ATPI1_ACTTE
ID ATPI1_ACTTE Reviewed; 285 AA.
AC A0A6P8HC43;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 25-MAY-2022, entry version 7.
DE RecName: Full=Actinia tenebrosa protease inhibitors {ECO:0000303|PubMed:31842369};
DE AltName: Full=Carboxypeptidase inhibitor SmCI-like;
DE Contains:
DE RecName: Full=ATPI-I {ECO:0000303|PubMed:31842369};
DE Contains:
DE RecName: Full=ATPI-II {ECO:0000303|PubMed:31842369};
DE Flags: Precursor;
OS Actinia tenebrosa (Australian red waratah sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Actinia.
OX NCBI_TaxID=6105;
RN [1] {ECO:0000312|Proteomes:UP000515163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=31641475; DOI=10.1002/ece3.5633;
RA Surm J.M., Stewart Z.K., Papanicolaou A., Pavasovic A., Prentis P.J.;
RT "The draft genome of Actinia tenebrosa reveals insights into toxin
RT evolution.";
RL Ecol. Evol. 9:11314-11328(2019).
RN [2]
RP PROTEIN SEQUENCE OF 88-145 AND 226-285, FUNCTION, MASS SPECTROMETRY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND 3D-STRUCTURE
RP MODELING IN COMPLEX WITH SUBSTRATES.
RX PubMed=31842369; DOI=10.3390/md17120701;
RA Chen X., Leahy D., Van Haeften J., Hartfield P., Prentis P.J.,
RA van der Burg C.A., Surm J.M., Pavasovic A., Madio B., Hamilton B.R.,
RA King G.F., Undheim E.A.B., Brattsand M., Harris J.M.;
RT "A versatile and robust serine protease inhibitor scaffold from Actinia
RT tenebrosa.";
RL Mar. Drugs 17:0-0(2019).
CC -!- FUNCTION: [ATPI-I]: May be involved in regulating functions and
CC processes within the digestive system (Probable). Shows serine protease
CC inhibitory activities (PubMed:31842369). Strongly inhibits trypsin
CC (Ki=0.05 nM), chymotrypsin (Ki=7.4 nM), and kallikreins (KLK5, KLK7 and
CC KLK14) (PubMed:31842369). {ECO:0000269|PubMed:31842369,
CC ECO:0000305|PubMed:31842369}.
CC -!- FUNCTION: [ATPI-II]: May be involved in regulating functions and
CC processes within the digestive system (Probable). Shows serine protease
CC inhibitory activities (PubMed:31842369). Strongly inhibits trypsin
CC (Ki=0.08 nM), chymotrypsin (Ki=2.9 nM), and kallikreins (KLK5, KLK7 and
CC KLK14) (PubMed:31842369). {ECO:0000269|PubMed:31842369,
CC ECO:0000305|PubMed:31842369}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [ATPI-I]:
CC Temperature dependence:
CC Is resistant to heat-induced denaturation (95 degrees Celsius).
CC {ECO:0000269|PubMed:31842369};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DMW6}.
CC Nematocyst {ECO:0000250|UniProtKB:P0DMW6}.
CC -!- TISSUE SPECIFICITY: [ATPI-I]: Mostly expressed in the mesenterial
CC filaments, with relatively low levels (3-4 fold) of expression in the
CC acrorhagi. Expression levels in tentacles are detectable, but very low.
CC {ECO:0000269|PubMed:31842369}.
CC -!- MASS SPECTROMETRY: [ATPI-I]: Mass=6719.9; Method=MALDI; Note=Average
CC mass.; Evidence={ECO:0000269|PubMed:31842369};
CC -!- MASS SPECTROMETRY: [ATPI-II]: Mass=6606.5; Method=MALDI; Note=Average
CC mass.; Evidence={ECO:0000269|PubMed:31842369};
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2
CC potassium channel toxin subfamily. {ECO:0000305}.
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DR Proteomes; UP000515163; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd00109; KU; 4.
DR Gene3D; 4.10.410.10; -; 4.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 4.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 4.
DR SUPFAM; SSF57362; SSF57362; 4.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 4.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Nematocyst;
KW Potassium channel impairing toxin; Protease inhibitor; Reference proteome;
KW Repeat; Secreted; Serine protease inhibitor; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..87
FT /evidence="ECO:0000305"
FT /id="PRO_0000452711"
FT CHAIN 88..145
FT /note="ATPI-II"
FT /evidence="ECO:0000269|PubMed:31842369"
FT /id="PRO_0000452712"
FT PROPEP 146..225
FT /evidence="ECO:0000305"
FT /id="PRO_0000452713"
FT CHAIN 226..285
FT /note="ATPI-I"
FT /evidence="ECO:0000269|PubMed:31842369"
FT /id="PRO_5028159550"
FT DOMAIN 28..78
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 91..141
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 161..211
FT /note="BPTI/Kunitz inhibitor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 231..281
FT /note="BPTI/Kunitz inhibitor 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 28..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 37..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 53..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 91..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 100..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 116..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 161..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 170..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 186..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 231..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 240..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 256..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 285 AA; 32113 MW; 2B719315DCBE1B50 CRC64;
MARTASTILF LLCLVLITGY TMARQEHCNL PLEKGKCGGR FERFYYNSHK GKCESFFYGG
CSGNDNNFEN EEECDKACGA FMTMADANSF CNLPAVVGRC KGYFPRYFYN TEAGKCQRFI
YGGCGGNRNN FETVXDCRAT CHPREKRALA DMTMADANSF CQLPAVVGRC RGRFPRYYYN
TEAGKCQRFI YGGCXGNRNN FETVEDCRAT CHPREKRALA DMTMADANSF CQLPAVVGKC
RGYFPRYYYN TEAGKCQQFI YGGCGGNRNN FETVEDCRAT CHSHA
