ID NOS2_CAPHI Reviewed; 110 AA. AC Q28314; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 25-NOV-2008, entry version 56. DE RecName: Full=Nitric oxide synthase, inducible; DE EC=1.14.13.39; DE AltName: Full=Inducible NO synthase; DE Short=Inducible NOS; DE Short=iNOS; DE AltName: Full=NOS type II; DE Flags: Fragment; GN Name=NOS2; OS Capra hircus (Goat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Capra. OX NCBI_TaxID=9925; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Peripheral blood monocyte; RX MEDLINE=96183637; PubMed=8603979; RA Adler H., Adler B., Peveri P., Werner E.R., Wachter H., Peterhans E., RA Jungi T.W.; RT "Differential regulation of inducible nitric oxide synthase production RT in bovine and caprine macrophages."; RL J. Infect. Dis. 173:971-978(1996). CC -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule CC with diverse functions throughout the body. CC -!- CATALYTIC ACTIVITY: L-arginine + n NADPH + m O(2) = citrulline + CC nitric oxide + n NADP(+). CC -!- COFACTOR: Heme group (By similarity). CC -!- COFACTOR: Binds 1 FAD (By similarity). CC -!- COFACTOR: Binds 1 FMN (By similarity). CC -!- COFACTOR: Metrahydrobiopterin (BH4). May stabilize the dimeric CC form of the enzyme (By similarity). CC -!- ENZYME REGULATION: Regulated by calcium/calmodulin (By CC similarity). CC -!- SUBUNIT: Homodimer. Binds SLC9A3R1 (By similarity). CC -!- INDUCTION: By lipopolysaccharide (LPS). CC -!- SIMILARITY: Belongs to the NOS family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U29085; AAB02338.1; -; mRNA. DR HSSP; P35228; 4NOS. DR SMR; Q28314; 1-110. DR HOVERGEN; Q28314; -. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0004517; F:nitric-oxide synthase activity; IEA:InterPro. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR004030; NO_synthase_oxygenase_reg. DR Gene3D; G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 1. DR Pfam; PF02898; NO_synthase; 1. DR PROSITE; PS60001; NOS; 1. PE 2: Evidence at transcript level; KW Calcium; Calmodulin-binding; FAD; FMN; Heme; Iron; Metal-binding; KW NADP; Oxidoreductase. FT CHAIN <1 >110 Nitric oxide synthase, inducible. FT /FTId=PRO_0000170928. FT METAL 35 35 Iron (heme axial ligand) (By similarity). FT NON_TER 1 1 FT NON_TER 110 110 SQ SEQUENCE 110 AA; 12654 MW; D72188FB257EC518 CRC64; VEAVTKEIET TGTYQLTGDE LIFATKQAWR NAPRCIGRIQ WSNLQVFDAR SCSTAQEMFE HICRHVRYAT NNGNIRSAIT VFPQRSDGKH DFRVWNAQLI RYAGYQMPDG //