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O19132

- NOS1_RABIT

UniProt

O19132 - NOS1_RABIT

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Protein

Nitric oxide synthase, brain

Gene

NOS1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR (By similarity).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • hemeBy similarity
  • FADBy similarityNote: Binds 1 FAD.By similarity
  • FMNBy similarityNote: Binds 1 FMN.By similarity
  • 5,6,7,8-tetrahydrobiopterinBy similarityNote: Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.By similarity

Enzyme regulationi

Stimulated by calcium/calmodulin. Inhibited by n-Nos-inhibiting protein (PIN) which may prevent the dimerization of the protein. Inhibited by NOSIP (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi421 – 4211Iron (heme axial ligand)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi887 – 91832FMNPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi1033 – 104412FADBy similarityAdd
BLAST
Nucleotide bindingi1176 – 118611FADBy similarityAdd
BLAST
Nucleotide bindingi1251 – 126919NADPBy similarityAdd
BLAST
Nucleotide bindingi1349 – 136416NADPBy 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

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nitric oxide synthase, brain (EC:1.14.13.39)
Alternative name(s):
Constitutive NOS
NC-NOS
NOS type I
Neuronal NOS
Short name:
N-NOS
Short name:
nNOS
Peptidyl-cysteine S-nitrosylase NOS1
bNOS
Gene namesi
Name:NOS1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

Cell membranesarcolemma By similarity; Peripheral membrane protein By similarity. Cell projectiondendritic spine By similarity
Note: In skeletal muscle, it is localized beneath the sarcolemma of fast-twitch muscle fiber by associating with the dystrophin glycoprotein complex. In neurons, enriched in dendritic spines (By similarity).By similarity

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14351435Nitric oxide synthase, brainPRO_0000170923Add
BLAST

Post-translational modificationi

Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and Hsp40 (in vitro).By similarity

Keywords - PTMi

Ubl conjugation

Interactioni

Subunit structurei

Homodimer. Interacts with DLG4; the interaction possibly being prevented by the association between NOS1 and CAPON. Forms a ternary complex with CAPON and RASD1. Forms a ternary complex with CAPON and SYN1. Interacts with ZDHHC23. Interacts with NOSIP; which may impair its synaptic location (By similarity). Interacts with HTR4. Interacts with VAC14 (By similarity). Interacts with SLC6A4 (By similarity). Interacts (via N-terminal domain) with DLG4 (via N-terminal tandem pair of PDZ domains) (By similarity).By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000020745.

Structurei

3D structure databases

ProteinModelPortaliO19132.
SMRiO19132. Positions 7-133, 304-722, 756-1419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 9983PDZPROSITE-ProRule annotationAdd
BLAST
Domaini761 – 941181Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini996 – 1243248FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 206206Interaction with NOSIPBy similarityAdd
BLAST
Regioni164 – 24683PIN (nNOS-inhibiting protein) bindingBy similarityAdd
BLAST
Regioni731 – 75121Calmodulin-bindingSequence AnalysisAdd
BLAST
Regioni756 – 77520Tetrahydrobiopterin-bindingBy similarityAdd
BLAST

Domaini

The PDZ domain in the N-terminal part of the neuronal isoform participates in protein-protein interaction, and is responsible for targeting nNos to synaptic membranes in muscles. Mediates interaction with VAC14 (By similarity).By similarity

