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Nitric oxide synthase, brain (EC 1.14.13.39) (Constitutive NOS) (NC-NOS) (NOS type I) (Neuronal NOS) (N-NOS) (nNOS) (Peptidyl-cysteine S-nitrosylase NOS1) (bNOS)

 NOS1_MOUSE              Reviewed;        1429 AA.
Q9Z0J4; Q3UR10; Q64208;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
05-JUL-2017, entry version 176.
RecName: Full=Nitric oxide synthase, brain;
EC=1.14.13.39;
AltName: Full=Constitutive NOS;
AltName: Full=NC-NOS;
AltName: Full=NOS type I;
AltName: Full=Neuronal NOS;
Short=N-NOS;
Short=nNOS;
AltName: Full=Peptidyl-cysteine S-nitrosylase NOS1;
AltName: Full=bNOS;
Name=Nos1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS N-NOS-1 AND N-NOS-2).
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=7686743; DOI=10.1006/bbrc.1993.1726;
Ogura T., Yokoyama T., Fujisawa H., Kurashima Y., Esumi H.;
"Structural diversity of neuronal oxide synthase mRNA in the nervous
system.";
Biochem. Biophys. Res. Commun. 193:1014-1022(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NNOS MU).
TISSUE=Skeletal muscle;
PubMed=8626668; DOI=10.1074/jbc.271.19.11204;
Silvagno F., Xia H., Bredt D.S.;
"Neuronal nitric-oxide synthase-mu, an alternatively spliced isoform
expressed in differentiated skeletal muscle.";
J. Biol. Chem. 271:11204-11208(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1320-1429.
STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
ALTERNATIVE SPLICING (ISOFORMS NNOS BETA; NNOS GAMMA AND NNOS MU).
PubMed=9208206; DOI=10.1159/000111211;
Brenman J.E., Xia H., Chao D.S., Black S.M., Bredt D.S.;
"Regulation of neuronal nitric oxide synthase through alternative
transcripts.";
Dev. Neurosci. 19:224-231(1997).
[5]
INTERACTION WITH DLG4.
PubMed=10623522; DOI=10.1006/jmbi.1999.3350;
Tochio H., Hung F., Li M., Bredt D.S., Zhang M.;
"Solution structure and backbone dynamics of the second PDZ domain of
postsynaptic density-95.";
J. Mol. Biol. 295:225-237(2000).
[6]
INTERACTION WITH RASD1 AND CAPON.
PubMed=11086993; DOI=10.1016/S0896-6273(00)00095-7;
Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H.;
"Dexras1: a G protein specifically coupled to neuronal nitric oxide
synthase via CAPON.";
Neuron 28:183-193(2000).
[7]
INTERACTION WITH HTR4.
PubMed=15466885; DOI=10.1242/jcs.01379;
Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
Marin P., Dumuis A., Bockaert J.;
"New sorting nexin (SNX27) and NHERF specifically interact with the 5-
HT4a receptor splice variant: roles in receptor targeting.";
J. Cell Sci. 117:5367-5379(2004).
[8]
FUNCTION AS NITROSYLASE.
PubMed=17293453; DOI=10.1073/pnas.0611620104;
Mustafa A.K., Kumar M., Selvakumar B., Ho G.P., Ehmsen J.T.,
Barrow R.K., Amzel L.M., Snyder S.H.;
"Nitric oxide S-nitrosylates serine racemase, mediating feedback
inhibition of D-serine formation.";
Proc. Natl. Acad. Sci. U.S.A. 104:2950-2955(2007).
[9]
INTERACTION WITH SLC6A4.
PubMed=17452640; DOI=10.1073/pnas.0610964104;
Chanrion B., Mannoury la Cour C., Bertaso F., Lerner-Natoli M.,
Freissmuth M., Millan M.J., Bockaert J., Marin P.;
"Physical interaction between the serotonin transporter and neuronal
nitric oxide synthase underlies reciprocal modulation of their
activity.";
Proc. Natl. Acad. Sci. U.S.A. 104:8119-8124(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-857 AND
SER-858, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 725-747 IN COMPLEX WITH
CALMODULIN.
