O54705 (NOS2_CAVPO) 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
NOS type II
Peptidyl-cysteine S-nitrosylase NOS2

Gene names

Name:	NOS2
Synonyms:	NOS

Organism

Cavia porcellus (Guinea pig) [Reference proteome]

Taxonomic identifier

10141 [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 › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	1149 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. 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.
Subunit structure	Homodimer. Binds SLC9A3R1 By similarity.
Tissue specificity	Expressed in the lung and colon. Not detected in the heart, aorta, liver, kidney, and spleen.
Induction	By lipopolysaccharide (LPS); in kidney, spleen, and colon. Expression is reduced in the presence of LPS in lung.
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	defense response to bacterium Inferred from sequence or structural similarity. Source: UniProtKB nitric oxide biosynthetic process Inferred from electronic annotation. Source: InterPro peptidyl-cysteine S-nitrosylation Inferred from sequence or structural similarity. Source: UniProtKB superoxide metabolic process 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 – 1149	1149	Nitric oxide synthase, inducible		PRO_0000170929
Regions
	Domain	538 – 676	139	Flavodoxin-like
	Domain	729 – 969	241	FAD-binding FR-type
	Nucleotide binding	622 – 653	32	FMN By similarity
	Nucleotide binding	766 – 777	12	FAD By similarity
	Nucleotide binding	902 – 912	11	FAD By similarity
	Nucleotide binding	977 – 995	19	NADP By similarity
	Nucleotide binding	1075 – 1090	16	NADP By similarity
	Region	508 – 528	21	Calmodulin-binding Potential
Sites
	Metal binding	199	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O54705 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 66D595A2486DB50E	FASTA	1,149	130,632
	10 20 30 40 50 60 MACPWNFLWK LKSSRYDLTE EKDINNNVGK ASHLYSPEIQ DDPKYCSPGK HQNGSSQSLT 70 80 90 100 110 120 GTAKKVPESQ SKPHKPSPTC SQHMKIKNWG NGMILQDTLH TKAKTNFTCK PKSCLGSVMN 130 140 150 160 170 180 PRSMTRGPRD TPIPPDELLP QAIEFVNQYY DSFKEAKIEE YLARVETVTK EIETTGTYQL 190 200 210 220 230 240 TGDELIFATK LAWRNAPRCI GRIQWSNLQV FDARSCHTAQ EMFEHICRHV RYSTNNGNIR 250 260 270 280 290 300 SAITVFPQRT DGKHDFRVWN AQLIRYAGYQ MPDGTIQGDP ANLEFTQLCI DLGWKPRYGR 310 320 330 340 350 360 FDVLPLILQA DGRDPELFEI PPDLVLEVPM EHPKYEWFQD LGLKWYALPA VANMLLEVGG 370 380 390 400 410 420 LEFPACPFNG WYMGTEIGVR DFCDAQRYNI LEEVGRRMGL ETHTLASLWK DRAVTEINVA 430 440 450 460 470 480 VLHSFQKQNV TIMDHHSAAE SFMKHMQNEY RARGGCPADW IWLVPPISGS ITPVFHQEML 490 500 510 520 530 540 NYILSPFYYY QVEAWKTHVW QDETRRPKRR EIPFRVLAKA TLFASLLMRK MMASRVRATI 550 560 570 580 590 600 LFATETGKSE ALAQDLGALF SCAFNPKVLC MDQYQLSSLE EEKLLLVVTS TFGNGDCPGN 610 620 630 640 650 660 GETLKKSLFV LKKLTNTFRY AVFGLGSSMY PRFCAFAHDI DIKLSQLGAS QLTPVGEGDE 670 680 690 700 710 720 LSGQEDAFCT WAVQTFQAAC AAFDVRGRHH ITIPKRYTSS VTWEPYHYRL VQDSQPLDLN 730 740 750 760 770 780 KALSRMHATD VFTMRLKSQK NLQSPKSSRT TLLMELSCDD SRSLAYLPGE HLGVFPCNQP 790 800 810 820 830 840 ALVQGILECV VDNPGPHHTV CLEVLDDSGS YWAKDKRLPP CSLSQALTYF LDITTPPTQL 850 860 870 880 890 900 QLQKLARLAT EQAERLRLES LSQPSEYNKW KFTNSPTFLE VLEEFPSLRV PAAFLLSQLP 910 920 930 940 950 960 ILKPRYYSIS SSLDHTPAEV HLTVAVVTYR TRDGRGPLHH GVCSTWFSGL KPQDPVPCLV 970 980 990 1000 1010 1020 RSVNSFQLPK DPSQPCILIG PGTGIAPFRS FWQQRLHNLK HTGLQGGRMT LLFGCRHPEE 1030 1040 1050 1060 1070 1080 DHIYKEEMQE MVQKGVLHEV HTAYSRLPGK PKAYVQDILR QQLAREVLRV LHEEPGHLYV 1090 1100 1110 1120 1130 1140 CGNVLMAQDV ACTLKQLLAA KLNLNEEQVE DYFFQLKSQK RYHEDIFGAV FPHGVKKDRA ERPPGDDKL

References

[1]

"Molecular cloning and characterization of Ca2+-dependent inducible nitric oxide synthase from guinea-pig lung." Shirato M., Sakamoto T., Uchida Y., Nomura A., Ishii Y., Iijima H., Goto Y., Hasegawa S. Biochem. J. 333:795-799(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Hartley. Tissue: Lung.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF027180 mRNA. Translation: AAC33177.1.
RefSeq	NP_001166455.1. NM_001172984.1.
3D structure databases
ProteinModelPortal	O54705.
SMR	O54705. Positions 82-501, 702-1129.
ModBase	Search...
Protein-protein interaction databases
STRING	10141.ENSCPOP00000017277.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100135576.
Organism-specific databases
CTD	4843.
Phylogenomic databases
eggNOG	COG4362.
HOGENOM	HOG000220884.
HOVERGEN	HBG000159.
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...

Entry information

Entry name

NOS2_CAVPO

Accession

Primary (citable) accession number: O54705

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	April 3, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program