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Death-associated inhibitor of apoptosis 1 (EC 2.3.2.27) (Apoptosis 1 inhibitor) (E3 ubiquitin-protein ligase th) (Inhibitor of apoptosis 1) (Protein thread) (RING-type E3 ubiquitin transferase Diap1)

 DIAP1_DROME             Reviewed;         438 AA.
Q24306; A4V1Z9; A9UN33; Q0E8E4; Q8MRM5; Q9VUX5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 2.
27-SEP-2017, entry version 173.
RecName: Full=Death-associated inhibitor of apoptosis 1;
EC=2.3.2.27 {ECO:0000269|PubMed:14517550, ECO:0000269|PubMed:21145488, ECO:0000269|PubMed:22304967};
AltName: Full=Apoptosis 1 inhibitor;
AltName: Full=E3 ubiquitin-protein ligase th;
AltName: Full=Inhibitor of apoptosis 1;
AltName: Full=Protein thread;
AltName: Full=RING-type E3 ubiquitin transferase Diap1 {ECO:0000305};
Name=Diap1; Synonyms=Iap1, th; ORFNames=CG12284;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Eye imaginal disk;
PubMed=8548811; DOI=10.1016/0092-8674(95)90150-7;
Hay B.A., Wassarman D.A., Rubin G.M.;
"Drosophila homologs of baculovirus inhibitor of apoptosis proteins
function to block cell death.";
Cell 83:1253-1262(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Ovary;
Stapleton M., Booth B., Carlson J.W., Frise E., Kapadia B., Park S.,
Wan K.H., Yu C., Celniker S.E.;
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-438.
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
INTERACTION WITH DRONC.
TISSUE=Embryo;
PubMed=10675329; DOI=10.1093/emboj/19.4.598;
Meier P., Silke J., Leevers S.J., Evan G.I.;
"The Drosophila caspase DRONC is regulated by DIAP1.";
EMBO J. 19:598-611(2000).
[7]
INTERACTION WITH STRICA.
PubMed=11550090; DOI=10.1038/sj.cdd.4400864;
Doumanis J., Quinn L., Richardson H., Kumar S.;
"STRICA, a novel Drosophila melanogaster caspase with an unusual
serine/threonine-rich prodomain, interacts with DIAP1 and DIAP2.";
Cell Death Differ. 8:387-394(2001).
[8]
FUNCTION, INTERACTION WITH HTRA2, AND CLEAVAGE.
PubMed=17397804; DOI=10.1016/j.bbrc.2007.03.079;
Igaki T., Suzuki Y., Tokushige N., Aonuma H., Takahashi R., Miura M.;
"Evolution of mitochondrial cell death pathway: Proapoptotic role of
HtrA2/Omi in Drosophila.";
Biochem. Biophys. Res. Commun. 356:993-997(2007).
[9]
FUNCTION, INTERACTION WITH HTRA2, CLEAVAGE, AND MUTAGENESIS OF ILE-162
AND ILE-165.
STRAIN=Berkeley; TISSUE=Testis;
PubMed=18259196; DOI=10.1038/cdd.2008.19;
Khan F.S., Fujioka M., Datta P., Fernandes-Alnemri T., Jaynes J.B.,
Alnemri E.S.;
"The interaction of DIAP1 with dOmi/HtrA2 regulates cell death in
Drosophila.";
Cell Death Differ. 15:1073-1083(2008).
[10]
REVIEW ON FUNCTION.
PubMed=19217783; DOI=10.1016/j.tcb.2009.01.004;
Broemer M., Meier P.;
"Ubiquitin-mediated regulation of apoptosis.";
Trends Cell Biol. 19:130-140(2009).
[11]
FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE OF THE NEDD8 CONJUGATION
PATHWAY, AND CATALYTIC ACTIVITY.
PubMed=21145488; DOI=10.1016/j.molcel.2010.11.011;
Broemer M., Tenev T., Rigbolt K.T., Hempel S., Blagoev B., Silke J.,
Ditzel M., Meier P.;
"Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3
ligases.";
Mol. Cell 40:810-822(2010).
[12]
REVIEW ON FUNCTION.
PubMed=22095281; DOI=10.1038/cdd.2011.163;
Darding M., Meier P.;
"IAPs: guardians of RIPK1.";
Cell Death Differ. 19:58-66(2012).
[13]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=22304967; DOI=10.1016/j.molcel.2011.12.032;
Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A.,
Lee E.;
"XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt
signaling.";
Mol. Cell 45:619-628(2012).
[14]
INTERACTION WITH UBR3.
PubMed=25146930; DOI=10.1038/cdd.2014.115;
Huang Q., Tang X., Wang G., Fan Y., Ray L., Bergmann A.,
Belenkaya T.Y., Ling X., Yan D., Lin Y., Ye X., Shi W., Zhou X.,
Lu F., Qu J., Lin X.;
"Ubr3 E3 ligase regulates apoptosis by controlling the activity of
DIAP1 in Drosophila.";
Cell Death Differ. 21:1961-1970(2014).
[15]
INTERACTION WITH UBR3.
PubMed=26383956; DOI=10.1126/science.aac5677;
Zanet J., Benrabah E., Li T., Pelissier-Monier A.,
Chanut-Delalande H., Ronsin B., Bellen H.J., Payre F., Plaza S.;
"Pri sORF peptides induce selective proteasome-mediated protein
processing.";
Science 349:1356-1358(2015).
[16]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 215-310.
PubMed=11511363; DOI=10.1016/S1097-2765(01)00282-9;
Wu J.W., Cocina A.E., Chai J., Hay B.A., Shi Y.;
"Structural analysis of a functional DIAP1 fragment bound to grim and
hid peptides.";
Mol. Cell 8:95-104(2001).
[17]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 201-324 IN COMPLEX WITH
DRONC, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=14517550; DOI=10.1038/nsb989;
Chai J., Yan N., Huh J.R., Wu J.-W., Li W., Hay B.A., Shi Y.;
"Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-
dependent Dronc ubiquitination.";
Nat. Struct. Biol. 10:892-898(2003).
-!- FUNCTION: Anti-apoptotic protein which functions as a caspase
regulator, using its E3 ubiquitin-protein ligase activity to
smother caspase activity. Binds, ubiquitinates and inactivates
initiator caspase Dronc, and effector caspases Drice and Dcp-1.
Acts as a Nedd8-E3 ubiquitin-protein ligase for Drice. Suppresses
apoptosis by targeting the apoptosome for ubiquitination and
inactivation. Plays an important role in cell motility.
Overexpression suppresses rpr and hid-dependent cell death in the
eye. Interaction of Diap1 with Dronc is required to suppress
Dronc-mediated cell death through Diap1-mediated ubiquitination of
Dronc. Acts as a positive regulator of Wnt signaling.
{ECO:0000269|PubMed:14517550, ECO:0000269|PubMed:17397804,
ECO:0000269|PubMed:18259196, ECO:0000269|PubMed:21145488,
ECO:0000269|PubMed:22304967, ECO:0000269|PubMed:8548811}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:14517550,
ECO:0000269|PubMed:21145488, ECO:0000269|PubMed:22304967}.
-!- SUBUNIT: Interacts (via BIR 2 domain) with Dronc (via residues
114-125). Rpr, hid and grim can outcompete Dronc for binding Diap1
therefore removing Diap1-mediated ubiquitination. Interacts (via
BIR 2 domain) with HtrA2; this displaces any bound Dronc.
Interacts with Strica (PubMed:11550090). The N-terminally cleaved
form interacts with Ubr3 (via UBR-type zinc finger)
(PubMed:25146930, PubMed:26383956); the interaction promotes the
recruitment and uniquitination of substrate capases such as Dronc
(PubMed:25146930). {ECO:0000269|PubMed:10675329,
ECO:0000269|PubMed:11550090, ECO:0000269|PubMed:14517550,
ECO:0000269|PubMed:17397804, ECO:0000269|PubMed:18259196,
ECO:0000269|PubMed:25146930, ECO:0000269|PubMed:26383956}.
-!- INTERACTION:
P25843:chic; NbExp=2; IntAct=EBI-456419, EBI-156199;
Q9XYF4:Dronc; NbExp=11; IntAct=EBI-456419, EBI-108311;
Q24106:hid; NbExp=9; IntAct=EBI-456419, EBI-135509;
Q86PE7:IKKepsilon; NbExp=3; IntAct=EBI-456419, EBI-987197;
Q24475:rpr; NbExp=7; IntAct=EBI-456419, EBI-106786;
-!- PTM: Ubiquitinated and degraded by HtrA2 in apoptotic cells;
proteolytic cleavage at specific sites in the BIR domain linker
region generating inactive fragments. Mutation of one site reduces
but does not abolish cleavage as another site is selected by the
protease. {ECO:0000269|PubMed:17397804,
ECO:0000269|PubMed:18259196}.
-!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM50178.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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EMBL; L49440; AAC41609.1; -; mRNA.
EMBL; AE014296; AAF49548.1; -; Genomic_DNA.
EMBL; AE014296; AAG22319.1; -; Genomic_DNA.
