ID   NOS1_MOUSE              Reviewed;        1429 AA.
AC   Q9Z0J4; Q3UR10; Q64208;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 219.
DE   RecName: Full=Nitric oxide synthase 1 {ECO:0000312|MGI:MGI:97360};
DE            EC=1.14.13.39 {ECO:0000250|UniProtKB:P29476};
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=Nitric oxide synthase, brain {ECO:0000305};
DE            Short=bNOS {ECO:0000305};
DE   AltName: Full=Peptidyl-cysteine S-nitrosylase NOS1;
GN   Name=Nos1 {ECO:0000312|MGI:MGI:97360};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS N-NOS-1 AND N-NOS-2).
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=7686743; DOI=10.1006/bbrc.1993.1726;
RA   Ogura T., Yokoyama T., Fujisawa H., Kurashima Y., Esumi H.;
RT   "Structural diversity of neuronal oxide synthase mRNA in the nervous
RT   system.";
RL   Biochem. Biophys. Res. Commun. 193:1014-1022(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NNOS MU).
RC   TISSUE=Skeletal muscle;
RX   PubMed=8626668; DOI=10.1074/jbc.271.19.11204;
RA   Silvagno F., Xia H., Bredt D.S.;
RT   "Neuronal nitric-oxide synthase-mu, an alternatively spliced isoform
RT   expressed in differentiated skeletal muscle.";
RL   J. Biol. Chem. 271:11204-11208(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1320-1429.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH DMD.
RX   PubMed=7545544; DOI=10.1016/0092-8674(95)90471-9;
RA   Brenman J.E., Chao D.S., Xia H., Aldape K., Bredt D.S.;
RT   "Nitric oxide synthase complexed with dystrophin and absent from skeletal
RT   muscle sarcolemma in Duchenne muscular dystrophy.";
RL   Cell 82:743-752(1995).
RN   [5]
RP   ALTERNATIVE SPLICING (ISOFORMS NNOS BETA; NNOS GAMMA AND NNOS MU).
RX   PubMed=9208206; DOI=10.1159/000111211;
RA   Brenman J.E., Xia H., Chao D.S., Black S.M., Bredt D.S.;
RT   "Regulation of neuronal nitric oxide synthase through alternative
RT   transcripts.";
RL   Dev. Neurosci. 19:224-231(1997).
RN   [6]
RP   INTERACTION WITH DLG4.
RX   PubMed=10623522; DOI=10.1006/jmbi.1999.3350;
RA   Tochio H., Hung F., Li M., Bredt D.S., Zhang M.;
RT   "Solution structure and backbone dynamics of the second PDZ domain of
RT   postsynaptic density-95.";
RL   J. Mol. Biol. 295:225-237(2000).
RN   [7]
RP   INTERACTION WITH RASD1 AND CAPON.
RX   PubMed=11086993; DOI=10.1016/s0896-6273(00)00095-7;
RA   Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H.;
RT   "Dexras1: a G protein specifically coupled to neuronal nitric oxide
RT   synthase via CAPON.";
RL   Neuron 28:183-193(2000).
RN   [8]
RP   INTERACTION WITH HTR4.
RX   PubMed=15466885; DOI=10.1242/jcs.01379;
RA   Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA   Marin P., Dumuis A., Bockaert J.;
RT   "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a
RT   receptor splice variant: roles in receptor targeting.";
RL   J. Cell Sci. 117:5367-5379(2004).
RN   [9]
RP   FUNCTION AS NITROSYLASE.
RX   PubMed=17293453; DOI=10.1073/pnas.0611620104;
RA   Mustafa A.K., Kumar M., Selvakumar B., Ho G.P., Ehmsen J.T., Barrow R.K.,
RA   Amzel L.M., Snyder S.H.;
RT   "Nitric oxide S-nitrosylates serine racemase, mediating feedback inhibition
RT   of D-serine formation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2950-2955(2007).
RN   [10]
RP   INTERACTION WITH SLC6A4.