Valentine K.G., Ng H.L., Schneeweis L., Kranz J.K., Frederick K.K.,
Alber T., Wand A.J.;
"Crystal structure of calmodulin-neuronal nitric oxide synthase
complex.";
Submitted (DEC-2006) to the PDB data bank.
-!- 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.
Isoform NNOS Mu may be an effector enzyme for the dystrophin
complex. {ECO:0000269|PubMed:17293453}.
-!- CATALYTIC ACTIVITY: 2 L-arginine + 3 NADPH + 4 O(2) = 2 L-
citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD. {ECO:0000250};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
Note=Binds 1 FMN. {ECO:0000250};
-!- COFACTOR:
Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250};
Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of
the enzyme. {ECO:0000250};
-!- 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). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Forms a ternary complex with CAPON and SYN1.
Interacts with ZDHHC23. Interacts with NOSIP; which may impair its
synaptic location (By similarity). Interacts with DLG4; the
interaction possibly being prevented by the association between
NOS1 and CAPON. Interacts with HTR4. Forms a ternary complex with
CAPON and RASD1. Interacts with VAC14 (By similarity). Interacts
(via N-terminal domain) with DLG4 (via N-terminal tandem pair of
PDZ domains) (By similarity). Interacts with SLC6A4. {ECO:0000250,
ECO:0000269|PubMed:10623522, ECO:0000269|PubMed:11086993,
ECO:0000269|PubMed:15466885, ECO:0000269|PubMed:17452640,
ECO:0000269|Ref.11}.
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral
membrane protein. Cell projection, dendritic spine {ECO:0000250}.
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). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=N-NOS-1;
IsoId=Q9Z0J4-1; Sequence=Displayed;
Name=N-NOS-2;
IsoId=Q9Z0J4-2; Sequence=VSP_003578;
Name=NNOS beta;
IsoId=Q9Z0J4-3; Sequence=VSP_003575, VSP_003576;
Name=NNOS gamma;
IsoId=Q9Z0J4-4; Sequence=VSP_003577;
Name=NNOS Mu; Synonyms=Muscle-specific;
IsoId=Q9Z0J4-5; Sequence=VSP_003579;
-!- TISSUE SPECIFICITY: Widely expressed in the nervous system:
expressed in cerebrum, olfactory bulb, hippocampus, midbrain,
cerebellum, pons, medulla oblongata, and spinal cord. Also found
in skeletal muscle, where it is localized beneath the sarcolemma
of fast twitch muscle fibers, and in spleen, heart, kidney, and
liver. N-NOS-1 and N-NOS-2 are found in all parts of the nervous
system. NNOS beta and gamma occur in a region-specific manner in
the brain and NNOS beta expression is developmentally regulated.
NNOS Mu is only found in mature skeletal and cardiac muscles.
-!- INDUCTION: By cholinergic agonists acting at inositol phosphate-
linked muscarinic receptors in cardiac myocytes.
-!- DOMAIN: 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). {ECO:0000250}.
-!- PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of
Hsp70 and Hsp40 (in vitro). {ECO:0000250}.
-!- DISEASE: Note=In MDX mice (mouse model of dystrophinopathy) the
dystrophin complex is disrupted and nNOS is displaced from
sarcolemma and accumulates in the cytosol.
-!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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EMBL; D14552; BAA03415.1; -; mRNA.
EMBL; S81982; AAB36469.1; -; mRNA.
EMBL; AK141904; BAE24878.1; -; mRNA.
CCDS; CCDS19606.1; -. [Q9Z0J4-1]
PIR; JN0609; JN0609.
RefSeq; NP_032738.1; NM_008712.3. [Q9Z0J4-1]
RefSeq; XP_017176196.1; XM_017320707.1. [Q9Z0J4-1]
UniGene; Mm.442195; -.
UniGene; Mm.44249; -.
PDB; 2O60; X-ray; 1.55 A; B=725-747.
PDBsum; 2O60; -.
ProteinModelPortal; Q9Z0J4; -.
SMR; Q9Z0J4; -.
