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Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]

 CASP2_MOUSE             Reviewed;         452 AA.
P29594; O08737; Q3TCM0; Q8C9H7; Q8K241;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 5.
05-JUN-2019, entry version 181.
RecName: Full=Caspase-2;
Short=CASP-2;
EC=3.4.22.55;
AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 2;
Short=NEDD-2;
AltName: Full=Protease ICH-1;
Contains:
RecName: Full=Caspase-2 subunit p18;
Contains:
RecName: Full=Caspase-2 subunit p13;
Contains:
RecName: Full=Caspase-2 subunit p12;
Flags: Precursor;
Name=Casp2; Synonyms=Ich1, Nedd-2, Nedd2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF CYS-320.
STRAIN=BALB/cJ;
PubMed=7958843; DOI=10.1101/gad.8.14.1613;
Kumar S., Kinoshita M., Noda M., Copeland N.G., Jenkins N.A.;
"Induction of apoptosis by the mouse Nedd2 gene, which encodes a
protein similar to the product of the Caenorhabditis elegans cell
death gene ced-3 and the mammalian IL-1 beta-converting enzyme.";
Genes Dev. 8:1613-1626(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/An;
PubMed=9038361; DOI=10.1016/S0014-5793(97)00026-4;
van de Craen M., Vandenabeele P., Declercq W., van den Brande I.,
van Loo G., Molemans F., Schotte P., van Criekinge W., Beyaert R.,
Fiers W.;
"Characterization of seven murine caspase family members.";
FEBS Lett. 403:61-69(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
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]
PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE.
TISSUE=Brain;
PubMed=1378265; DOI=10.1016/0006-291X(92)91747-E;
Kumar S., Tomooka Y., Noda M.;
"Identification of a set of genes with developmentally down-regulated
expression in the mouse brain.";
Biochem. Biophys. Res. Commun. 185:1155-1161(1992).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. Might function by either
activating some proteins required for cell death or inactivating
proteins necessary for cell survival (PubMed:7958843). Associates
with PIDD1 and CRADD to form the PIDDosome, a complex that
activates CASP2 and triggers apoptosis in response to genotoxic
stress (By similarity). {ECO:0000250|UniProtKB:P42575,
ECO:0000269|PubMed:7958843}.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for an Asp residue at P1, with 316-asp
being essential for proteolytic activity and has a preferred
cleavage sequence of Val-Asp-Val-Ala-Asp-|-.; EC=3.4.22.55;
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a p18 subunit and a p12
subunit. Forms a complex named the PIDDosome with PIDD1 and CRADD.
Interacts with NOL3 (via CARD domain); inhibits CASP2 activity in
a phosphorylation-dependent manner.
{ECO:0000250|UniProtKB:P42575}.
-!- TISSUE SPECIFICITY: High level expression seen in the embryonic
CNS, liver, lung, kidney, small intestine, and hair follicles of
vibrissae. Moderate expression seen in the skin, oral mucosa,
skeletal muscle, submandibular gland and thymus. In the adult, it
is highly expressed in spleen, lung and kidney. Moderately in the
brain, heart, testis, liver. Low levels in the thymus, skeletal
muscle, ovary and gut.
-!- DEVELOPMENTAL STAGE: During embryonic development is highly
expressed in several types of mouse tissue undergoing high rates
of programmed cell death such as central nervous system and
kidney.
-!- DOMAIN: The CARD domain mediates a direct interaction with CRADD.
{ECO:0000250|UniProtKB:P42575}.
-!- PTM: The mature protease can process its own propeptide, but not
that of other caspases. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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EMBL; D28492; BAA25876.1; -; mRNA.
EMBL; Y13085; CAA73527.1; -; mRNA.
EMBL; AK042072; BAC31153.1; -; mRNA.
EMBL; AK170649; BAE41936.1; -; mRNA.
EMBL; BC034262; AAH34262.1; -; mRNA.
CCDS; CCDS20064.1; -.
RefSeq; NP_031636.1; NM_007610.2.
SMR; P29594; -.
BioGrid; 198496; 1.
ComplexPortal; CPX-3901; Caspase-2 complex.
ComplexPortal; CPX-3963; Caspase-2 PIDDosome.
CORUM; P29594; -.
STRING; 10090.ENSMUSP00000031895; -.
MEROPS; C14.006; -.
iPTMnet; P29594; -.
PhosphoSitePlus; P29594; -.
EPD; P29594; -.
MaxQB; P29594; -.
PaxDb; P29594; -.
PeptideAtlas; P29594; -.
PRIDE; P29594; -.
Ensembl; ENSMUST00000031895; ENSMUSP00000031895; ENSMUSG00000029863.
GeneID; 12366; -.
KEGG; mmu:12366; -.
UCSC; uc009bqq.2; mouse.
CTD; 835; -.
MGI; MGI:97295; Casp2.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000156657; -.
HOGENOM; HOG000290714; -.
InParanoid; P29594; -.
KO; K02186; -.
OMA; VMVLMTH; -.
OrthoDB; 1092723at2759; -.
PhylomeDB; P29594; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.55; 3474.
Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
Reactome; R-MMU-205025; NADE modulates death signalling.
Reactome; R-MMU-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
PRO; PR:P29594; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000029863; Expressed in 274 organ(s), highest expression level in membranous labyrinth.
ExpressionAtlas; P29594; baseline and differential.
Genevisible; P29594; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0004197; F:cysteine-type endopeptidase activity; ISO:MGI.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; ISO:MGI.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IGI:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
GO; GO:0001554; P:luteolysis; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0003407; P:neural retina development; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0016485; P:protein processing; ISO:MGI.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR035702; Caspase_2.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
PANTHER; PTHR10454:SF151; PTHR10454:SF151; 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;
Acetylation; Apoptosis; Complete proteome; Hydrolase; Phosphoprotein;
Protease; Reference proteome; Thiol protease; Zymogen.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P42575}.
PROPEP 2 169 {ECO:0000250}.
/FTId=PRO_0000004546.
CHAIN 170 333 Caspase-2 subunit p18. {ECO:0000250}.
/FTId=PRO_0000004547.
CHAIN 334 452 Caspase-2 subunit p13. {ECO:0000250}.
/FTId=PRO_0000004548.
CHAIN 348 452 Caspase-2 subunit p12. {ECO:0000250}.
/FTId=PRO_0000004549.
DOMAIN 32 121 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
ACT_SITE 277 277 {ECO:0000250}.
ACT_SITE 320 320 {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P42575}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000250|UniProtKB:P42575}.
MOD_RES 340 340 Phosphoserine.
{ECO:0000250|UniProtKB:P42575}.
MUTAGEN 320 320 C->G: Loss of function.
{ECO:0000269|PubMed:7958843}.
CONFLICT 85 102 VELLNLLPKRGPQAFDAF -> EGCGGWRGPAFVCFVGGA
(in Ref. 3; BAE41936). {ECO:0000305}.
CONFLICT 88 88 Missing (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 234 234 K -> R (in Ref. 3; BAC31153).
{ECO:0000305}.
SEQUENCE 452 AA; 50661 MW; A4DE25A712FAB855 CRC64;
MAAPSGRSQS SLHRKGLMAA DRRSRILAVC GMHPDHQETL KKNRVVLAKQ LLLSELLEHL
LEKDIITLEM RELIQAKGGS FSQNVELLNL LPKRGPQAFD AFCEALRETR QGHLEDLLLT
TLSDIQHVLP PLSCDYDTSL PFSVCESCPP HKQLRLSTDA TEHSLDNGDG PPCLLVKPCT
PEFYQAHYQL AYRLQSQPRG LALVLSNVHF TGEKDLEFRS GGDVDHTTLV TLFKLLGYNV
HVLHDQTAQE MQEKLQNFAQ LPAHRVTDSC VVALLSHGVE GGIYGVDGKL LQLQEVFRLF
DNANCPSLQN KPKMFFIQAC RGDETDRGVD QQDGKNHTQS PGCEESDAGK EELMKMRLPT
RSDMICGYAC LKGNAAMRNT KRGSWYIEAL TQVFSERACD MHVADMLVKV NALIKEREGY
APGTEFHRCK EMSEYCSTLC QQLYLFPGYP PT


