CASP3_MOUSE
ID CASP3_MOUSE Reviewed; 277 AA.
AC P70677; O08668; Q8CHV5; Q9QWI4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Caspase-3;
DE Short=CASP-3;
DE EC=3.4.22.56 {ECO:0000269|PubMed:12124386, ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:33725486};
DE AltName: Full=Apopain;
DE AltName: Full=Cysteine protease CPP32;
DE Short=CPP-32;
DE AltName: Full=LICE;
DE AltName: Full=Protein Yama;
DE AltName: Full=SREBP cleavage activity 1;
DE Short=SCA-1;
DE Contains:
DE RecName: Full=Caspase-3 subunit p17;
DE Contains:
DE RecName: Full=Caspase-3 subunit p12;
DE Flags: Precursor;
GN Name=Casp3; Synonyms=Cpp32;
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 [GENOMIC DNA / MRNA].
RX PubMed=8761296;
RA Juan T.S.-C., McNiece I.K., Jenkins N.A., Gilbert D.J., Copeland N.G.,
RA Fletcher F.A.;
RT "Molecular characterization of mouse and rat CPP32 beta gene encoding a
RT cysteine protease resembling interleukin-1 beta converting enzyme and CED-
RT 3.";
RL Oncogene 13:749-755(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9070890; DOI=10.1006/bbrc.1996.6002;
RA Mukasa T., Urase K., Momoi M.Y., Kimura I., Momoi T.;
RT "Specific expression of CPP32 in sensory neurons of mouse embryos and
RT activation of CPP32 in the apoptosis induced by a withdrawal of NGF.";
RL Biochem. Biophys. Res. Commun. 231:770-774(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/An;
RX PubMed=9038361; DOI=10.1016/s0014-5793(97)00026-4;
RA van de Craen M., Vandenabeele P., Declercq W., van den Brande I.,
RA van Loo G., Molemans F., Schotte P., van Criekinge W., Beyaert R.,
RA Fiers W.;
RT "Characterization of seven murine caspase family members.";
RL FEBS Lett. 403:61-69(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Fernandes-Alnemri T., Litwack G., Alnemri E.S.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-277.
RA Denis F., Alam A., Cohen L., Hartgers F., Braun M., Martinez O.,
RA Fortin J.-P., Sekaly R.-P.;
RT "Multiple pathways of apoptosis converging on the CPP32 protease.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12124386; DOI=10.1074/jbc.m203805200;
RA Xu J., Liu D., Songyang Z.;
RT "The role of Asp-462 in regulating Akt activity.";
RL J. Biol. Chem. 277:35561-35566(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25231987; DOI=10.1074/jbc.m114.583419;
RA Suzuki J., Imanishi E., Nagata S.;
RT "Exposure of phosphatidylserine by Xk-related protein family members during
RT apoptosis.";
RL J. Biol. Chem. 289:30257-30267(2014).
RN [13]
RP FUNCTION.
RX PubMed=30878284; DOI=10.1016/j.molcel.2019.02.013;
RA Ning X., Wang Y., Jing M., Sha M., Lv M., Gao P., Zhang R., Huang X.,
RA Feng J.M., Jiang Z.;
RT "Apoptotic caspases suppress type i interferon production via the cleavage
RT of cGAS, MAVS, and IRF3.";
RL Mol. Cell 74:19-31(2019).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33725486; DOI=10.1016/j.molcel.2021.02.025;
RA Maruoka M., Zhang P., Mori H., Imanishi E., Packwood D.M., Harada H.,
RA Kosako H., Suzuki J.;
RT "Caspase cleavage releases a nuclear protein fragment that stimulates
RT phospholipid scrambling at the plasma membrane.";
RL Mol. Cell 81:1397-1410(2021).
CC -!- FUNCTION: Involved in the activation cascade of caspases responsible
CC for apoptosis execution. At the onset of apoptosis it proteolytically
CC cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217'
CC bond. Cleaves and activates sterol regulatory element binding proteins
CC (SREBPs) between the basic helix-loop-helix leucine zipper domain and
CC the membrane attachment domain. Cleaves and activates caspase-6, -7 and
CC -9. Triggers cell adhesion in sympathetic neurons through RET cleavage
CC (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing
CC the mature cytokine which is involved in a variety of inflammatory
CC processes (By similarity). Cleaves and inhibits serine/threonine-
CC protein kinase AKT1 in response to oxidative stress (PubMed:12124386).
CC Acts as an inhibitor of type I interferon production during virus-
CC induced apoptosis by mediating cleavage of antiviral proteins CGAS,
CC IRF3 and MAVS, thereby preventing cytokine overproduction
CC (PubMed:30878284). Cleaves XRCC4 and phospholipid scramblase proteins
CC XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on
CC apoptotic cell surface (PubMed:25231987, PubMed:33725486).
