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Caspase-9 (CASP-9) (EC 3.4.22.62) (Apoptotic protease Mch-6) (Apoptotic protease-activating factor 3) (APAF-3) (ICE-like apoptotic protease 6) (ICE-LAP6) [Cleaved into: Caspase-9 subunit p35; Caspase-9 subunit p10]

 CASP9_MOUSE             Reviewed;         454 AA.
Q8C3Q9;
06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
30-AUG-2017, entry version 146.
RecName: Full=Caspase-9;
Short=CASP-9;
EC=3.4.22.62;
AltName: Full=Apoptotic protease Mch-6;
AltName: Full=Apoptotic protease-activating factor 3;
Short=APAF-3;
AltName: Full=ICE-like apoptotic protease 6;
Short=ICE-LAP6;
Contains:
RecName: Full=Caspase-9 subunit p35;
Contains:
RecName: Full=Caspase-9 subunit p10;
Flags: Precursor;
Name=Casp9; Synonyms=Mch6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION AT TYR-191 BY ABL1.
PubMed=15657060; DOI=10.1074/jbc.M413787200;
Raina D., Pandey P., Ahmad R., Bharti A., Ren J., Kharbanda S.,
Weichselbaum R., Kufe D.;
"c-Abl tyrosine kinase regulates caspase-9 autocleavage in the
apoptotic response to DNA damage.";
J. Biol. Chem. 280:11147-11151(2005).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. Binding of caspase-9 to Apaf-
1 leads to activation of the protease which then cleaves and
activates caspase-3. Promotes DNA damage-induced apoptosis in a
ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-
ribose) polymerase (PARP) (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at
position P1 and with a marked preference for His at position P2.
It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 35 kDa (p35) and a 10
kDa (p10) subunit. Caspase-9 and APAF1 bind to each other via
their respective NH2-terminal CED-3 homologous domains in the
presence of cytochrome C and ATP. Interacts (inactive form) with
EFHD2. Interacts with HAX1. Interacts with BIRC2/c-IAP1,
XIAP/BIRC4, BIRC5/survivin, BIRC6/bruce and BIRC7/livin. Interacts
with ABL1 (via SH3 domain); the interaction is direct and
increased in the response of cells to genotoxic stress and ABL1/c-
Abl activation (By similarity). {ECO:0000250}.
-!- PTM: Cleavages at Asp-353 by granzyme B and at Asp-368 by caspase-
3 generate the two active subunits. Caspase-8 and -10 can also be
involved in these processing events (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated at Thr-163 by MAPK1/ERK2. Phosphorylation at
Thr-163 is sufficient to block caspase-9 processing and subsequent
caspase-3 activation (By similarity). Phosphorylation on Tyr-191
by ABL1/c-Abl; occurs in the response of cells to DNA damage.
{ECO:0000250, ECO:0000269|PubMed:15657060}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK085095; BAC39365.1; -; mRNA.
EMBL; AL928577; CAM23134.1; -; Genomic_DNA.
EMBL; CH466615; EDL13399.1; -; Genomic_DNA.
EMBL; BC056372; AAH56372.1; -; mRNA.
EMBL; BC056447; AAH56447.1; -; mRNA.
CCDS; CCDS18883.1; -.
RefSeq; NP_056548.2; NM_015733.5.
UniGene; Mm.88829; -.
ProteinModelPortal; Q8C3Q9; -.
SMR; Q8C3Q9; -.
BioGrid; 198501; 4.
DIP; DIP-60482N; -.
STRING; 10090.ENSMUSP00000030747; -.
MEROPS; C14.010; -.
iPTMnet; Q8C3Q9; -.
PhosphoSitePlus; Q8C3Q9; -.
EPD; Q8C3Q9; -.
MaxQB; Q8C3Q9; -.
PaxDb; Q8C3Q9; -.
PRIDE; Q8C3Q9; -.
Ensembl; ENSMUST00000030747; ENSMUSP00000030747; ENSMUSG00000028914.
