NOS1_SHEEP
ID NOS1_SHEEP Reviewed; 186 AA.
AC Q29498; P79210;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Nitric oxide synthase, brain;
DE EC=1.14.13.39;
DE AltName: Full=BNOS;
DE AltName: Full=Constitutive NOS;
DE AltName: Full=NC-NOS;
DE AltName: Full=NOS type I;
DE AltName: Full=Neuronal NOS;
DE Short=N-NOS;
DE Short=NNOS;
DE AltName: Full=Peptidyl-cysteine S-nitrosylase NOS1;
DE Flags: Fragments;
GN Name=NOS1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
RA Mimmack M.L.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-186.
RC TISSUE=Neuron;
RA Aguan K., Weiner C.P.;
RT "Effect of hypoxia on the expression pattern of neuronal nitric oxide
RT synthase gene in the sheep fetal brain microvasculature.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC diverse functions throughout the body. In the brain and peripheral
CC nervous system, NO displays many properties of a neurotransmitter.
CC Probably has nitrosylase activity and mediates cysteine S-nitrosylation
CC of cytoplasmic target proteins such SRR (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline
CC + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN. {ECO:0000250};
CC -!- COFACTOR:
CC Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250};
CC Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the
CC enzyme. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Stimulated by calcium/calmodulin. Inhibited by n-
CC Nos-inhibiting protein (PIN) which may prevent the dimerization of the
CC protein. Inhibited by NOSIP (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with DLG4; the interaction possibly being
CC prevented by the association between NOS1 and CAPON. Forms a ternary
CC complex with CAPON and RASD1. Forms a ternary complex with CAPON and
CC SYN1. Interacts with ZDHHC23. Interacts with NOSIP; which may impair
CC its synaptic location (By similarity). Interacts with HTR4 (By
CC similarity). Interacts with SLC6A4. Interacts with VAC14 (By
CC similarity). Interacts (via N-terminal domain) with DLG4 (via N-
CC terminal tandem pair of PDZ domains). Interacts with SLC6A4. Forms a
CC complex with ASL, ASS1 and SLC7A1; the complex regulates cell-
CC autonomous L-arginine synthesis and citrulline recycling while
CC channeling extracellular L-arginine to nitric oxide synthesis pathway
CC (By similarity). {ECO:0000250|UniProtKB:P29476,
CC ECO:0000250|UniProtKB:Q9Z0J4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell projection, dendritic
CC spine {ECO:0000250}. Note=In skeletal muscle, NNOS is localized beneath
CC the sarcolemma of fast-twitch muscle fiber by associating with the
CC dystrophin glycoprotein complex. In neurons, enriched in dendritic
CC spines (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and
CC Hsp40 (in vitro). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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DR EMBL; X99042; CAA67503.1; -; Genomic_DNA.
DR EMBL; U76739; AAB40706.1; -; mRNA.
DR AlphaFoldDB; Q29498; -.
DR SMR; Q29498; -.
DR STRING; 9940.ENSOARP00000004517; -.
DR eggNOG; KOG1158; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004517; F:nitric-oxide synthase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00595; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Calmodulin-binding; Cell membrane; Cell projection; FAD; Flavoprotein; FMN;
KW Heme; Iron; Membrane; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome; Synapse; Ubl conjugation.
FT CHAIN <1..>186
FT /note="Nitric oxide synthase, brain"
FT /id="PRO_0000170925"
FT DOMAIN <1..51
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT BINDING 115..126
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT NON_CONS 73..74
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 186
SQ SEQUENCE 186 AA; 20486 MW; 021B7925AE35CB97 CRC64;
GGAAEQSGLI QAGDIILAVN GQPLVDLSYD SALEVFRGIA SETHVVLILR GPEGFTTHLE
TTFTGDGTPK TIHNVHKKRV SAARLLSRQN LQSPKSSRST IFVRLHTNGN QELQYQPGDH
LGVFPGNHED LVNALIERLE DAPPANQLVK VELLEERNTA LGVISNWTDE HRLPPCTIFQ
AFKYYL
