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Q9TUX8

- NOS3_CANFA

UniProt

Q9TUX8 - NOS3_CANFA

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Protein

Nitric oxide synthase, endothelial

Gene

NOS3

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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.By similarity

Catalytic activityi

2 L-arginine + 3 NADPH + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O.

Cofactori

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.By similarity

Enzyme regulationi

Stimulated by calcium/calmodulin. Inhibited by NOSIP and NOSTRIN By similarity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi96 – 961ZincBy similarity
Metal bindingi101 – 1011ZincBy similarity
Metal bindingi186 – 1861Iron (heme axial ligand)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi651 – 68232FMNPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi795 – 80612FADBy similarityAdd
BLAST
Nucleotide bindingi937 – 94711FADBy similarityAdd
BLAST
Nucleotide bindingi1012 – 103019NADPBy similarityAdd
BLAST
Nucleotide bindingi1110 – 112516NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. FMN binding Source: InterPro
  3. heme binding Source: InterPro
  4. iron ion binding Source: InterPro
  5. NADP binding Source: InterPro
  6. nitric-oxide synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. nitric oxide biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Calmodulin-binding, FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Nitric oxide synthase, endothelial (EC:1.14.13.39)
Alternative name(s):
Constitutive NOS
Short name:
cNOS
EC-NOS
Endothelial NOS
Short name:
eNOS
NOS type III
Short name:
NOSIII
Gene namesi
Name:NOS3
Synonyms:NOS
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

Membranecaveola By similarity. Cytoplasmcytoskeleton By similarity. Golgi apparatus By similarity. Cell membrane 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

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-KW
  2. Golgi apparatus Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 12051204Nitric oxide synthase, endothelialPRO_0000289580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Lipidationi15 – 151S-palmitoyl cysteineBy similarity
Lipidationi26 – 261S-palmitoyl cysteineBy similarity
Modified residuei116 – 1161Phosphoserine; by CDK5By similarity
Modified residuei143 – 1431PhosphoserineBy similarity
Modified residuei497 – 4971Phosphothreonine; by AMPKBy similarity
Modified residuei635 – 6351PhosphoserineBy similarity
Modified residuei1177 – 11771PhosphothreonineBy similarity
Modified residuei1179 – 11791Phosphoserine; by AMPKBy similarity

Post-translational modificationi

Phosphorylation by AMPK at Ser-1179 in the presence of Ca2+-calmodulin (CaM) activates activity. In absence of Ca2+-calmodulin, AMPK also phosphorylates Thr-497, resulting in inhibition of activity. Phosphorylation of Ser-116 by CDK5 reduces activity By similarity.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Interactioni

Subunit structurei

Homodimer. Interacts with NOSIP and NOSTRIN By similarity.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000006985.

Structurei

3D structure databases

ProteinModelPortaliQ9TUX8.
SMRiQ9TUX8. Positions 67-482, 731-1164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini522 – 705184Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini758 – 1004247FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 488389Interaction with NOSIPBy similarityAdd
BLAST
Regioni492 – 51221Calmodulin-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the NOS family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG4362.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
InParanoidiQ9TUX8.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 2 hits.
3.90.340.10. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR012144. NOS_euk.
IPR004030. NOS_N.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF000333. NOS. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9TUX8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPTSEPSR APALAPPPSP
60 70 80 90 100
PPAPDHSSPP LTRPPDGPKF PRVKNWEVGS ITYDTLSAQS QQDGPCTPRR
110 120 130 140 150
CLGSLVFPRK LQSRPSQNPA PPEQLLSQAR DFISQYYSSI KRSGSQAHEQ
160 170 180 190 200
RLQEVEAEVA ATGTYQLRES ELVFGAKQAW RNAPRCVGRI QWGKLQVFDA
210 220 230 240 250
RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRASGR GDFRIWNSQL
260 270 280 290 300
VRYAGYRQQD GSVRGDPANV EITELCIQHG WTPGNGRFDV LPLLLQAPDE
310 320 330 340 350
PPELFALPPE LVLEVPLEHP TLEWFAALGL RWYALPAVSN MLLEIGGLEF
360 370 380 390 400
PAAPFSGWYM STEIGTRNLC DPHRYNILED VAVCMDLDTR TTSSLWKDKA
410 420 430 440 450
AVEINLAVLH SYQLAKVTIV DHHAATASFM KHLENEQKAR GGCPADWAWI
460 470 480 490 500
VPPISGSLTP VFHQEMVNYV LSPAFRYQTD PWKGSASKGA GVTRKKTFKE
510 520 530 540 550
VANAVKISAS LMGTVMAKRV KATILYGSET GRAQSYAQQL GRLFRKAFDP
560 570 580 590 600
RVLCMDEYDV VSLEHETLVL VVTSTFGNGD PPENGESFAA ALMEMSGSYN
610 620 630 640 650
SSPRPEQHKS YKIRFNSVSC SDPLVSSWRR KRKESRNTDS AGALGTLRFC
660 670 680 690 700
VFGLGSRAYP HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFGGW
710 720 730 740 750
AQAAFQASWE TFCVGEDAKA AARDIFSPKR TWKRQRYRLS AQAEGLQLLP
760 770 780 790 800
GLIHVHRRKM VQATVLAVEN LQSSKSTRAT ILVRLDTGSQ EALQYQPGDH
810 820 830 840 850
IGICPPNRPG LVEALLSRVE DPPPPGEPVA VEQLEKGSPG GPPPSWVRDP
860 870 880 890 900
RLPPCTLRQA LTFFLDITSP PSPQLLRLLS TLAEESSEQQ ELESLSQDPR
910 920 930 940 950
RYEEWKWFRC PTLLEVLEQF PSVALPAPLL LTQLPLLQPR YYSVSSAPSA
960 970 980 990 1000
HPGEIHLTVA VLAYRTQDGL GPLHYGVCST WLSQLKAGDP VPCFIRGAPS
1010 1020 1030 1040 1050
FRLPPDPSLP CILVGPGTGI APFRGFWQGR LHDIYSKGLQ PAPMTLVFGC
1060 1070 1080 1090 1100
RCSQLDHLYR DEVQDAQQRG VFGRVLTAFS REPDSPKTYV QDILRTELAA
1110 1120 1130 1140 1150
EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGDME LDEAGDVIGV
1160 1170 1180 1190 1200
LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWALDPPGP

DTVGP
Length:1,205
Mass (Da):133,046
Last modified:May 1, 2000 - v1
Checksum:iC150CDEB01685BA5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF143503 mRNA. Translation: AAD52161.1.
UniGeneiCfa.108.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF143503 mRNA. Translation: AAD52161.1 .
UniGenei Cfa.108.

3D structure databases

ProteinModelPortali Q9TUX8.
SMRi Q9TUX8. Positions 67-482, 731-1164.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9615.ENSCAFP00000006985.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG4362.
HOGENOMi HOG000220884.
HOVERGENi HBG000159.
InParanoidi Q9TUX8.

Miscellaneous databases

NextBioi 20817281.

Family and domain databases

Gene3Di 1.20.990.10. 1 hit.
3.40.50.360. 2 hits.
3.90.340.10. 1 hit.
InterProi IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR012144. NOS_euk.
IPR004030. NOS_N.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000333. NOS. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMi SSF52218. SSF52218. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Assembly and characterization of canine heart endothelial nitric oxide synthase cDNA and 5'-flanking sequence by homology (RT-)PCR cloning."
    Schwemmer M., Bassenge E.
    Nitric Oxide 3:254-264(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.

Entry informationi

Entry nameiNOS3_CANFA
AccessioniPrimary (citable) accession number: Q9TUX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3