[1]	NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. TISSUE=Pulmonary artery; DOI=10.1016/S0305-0491(96)00288-X; PubMed=9149402 [NCBI, ExPASy, EBI, Israel, Japan] Zhang J., Patel J.M., Block E.R.; "Molecular cloning, characterization and expression of a nitric oxide synthase from porcine pulmonary artery endothelial cells."; Comp. Biochem. Physiol. 116B:485-491(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 1032-1205. Patel J.M., Block E.R.; Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets (By similarity).
CATALYTIC ACTIVITY: L-arginine + n NADPH + m O₂ = citrulline + nitric oxide + n NADP⁺.
COFACTOR: Heme group (By similarity).
COFACTOR: Binds 1 FAD (By similarity).
COFACTOR: Binds 1 FMN (By similarity).
COFACTOR: Metrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme (By similarity).
ENZYME REGULATION: Stimulated by calcium/calmodulin. Inhibited by NOSIP and NOSTRIN (By similarity).
SUBUNIT: Homodimer. Interacts with NOSIP and NOSTRIN (By similarity).
SUBCELLULAR LOCATION: Cell membrane, caveola (By similarity). Cytoplasm, cytoskeleton (By similarity). Golgi apparatus (By similarity). Note=Specifically associates with actin cytoskeleton in the G2 phase of the cell cycle; which is favored by interaction with NOSIP and results in a reduced enzymatic activity (By similarity).
INDUCTION: Repressed by proinflammatory cytokines.
SIMILARITY: Belongs to the NOS family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U59924; AAB39539.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33832; AAA84933.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_999460.1; -.

UniGene

Ssc.16364

3D structure databases

HSSP

P29473; 1D0C. [HSSP ENTRY / PDB]

SMR

Q28969; 67-482.

ModBase

Q28969.

Family and domain databases

InterPro

IPR003097; FAD-binding_1.
IPR008254; Flavodoxin/NO_synth.
IPR004030; NO_synthase_oxygenase_reg.
IPR012144; NOS.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 1.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
PF02898; NO_synthase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000333; NOS; 1.

PROSITE

PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PS60001; NOS; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q28969.

Genome annotation databases

GeneID

397557; -.

KEGG

ssc:397557; -.

Phylogenomic databases

HOVERGEN

Q28969; -.

Other

ProtoNet

Q28969.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton; FAD; FMN; Golgi apparatus; Heme; Iron; Lipoprotein; Membrane; Metal-binding; Myristate; NADP; Oxidoreductase; Palmitate; Phosphoprotein; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 1205`	`1204`	`Nitric oxide synthase, endothelial.`	`PRO_0000170945`
`DOMAIN`	`522 705`	`184`	`Flavodoxin-like.`
`DOMAIN`	`758 1004`	`247`	`FAD-binding FR-type.`
`NP_BIND`	`651 682`	`32`	`FMN (By similarity).`
`NP_BIND`	`795 806`	`12`	`FAD (By similarity).`
`NP_BIND`	`937 947`	`11`	`FAD (By similarity).`
`NP_BIND`	`1012 1030`	`19`	`NADP (By similarity).`
`NP_BIND`	`1110 1125`	`16`	`NADP (By similarity).`
`REGION`	`100 488`	`389`	`Interaction with NOSIP (By similarity).`
`REGION`	`492 512`	`21`	`Calmodulin-binding (Potential).`
`METAL`	`96 96`		`Zinc (By similarity).`
`METAL`	`101 101`		`Zinc (By similarity).`
`METAL`	`186 186`		`Iron (heme axial ligand) (By similarity).`
`MOD_RES`	`83 83`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`497 497`		`Phosphothreonine (By similarity).`
`MOD_RES`	`635 635`		`Phosphoserine (By similarity).`
`MOD_RES`	`1177 1177`		`Phosphothreonine (By similarity).`
`MOD_RES`	`1179 1179`		`Phosphoserine (By similarity).`
`LIPID`	`2 2`		`N-myristoyl glycine (By similarity).`
`LIPID`	`15 15`		`S-palmitoyl cysteine (By similarity).`
`LIPID`	`26 26`		`S-palmitoyl cysteine (By similarity).`

Sequence information

Length: 1205 AA [This is the length of the unprocessed precursor]

Molecular weight: 133406 Da [This is the MW of the unprocessed precursor]

CRC64: C5B8B5E61AADAACF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PATPAPEPSR APAPATPHAP EHSPAPNSPT 

        70         80         90        100        110        120 
LTRPPEGPKF PRVKNWEVGS ITYDTLCAQS QQDGPCTPRR CLGSLVLPRK LQSRPSPGPP 

       130        140        150        160        170        180 
PAEQLLSQAR DFINQYYSSI KRSGSQAHEE RLQEVEAEVA TTGTYHLGES ELVFGAKQAW 

       190        200        210        220        230        240 
RNAPRCVGRI QWGKLQVFDA RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRTPGR 

       250        260        270        280        290        300 
GDFRIWNSQL VRYAGYRQQD GSVRGDPANV EITELCIQHG WTPGNGRFDV LPLLLQAPDE 

       310        320        330        340        350        360 
PPELFALPPE LVLEVPLEHP TLEWFAALGL RWYALPAVSN MLLEIGGLEF PAAPFSGWYM 

       370        380        390        400        410        420 
STEIGTRNLC DPHRYNILED VAVCMDLDTR TTSSLWKDKA AVEINLAVLH SYQLAKVTIV 

       430        440        450        460        470        480 
DHHAATASFM KHLENEQKAR GGCPADWAWI VPPISGSLTP VFHQEMVNYV LSPAFRYQPD 

       490        500        510        520        530        540 
PWKGSAAKGT GIARKKTFKE VANAVKISAS LMATVMPKRV KASILYASET VRAQSYAQQL 

       550        560        570        580        590        600 
GRLFRKAFDP RVLCMDEYDV VSLEHETLVL VVTSTFGNGD PPENGESFAA ALMEMSGPYN 

       610        620        630        640        650        660 
GSPRPEQHRS YKIRFNSVSC SDPLVSSWRR KRKESSNTDS AGALGTLRFC VFGLGSRAYP 

       670        680        690        700        710        720 
HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFRGW AQAAFQASCE TFCVGEDAKA 

       730        740        750        760        770        780 
AARDIFSPKR SWKRQRYRLS AQVEGLQLLP GLVHVHRRKM FQATVLSVEN LQSSKSTRAT 

       790        800        810        820        830        840 
ILVRLDTEGQ EGLQYQPGDH IGICPPNRTG LVEALLSRVE DPTPPTESVG VEQLEKGSPG 

       850        860        870        880        890        900 
GPPPSWVRDP RLPPYTLRQA LTFFLDITSP PSPRLLRVLS TLAEEPSEQQ ELETLSQDPR 

       910        920        930        940        950        960 
RYEEWKWFRC PTLLEVLEQF PSVALPTPLL LTQLALLQPR YYSVSSAPST YPGEIHPTVA 

       970        980        990       1000       1010       1020 
VLAYRTQDGL GPLHYGVCST WLGQLKPGDP VPCFIRAAPS FRLPPDPSLP CILVGPGTGI 

      1030       1040       1050       1060       1070       1080 
APFRGFWQER LHDIESKGLQ PAPMTLVFGC RCSQLDHLYR DEVQDAQQRG VFGRVLTAFS 

      1090       1100       1110       1120       1130       1140 
REPDSPKTYV QDILRTELAA EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGNME 

      1150       1160       1170       1180       1190       1200 
LDEAGDVIGV LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWTFDPPGP 


DTPGP

Q28969 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools