NOS1_HUMAN
ID NOS1_HUMAN Reviewed; 1434 AA.
AC P29475; E9PH30; O75713;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Nitric oxide synthase, brain;
DE EC=1.14.13.39;
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 AltName: Full=bNOS;
GN Name=NOS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=7528745; DOI=10.1016/s0021-9258(20)30099-5;
RA Hall A.V., Antoniou H., Wang Y., Cheung A.H., Arbus A.M., Olson S.L.,
RA Lu W.C., Kau C.-L., Marsden P.A.;
RT "Structural organization of the human neuronal nitric oxide synthase gene
RT (NOS1).";
RL J. Biol. Chem. 269:33082-33090(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum;
RX PubMed=7515942; DOI=10.1046/j.1471-4159.1994.63010140.x;
RA Fujisawa H., Ogura T., Kurashima Y., Yokoyama T., Yamashita J., Esumi H.;
RT "Expression of two types of nitric oxide synthase mRNA in human
RT neuroblastoma cell lines.";
RL J. Neurochem. 63:140-145(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=7678401; DOI=10.1016/0014-5793(93)81210-q;
RA Nakane M., Schmidt H.H.H.W., Pollock J.S., Foerstermann U., Murad F.;
RT "Cloned human brain nitric oxide synthase is highly expressed in skeletal
RT muscle.";
RL FEBS Lett. 316:175-180(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=8879752; DOI=10.1007/bf02150230;
RA Park C.-S., Gianotti C., Park R., Krishna G.;
RT "Neuronal isoform of nitric oxide synthase is expressed at low levels in
RT human retina.";
RL Cell. Mol. Neurobiol. 16:499-515(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3 AND 4).
RC TISSUE=Testis;
RX PubMed=9111048; DOI=10.1074/jbc.272.17.11128;
RA Wang Y., Goligorsky M.S., Lin M., Wilcox J.N., Marsden P.A.;
RT "A novel, testis-specific mRNA transcript encoding an NH2-terminal
RT truncated nitric-oxide synthase.";
RL J. Biol. Chem. 272:11392-11401(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-228; ALA-394; ASP-725;
RP ASP-864 AND ARG-1064.
RG NIEHS SNPs program;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 835-901 (ISOFORM 5), AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Skeletal muscle;
RX PubMed=9791007; DOI=10.1006/bbrc.1998.9578;
RA Larsson B., Phillips S.C.;
RT "Isolation and characterization of a novel, human neuronal nitric oxide
RT synthase cDNA.";
RL Biochem. Biophys. Res. Commun. 251:898-902(1998).
RN [9] {ECO:0007744|PDB:4D1N}
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 302-721 IN COMPLEX WITH
RP 5,6,7,8-TETRAHYDROBIOPTERIN; L-ARGININE AND HEME, AND COFACTOR.
RX PubMed=25286850; DOI=10.1107/s1399004714017064;
RA Li H., Jamal J., Plaza C., Pineda S.H., Chreifi G., Jing Q., Cinelli M.A.,
RA Silverman R.B., Poulos T.L.;
RT "Structures of human constitutive nitric oxide synthases.";
RL Acta Crystallogr. D 70:2667-2674(2014).
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.
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;
CC Evidence={ECO:0000269|PubMed:25286850};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD.;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Note=Binds 1 FMN.;
CC -!- COFACTOR:
CC Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000269|PubMed:25286850};
CC Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the
CC enzyme. {ECO:0000269|PubMed:25286850};
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.
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 -!- INTERACTION:
CC P29475; Q08AM6: VAC14; NbExp=5; IntAct=EBI-7164065, EBI-2107455;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane
CC protein. Cell projection, dendritic spine {ECO:0000250}. Note=In
CC skeletal muscle, it is localized beneath the sarcolemma of fast-twitch
CC muscle fiber by associating with the dystrophin glycoprotein complex.