RX   PubMed=17452640; DOI=10.1073/pnas.0610964104;
RA   Chanrion B., Mannoury la Cour C., Bertaso F., Lerner-Natoli M.,
RA   Freissmuth M., Millan M.J., Bockaert J., Marin P.;
RT   "Physical interaction between the serotonin transporter and neuronal nitric
RT   oxide synthase underlies reciprocal modulation of their activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8119-8124(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-857 AND SER-858, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [12]
RP   INTERACTION WITH ASL; ASS1 AND SLC7A1.
RX   PubMed=22081021; DOI=10.1038/nm.2544;
RA   Erez A., Nagamani S.C., Shchelochkov O.A., Premkumar M.H., Campeau P.M.,
RA   Chen Y., Garg H.K., Li L., Mian A., Bertin T.K., Black J.O., Zeng H.,
RA   Tang Y., Reddy A.K., Summar M., O'Brien W.E., Harrison D.G., Mitch W.E.,
RA   Marini J.C., Aschner J.L., Bryan N.S., Lee B.;
RT   "Requirement of argininosuccinate lyase for systemic nitric oxide
RT   production.";
RL   Nat. Med. 17:1619-1626(2011).
RN   [13] {ECO:0007744|PDB:2O60}
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 725-747 IN COMPLEX WITH
RP   CALMODULIN, AND REGION.
RA   Valentine K.G., Ng H.L., Schneeweis L., Kranz J.K., Frederick K.K.,
RA   Alber T., Wand A.J.;
RT   "Crystal structure of calmodulin-neuronal nitric oxide synthase complex.";
RL   Submitted (DEC-2006) to the PDB data bank.
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. Isoform NNOS Mu may be an
CC       effector enzyme for the dystrophin complex.
CC       {ECO:0000269|PubMed:17293453}.
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         Evidence={ECO:0000250|UniProtKB:P29476};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898;
CC         Evidence={ECO:0000250|UniProtKB:P29476};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P29475};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P29476};
CC       Note=Binds 1 FAD. {ECO:0000250|UniProtKB:P29476};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P29476};
CC       Note=Binds 1 FMN. {ECO:0000250|UniProtKB:P29476};
CC   -!- COFACTOR:
CC       Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC         Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:P29475};
CC       Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the
CC       enzyme. {ECO:0000250|UniProtKB:P29475};
CC   -!- ACTIVITY REGULATION: Stimulated by calcium/calmodulin. Inhibited by
CC       DYNLL1 that prevents the dimerization of the protein. Inhibited by
CC       NOSIP. {ECO:0000250|UniProtKB:P29476}.
CC   -!- SUBUNIT: Homodimer. Interacts with DLG4; the interaction possibly being
CC       prevented by the association between NOS1 and CAPON (By similarity).
CC       Forms a ternary complex with CAPON and RASD1 (PubMed:11086993). Forms a
CC       ternary complex with CAPON and SYN1 (By similarity). Interacts with
CC       ZDHHC23 (By similarity). Interacts with NOSIP; which may impair its
CC       synaptic location (By similarity). Interacts with HTR4
CC       (PubMed:15466885). Interacts with VAC14 (By similarity). Interacts (via
CC       N-terminal domain) with DLG4 (via N-terminal tandem pair of PDZ
CC       domains) (PubMed:10623522). Interacts with SLC6A4 (PubMed:17452640).
CC       Forms a 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       (PubMed:22081021). Interacts with DMD; localizes NOS1 to sarcolemma in
CC       muscle cells (PubMed:7545544). Interacts with DYNLL1; inhibits the
CC       nitric oxide synthase activity (By similarity).
CC       {ECO:0000250|UniProtKB:P29476, ECO:0000269|PubMed:10623522,
CC       ECO:0000269|PubMed:11086993, ECO:0000269|PubMed:15466885,
CC       ECO:0000269|PubMed:17452640, ECO:0000269|PubMed:22081021,
CC       ECO:0000269|PubMed:7545544, ECO:0000269|Ref.13}.
