NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Endothelial cell;
DOI=10.1016/S0165-3806(98)00145-X; PubMed=9838160 [NCBI, ExPASy, EBI, Israel, Japan]
Aguan K., Murotsuki J., Gagnon R., Thompson L.P., Weiner C.P.;
"Effect of chronic hypoxemia on the regulation of nitric-oxide synthase in the fetal sheep brain.";
Brain Res. Dev. Brain Res. 111:271-277(1998).

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 hypoxemia in fetal brain.
SIMILARITY: Belongs to the NOS family.

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

U76736; AAB40703.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P29474; 1M9M. [HSSP ENTRY / PDB]

SMR

P97270; 1-98.

ModBase

P97270.

Family and domain databases

InterPro

IPR004030; NO_synthase_oxygenase_reg.
Graphical view of domain structure.

Pfam

PF02898; NO_synthase; 1.
Pfam graphical view of domain structure.

PROSITE

PS60001; NOS; PARTIAL.

BLOCKS

P97270.

Phylogenomic databases

HOVERGEN

P97270; -.

Other

ProtoNet

P97270.

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; Membrane; Metal-binding; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >100`	`>100`	`Nitric oxide synthase, endothelial.`	`PRO_0000170942`
`NON_TER`	`1 1`
`NON_TER`	`100 100`

Sequence information

Length: 100 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 11271 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 867D7F89F4B132A8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
WYMSTEIGTR NLCDPHRYNI LEDVAVCMDL DTRTTSSLWK DKAAVEINVA VLHSYQLAKV 

        70         80         90        100 
TIVDHHAATV SFMKHLENEQ KGRGGCPADW GWDPCPPSRA

P97270 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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