CATV_NPVAC
ID CATV_NPVAC Reviewed; 323 AA.
AC P25783; Q96589;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Viral cathepsin;
DE Short=V-cath;
DE EC=3.4.22.50;
DE AltName: Full=Cysteine proteinase;
DE Short=CP;
DE Flags: Precursor;
GN Name=VCATH; ORFNames=ORF127;
OS Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=46015;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C6;
RA Kuzio J., Faulkner P.;
RT "Identification of a cysteine proteinase encoded by the Autographa
RT californica nuclear polyhedrosis virus.";
RL (In) Goosen M.F.A., Daugulis A.J., Faulkner P. (eds.);
RL Insect cell culture engineering, pp.17-50, Marcel Dekker, New York (1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6;
RX PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT "The complete DNA sequence of Autographa californica nuclear polyhedrosis
RT virus.";
RL Virology 202:586-605(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-323.
RX PubMed=1363350; DOI=10.1515/bchm3.1992.373.2.1211;
RA Rawlings N.D., Pearl L.H., Buttle D.J.;
RT "The baculovirus Autographa californica nuclear polyhedrosis virus genome
RT includes a papain-like sequence.";
RL Biol. Chem. Hoppe-Seyler 373:1211-1215(1992).
RN [4]
RP CHARACTERIZATION.
RX PubMed=8590630; DOI=10.1515/bchm3.1995.376.10.611;
RA Bromme D., Okamoto K.;
RT "The baculovirus cysteine protease has a cathepsin B-like S2-subsite
RT specificity.";
RL Biol. Chem. Hoppe-Seyler 376:611-615(1995).
RN [5]
RP CHARACTERIZATION.
RX PubMed=7730794; DOI=10.1099/0022-1317-76-5-1091;
RA Slack J.M., Kuzio J., Faulkner P.;
RT "Characterization of v-cath, a cathepsin L-like proteinase expressed by the
RT baculovirus Autographa californica multiple nuclear polyhedrosis virus.";
RL J. Gen. Virol. 76:1091-1098(1995).
RN [6]
RP PROTEOLYTIC CLEAVAGE, AND FUNCTION.
RX PubMed=12069520; DOI=10.1006/viro.2002.1378;
RA Hom L.G., Ohkawa T., Trudeau D., Volkman L.E.;
RT "Autographa californica M nucleopolyhedrovirus ProV-CATH is activated
RT during infected cell death.";
RL Virology 296:212-218(2002).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CHIA.
RX PubMed=21289117; DOI=10.1128/jvi.02165-10;
RA Hodgson J.J., Arif B.M., Krell P.J.;
RT "Interaction of Autographa californica multiple nucleopolyhedrovirus
RT cathepsin protease progenitor (proV-CATH) with insect baculovirus chitinase
RT as a mechanism for proV-CATH cellular retention.";
RL J. Virol. 85:3918-3929(2011).
CC -!- FUNCTION: Cysteine protease that plays an essential role in host
CC liquefaction to facilitate horizontal transmission of the virus.
CC Accumulates within infected cells as an inactive proenzyme (proV-CATH),
CC which is activated by proteolytic cleavage upon cell death.
CC {ECO:0000269|PubMed:12069520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase of broad specificity, hydrolyzing substrates of
CC both cathepsin L and cathepsin B.; EC=3.4.22.50;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0-5.5.;
CC -!- SUBUNIT: Interacts with chitinase/CHIA; this interaction maintains
CC VCATH in the host reticulum endoplasmic. {ECO:0000269|PubMed:21289117}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum
CC {ECO:0000269|PubMed:21289117}. Note=Retained in the host reticulum by
CC its interaction with chitinase/CHIA. {ECO:0000269|PubMed:21289117}.
CC -!- PTM: Synthesized as an inactive proenzyme and activated by proteolytic
CC removal of the inhibitory propeptide. {ECO:0000269|PubMed:12069520}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA49713.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M67451; AAA46752.1; -; Genomic_DNA.
DR EMBL; L22858; AAA66757.1; -; Genomic_DNA.
DR EMBL; X70124; CAA49713.1; ALT_INIT; Genomic_DNA.
DR PIR; S62736; S62736.
DR RefSeq; NP_054157.1; NC_001623.1.
DR SMR; P25783; -.
DR MEROPS; C01.083; -.
DR GeneID; 1403960; -.
DR KEGG; vg:1403960; -.
DR BRENDA; 3.4.22.50; 583.
DR Proteomes; UP000008292; Genome.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Host endoplasmic reticulum; Hydrolase;
KW Protease; Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..112
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000322201"
FT CHAIN 113..323
FT /note="Viral cathepsin"
FT /id="PRO_0000050572"
FT ACT_SITE 136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 133..174
FT /evidence="ECO:0000250"
FT DISULFID 167..207
FT /evidence="ECO:0000250"
FT DISULFID 262..310
FT /evidence="ECO:0000250"
SQ SEQUENCE 323 AA; 36938 MW; F23876A6ED303FC8 CRC64;
MNKILFYLFV YGVVNSAAYD LLKAPNYFEE FVHRFNKDYG SEVEKLRRFK IFQHNLNEII
NKNQNDSAKY EINKFSDLSK DETIAKYTGL SLPIQTQNFC KVIVLDQPPG KGPLEFDWRR
LNKVTSVKNQ GMCGACWAFA TLASLESQFA IKHNQLINLS EQQMIDCDFV DAGCNGGLLH
TAFEAIIKMG GVQLESDYPY EADNNNCRMN SNKFLVQVKD CYRYITVYEE KLKDLLRLVG
PIPMAIDAAD IVNYKQGIIK YCFNSGLNHA VLLVGYGVEN NIPYWTFKNT WGTDWGEDGF
FRVQQNINAC GMRNELASTA VIY