CC   -!- INTERACTION:
CC       Q9Z0J4; Q05769: Ptgs2; NbExp=4; IntAct=EBI-397596, EBI-298933;
CC       Q9Z0J4; Q60857: Slc6a4; NbExp=4; IntAct=EBI-397596, EBI-15633326;
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC       {ECO:0000269|PubMed:7545544}; Peripheral membrane protein
CC       {ECO:0000255}. Cell projection, dendritic spine
CC       {ECO:0000250|UniProtKB:P29476}. Note=In skeletal muscle, it is
CC       localized beneath the sarcolemma of fast-twitch muscle fiber by
CC       associating with the dystrophin glycoprotein complex (PubMed:7545544).
CC       In neurons, enriched in dendritic spines (By similarity).
CC       {ECO:0000250|UniProtKB:P29476, ECO:0000269|PubMed:7545544}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=N-NOS-1;
CC         IsoId=Q9Z0J4-1; Sequence=Displayed;
CC       Name=N-NOS-2;
CC         IsoId=Q9Z0J4-2; Sequence=VSP_003578;
CC       Name=NNOS beta;
CC         IsoId=Q9Z0J4-3; Sequence=VSP_003575, VSP_003576;
CC       Name=NNOS gamma;
CC         IsoId=Q9Z0J4-4; Sequence=VSP_003577;
CC       Name=NNOS Mu; Synonyms=Muscle-specific;
CC         IsoId=Q9Z0J4-5; Sequence=VSP_003579;
CC   -!- TISSUE SPECIFICITY: Widely expressed in the nervous system: expressed
CC       in cerebrum, olfactory bulb, hippocampus, midbrain, cerebellum, pons,
CC       medulla oblongata, and spinal cord. Also found in skeletal muscle,
CC       where it is localized beneath the sarcolemma of fast twitch muscle
CC       fibers, and in spleen, heart, kidney, and liver. N-NOS-1 and N-NOS-2
CC       are found in all parts of the nervous system. NNOS beta and gamma occur
CC       in a region-specific manner in the brain and NNOS beta expression is
CC       developmentally regulated. NNOS Mu is only found in mature skeletal and
CC       cardiac muscles.
CC   -!- INDUCTION: By cholinergic agonists acting at inositol phosphate-linked
CC       muscarinic receptors in cardiac myocytes.
CC   -!- DOMAIN: The PDZ domain participates in protein-protein interaction, and
CC       is responsible for targeting nNos to synaptic membranes. Mediates
CC       interaction with VAC14. {ECO:0000250|UniProtKB:P29476}.
CC   -!- PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and
CC       Hsp40 (in vitro). {ECO:0000250|UniProtKB:P29476}.
CC   -!- DISEASE: Note=In MDX mice (mouse model of dystrophinopathy) the
CC       dystrophin complex is disrupted and nNOS is displaced from sarcolemma
CC       and accumulates in the cytosol.
CC   -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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DR   EMBL; D14552; BAA03415.1; -; mRNA.
DR   EMBL; S81982; AAB36469.1; -; mRNA.
DR   EMBL; AK141904; BAE24878.1; -; mRNA.
DR   CCDS; CCDS19606.1; -. [Q9Z0J4-1]
DR   PIR; JN0609; JN0609.
DR   RefSeq; NP_032738.1; NM_008712.3. [Q9Z0J4-1]
DR   RefSeq; XP_017176196.1; XM_017320707.1.
DR   PDB; 2O60; X-ray; 1.55 A; B=725-747.
DR   PDBsum; 2O60; -.
DR   AlphaFoldDB; Q9Z0J4; -.
DR   BMRB; Q9Z0J4; -.
DR   SMR; Q9Z0J4; -.
DR   BioGRID; 201805; 24.
DR   CORUM; Q9Z0J4; -.
DR   DIP; DIP-31556N; -.
DR   IntAct; Q9Z0J4; 11.
DR   MINT; Q9Z0J4; -.
DR   STRING; 10090.ENSMUSP00000120421; -.
DR   BindingDB; Q9Z0J4; -.
DR   ChEMBL; CHEMBL4719; -.
DR   iPTMnet; Q9Z0J4; -.
DR   PhosphoSitePlus; Q9Z0J4; -.
DR   MaxQB; Q9Z0J4; -.
DR   PaxDb; 10090-ENSMUSP00000099617; -.
DR   PeptideAtlas; Q9Z0J4; -.