CC {ECO:0000250|UniProtKB:P42574, ECO:0000269|PubMed:12124386,
CC ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:30878284,
CC ECO:0000269|PubMed:33725486}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Strict requirement for an Asp residue at positions P1 and P4.
CC It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a
CC hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid
CC residue at P3, although Val or Ala are also accepted at this
CC position.; EC=3.4.22.56; Evidence={ECO:0000269|PubMed:12124386,
CC ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:33725486};
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12)
CC subunit. Interacts with BIRC6/bruce. {ECO:0000250}.
CC -!- INTERACTION:
CC P70677; P42859: Htt; NbExp=2; IntAct=EBI-1790419, EBI-5327353;
CC P70677; P11103: Parp1; NbExp=3; IntAct=EBI-1790419, EBI-642213;
CC P70677; P62270: Rps18; NbExp=5; IntAct=EBI-1790419, EBI-352460;
CC P70677; Q96EK4: THAP11; Xeno; NbExp=2; IntAct=EBI-1790419, EBI-1790529;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highest expression in spleen, lung, liver, kidney
CC and heart. Lower expression in brain, skeletal muscle and testis.
CC -!- PTM: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10
CC generates the two active subunits. Additional processing of the
CC propeptides is likely due to the autocatalytic activity of the
CC activated protease. Active heterodimers between the small subunit of
CC caspase-7 protease and the large subunit of caspase-3 also occur and
CC vice versa (By similarity). {ECO:0000250}.
CC -!- PTM: S-nitrosylated on its catalytic site cysteine in unstimulated
CC human cell lines and denitrosylated upon activation of the Fas
CC apoptotic pathway, associated with an increase in intracellular caspase
CC activity. Fas therefore activates caspase-3 not only by inducing the
CC cleavage of the caspase zymogen to its active subunits, but also by
CC stimulating the denitrosylation of its active site thiol (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR EMBL; U54803; AAC52768.1; -; Genomic_DNA.
DR EMBL; U54802; AAC52768.1; JOINED; Genomic_DNA.
DR EMBL; U49929; AAC52764.1; -; mRNA.
DR EMBL; D86352; BAA21727.1; -; mRNA.
DR EMBL; Y13086; CAA73528.1; -; mRNA.
DR EMBL; U19522; AAC53196.1; -; mRNA.
DR EMBL; BC038825; AAH38825.2; -; mRNA.
DR EMBL; U63720; AAD09504.1; -; mRNA.
DR CCDS; CCDS22294.1; -.
DR PIR; JC5410; JC5410.
DR RefSeq; NP_001271338.1; NM_001284409.1.
DR RefSeq; NP_033940.1; NM_009810.3.
DR RefSeq; XP_017168032.1; XM_017312543.1.
DR AlphaFoldDB; P70677; -.
DR SMR; P70677; -.
DR BioGRID; 198497; 28.
DR ComplexPortal; CPX-3803; Caspase-3 complex.
DR DIP; DIP-44076N; -.
DR ELM; P70677; -.
DR IntAct; P70677; 11.
DR MINT; P70677; -.
DR STRING; 10090.ENSMUSP00000091238; -.
DR BindingDB; P70677; -.
DR ChEMBL; CHEMBL5632; -.
DR MEROPS; C14.003; -.
DR iPTMnet; P70677; -.
DR PhosphoSitePlus; P70677; -.
DR SwissPalm; P70677; -.
DR EPD; P70677; -.
DR jPOST; P70677; -.
DR MaxQB; P70677; -.
DR PaxDb; P70677; -.
DR PeptideAtlas; P70677; -.
DR PRIDE; P70677; -.
DR ProteomicsDB; 283677; -.
DR Antibodypedia; 1222; 2462 antibodies from 54 providers.
DR DNASU; 12367; -.
DR Ensembl; ENSMUST00000093517; ENSMUSP00000091238; ENSMUSG00000031628.
DR Ensembl; ENSMUST00000211115; ENSMUSP00000147767; ENSMUSG00000031628.
DR GeneID; 12367; -.
DR KEGG; mmu:12367; -.
DR UCSC; uc009lql.2; mouse.
DR CTD; 836; -.
DR MGI; MGI:107739; Casp3.
DR VEuPathDB; HostDB:ENSMUSG00000031628; -.
DR eggNOG; KOG3573; Eukaryota.
DR GeneTree; ENSGT00940000153232; -.
DR HOGENOM; CLU_036904_2_0_1; -.