GeneID; 12371; -.
KEGG; mmu:12371; -.
UCSC; uc008vpi.2; mouse.
CTD; 842; -.
MGI; MGI:1277950; Casp9.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
HOVERGEN; HBG059022; -.
InParanoid; Q8C3Q9; -.
KO; K04399; -.
OMA; GSWYIET; -.
OrthoDB; EOG091G05YD; -.
PhylomeDB; Q8C3Q9; -.
TreeFam; TF102023; -.
Reactome; R-MMU-111458; Formation of apoptosome.
Reactome; R-MMU-111459; Activation of caspases through apoptosome-mediated cleavage.
Reactome; R-MMU-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-MMU-418889; Ligand-independent caspase activation via DCC.
ChiTaRS; Casp9; mouse.
PRO; PR:Q8C3Q9; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028914; -.
ExpressionAtlas; Q8C3Q9; baseline and differential.
Genevisible; Q8C3Q9; MM.
GO; GO:0043293; C:apoptosome; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:MGI.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IDA:MGI.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0034349; P:glial cell apoptotic process; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; NAS:ParkinsonsUK-UCL.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:MGI.
GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
GO; GO:0032025; P:response to cobalt ion; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0009411; P:response to UV; IMP:MGI.
GO; GO:0042770; P:signal transduction in response to DNA damage; ISS:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR033171; Caspase-9.
InterPro; IPR029030; Caspase-like_dom.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454:SF173; PTHR10454:SF173; 1.
Pfam; PF00619; CARD; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00114; CARD; 1.
SMART; SM00115; CASc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Apoptosis; Complete proteome; Hydrolase; Phosphoprotein; Protease;
Reference proteome; Thiol protease; Zymogen.
PROPEP 1 ? {ECO:0000255}.
/FTId=PRO_0000421172.
CHAIN ? 353 Caspase-9 subunit p35. {ECO:0000250}.
/FTId=PRO_0000421173.
PROPEP 354 367 {ECO:0000250}.
/FTId=PRO_0000421174.
CHAIN 368 454 Caspase-9 subunit p10. {ECO:0000250}.
/FTId=PRO_0000421175.
DOMAIN 1 92 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
ACT_SITE 275 275 {ECO:0000250}.
ACT_SITE 325 325 {ECO:0000250}.
MOD_RES 163 163 Phosphothreonine; by MAPK1.
{ECO:0000250|UniProtKB:P55211}.
MOD_RES 191 191 Phosphotyrosine; by ABL1.
{ECO:0000269|PubMed:15657060}.
MOD_RES 340 340 Phosphoserine.
{ECO:0000250|UniProtKB:P55211}.
MOD_RES 348 348 Phosphoserine.
{ECO:0000250|UniProtKB:P55211}.
SEQUENCE 454 AA; 49979 MW; 438A67EA66A6EE78 CRC64;
MDEADRQLLR RCRVRLVSEL QVAELWDALL SRELFTRDMI EDIQQAGSGS RRDQARQLVT
DLETRGRQAL PLFISCLEDT GQGTLASLLQ SGRQAAKQDP EAVKPLDHLV PVVLGPMGLT
AKEQRVVKLD PSQPAVGNLT PVVLGPEELW PARLKPEVLR PETPRPVDIG SGGAHDVCVP
GKIRGHADMA YTLDSDPCGH CLIINNVNFC PSSGLGTRTG SNLDRDKLEH RFRWLRFMVE
VKNDLTAKKM VTALMEMAHR NHRALDCFVV VILSHGCQAS HLQFPGAVYG TDGCSVSIEK
IVNIFNGSGC PSLGGKPKLF FIQACGGEQK DHGFEVACTS SQGRTLDSDS EPDAVPYQEG
PRPLDQLDAV SSLPTPSDIL VSYSTFPGFV SWRDKKSGSW YIETLDGILE QWARSEDLQS
LLLRVANAVS AKGTYKQIPG CFNFLRKKLF FKTS


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