DR   ProteomicsDB; 295504; -. [Q9Z0J4-1]
DR   ProteomicsDB; 295505; -. [Q9Z0J4-2]
DR   ProteomicsDB; 295506; -. [Q9Z0J4-3]
DR   ProteomicsDB; 295507; -. [Q9Z0J4-4]
DR   ProteomicsDB; 295508; -. [Q9Z0J4-5]
DR   ABCD; Q9Z0J4; 2 sequenced antibodies.
DR   Antibodypedia; 3691; 1055 antibodies from 47 providers.
DR   DNASU; 18125; -.
DR   Ensembl; ENSMUST00000142742.9; ENSMUSP00000120421.2; ENSMUSG00000029361.19. [Q9Z0J4-1]
DR   Ensembl; ENSMUST00000171055.2; ENSMUSP00000127432.2; ENSMUSG00000029361.19. [Q9Z0J4-1]
DR   GeneID; 18125; -.
DR   KEGG; mmu:18125; -.
DR   UCSC; uc008zfy.2; mouse. [Q9Z0J4-1]
DR   AGR; MGI:97360; -.
DR   CTD; 4842; -.
DR   MGI; MGI:97360; Nos1.
DR   VEuPathDB; HostDB:ENSMUSG00000029361; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   GeneTree; ENSGT00940000159357; -.
DR   InParanoid; Q9Z0J4; -.
DR   OrthoDB; 276396at2759; -.
DR   PhylomeDB; Q9Z0J4; -.
DR   Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-MMU-392154; Nitric oxide stimulates guanylate cyclase.
DR   Reactome; R-MMU-5578775; Ion homeostasis.
DR   BioGRID-ORCS; 18125; 0 hits in 75 CRISPR screens.
DR   ChiTaRS; Nos1; mouse.
DR   EvolutionaryTrace; Q9Z0J4; -.
DR   PRO; PR:Q9Z0J4; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9Z0J4; Protein.
DR   Bgee; ENSMUSG00000029361; Expressed in anterior amygdaloid area and 137 other cell types or tissues.
DR   ExpressionAtlas; Q9Z0J4; baseline and differential.
DR   GO; GO:0042582; C:azurophil granule; ISO:MGI.
DR   GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR   GO; GO:0071944; C:cell periphery; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0001917; C:photoreceptor inner segment; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR   GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR   GO; GO:0099091; C:postsynaptic specialization, intracellular component; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:BHF-UCL.
DR   GO; GO:0030141; C:secretory granule; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR   GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR   GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR   GO; GO:0046870; F:cadmium ion binding; ISO:MGI.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR   GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI.
DR   GO; GO:0010181; F:FMN binding; ISO:MGI.
DR   GO; GO:0020037; F:heme binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0050661; F:NADP binding; ISO:MGI.
DR   GO; GO:0070402; F:NADPH binding; ISO:MGI.
DR   GO; GO:0004517; F:nitric-oxide synthase activity; IDA:BHF-UCL.
DR   GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR   GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR   GO; GO:0017080; F:sodium channel regulator activity; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR   GO; GO:0006527; P:arginine catabolic process; ISO:MGI.
DR   GO; GO:0048148; P:behavioral response to cocaine; ISO:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0071872; P:cellular response to epinephrine stimulus; ISO:MGI.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR   GO; GO:0033555; P:multicellular organismal response to stress; ISO:MGI.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR   GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:MGI.
DR   GO; GO:0061875; P:negative regulation of hepatic stellate cell contraction; ISO:MGI.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR   GO; GO:0034760; P:negative regulation of iron ion transmembrane transport; ISO:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR   GO; GO:0043267; P:negative regulation of potassium ion transport; IMP:MGI.
DR   GO; GO:0051612; P:negative regulation of serotonin uptake; IDA:UniProtKB.
DR   GO; GO:0045906; P:negative regulation of vasoconstriction; ISO:MGI.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0007263; P:nitric oxide mediated signal transduction; ISO:MGI.
DR   GO; GO:0106071; P:positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:BHF-UCL.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR   GO; GO:1902307; P:positive regulation of sodium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0098735; P:positive regulation of the force of heart contraction; IMP:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0006813; P:potassium ion transport; IMP:MGI.
