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O19132 (NOS1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NOS1
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length1435 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

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.

Enzyme regulation

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

Subunit structure

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.

Subcellular location

Cell membranesarcolemma; 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.

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the NOS family.

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Contains 1 PDZ (DHR) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14351435Nitric oxide synthase, brain
PRO_0000170923

Regions

Domain17 – 9983PDZ
Domain761 – 941181Flavodoxin-like
Domain996 – 1243248FAD-binding FR-type
Nucleotide binding887 – 91832FMN By similarity
Nucleotide binding1033 – 104412FAD By similarity
Nucleotide binding1176 – 118611FAD By similarity
Nucleotide binding1251 – 126919NADP By similarity
Nucleotide binding1349 – 136416NADP By similarity
Region1 – 206206Interaction with NOSIP By similarity
Region164 – 24683PIN (nNOS-inhibiting protein) binding By similarity
Region731 – 75121Calmodulin-binding Potential
Region756 – 77520Tetrahydrobiopterin-binding By similarity

Sites

Metal binding4211Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
O19132 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 3ED87ECDD83A7A5A

FASTA1,435160,865
        10         20         30         40         50         60 
MEEHVFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA 

        70         80         90        100        110        120 
GDIILAVNGR PLVDLSYDSA LEVLRGVASE THVVLILRGP EGFTTNLETT FTGDGTPKTI 

       130        140        150        160        170        180 
RVTQPLGAPT KAVDLSHQPP SAGKEQPRPV DGAAGPGSWP QPTQGHGQEA GSPSRANGLA 

       190        200        210        220        230        240 
PRTSSQDPAK KSGWAGLQGS GDKNELLKEI EPVLTLLAGG SKAVDGGGPA KAETRDTGVQ 

       250        260        270        280        290        300 
VDRDFDAKSH KPLPLGVEND RVFSDLWGKG SAPVVLNNPY SEKEQPPASG KQSPTKNGSP 

       310        320        330        340        350        360 
SKCPRFLKVK NWETDVVLTD TLHLKSTLET GCTEHICMGS IMFPSQHTRR PEDIRTKEQL 

       370        380        390        400        410        420 
FPLAKEFIDQ YYSSIKRFGS KAHMERLEEV NKEIESTSTY QLKDTELIYG AKHAWRNASR 

       430        440        450        460        470        480 
CVGRIQWSKL QVFDARDCTT AHGMFNYICN HIKYATNKGN LRSAITIFPQ RTDGKHDFRV 

       490        500        510        520        530        540 
WNSQLIRYAG YKQPDGSTLG DPANVQFTEI CIQQGWKPPR SRFDVLPLLL QANGNDPELF 

       550        560        570        580        590        600 
QIPPELVLEV PIRHPKFEWF KDLGLKWYGL PAVSNMLLEI GGLEFSACPF SGWYMGTEIG 

       610        620        630        640        650        660 
VRDYCDNSRY NILEEVAKKM NLDMRKTSSL WKDQALVEIN IAVLYSFQSD KVTIVDHHSA 

       670        680        690        700        710        720 
TESFIKHMEN EYRCRGGCPA DWVWIVPPMS GSITPVFHQE MLNYRLTPCF EYQPDPWNTH 

       730        740        750        760        770        780 
VWKGTNGTPT KRRAIGFKKL AEAVKFSAKL MGQAMAKRVK ATILYATETG KSQAYAKTLC 

       790        800        810        820        830        840 
EIFKHAFDAK VMSMEEYDIV HLEHETLVLV VTSTFGNGDP PENGEKFRCA LMEMRHPNSL 

       850        860        870        880        890        900 
QEERKSYKVR FNSVSSYSDS RKSSGDGPDV RDHFESAGPL ANVRFSVFGL GSRAYPHFCA 

       910        920        930        940        950        960 
FGHAVDTLLE ELGGERILKM REGDELCGQE EAFRTWAKKV FKAACDVFCV GDDVNIEKAN 

       970        980        990       1000       1010       1020 
NSLISNDRSW KRNKFRLTYV AEAPGLTQGL SSVHKKRVSA ARLLSRQNLQ SPKSSRSTIF 

      1030       1040       1050       1060       1070       1080 
VRLHTNGSQE LQYQPGDHLG VFPGNHEDLV NALIERLEDA PPANQMVKVE LLEERNTALG 

      1090       1100       1110       1120       1130       1140 
VISNWKDEPR LPPCTVFQAF KYYLDITTPP TPLQLQQFAS LASNEKEKQR LLVLSKGLQE 

      1150       1160       1170       1180       1190       1200 
YEEWKWGKNP TIVEVLEEFP SIQMPATLLL TQLSLLQPRY YSISSSPDMY PDEVHLTVAI 

      1210       1220       1230       1240       1250       1260 
VSYHTRDGEG PIHHGVCSSW LNRIPADEVV PCFVRGAPSF RLPRNPQVPC ILVGPGTAFA 

      1270       1280       1290       1300       1310       1320 
PFRSFWQQRQ FDIQHKGMSP CPMVLVFGCR QSKIDHIYRE EALQAKNKGV FRELYTAYSR 

      1330       1340       1350       1360       1370       1380 
EPDKPKKYVQ DILQEQLAEQ VYRALKEQGG HIYVCGDVTM AADVLKAVQR IMAQQGKLSA 

      1390       1400       1410       1420       1430 
EDAGVFISRL RDDNRYHEDI FGVTLRTYEV TNRLRSESIA FIEESKKDTD EVFSS 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U91584 mRNA. Translation: AAB68663.1.
RefSeqNP_001075854.1. NM_001082385.1.
UniGeneOcu.2169.

3D structure databases

ProteinModelPortalO19132.
SMRO19132. Positions 7-133, 304-722, 756-1419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000020745.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009243.

Organism-specific databases

CTD4842.

Phylogenomic databases

eggNOGCOG4362.
HOGENOMHOG000220884.
HOVERGENHBG000159.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
2.30.42.10. 1 hit.
3.40.50.360. 2 hits.
3.90.340.10. 1 hit.
InterProIPR003097. 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.
IPR004030. NO_synthase_oxygenase_dom.
IPR012144. NOS_euk.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001478. PDZ.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. 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]
PIRSFPIRSF000333. NOS. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SMARTSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
SSF52218. SSF52218. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNOS1_RABIT
AccessionPrimary (citable) accession number: O19132
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families