ID   DNA2_ACAPL              Reviewed;         358 AA.
AC   Q75WF2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Plancitoxin-1;
DE            EC=3.1.22.1;
DE   AltName: Full=Plancitoxin I;
DE            Short=Plan-I;
DE   Contains:
DE     RecName: Full=Plancitoxin-1 subunit alpha;
DE   Contains:
DE     RecName: Full=Plancitoxin-1 subunit beta;
DE   Flags: Precursor;
OS   Acanthaster planci (Crown-of-thorns starfish).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC   Valvatacea; Valvatida; Acanthasteridae; Acanthaster.
OX   NCBI_TaxID=133434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-68 AND 119-153, AND
RP   TOXIC DOSE.
RC   TISSUE=Spine;
RX   PubMed=15450924; DOI=10.1016/j.toxicon.2004.06.012;
RA   Shiomi K., Midorikawa S., Ishida M., Nagashima Y., Nagai H.;
RT   "Plancitoxins, lethal factors from the crown-of-thorns starfish Acanthaster
RT   planci, are deoxyribonucleases II.";
RL   Toxicon 44:499-506(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=2389250; DOI=10.1016/0041-0101(90)90291-e;
RA   Shiomi K., Yamamoto S., Yamanaka H., Kikuchi T., Konno K.;
RT   "Liver damage by the crown-of-thorns starfish (Acanthaster planci) lethal
RT   factor.";
RL   Toxicon 28:469-475(1990).
RN   [3]
RP   FUNCTION.
RX   PubMed=16973201; DOI=10.1016/j.toxicon.2006.08.005;
RA   Ota E., Nagashima Y., Shiomi K., Sakurai T., Kojima C., Waalkes M.P.,
RA   Himeno S.;
RT   "Caspase-independent apoptosis induced in rat liver cells by plancitoxin I,
RT   the major lethal factor from the crown-of-thorns starfish Acanthaster
RT   planci venom.";
RL   Toxicon 48:1002-1010(2006).
CC   -!- FUNCTION: Hydrolyzes DNA with an optimum pH of 7.2. Is potently
CC       hepatotoxic. It induces caspase-independent apoptosis (on rat liver
CC       cells) through the following procedure: binding to a specific receptor
CC       in the cytoplasmic membrane, entering the cell, entering the nucleus
CC       and degrading DNA. {ECO:0000269|PubMed:16973201,
CC       ECO:0000269|PubMed:2389250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC         phosphooligonucleotide end-products.; EC=3.1.22.1;
CC   -!- SUBUNIT: Plancitoxin is a heterodimer of alpha and beta subunits;
CC       disulfide-linked by a single disulfide bond.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Venom gland.
CC   -!- TOXIC DOSE: LD(50) is 140 ug/kg by intraventricular injection into
CC       mice. {ECO:0000269|PubMed:15450924}.
CC   -!- SIMILARITY: Belongs to the DNase II family. {ECO:0000305}.
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DR   EMBL; AB121229; BAD13432.1; -; mRNA.
DR   AlphaFoldDB; Q75WF2; -.
DR   SMR; Q75WF2; -.
DR   PRIDE; Q75WF2; -.
DR   BRENDA; 3.1.22.1; 8237.
DR   Proteomes; UP000694845; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004531; F:deoxyribonuclease II activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004947; DNase_II.
DR   PANTHER; PTHR10858; PTHR10858; 1.
DR   Pfam; PF03265; DNase_II; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Direct protein sequencing; Disulfide bond; Endonuclease;
KW   Glycoprotein; Hydrolase; Nuclease; Reference proteome; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:15450924"
FT   CHAIN           27..118
FT                   /note="Plancitoxin-1 subunit beta"
FT                   /id="PRO_0000272031"
FT   CHAIN           119..358
FT                   /note="Plancitoxin-1 subunit alpha"
FT                   /id="PRO_0000272032"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   358 AA;  39686 MW;  84EAF926446A715A CRC64;
     MPSSVIMFTF LALTVLTAVM VGTSEAVSCM DNKNKPVDWF IVYKLPQDSA SSKPVIREGY
     GQMYMDVNNQ ALKFSSTSLK DDDHAIAYTV DDIYKNHGKG NLAHVMYNDQ PPAGEEIQSG
     LVGHTKGVLA FDGTSGFWLV HSVPKFPLPA SKSYNWPDNA KRNGQTLLCI TFKYDQFEKI
     GQQLKYNYPG VYDSDLPSKL VGKTPSIVDL VKNVHVTSPP WNRQLNLQSK SGQTFVSFNK
     ASKWGEDLYK NWLATHFKSG LYCETWQNGG RNLNSSCEAG LNVYNVKKVS LSGGSDFKGT
     KDHSKWAVTT KSGLKWTCIG GINRQTSQMY RGGGAVCLEN ANVHKAFYDS VAEYEPCT