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Related Genes :
[Casp2 Ich1 Nedd-2 Nedd2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[CASP2 ICH1 NEDD2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[Casp2 Ich1] Caspase-2 (CASP-2) (EC 3.4.22.55) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[CASP10 MCH4] Caspase-10 (CASP-10) (EC 3.4.22.63) (Apoptotic protease Mch-4) (FAS-associated death domain protein interleukin-1B-converting enzyme 2) (FLICE2) (ICE-like apoptotic protease 4) [Cleaved into: Caspase-10 subunit p23/17; Caspase-10 subunit p12]
[CASP6 MCH2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[ced-3 C48D1.2] Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]
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[CASP3 CPP32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP2 ICH1] Caspase-2 (CASP-2) (EC 3.4.22.55) (ICH-1L/1S) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (IRP) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Casp6 Mch2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[CASP8 MCH5] Caspase-8 (CASP-8) (EC 3.4.22.61) (Apoptotic cysteine protease) (Apoptotic protease Mch-5) (CAP4) (FADD-homologous ICE/ced-3-like protease) (FADD-like ICE) (FLICE) (ICE-like apoptotic protease 5) (MORT1-associated ced-3 homolog) (MACH) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]
[Casp4 Casp11 Caspl Ich3] Caspase-4 (CASP-4) (EC 3.4.22.64) (Caspase-11) (CASP-11) (Protease ICH-3) [Cleaved into: Caspase-4 subunit p10; Caspase-4 subunit p20]
[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Casp7 Lice2 Mch3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (Cysteine protease LICE2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[Cflar Cash] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[csp-2 Y73B6BL.7] Putative inactive caspase B [Cleaved into: Putative inactive caspase B subunit p31; Putative inactive caspase B subunit p17; Putative inactive caspase subunit p14]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[CASP7 MCH3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (CMH-1) (ICE-like apoptotic protease 3) (ICE-LAP3) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[Dredd DCP2 CG7486] Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10]
[ORF1] Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]
[ORF1] Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]
[ORF1] Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]
[ORF1] Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]
[ORF1] Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]
[ORF1] Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]

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