DR   GO; GO:0050767; P:regulation of neurogenesis; IDA:CACAO.
DR   GO; GO:0060078; P:regulation of postsynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0002028; P:regulation of sodium ion transport; IMP:MGI.
DR   GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR   GO; GO:0009408; P:response to heat; ISO:MGI.
DR   GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
DR   GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR   GO; GO:0098924; P:retrograde trans-synaptic signaling by nitric oxide; IMP:SynGO.
DR   GO; GO:0006941; P:striated muscle contraction; IMP:MGI.
DR   GO; GO:0099163; P:synaptic signaling by nitric oxide; IDA:SynGO.
DR   GO; GO:0042311; P:vasodilation; ISO:MGI.
DR   GO; GO:0042178; P:xenobiotic catabolic process; IMP:MGI.
DR   CDD; cd06202; Nitric_oxide_synthase; 1.
DR   CDD; cd00795; NOS_oxygenase_euk; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.90.440.10; Nitric Oxide Synthase;Heme Domain;Chain A domain 2; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR044943; NOS_dom_1.
DR   InterPro; IPR044940; NOS_dom_2.
DR   InterPro; IPR044944; NOS_dom_3.
DR   InterPro; IPR012144; NOS_euk.
DR   InterPro; IPR004030; NOS_N.
DR   InterPro; IPR036119; NOS_N_sf.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR   PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF02898; NO_synthase; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   PIRSF; PIRSF000333; NOS; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF56512; Nitric oxide (NO) synthase oxygenase domain; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR   PROSITE; PS60001; NOS; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   Genevisible; Q9Z0J4; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calmodulin-binding; Cell membrane;
KW   Cell projection; FAD; Flavoprotein; FMN; Heme; Iron; Membrane;
KW   Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Synapse; Ubl conjugation.
FT   CHAIN           1..1429
FT                   /note="Nitric oxide synthase 1"
FT                   /id="PRO_0000170922"
FT   DOMAIN          17..99
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          755..935
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   DOMAIN          990..1237
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          1..200
FT                   /note="Interaction with NOSIP"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   REGION          114..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..240
FT                   /note="Interaction with DYNLL1/PIN"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   REGION          271..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..745
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:2O60"
FT   COMPBIAS        114..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         334
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         415
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         478
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         587
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         588
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         592
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         677
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         678
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         691
FT                   /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT                   /ligand_id="ChEBI:CHEBI:59560"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         706
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P29475"
FT   BINDING         761
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         762
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         763
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         765
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         766
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         807
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         808
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         812
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         886
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         891
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         893
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         919
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         923
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1010
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1032
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1173
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1174
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1175
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1176
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1191
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1193
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1196
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1197
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1210
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1211
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1212
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1251
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1284
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1313
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1314
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1320
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1322
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1324
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1357
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1398
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   BINDING         1400
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   MOD_RES         280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         847
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29476"
FT   MOD_RES         857
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         858
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..331
FT                   /note="Missing (in isoform NNOS gamma)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003577"
FT   VAR_SEQ         1..230
FT                   /note="Missing (in isoform NNOS beta)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003575"
FT   VAR_SEQ         231..236
FT                   /note="TGIQVD -> MRGLGS (in isoform NNOS beta)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003576"
FT   VAR_SEQ         504..608
FT                   /note="Missing (in isoform N-NOS-2)"
FT                   /evidence="ECO:0000303|PubMed:7686743"
FT                   /id="VSP_003578"
FT   VAR_SEQ         839
FT                   /note="K -> KYPEPLRFFPRKGPSLSHVDSEAHSLVAARDSQHR (in isoform
FT                   NNOSMu)"
FT                   /evidence="ECO:0000303|PubMed:8626668"
FT                   /id="VSP_003579"
FT   CONFLICT        1320
FT                   /note="K -> Q (in Ref. 3; BAE24878)"
FT                   /evidence="ECO:0000305"
FT   HELIX           731..744
FT                   /evidence="ECO:0007829|PDB:2O60"
SQ   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
//