CC In neurons, enriched in dendritic spines (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Isoform 3 is produced by different alternative splicing
CC events implicating either the untranslated exons TEX1 (TN-NOS) or
CC TEX1B (TN-NOSB) leading to a N-terminally truncated protein which
CC possesses enzymatic activity comparable to that of isoform 1. The
CC C-terminally truncated isoform 4 is produced by insertion of the TEX2
CC exon between exons 3 and 4 of isoform 1, leading to a frameshift and
CC a premature stop codon. {ECO:0000269|PubMed:9791007};
CC Name=1; Synonyms=N-NOS-1;
CC IsoId=P29475-1; Sequence=Displayed;
CC Name=2; Synonyms=N-NOS-2;
CC IsoId=P29475-2; Sequence=VSP_003574;
CC Name=3; Synonyms=TN-NOS, TN-NOSB;
CC IsoId=P29475-3; Sequence=VSP_003571;
CC Name=4; Synonyms=TEX2-insertion;
CC IsoId=P29475-4; Sequence=VSP_003572, VSP_003573;
CC Name=5; Synonyms=nNOSmu;
CC IsoId=P29475-5; Sequence=VSP_044916;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed: detected in
CC skeletal muscle and brain, also in testis, lung and kidney, and at low
CC levels in heart, adrenal gland and retina. Not detected in the
CC platelets. Isoform 3 is expressed only in testis. Isoform 4 is detected
CC in testis, skeletal muscle, lung, and kidney, at low levels in the
CC brain, but not in the heart and adrenal gland.
CC -!- DOMAIN: The PDZ domain in the N-terminal part of the neuronal isoform
CC participates in protein-protein interaction, and is responsible for
CC targeting nNos to synaptic membranes in muscles. Mediates interaction
CC with VAC14 (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}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/nos1/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Nitric oxide synthase entry;
CC URL="https://en.wikipedia.org/wiki/Nitric_oxide_synthase";
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DR EMBL; U17327; AAA62405.1; -; mRNA.
DR EMBL; U17326; AAB60654.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U17299; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17300; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17301; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17302; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17303; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17304; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17305; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17307; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17308; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17309; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17310; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17311; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17312; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17313; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17314; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17315; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17316; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17317; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17318; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17319; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17320; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17321; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17322; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17323; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17324; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; U17325; AAB60654.1; JOINED; Genomic_DNA.
DR EMBL; D16408; BAA03895.1; -; mRNA.
DR EMBL; L02881; AAA36376.1; -; mRNA.
DR EMBL; U31466; AAB49040.1; -; mRNA.
DR EMBL; U66362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY445095; AAR07069.1; -; Genomic_DNA.
DR EMBL; AC026364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ004918; CAA06218.1; -; mRNA.
DR CCDS; CCDS41842.1; -. [P29475-1]
DR CCDS; CCDS55890.1; -. [P29475-5]
DR PIR; G01946; G01946.
DR RefSeq; NP_000611.1; NM_000620.4. [P29475-1]
DR RefSeq; NP_001191142.1; NM_001204213.1. [P29475-3]
DR RefSeq; NP_001191143.1; NM_001204214.1. [P29475-3]
DR RefSeq; NP_001191147.1; NM_001204218.1. [P29475-5]
DR RefSeq; XP_011536700.1; XM_011538398.2.
DR RefSeq; XP_016874834.1; XM_017019345.1.
DR RefSeq; XP_016874835.1; XM_017019346.1.
DR RefSeq; XP_016874836.1; XM_017019347.1.
DR PDB; 4D1N; X-ray; 2.03 A; A/B/C/D=302-721.
DR PDB; 4UCH; X-ray; 2.20 A; A/B=302-723.
DR PDB; 4UH5; X-ray; 1.98 A; A/B=302-722.
DR PDB; 4UH6; X-ray; 1.98 A; A/B=302-722.
DR PDB; 4V3U; X-ray; 2.30 A; A/B/C/D=302-721.
DR PDB; 5ADF; X-ray; 1.97 A; A/B=302-722.
DR PDB; 5ADG; X-ray; 1.98 A; A/B=302-722.
DR PDB; 5ADI; X-ray; 2.20 A; A/B=302-722.
DR PDB; 5FVU; X-ray; 2.22 A; A/B=302-722.
DR PDB; 5FVV; X-ray; 2.05 A; A/B=302-722.
DR PDB; 5FVW; X-ray; 2.20 A; A/B=302-722.
DR PDB; 5FVX; X-ray; 2.30 A; A/B=302-722.
DR PDB; 5UO1; X-ray; 1.90 A; A/B=302-722.
DR PDB; 5UO2; X-ray; 1.95 A; A/B=302-722.
DR PDB; 5UO3; X-ray; 2.20 A; A/B=302-722.
DR PDB; 5UO4; X-ray; 2.00 A; A/B=302-722.
DR PDB; 5UO5; X-ray; 2.00 A; A/B=302-722.
DR PDB; 5UO6; X-ray; 1.96 A; A/B=302-722.
DR PDB; 5UO7; X-ray; 2.06 A; A/B=302-722.
DR PDB; 5VUV; X-ray; 1.98 A; A/B=302-722.
DR PDB; 5VUW; X-ray; 2.03 A; A/B=302-722.
DR PDB; 5VUX; X-ray; 2.30 A; A/B=302-722.
DR PDB; 5VUY; X-ray; 2.15 A; A/B=302-722.
DR PDB; 5VUZ; X-ray; 1.97 A; A/B=302-722.
DR PDB; 5VV0; X-ray; 1.80 A; A/B=302-722.
DR PDB; 5VV1; X-ray; 1.95 A; A/B=302-722.
DR PDB; 5VV2; X-ray; 2.00 A; A/B=302-722.
DR PDB; 5VV3; X-ray; 2.18 A; A/B=302-722.
DR PDB; 5VV4; X-ray; 2.10 A; A/B=302-722.
DR PDB; 5VV5; X-ray; 2.15 A; A/B=302-722.
DR PDB; 6AUY; X-ray; 1.92 A; A/B=302-722.
DR PDB; 6AUZ; X-ray; 2.00 A; A/B=302-722.
DR PDB; 6AV0; X-ray; 2.00 A; A/B=302-722.
DR PDB; 6AV1; X-ray; 2.45 A; A/B=302-722.
DR PDB; 6AV2; X-ray; 2.10 A; A/B=302-722.
DR PDB; 6AV3; X-ray; 1.95 A; A/B=302-722.
DR PDB; 6AV4; X-ray; 1.87 A; A/B=302-722.
DR PDB; 6AV5; X-ray; 1.90 A; A/B=302-722.
DR PDB; 6CIC; X-ray; 1.75 A; A/B=302-722.
DR PDB; 6CID; X-ray; 1.75 A; A/B=302-722.
DR PDB; 6NG1; X-ray; 2.15 A; A/B=302-722.
DR PDB; 6NG2; X-ray; 1.93 A; A/B=302-722.
DR PDB; 6NG4; X-ray; 1.78 A; A/B=302-722.
DR PDB; 6NG5; X-ray; 1.96 A; A/B=302-722.
DR PDB; 6NG6; X-ray; 2.04 A; A/B=302-722.
DR PDB; 6NG7; X-ray; 2.00 A; A/B=302-722.
DR PDB; 6NG8; X-ray; 1.90 A; A/B=302-722.
DR PDB; 6NGA; X-ray; 1.98 A; A/B=302-722.
DR PDB; 6NGB; X-ray; 1.90 A; A/B=302-722.
DR PDB; 6NGC; X-ray; 2.00 A; A/B=302-722.
DR PDB; 6NGD; X-ray; 1.80 A; A/B=302-722.
DR PDB; 6NGE; X-ray; 2.10 A; A/B=302-722.
DR PDB; 6NGF; X-ray; 1.99 A; A/B=302-722.
DR PDB; 6NGH; X-ray; 2.00 A; A/B=302-722.
DR PDB; 6NGI; X-ray; 1.80 A; A/B=302-722.
DR PDB; 6NHB; X-ray; 2.03 A; A/B=302-722.
DR PDB; 6NHC; X-ray; 2.16 A; A/B=302-722.
DR PDB; 6PNA; X-ray; 1.95 A; A/B=302-722.
DR PDB; 6PNB; X-ray; 2.05 A; A/B=302-722.
DR PDB; 6PNC; X-ray; 2.15 A; A/B=302-722.
DR PDB; 6PND; X-ray; 2.40 A; A/B=302-722.
DR PDB; 6PNE; X-ray; 2.10 A; A/B=302-722.
DR PDB; 6PNF; X-ray; 2.10 A; A/B=302-722.
DR PDB; 6PNG; X-ray; 1.77 A; A/B=302-722.
DR PDB; 6PNH; X-ray; 1.85 A; A/B=302-722.
DR PDB; 6PO5; X-ray; 1.82 A; A/B=302-722.
DR PDB; 6PO7; X-ray; 1.95 A; A/B=302-722.
DR PDB; 6PO8; X-ray; 1.90 A; A/B=302-722.
DR PDB; 6PO9; X-ray; 1.81 A; A/B=302-722.
DR PDB; 6POA; X-ray; 1.81 A; A/B=302-722.
DR PDB; 6POB; X-ray; 1.95 A; A/B=302-722.
DR PDB; 6POC; X-ray; 2.00 A; A/B=302-722.
DR PDB; 6POT; X-ray; 2.30 A; A/B=302-722.
DR PDBsum; 4D1N; -.
DR PDBsum; 4UCH; -.
DR PDBsum; 4UH5; -.
DR PDBsum; 4UH6; -.
DR PDBsum; 4V3U; -.
DR PDBsum; 5ADF; -.
DR PDBsum; 5ADG; -.
DR PDBsum; 5ADI; -.
DR PDBsum; 5FVU; -.
DR PDBsum; 5FVV; -.
DR PDBsum; 5FVW; -.
DR PDBsum; 5FVX; -.
DR PDBsum; 5UO1; -.
DR PDBsum; 5UO2; -.
DR PDBsum; 5UO3; -.
DR PDBsum; 5UO4; -.
DR PDBsum; 5UO5; -.
DR PDBsum; 5UO6; -.
DR PDBsum; 5UO7; -.
DR PDBsum; 5VUV; -.
DR PDBsum; 5VUW; -.
DR PDBsum; 5VUX; -.
DR PDBsum; 5VUY; -.
DR PDBsum; 5VUZ; -.
DR PDBsum; 5VV0; -.
DR PDBsum; 5VV1; -.
DR PDBsum; 5VV2; -.
DR PDBsum; 5VV3; -.
DR PDBsum; 5VV4; -.
DR PDBsum; 5VV5; -.
DR PDBsum; 6AUY; -.
DR PDBsum; 6AUZ; -.
DR PDBsum; 6AV0; -.
DR PDBsum; 6AV1; -.
DR PDBsum; 6AV2; -.
DR PDBsum; 6AV3; -.
DR PDBsum; 6AV4; -.
DR PDBsum; 6AV5; -.
DR PDBsum; 6CIC; -.
DR PDBsum; 6CID; -.
DR PDBsum; 6NG1; -.
DR PDBsum; 6NG2; -.
DR PDBsum; 6NG4; -.
DR PDBsum; 6NG5; -.
DR PDBsum; 6NG6; -.
DR PDBsum; 6NG7; -.
DR PDBsum; 6NG8; -.
DR PDBsum; 6NGA; -.
DR PDBsum; 6NGB; -.
DR PDBsum; 6NGC; -.
DR PDBsum; 6NGD; -.
DR PDBsum; 6NGE; -.
DR PDBsum; 6NGF; -.
DR PDBsum; 6NGH; -.
DR PDBsum; 6NGI; -.
DR PDBsum; 6NHB; -.
DR PDBsum; 6NHC; -.
DR PDBsum; 6PNA; -.
DR PDBsum; 6PNB; -.
DR PDBsum; 6PNC; -.
DR PDBsum; 6PND; -.
DR PDBsum; 6PNE; -.
DR PDBsum; 6PNF; -.
DR PDBsum; 6PNG; -.
DR PDBsum; 6PNH; -.
DR PDBsum; 6PO5; -.
DR PDBsum; 6PO7; -.
DR PDBsum; 6PO8; -.
DR PDBsum; 6PO9; -.
DR PDBsum; 6POA; -.
DR PDBsum; 6POB; -.
DR PDBsum; 6POC; -.
DR PDBsum; 6POT; -.
DR AlphaFoldDB; P29475; -.
DR BMRB; P29475; -.
DR SMR; P29475; -.
DR BioGRID; 110905; 35.
DR CORUM; P29475; -.
DR DIP; DIP-40999N; -.
DR IntAct; P29475; 7.
DR MINT; P29475; -.
DR STRING; 9606.ENSP00000477999; -.
DR BindingDB; P29475; -.
DR ChEMBL; CHEMBL3568; -.
DR DrugBank; DB02143; 1-hydroxy-2-isopropylguanidine.
DR DrugBank; DB02727; 2-butyl-1-hydroxyguanidine.
DR DrugBank; DB01997; 3-Bromo-7-Nitroindazole.
DR DrugBank; DB03892; 5-N-Allyl-arginine.
DR DrugBank; DB03710; [(1S)-4-(1-Aminobutylideneamino)-1-carboxybutyl]azanium.
DR DrugBank; DB00155; Citrulline.
DR DrugBank; DB00843; Donepezil.
DR DrugBank; DB00997; Doxorubicin.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB03247; Flavin mononucleotide.
DR DrugBank; DB01942; Formic acid.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB02077; L-N(omega)-nitroarginine-(4R)-amino-L-proline amide.
DR DrugBank; DB01821; L-N(omega)-Nitroarginine-2,4-L-diaminobutyric amide.
DR DrugBank; DB09241; Methylene blue.
DR DrugBank; DB03144; N(5)-[(hydroxyamino)(imino)methyl]-L-ornithine.
DR DrugBank; DB03449; N-(4-{2-[(3-chlorobenzyl)amino]ethyl}phenyl)thiophene-2-carboximidamide.
DR DrugBank; DB02044; N-[3-(aminomethyl)benzyl]acetamidine.
DR DrugBank; DB02644; N-omega-propyl-L-arginine.
DR DrugBank; DB08019; N-{(3R,4S)-4-[(6-amino-4-methylpyridin-2-yl)methyl]pyrrolidin-3-yl}-N'-(3-chlorobenzyl)ethane-1,2-diamine.
DR DrugBank; DB08018; N-{(3S,4S)-4-[(6-AMINO-4-METHYLPYRIDIN-2-YL)METHYL]PYRROLIDIN-3-YL}-N'-(4-CHLOROBENZYL)ETHANE-1,2-DIAMINE.
DR DrugBank; DB02027; N-{(4S)-4-Amino-5-[(2-aminoethyl)amino]pentyl}-N'-nitroguanidine.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR DrugBank; DB04223; Nitroarginine.
DR DrugBank; DB06096; NXN-188.
DR DrugBank; DB02991; S-Ethyl-N-[4-(Trifluoromethyl)Phenyl]Isothiourea.
DR DrugBank; DB03707; S-Ethyl-N-Phenyl-Isothiourea.
DR DrugCentral; P29475; -.
DR GuidetoPHARMACOLOGY; 1251; -.
DR iPTMnet; P29475; -.
DR PhosphoSitePlus; P29475; -.
DR BioMuta; NOS1; -.
DR DMDM; 1709333; -.
DR jPOST; P29475; -.
DR MassIVE; P29475; -.
DR MaxQB; P29475; -.
DR PaxDb; P29475; -.
DR PeptideAtlas; P29475; -.
DR PRIDE; P29475; -.
DR ProteomicsDB; 20446; -.
DR ProteomicsDB; 54578; -. [P29475-1]
DR ProteomicsDB; 54579; -. [P29475-2]
DR ProteomicsDB; 54580; -. [P29475-3]
DR ProteomicsDB; 54581; -. [P29475-4]
DR ABCD; P29475; 2 sequenced antibodies.
DR Antibodypedia; 3691; 951 antibodies from 47 providers.
DR DNASU; 4842; -.
DR Ensembl; ENST00000317775.11; ENSP00000320758.6; ENSG00000089250.20. [P29475-1]
DR Ensembl; ENST00000338101.8; ENSP00000337459.4; ENSG00000089250.20. [P29475-5]
DR Ensembl; ENST00000618760.4; ENSP00000477999.1; ENSG00000089250.20. [P29475-5]
DR GeneID; 4842; -.
DR KEGG; hsa:4842; -.
DR MANE-Select; ENST00000317775.11; ENSP00000320758.6; NM_000620.5; NP_000611.1.
DR UCSC; uc001twm.3; human. [P29475-1]
DR CTD; 4842; -.
DR DisGeNET; 4842; -.
DR GeneCards; NOS1; -.
DR HGNC; HGNC:7872; NOS1.
DR HPA; ENSG00000089250; Group enriched (brain, skeletal muscle, tongue).
DR MalaCards; NOS1; -.
DR MIM; 163731; gene.
DR neXtProt; NX_P29475; -.
DR OpenTargets; ENSG00000089250; -.
DR Orphanet; 930; Idiopathic achalasia.
DR PharmGKB; PA252; -.
DR VEuPathDB; HostDB:ENSG00000089250; -.
DR eggNOG; KOG1158; Eukaryota.
DR GeneTree; ENSGT00940000159357; -.
DR HOGENOM; CLU_001570_16_0_1; -.
DR InParanoid; P29475; -.
DR OMA; KCPEPLR; -.
DR PhylomeDB; P29475; -.
DR TreeFam; TF324410; -.
DR BioCyc; MetaCyc:HS01647-MON; -.
DR BRENDA; 1.14.13.39; 2681.
DR PathwayCommons; P29475; -.
DR Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-HSA-392154; Nitric oxide stimulates guanylate cyclase.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR SignaLink; P29475; -.
DR SIGNOR; P29475; -.
DR BioGRID-ORCS; 4842; 17 hits in 1076 CRISPR screens.
DR ChiTaRS; NOS1; human.
DR GeneWiki; NOS1; -.
DR GenomeRNAi; 4842; -.
DR Pharos; P29475; Tchem.
DR PRO; PR:P29475; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P29475; protein.
DR Bgee; ENSG00000089250; Expressed in body of tongue and 123 other tissues.
DR ExpressionAtlas; P29475; baseline and differential.
DR Genevisible; P29475; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0071944; C:cell periphery; ISS:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:ARUK-UCL.
DR GO; GO:0005856; C:cytoskeleton; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISS:BHF-UCL.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; ISS:BHF-UCL.
DR GO; GO:0012506; C:vesicle membrane; IBA:GO_Central.
DR GO; GO:0034618; F:arginine binding; TAS:BHF-UCL.
DR GO; GO:0046870; F:cadmium ion binding; ISS:BHF-UCL.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:ARUK-UCL.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:BHF-UCL.
DR GO; GO:0010181; F:FMN binding; ISS:BHF-UCL.
DR GO; GO:0020037; F:heme binding; ISS:BHF-UCL.
DR GO; GO:0050661; F:NADP binding; ISS:BHF-UCL.
DR GO; GO:0004517; F:nitric-oxide synthase activity; IDA:CACAO.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0097110; F:scaffold protein binding; ISS:BHF-UCL.
DR GO; GO:0017080; F:sodium channel regulator activity; ISS:BHF-UCL.
DR GO; GO:0034617; F:tetrahydrobiopterin binding; NAS:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:BHF-UCL.
DR GO; GO:0006527; P:arginine catabolic process; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; TAS:Reactome.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:BHF-UCL.
DR GO; GO:0033555; P:multicellular organismal response to stress; IMP:BHF-UCL.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0007520; P:myoblast fusion; TAS:BHF-UCL.
DR GO; GO:0045776; P:negative regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; ISS:BHF-UCL.
DR GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; TAS:BHF-UCL.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; ISS:BHF-UCL.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; ISS:BHF-UCL.
DR GO; GO:0051612; P:negative regulation of serotonin uptake; ISS:BHF-UCL.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; TAS:BHF-UCL.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:GO_Central.
DR GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; ISS:BHF-UCL.
DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0035066; P:positive regulation of histone acetylation; ISS:BHF-UCL.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:ARUK-UCL.
DR GO; GO:1902307; P:positive regulation of sodium ion transmembrane transport; ISS:BHF-UCL.
DR GO; GO:0098735; P:positive regulation of the force of heart contraction; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; TAS:BHF-UCL.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; TAS:BHF-UCL.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; TAS:BHF-UCL.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:BHF-UCL.
DR GO; GO:0009408; P:response to heat; IDA:BHF-UCL.
DR GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IEP:BHF-UCL.
DR GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0098924; P:retrograde trans-synaptic signaling by nitric oxide; IBA:GO_Central.
DR GO; GO:0006941; P:striated muscle contraction; ISS:BHF-UCL.
DR GO; GO:0042311; P:vasodilation; IDA:BHF-UCL.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISS:BHF-UCL.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR Gene3D; 3.90.1230.10; -; 1.
DR Gene3D; 3.90.340.10; -; 1.
DR Gene3D; 3.90.440.10; -; 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 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; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF56512; SSF56512; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS60001; NOS; 1.
DR PROSITE; PS50106; PDZ; 1.
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..1434
FT /note="Nitric oxide synthase, brain"
FT /id="PRO_0000170921"
FT DOMAIN 17..99
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 760..940
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT DOMAIN 995..1242
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..205
FT /note="Interaction with NOSIP"
FT /evidence="ECO:0000250"
FT REGION 112..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..245
FT /note="PIN (nNOS-inhibiting protein) binding"
FT REGION 276..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..750
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 280..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 339
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000269|PubMed:25286850,
FT ECO:0007744|PDB:4D1N"
FT BINDING 420
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:0000269|PubMed:25286850,
FT ECO:0007744|PDB:4D1N"
FT BINDING 483
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:25286850,
FT ECO:0007744|PDB:4D1N"
FT BINDING 592
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:25286850,
FT ECO:0007744|PDB:4D1N"
FT BINDING 593
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:25286850,
FT ECO:0007744|PDB:4D1N"
FT BINDING 597
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:25286850,
FT ECO:0007744|PDB:4D1N"
FT BINDING 682
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000269|PubMed:25286850,
FT ECO:0007744|PDB:4D1N"
FT BINDING 683
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000269|PubMed:25286850,
FT ECO:0007744|PDB:4D1N"
FT BINDING 696
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000269|PubMed:25286850,
FT ECO:0007744|PDB:4D1N"
FT BINDING 711
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:25286850,
FT ECO:0007744|PDB:4D1N"
FT BINDING 886..917
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 1032..1043
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 1175..1185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 1250..1268
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 1348..1363
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29476"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0J4"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0J4"
FT VAR_SEQ 1..336
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003571"
FT VAR_SEQ 285..407
FT /note="PPTSGKQSPTKNGSPSKCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYIC
FT MGSIMHPSQHARRPEDVRTKGQLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDT
FT TSTYQLKDTELI -> MRKLRITEGFGVQRGSHNHPPPQENSPPQRMAAPPSVHASSRS
FT RTGRLRWFSLTPSTLRAHWKRDALSTSAWAPSCILLSMQGGLKTSAQKDSSSLSPKSLL
FT INTIHQLKDLAPKPTWKGWKR (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003572"
FT VAR_SEQ 408..1434
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003573"
FT VAR_SEQ 509..613
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7515942,
FT ECO:0000303|PubMed:7678401"
FT /id="VSP_003574"
FT VAR_SEQ 844
FT /note="K -> KYPEPLRFFPRKGPPLPNGDTEVHGLAAARDSQHR (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:9791007"
FT /id="VSP_044916"
FT VARIANT 228
FT /note="P -> S (in dbSNP:rs9658279)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_018948"
FT VARIANT 394
FT /note="D -> A (in dbSNP:rs9658356)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_018949"
FT VARIANT 725
FT /note="N -> D (in dbSNP:rs9658403)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_018950"
FT VARIANT 864
FT /note="G -> D (in dbSNP:rs9658445)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_018951"
FT VARIANT 1064
FT /note="Q -> R (in dbSNP:rs9658482)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_018952"
FT CONFLICT 131
FT /note="K -> E (in Ref. 4; AAB49040)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..184
FT /note="LAPRPPG -> WPQAPR (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 492..493
FT /note="QP -> HR (in Ref. 3; AAA36376)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="V -> L (in Ref. 3; AAA36376)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="G -> A (in Ref. 3; AAA36376)"
FT /evidence="ECO:0000305"
FT CONFLICT 1407
FT /note="Y -> I (in Ref. 3; AAA36376)"
FT /evidence="ECO:0000305"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:6CID"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:6NG6"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 356..373
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 380..396
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 403..415
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 440..455
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 471..475
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 504..512
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:6POA"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 557..562
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 565..568
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 595..599
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 601..604
FT /evidence="ECO:0007829|PDB:6CID"
FT TURN 606..609
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 612..618
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 630..648
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 656..674
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 681..684
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 687..689
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 690..692
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 694..697
FT /evidence="ECO:0007829|PDB:6CID"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:6AV1"
FT STRAND 706..711
FT /evidence="ECO:0007829|PDB:6CID"
FT HELIX 715..718
FT /evidence="ECO:0007829|PDB:6CID"
SQ SEQUENCE 1434 AA; 160970 MW; 99235793B953BF37 CRC64;
MEDHMFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA
GDIILAVNGR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI
RVTQPLGPPT KAVDLSHQPP AGKEQPLAVD GASGPGNGPQ HAYDDGQEAG SLPHANGLAP
RPPGQDPAKK ATRVSLQGRG ENNELLKEIE PVLSLLTSGS RGVKGGAPAK AEMKDMGIQV
DRDLDGKSHK PLPLGVENDR VFNDLWGKGN VPVVLNNPYS EKEQPPTSGK QSPTKNGSPS
KCPRFLKVKN WETEVVLTDT LHLKSTLETG CTEYICMGSI MHPSQHARRP EDVRTKGQLF
PLAKEFIDQY YSSIKRFGSK AHMERLEEVN KEIDTTSTYQ LKDTELIYGA KHAWRNASRC
VGRIQWSKLQ VFDARDCTTA HGMFNYICNH VKYATNKGNL RSAITIFPQR TDGKHDFRVW
NSQLIRYAGY KQPDGSTLGD PANVQFTEIC IQQGWKPPRG RFDVLPLLLQ ANGNDPELFQ
IPPELVLEVP IRHPKFEWFK DLGLKWYGLP AVSNMLLEIG GLEFSACPFS GWYMGTEIGV
RDYCDNSRYN ILEEVAKKMN LDMRKTSSLW KDQALVEINI AVLYSFQSDK VTIVDHHSAT
ESFIKHMENE YRCRGGCPAD WVWIVPPMSG SITPVFHQEM LNYRLTPSFE YQPDPWNTHV
WKGTNGTPTK RRAIGFKKLA EAVKFSAKLM GQAMAKRVKA TILYATETGK SQAYAKTLCE
IFKHAFDAKV MSMEEYDIVH LEHETLVLVV TSTFGNGDPP ENGEKFGCAL MEMRHPNSVQ
EERKSYKVRF NSVSSYSDSQ KSSGDGPDLR DNFESAGPLA NVRFSVFGLG SRAYPHFCAF
GHAVDTLLEE LGGERILKMR EGDELCGQEE AFRTWAKKVF KAACDVFCVG DDVNIEKANN
SLISNDRSWK RNKFRLTFVA EAPELTQGLS NVHKKRVSAA RLLSRQNLQS PKSSRSTIFV
RLHTNGSQEL QYQPGDHLGV FPGNHEDLVN ALIERLEDAP PVNQMVKVEL LEERNTALGV
ISNWTDELRL PPCTIFQAFK YYLDITTPPT PLQLQQFASL ATSEKEKQRL LVLSKGLQEY
EEWKWGKNPT IVEVLEEFPS IQMPATLLLT QLSLLQPRYY SISSSPDMYP DEVHLTVAIV
SYRTRDGEGP IHHGVCSSWL NRIQADELVP CFVRGAPSFH LPRNPQVPCI LVGPGTGIAP
FRSFWQQRQF DIQHKGMNPC PMVLVFGCRQ SKIDHIYREE TLQAKNKGVF RELYTAYSRE
PDKPKKYVQD ILQEQLAESV YRALKEQGGH IYVCGDVTMA ADVLKAIQRI MTQQGKLSAE
DAGVFISRMR DDNRYHEDIF GVTLRTYEVT NRLRSESIAF IEESKKDTDE VFSS
