

VL → AF in AAC48479. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q27995 [UniParc].

Last modified November 28, 2006. Version 3.
Checksum: 52A52C984462F692
Show »

FASTA

1,156

131,208

        10         20         30         40         50         60 
MACPWQFLFK IKSQKVDLAT ELDINNNVGK FYQPPSSPVT QDDPKRHSPG KHGNESPQPL 

        70         80         90        100        110        120 
TGTVKTSPES LSKLDAPPSA CPRHVRIKNW GSGVTFQDTL HQKAKGDLSC KSKSCLASIM 

       130        140        150        160        170        180 
NPKSLTIGPR DKPTPPDELL PQAIEFVNQY YGSFKEAKIE EHLARVEAVT KEIETTGTYQ 

       190        200        210        220        230        240 
LTGDELIFAT KQAWRNAPRC IGRIQWSNLQ VFDARSCSTA QEMFEHICRH VRYATNNGNI 

       250        260        270        280        290        300 
RSAITVFPQR SDGKHDFRVW NAQLIRYAGY QMPDGSIRGD PANVEFTQLC IDLGWKPKYG 

       310        320        330        340        350        360 
RFDVLPLVLQ ADGRDPELFE IPPDLVLEVP MEHPRYEWFR ELELKWYALP AVANMLLEVG 

       370        380        390        400        410        420 
GLEFPGCPFN GWYMGTEVGV RDFCDAQRYN ILEEVGRRMG LETHKVASLW KDRAVVEINV 

       430        440        450        460        470        480 
AVLHSFQKQN VTIMDHHSAA ESFMKYMQNE YRSRGGCPAD WIWLVPPISG SITPVFHQEM 

       490        500        510        520        530        540 
LNYVLSPFYY YQVEPWKTHV WQDERRRPQR REIRFKVLVK AVFFASVLMH KAMASRVRAT 

       550        560        570        580        590        600 
ILFATETGRS ETLAQDLGAL FSCAFNPKVL CMDQYQLSHL EEEQLLLVVT STFGNGDSPG 

       610        620        630        640        650        660 
NGEKLKKSLL MLKELTNTFR YAVFGLGSSM YPQFCAFAHD IDQKLSQLGA SQLAPTGEGD 

       670        680        690        700        710        720 
ELSGQEEAFR SWAVQTFKAA CETFDVSGKH HIEIPKLYTS NVTWDPQHYR LVQDSEPLDL 

       730        740        750        760        770        780 
NKALSSMHAK HVFTMRLKSQ QNLQSPKSSR TTLLVELSCE GSQAPSYLPG EHLGVFPCNQ 

       790        800        810        820        830        840 
PALVQGILER VVDGPAPHQP VRLETLCENG SYWVKDKRLP PCSLSQALTY FLDITTPPTQ 

       850        860        870        880        890        900 
LLLRKLAQLA TEEAEKQRLE TLCQPSDYNK WKFTNSPTFL EVLEEFPSLR VSASFLLSQL 

       910        920        930        940        950        960 
PILKPRYYSI SSSRDLTPTE IHLTVAVLTY RTRDGQGPLH HGVCSTWLSS LKPQDPVPCF 

       970        980        990       1000       1010       1020 
VRSASGFQLP EDRSRPCILI GPGTGIAPFR SFWQQRLHEA EHKGLQGGRM TLVFGCRRPE 

      1030       1040       1050       1060       1070       1080 
EDHLYWEEML EMARKGVLHE VHTAYSRLPD QPKVYVQDIL RQRLAGEVLR VLHEEQGHLY 

      1090       1100       1110       1120       1130       1140 
VCGDVRMARD VARTLKQLMA TALSLNEEQV EDYFFQLKNQ KRYHEDIFGA VFPYEVKKDG 

      1150 
AAGLPSNPRA PGAHRS

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References

[1]	"Cloning and characterization of bovine inducible nitric oxide synthase." Widdison S., Ashley G.R., Howard C.J., Coffey T.J. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Inducible nitric oxide synthase in cattle. Differential cytokine regulation of nitric oxide synthase in bovine and murine macrophages." Adler H., Frech B., Thoeny M., Pfister H., Peterhans E., Jungi T.W. J. Immunol. 154:4710-4718(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 166-275. Tissue: Bone marrow macrophage.
[3]	"Three members of the nitric oxide synthase II gene family (NOS2A, NOS2B, and NOS2C) colocalize to human chromosome 17." Bloch K.D., Wolfram J.R., Brown D.M., Roberts J.D. Jr., Zapol D.G., Lepore J.J., Filippov G., Thomas J.E., Jacob H.J., Bloch D.B. Genomics 27:526-530(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 987-1122. Tissue: Pulmonary artery.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ676956 mRNA. Translation: ABG74910.1. U14640 mRNA. Translation: AAC48470.2. U18331 mRNA. Translation: AAC48479.1.
IPI	IPI00710206.
PIR	I46074.
RefSeq	NP_001070267.1. NM_001076799.1.
UniGene	Bt.23126.
3D structure databases
ProteinModelPortal	Q27995.
SMR	Q27995. Positions 83-502, 703-1130.
ModBase	Search...
Proteomic databases
PRIDE	Q27995.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	282876.
KEGG	bta:282876.
Organism-specific databases
CTD	4843.
Phylogenomic databases
eggNOG	COG4362.
HOGENOM	HOG000220884.
HOVERGEN	HBG000159.
InParanoid	Q27995.
KO	K13241.
OrthoDB	EOG4D26P1.
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
NextBio	20806404.

Entry information

Entry name

NOS2_BOVIN

Accession

Primary (citable) accession number: Q27995
Secondary accession number(s): Q06Q84, Q27985

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 28, 2006
Last modified:	April 3, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents