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   16-JUN-2009, entry version 78.
DE   RecName: Full=Nitric oxide synthase, brain;
DE            EC=1.14.13.39;
DE   AltName: Full=BNOS;
DE   AltName: Full=NOS type I;
DE   AltName: Full=Neuronal NOS;
DE            Short=N-NOS;
DE            Short=NNOS;
DE   AltName: Full=Constitutive NOS;
DE   AltName: Full=NC-NOS;
DE   Flags: Fragments;
GN   Name=NOS1;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE OF 1-73.
RA   Mimmack M.L.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE 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
CC       with diverse functions throughout the body. In the brain and
CC       peripheral nervous system, NO displays many properties of a
CC       neurotransmitter.
CC   -!- CATALYTIC ACTIVITY: L-arginine + n NADPH + n H(+) + m O(2) =
CC       citrulline + nitric oxide + n NADP(+).
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- COFACTOR: Binds 1 FAD (By similarity).
CC   -!- COFACTOR: Binds 1 FMN (By similarity).
CC   -!- COFACTOR: Tetrahydrobiopterin (BH4). May stabilize the dimeric
CC       form of the enzyme (By similarity).
CC   -!- ENZYME REGULATION: Stimulated by calcium/calmodulin. Inhibited by
CC       n-Nos-inhibiting protein (PIN) which may prevent the dimerization
CC       of the protein. Inhibited by NOSIP (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with DLG4; the interaction possibly
CC       being prevented by the association between NOS1 and CAPON. Forms a
CC       ternary complex with CAPON and RASD1. Forms a ternary complex with
CC       CAPON and SYN1. Interacts with ZDHHC23. Interacts with NOSIP;
CC       which may impair its synaptic location (By similarity). Interacts
CC       with HTR4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral
CC       membrane protein (By similarity). Cell projection, dendritic spine
CC       (By similarity). Note=In skeletal muscle, NNOS is localized
CC       beneath the sarcolemma of fast-twitch muscle fiber by associating
CC       with the dystrophin glycoprotein complex. In neurons, enriched in
CC       dendritic spines (By similarity).
CC   -!- SIMILARITY: Belongs to the NOS family.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; X99042; CAA67503.1; -; Genomic_DNA.
DR   EMBL; U76739; AAB40706.1; -; mRNA.
DR   UniGene; Oar.522; -.
DR   HSSP; P29476; 1QAU.
DR   SMR; Q29498; 1-72, 72-186.
DR   HOVERGEN; Q29498; -.
DR   BRENDA; 1.14.13.39; 271.
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:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004517; F:nitric-oxide synthase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR004030; NO_synthase_oxygenase_reg.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   PROSITE; PS60001; NOS; PARTIAL.
DR   PROSITE; PS50106; PDZ; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; Cell membrane; Cell projection; FAD; FMN; Heme;
KW   Iron; Membrane; Metal-binding; NADP; Oxidoreductase.
FT   CHAIN        <1   >186       Nitric oxide synthase, brain.
FT                                /FTId=PRO_0000170925.
FT   DOMAIN       <1     51       PDZ.
FT   NP_BIND     115    126       FAD (By similarity).
FT   NON_CONS     73     74
FT   NON_TER       1      1
FT   NON_TER     186    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
//