DR InParanoid; P70677; -.
DR OMA; PDESYKM; -.
DR OrthoDB; 984395at2759; -.
DR PhylomeDB; P70677; -.
DR TreeFam; TF102023; -.
DR BRENDA; 3.4.22.56; 3474.
DR Reactome; R-MMU-111459; Activation of caspases through apoptosome-mediated cleavage.
DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-MMU-111469; SMAC, XIAP-regulated apoptotic response.
DR Reactome; R-MMU-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-MMU-205025; NADE modulates death signalling.
DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-MMU-418889; Caspase activation via Dependence Receptors in the absence of ligand.
DR Reactome; R-MMU-449836; Other interleukin signaling.
DR Reactome; R-MMU-5620971; Pyroptosis.
DR BioGRID-ORCS; 12367; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Casp3; mouse.
DR PRO; PR:P70677; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P70677; protein.
DR Bgee; ENSMUSG00000031628; Expressed in cortical plate and 260 other tissues.
DR ExpressionAtlas; P70677; baseline and differential.
DR Genevisible; P70677; MM.
DR GO; GO:0008303; C:caspase complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031264; C:death-inducing signaling complex; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:MGI.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IMP:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:MGI.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:MGI.
DR GO; GO:0005123; F:death receptor binding; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0016005; F:phospholipase A2 activator activity; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0061713; P:anterior neural tube closure; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0007413; P:axonal fasciculation; ISO:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0072734; P:cellular response to staurosporine; ISO:MGI.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IDA:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; ISO:MGI.
DR GO; GO:0097194; P:execution phase of apoptosis; IDA:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:ComplexPortal.
DR GO; GO:0044346; P:fibroblast apoptotic process; IDA:MGI.
DR GO; GO:0034349; P:glial cell apoptotic process; IMP:MGI.
DR GO; GO:0007507; P:heart development; IGI:MGI.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IC:ComplexPortal.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; NAS:ParkinsonsUK-UCL.
DR GO; GO:0008627; P:intrinsic apoptotic signaling pathway in response to osmotic stress; IDA:CAFA.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0071887; P:leukocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0001554; P:luteolysis; IEA:Ensembl.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:MGI.
DR GO; GO:0045786; P:negative regulation of cell cycle; IMP:MGI.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISO:MGI.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISS:UniProtKB.
DR GO; GO:1902512; P:positive regulation of apoptotic DNA fragmentation; IDA:ComplexPortal.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:CAFA.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0016485; P:protein processing; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0032025; P:response to cobalt ion; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; ISO:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; IDA:MGI.
DR GO; GO:0009411; P:response to UV; IDA:MGI.
DR GO; GO:0009611; P:response to wounding; IDA:MGI.
DR GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR CDD; cd00032; CASc; 1.
DR InterPro; IPR015471; Casp3/7.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR002398; Pept_C14.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR PANTHER; PTHR10454:SF31; PTHR10454:SF31; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Cytoplasm; Hydrolase; Phosphoprotein; Protease;
KW Reference proteome; S-nitrosylation; Thiol protease; Zymogen.
FT PROPEP 1..9
FT /evidence="ECO:0000250"
FT /id="PRO_0000004573"
FT PROPEP 10..28
FT /evidence="ECO:0000250"
FT /id="PRO_0000004574"
FT CHAIN 29..175
FT /note="Caspase-3 subunit p17"
FT /id="PRO_0000004575"
FT CHAIN 176..277
FT /note="Caspase-3 subunit p12"
FT /id="PRO_0000004576"
FT ACT_SITE 121
FT /evidence="ECO:0000250"
FT ACT_SITE 163
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P42574"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 163
FT /note="S-nitrosocysteine; in inhibited form"
FT /evidence="ECO:0000250|UniProtKB:P42574"
FT CONFLICT 63..65
FT /note="SRS -> ARN (in Ref. 6; AAD09504)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="E -> Q (in Ref. 6; AAD09504)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="I -> F (in Ref. 6; AAD09504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 31475 MW; CE91598F74826605 CRC64;
MENNKTSVDS KSINNFEVKT IHGSKSVDSG IYLDSSYKMD YPEMGICIII NNKNFHKSTG
MSSRSGTDVD AANLRETFMG LKYQVRNKND LTREDILELM DSVSKEDHSK RSSFVCVILS
HGDEGVIYGT NGPVELKKLT SFFRGDYCRS LTGKPKLFII QACRGTELDC GIETDSGTDE
EMACQKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC SMLKLYAHKL EFMHILTRVN
RKVATEFESF SLDSTFHAKK QIPCIVSMLT KELYFYH