EMBL; AE014296; AAN11757.1; -; Genomic_DNA.
EMBL; BT031197; ABY20438.2; -; mRNA.
EMBL; AY119524; AAM50178.1; ALT_SEQ; mRNA.
RefSeq; NP_001261916.1; NM_001274987.1.
RefSeq; NP_001261917.1; NM_001274988.1.
RefSeq; NP_001261918.1; NM_001274989.1.
RefSeq; NP_524101.2; NM_079377.3.
RefSeq; NP_730097.1; NM_168644.2.
RefSeq; NP_730098.1; NM_168645.2.
UniGene; Dm.6466; -.
PDB; 1JD4; X-ray; 2.70 A; A/B=201-323.
PDB; 1JD5; X-ray; 1.90 A; A=201-323.
PDB; 1JD6; X-ray; 2.70 A; A=201-323.
PDB; 1Q4Q; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=201-323.
PDB; 1SDZ; X-ray; 1.78 A; A=30-145.
PDB; 1SE0; X-ray; 1.75 A; A=30-145.
PDB; 3SIP; X-ray; 3.50 A; E/F=31-145.
PDB; 3SIQ; X-ray; 2.40 A; A/B/C/D/E/F=1-135.
PDBsum; 1JD4; -.
PDBsum; 1JD5; -.
PDBsum; 1JD6; -.
PDBsum; 1Q4Q; -.
PDBsum; 1SDZ; -.
PDBsum; 1SE0; -.
PDBsum; 3SIP; -.
PDBsum; 3SIQ; -.
ProteinModelPortal; Q24306; -.
SMR; Q24306; -.
BioGrid; 65064; 106.
IntAct; Q24306; 21.
MINT; MINT-1601077; -.
STRING; 7227.FBpp0305795; -.
MEROPS; I32.009; -.
PaxDb; Q24306; -.
PRIDE; Q24306; -.
EnsemblMetazoa; FBtr0075499; FBpp0075254; FBgn0260635.
EnsemblMetazoa; FBtr0075500; FBpp0075255; FBgn0260635.
EnsemblMetazoa; FBtr0075501; FBpp0075256; FBgn0260635.
EnsemblMetazoa; FBtr0333617; FBpp0305793; FBgn0260635.
EnsemblMetazoa; FBtr0333618; FBpp0305794; FBgn0260635.
EnsemblMetazoa; FBtr0333619; FBpp0305795; FBgn0260635.
GeneID; 39753; -.
KEGG; dme:Dmel_CG12284; -.
CTD; 39753; -.
FlyBase; FBgn0260635; Diap1.
eggNOG; KOG1101; Eukaryota.
eggNOG; ENOG410YPNM; LUCA.
GeneTree; ENSGT00500000044782; -.
InParanoid; Q24306; -.
KO; K16061; -.
OMA; AMYSEEA; -.
OrthoDB; EOG091G0CXH; -.
PhylomeDB; Q24306; -.
Reactome; R-DME-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-DME-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-DME-5675482; Regulation of necroptotic cell death.
Reactome; R-DME-8948747; Regulation of PTEN localization.
Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
SignaLink; Q24306; -.
EvolutionaryTrace; Q24306; -.
GenomeRNAi; 39753; -.
PMAP-CutDB; Q24306; -.
PRO; PR:Q24306; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0260635; -.
ExpressionAtlas; Q24306; differential.
Genevisible; Q24306; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0089720; F:caspase binding; IPI:FlyBase.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:FlyBase.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:FlyBase.
GO; GO:0061663; F:NEDD8 ligase activity; IDA:FlyBase.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:FlyBase.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:FlyBase.
GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:UniProtKB.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:FlyBase.
GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
GO; GO:0048800; P:antennal morphogenesis; IMP:FlyBase.
GO; GO:0006915; P:apoptotic process; IPI:FlyBase.
GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
GO; GO:0008354; P:germ cell migration; TAS:FlyBase.
GO; GO:0097340; P:inhibition of cysteine-type endopeptidase activity; IDA:FlyBase.
GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IMP:FlyBase.
GO; GO:0007275; P:multicellular organism development; TAS:FlyBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:FlyBase.
GO; GO:0046673; P:negative regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:FlyBase.
GO; GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:FlyBase.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:FlyBase.
GO; GO:0051865; P:protein autoubiquitination; IDA:FlyBase.
GO; GO:0070936; P:protein K48-linked ubiquitination; IMP:FlyBase.
GO; GO:0045116; P:protein neddylation; IDA:FlyBase.
GO; GO:0000209; P:protein polyubiquitination; IDA:FlyBase.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:FlyBase.
GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
GO; GO:0045035; P:sensory organ precursor cell division; IGI:FlyBase.
GO; GO:0007289; P:spermatid nucleus differentiation; IMP:FlyBase.
GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
CDD; cd00022; BIR; 2.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001370; BIR_rpt.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00653; BIR; 2.
SMART; SM00238; BIR; 2.
SMART; SM00184; RING; 1.
PROSITE; PS01282; BIR_REPEAT_1; 2.
PROSITE; PS50143; BIR_REPEAT_2; 2.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Metal-binding;
Reference proteome; Repeat; Transferase; Ubl conjugation;
Ubl conjugation pathway; Wnt signaling pathway; Zinc; Zinc-finger.
CHAIN 1 438 Death-associated inhibitor of apoptosis
1.
/FTId=PRO_0000122367.
REPEAT 44 110 BIR 1.
REPEAT 226 293 BIR 2.
ZN_FING 391 426 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
METAL 263 263 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 266 266 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 283 283 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 290 290 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
SITE 162 163 Cleavage; by HtrA2.
SITE 165 166 Cleavage; by HtrA2.
MUTAGEN 162 162 I->D: Destroys cleavage site.
{ECO:0000269|PubMed:18259196}.
MUTAGEN 165 165 I->D: Destroys cleavage site.
{ECO:0000269|PubMed:18259196}.
CONFLICT 319 319 S -> T (in Ref. 1; AAC41609).
{ECO:0000305}.
CONFLICT 324 325 VA -> DT (in Ref. 1; AAC41609).
{ECO:0000305}.
HELIX 40 42 {ECO:0000244|PDB:1SDZ}.
HELIX 44 48 {ECO:0000244|PDB:1SE0}.
TURN 50 53 {ECO:0000244|PDB:3SIQ}.
HELIX 61 66 {ECO:0000244|PDB:1SE0}.
STRAND 69 71 {ECO:0000244|PDB:1SE0}.
STRAND 78 80 {ECO:0000244|PDB:1SE0}.
TURN 81 83 {ECO:0000244|PDB:1SE0}.
STRAND 86 89 {ECO:0000244|PDB:1SE0}.
HELIX 96 103 {ECO:0000244|PDB:1SE0}.
TURN 108 112 {ECO:0000244|PDB:1SE0}.
HELIX 122 128 {ECO:0000244|PDB:1SE0}.
STRAND 135 137 {ECO:0000244|PDB:3SIP}.
HELIX 221 223 {ECO:0000244|PDB:1JD5}.
HELIX 226 232 {ECO:0000244|PDB:1JD5}.
HELIX 233 235 {ECO:0000244|PDB:1JD5}.
STRAND 240 242 {ECO:0000244|PDB:1Q4Q}.
HELIX 244 249 {ECO:0000244|PDB:1JD5}.
STRAND 252 254 {ECO:0000244|PDB:1JD5}.
STRAND 261 263 {ECO:0000244|PDB:1JD5}.
TURN 264 266 {ECO:0000244|PDB:1JD5}.
STRAND 269 271 {ECO:0000244|PDB:1JD5}.
HELIX 279 286 {ECO:0000244|PDB:1JD5}.
HELIX 291 297 {ECO:0000244|PDB:1JD5}.
HELIX 299 307 {ECO:0000244|PDB:1JD5}.
HELIX 309 317 {ECO:0000244|PDB:1JD5}.
SEQUENCE 438 AA; 48038 MW; 24CA8BC13F5DEF31 CRC64;
MASVVADLPS YGPIAFDQVD NNTNATQLFK NNINKTRMND LNREETRLKT FTDWPLDWLD
KRQLAQTGMY FTHAGDKVKC FFCGVEIGCW EQEDQPVPEH QRWSPNCPLL RRRTTNNVPI
NAEALDRILP PISYDICGAN DSTLEMREHA YAEGVIPMSQ LIQSIGMNAV NAAGSVTGTA
APQPRVTVAT HASTATQATG DVQPETCRPS AASGNYFPQY PEYAIETARL RTFEAWPRNL
KQKPHQLAEA GFFYTGVGDR VRCFSCGGGL MDWNDNDEPW EQHALWLSQC RFVKLMKGQL
YIDTVAAKPV LAEEKEESSS IGGVAVASTQ ASEEEQQTSL SSEEAVSGDV APSVAPTAAT
RIFNKIVEAT AVATPSTNSS GSTSIPEEKL CKICYGAEYN TAFLPCGHVV ACAKCASSVT
KCPLCRKPFT DVMRVYFS


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