BioGrid; 201805; 6.
DIP; DIP-31556N; -.
IntAct; Q9Z0J4; 6.
STRING; 10090.ENSMUSP00000120421; -.
BindingDB; Q9Z0J4; -.
ChEMBL; CHEMBL4719; -.
iPTMnet; Q9Z0J4; -.
PhosphoSitePlus; Q9Z0J4; -.
PaxDb; Q9Z0J4; -.
PeptideAtlas; Q9Z0J4; -.
PRIDE; Q9Z0J4; -.
DNASU; 18125; -.
Ensembl; ENSMUST00000142742; ENSMUSP00000120421; ENSMUSG00000029361. [Q9Z0J4-1]
Ensembl; ENSMUST00000171055; ENSMUSP00000127432; ENSMUSG00000029361. [Q9Z0J4-1]
GeneID; 18125; -.
KEGG; mmu:18125; -.
UCSC; uc008zfy.2; mouse. [Q9Z0J4-1]
CTD; 4842; -.
MGI; MGI:97360; Nos1.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
eggNOG; COG4362; LUCA.
GeneTree; ENSGT00840000129757; -.
HOGENOM; HOG000220884; -.
HOVERGEN; HBG000159; -.
InParanoid; Q9Z0J4; -.
KO; K13240; -.
PhylomeDB; Q9Z0J4; -.
Reactome; R-MMU-1222556; ROS, RNS production in phagocytes.
Reactome; R-MMU-392154; Nitric oxide stimulates guanylate cyclase.
Reactome; R-MMU-5578775; Ion homeostasis.
EvolutionaryTrace; Q9Z0J4; -.
PRO; PR:Q9Z0J4; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029361; -.
CleanEx; MM_NOS1; -.
ExpressionAtlas; Q9Z0J4; baseline and differential.
Genevisible; Q9Z0J4; MM.
GO; GO:0005856; C:cytoskeleton; IDA:BHF-UCL.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:BHF-UCL.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0010181; F:FMN binding; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
GO; GO:0004517; F:nitric-oxide synthase activity; IDA:BHF-UCL.
GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL.
GO; GO:0042738; P:exogenous drug catabolic process; IMP:MGI.
GO; GO:0033555; P:multicellular organismal response to stress; ISO:MGI.
GO; GO:0045776; P:negative regulation of blood pressure; IBA:GO_Central.
GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:MGI.
GO; GO:0051346; P:negative regulation of hydrolase activity; IMP:MGI.
GO; GO:0043267; P:negative regulation of potassium ion transport; IMP:MGI.
GO; GO:0051612; P:negative regulation of serotonin uptake; IDA:UniProtKB.
GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:BHF-UCL.
GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:GO_Central.
GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IDA:MGI.
GO; GO:1901206; P:positive regulation of adrenergic receptor signaling pathway involved in heart process; IMP:BHF-UCL.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IBA:GO_Central.
GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:GO_Central.
GO; GO:0035066; P:positive regulation of histone acetylation; IMP:BHF-UCL.
GO; GO:0098735; P:positive regulation of the force of heart contraction; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0050767; P:regulation of neurogenesis; IDA:CACAO.
GO; GO:0002028; P:regulation of sodium ion transport; IMP:MGI.
GO; GO:0009408; P:response to heat; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0098924; P:retrograde trans-synaptic signaling by nitric oxide; IMP:SynGO.
GO; GO:0006941; P:striated muscle contraction; IMP:MGI.
GO; GO:0042311; P:vasodilation; ISO:MGI.
Gene3D; 3.40.50.360; -; 1.
InterPro; IPR003097; FAD-binding_1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_dom.
InterPro; IPR012144; NOS_euk.
InterPro; IPR004030; NOS_N.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR001478; PDZ.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
Pfam; PF02898; NO_synthase; 1.
Pfam; PF00595; PDZ; 1.
PIRSF; PIRSF000333; NOS; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF56512; SSF56512; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PROSITE; PS60001; NOS; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calmodulin-binding; Cell membrane;
Cell projection; Complete proteome; FAD; Flavoprotein; FMN; Heme;
Iron; Membrane; Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 1429 Nitric oxide synthase, brain.
