IAP1_NPVAC
ID IAP1_NPVAC Reviewed; 286 AA.
AC P41435;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Apoptosis inhibitor 1;
DE AltName: Full=IAP-1;
GN Name=IAP1;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E2;
RX PubMed=1333113; DOI=10.1016/0042-6822(92)90281-s;
RA Braunagel S.C., Daniel K.D., Reilly L.M., Guarino L.A., Hong T.,
RA Summers M.D.;
RT "Sequence, genomic organization of the EcoRI-A fragment of Autographa
RT californica nuclear polyhedrosis virus, and identification of a viral-
RT encoded protein resembling the outer capsid protein VP8 of rotavirus.";
RL Virology 191:1003-1008(1992).
RN [3]
RP FUNCTION.
RX PubMed=19727595; DOI=10.1007/s11427-009-0105-5;
RA Zeng X., Nan F., Liang C., Song J., Wang Q., Vlak J.M., Chen X.;
RT "Functional analysis of the Autographa californica nucleopolyhedrovirus
RT IAP1 and IAP2.";
RL Sci. China, Ser. C, Life Sci. 52:761-770(2009).
RN [4]
RP FUNCTION.
RX PubMed=21795471; DOI=10.1099/vir.0.033332-0;
RA Ikeda M., Yamada H., Ito H., Kobayashi M.;
RT "Baculovirus IAP1 induces caspase-dependent apoptosis in insect cells.";
RL J. Gen. Virol. 92:2654-2663(2011).
CC -!- FUNCTION: Acts by blocking cellular apoptosis early in infection.
CC Later, stimulates caspase-3-like protease activity and induces
CC apoptosis, probably to favor the release of occluded virions.
CC {ECO:0000269|PubMed:19727595, ECO:0000269|PubMed:21795471}.
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DR EMBL; L22858; AAA66657.1; -; Genomic_DNA.
DR EMBL; M96361; AAA66796.1; -; Genomic_DNA.
DR PIR; D36828; D36828.
DR RefSeq; NP_054056.1; NC_001623.1.
DR PRIDE; P41435; -.
DR GeneID; 1403859; -.
DR KEGG; vg:1403859; -.
DR Proteomes; UP000008292; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR CDD; cd00022; BIR; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00653; BIR; 2.
DR SMART; SM00238; BIR; 2.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 2.
DR PROSITE; PS50143; BIR_REPEAT_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Apoptosis; Host-virus interaction; Metal-binding;
KW Modulation of host cell apoptosis by virus; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..286
FT /note="Apoptosis inhibitor 1"
FT /id="PRO_0000122369"
FT REPEAT 29..96
FT /note="BIR 1"
FT REPEAT 131..199
FT /note="BIR 2"
FT ZN_FING 238..274
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
SQ SEQUENCE 286 AA; 33320 MW; FFEE505A35EF1BEA CRC64;
MNEDTPPFYF ISVCDNFRDN TAEHVFDMLI ERHSSFENYP IENTAFINSL IVNGFKYNQV
DDHVVCEYCE AEIKNWSEDE CIEYAHVTLS PYCAYANKIA ERESFGDNIT INAVLVKEGK
PKCVYRCMSN LQSRMDTFVN FWPAALRDMI TNIAEAGLFY TGRGDETVCF FCDCCVRDWH
TNEDTWQRHA AENPQCYFVL SVKGKEFCQN SITVTHVDKR DDDNLNENAD DIEEKYECKV
CLERQRDAVL MPCRHFCVCV QCYFGLDQKC PTCRQDVTDF IKIFVV