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
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG4362.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
InParanoidiO19132.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
2.30.42.10. 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.
IPR001478. PDZ.
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.
PF00595. PDZ. 1 hit.
[Graphical view]
PIRSFiPIRSF000333. NOS. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF52218. 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.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O19132-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEEHVFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG
60 70 80 90 100
AAEQSGLIQA GDIILAVNGR PLVDLSYDSA LEVLRGVASE THVVLILRGP
110 120 130 140 150
EGFTTNLETT FTGDGTPKTI RVTQPLGAPT KAVDLSHQPP SAGKEQPRPV
160 170 180 190 200
DGAAGPGSWP QPTQGHGQEA GSPSRANGLA PRTSSQDPAK KSGWAGLQGS
210 220 230 240 250
GDKNELLKEI EPVLTLLAGG SKAVDGGGPA KAETRDTGVQ VDRDFDAKSH
260 270 280 290 300
KPLPLGVEND RVFSDLWGKG SAPVVLNNPY SEKEQPPASG KQSPTKNGSP
310 320 330 340 350
SKCPRFLKVK NWETDVVLTD TLHLKSTLET GCTEHICMGS IMFPSQHTRR
360 370 380 390 400
PEDIRTKEQL FPLAKEFIDQ YYSSIKRFGS KAHMERLEEV NKEIESTSTY
410 420 430 440 450
QLKDTELIYG AKHAWRNASR CVGRIQWSKL QVFDARDCTT AHGMFNYICN
460 470 480 490 500
HIKYATNKGN LRSAITIFPQ RTDGKHDFRV WNSQLIRYAG YKQPDGSTLG
510 520 530 540 550
DPANVQFTEI CIQQGWKPPR SRFDVLPLLL QANGNDPELF QIPPELVLEV
560 570 580 590 600
PIRHPKFEWF KDLGLKWYGL PAVSNMLLEI GGLEFSACPF SGWYMGTEIG
610 620 630 640 650
VRDYCDNSRY NILEEVAKKM NLDMRKTSSL WKDQALVEIN IAVLYSFQSD
660 670 680 690 700
KVTIVDHHSA TESFIKHMEN EYRCRGGCPA DWVWIVPPMS GSITPVFHQE
710 720 730 740 750
MLNYRLTPCF EYQPDPWNTH VWKGTNGTPT KRRAIGFKKL AEAVKFSAKL
760 770 780 790 800
MGQAMAKRVK ATILYATETG KSQAYAKTLC EIFKHAFDAK VMSMEEYDIV
810 820 830 840 850
HLEHETLVLV VTSTFGNGDP PENGEKFRCA LMEMRHPNSL QEERKSYKVR
860 870 880 890 900
FNSVSSYSDS RKSSGDGPDV RDHFESAGPL ANVRFSVFGL GSRAYPHFCA
910 920 930 940 950
FGHAVDTLLE ELGGERILKM REGDELCGQE EAFRTWAKKV FKAACDVFCV
960 970 980 990 1000
GDDVNIEKAN NSLISNDRSW KRNKFRLTYV AEAPGLTQGL SSVHKKRVSA
1010 1020 1030 1040 1050
ARLLSRQNLQ SPKSSRSTIF VRLHTNGSQE LQYQPGDHLG VFPGNHEDLV
1060 1070 1080 1090 1100
NALIERLEDA PPANQMVKVE LLEERNTALG VISNWKDEPR LPPCTVFQAF
1110 1120 1130 1140 1150
KYYLDITTPP TPLQLQQFAS LASNEKEKQR LLVLSKGLQE YEEWKWGKNP
1160 1170 1180 1190 1200
TIVEVLEEFP SIQMPATLLL TQLSLLQPRY YSISSSPDMY PDEVHLTVAI
1210 1220 1230 1240 1250
VSYHTRDGEG PIHHGVCSSW LNRIPADEVV PCFVRGAPSF RLPRNPQVPC
1260 1270 1280 1290 1300
ILVGPGTAFA PFRSFWQQRQ FDIQHKGMSP CPMVLVFGCR QSKIDHIYRE
1310 1320 1330 1340 1350
EALQAKNKGV FRELYTAYSR EPDKPKKYVQ DILQEQLAEQ VYRALKEQGG
1360 1370 1380 1390 1400
HIYVCGDVTM AADVLKAVQR IMAQQGKLSA EDAGVFISRL RDDNRYHEDI
1410 1420 1430
FGVTLRTYEV TNRLRSESIA FIEESKKDTD EVFSS
Length:1,435
Mass (Da):160,865
Last modified:January 1, 1998 - v1
Checksum:i3ED87ECDD83A7A5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91584 mRNA. Translation: AAB68663.1.
RefSeqiNP_001075854.1. NM_001082385.1.
UniGeneiOcu.2169.

Genome annotation databases

GeneIDi100009243.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91584 mRNA. Translation: AAB68663.1 .
RefSeqi NP_001075854.1. NM_001082385.1.
UniGenei Ocu.2169.

3D structure databases

ProteinModelPortali O19132.
SMRi O19132. Positions 7-133, 304-722, 756-1419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000020745.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009243.

Organism-specific databases

CTDi 4842.

Phylogenomic databases

eggNOGi COG4362.
HOGENOMi HOG000220884.
HOVERGENi HBG000159.
InParanoidi O19132.

Family and domain databases

Gene3Di 1.20.990.10. 1 hit.
2.30.42.10. 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.
IPR001478. PDZ.
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.
PF00595. PDZ. 1 hit.
[Graphical view ]
PIRSFi PIRSF000333. NOS. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SMARTi SM00228. PDZ. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 1 hit.
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.
PS50106. PDZ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of a cDNA encoding a constitutive nitric oxide synthase from rabbit brain."
    Jeong Y., Yim J.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.

Entry informationi

Entry nameiNOS1_RABIT
AccessioniPrimary (citable) accession number: O19132
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 127 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