/FTId=PRO_0000170922.
DOMAIN 17 99 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 755 935 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 990 1237 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 881 912 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
NP_BIND 1027 1038 FAD. {ECO:0000250}.
NP_BIND 1170 1180 FAD. {ECO:0000250}.
NP_BIND 1245 1263 NADP. {ECO:0000250}.
NP_BIND 1343 1358 NADP. {ECO:0000250}.
REGION 1 200 Interaction with NOSIP. {ECO:0000250}.
REGION 163 240 PIN (nNOS-inhibiting protein) binding.
{ECO:0000250}.
REGION 725 745 Calmodulin-binding.
REGION 750 769 Tetrahydrobiopterin-binding.
{ECO:0000250}.
METAL 415 415 Iron (heme axial ligand). {ECO:0000250}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 847 847 Phosphoserine.
{ECO:0000250|UniProtKB:P29476}.
MOD_RES 857 857 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 858 858 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 331 Missing (in isoform NNOS gamma).
{ECO:0000305}.
/FTId=VSP_003577.
VAR_SEQ 1 230 Missing (in isoform NNOS beta).
{ECO:0000305}.
/FTId=VSP_003575.
VAR_SEQ 231 236 TGIQVD -> MRGLGS (in isoform NNOS beta).
{ECO:0000305}.
/FTId=VSP_003576.
VAR_SEQ 504 608 Missing (in isoform N-NOS-2).
{ECO:0000303|PubMed:7686743}.
/FTId=VSP_003578.
VAR_SEQ 839 839 K -> KYPEPLRFFPRKGPSLSHVDSEAHSLVAARDSQHR
(in isoform NNOS Mu).
{ECO:0000303|PubMed:8626668}.
/FTId=VSP_003579.
CONFLICT 1320 1320 K -> Q (in Ref. 3; BAE24878).
{ECO:0000305}.
HELIX 731 744 {ECO:0000244|PDB:2O60}.
SEQUENCE 1429 AA; 160472 MW; 3782848D65B41BFC CRC64;
MEEHTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA
GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI
RVTQPLGTPT KAVDLSRQPS ASKDQPLAVD RVPGPSNGPQ HAQGRGQGAG SVSQANGVAI
DPTMKNTKAN LQDSGEQDEL LKEIEPVLSI LTGGGKAVNR GGPAKAEMKD TGIQVDRDLD
GKLHKAPPLG GENDRVFNDL WGKGNVPVVL NNPYSENEQS PASGKQSPTK NGSPSRCPRF
LKVKNWETDV VLTDTLHLKS TLETGCTEQI CMGSIMLPSH HIRKSEDVRT KDQLFPLAKE
FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE LIYGAKHAWR NASRCVGRIQ
WSKLQVFDAR DCTTAHGMFN YICNHVKYAT NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI
RYAGYKQPDG STLGDPANVE FTEICIQQGW KPPRGRFDVL PLLLQANGND PELFQIPPEL
VLEVPIRHPK FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD
NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD HHSATESFIK
HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL TPSFEYQPDP WNTHVWKGTN
GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA KRVKATILYA TETGKSQAYA KTLCEIFKHA
FDAKAMSMEE YDIVHLEHEA LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS
YKVRFNSVSS YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD
TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI EKANNSLISN
DRSWKRNKFR LTYVAEAPEL TQGLSNVHKK RVSAARLLSR QNLQSPKSSR STIFVRLHTN
GNQELQYQPG DHLGVFPGNH EDLVNALIER LEDAPPANHV VKVEMLEERN TALGVISNWK
DESRLPPCTI FQAFKYYLDI TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW
GKNPTMVEVL EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR
DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG TGIAPFRSFW
QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK NKGVFRELYT AYSREPDRPK
KYVQDVLQEQ LAESVYRALK EQGGHIYVCG DVTMAADVLK AIQRIMTQQG KLSEEDAGVF
ISRLRDDNRY HEDIFGVTLR TYEVTNRLRS ESIAFIEESK KDTDEVFSS


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