IELA_ANESU
ID IELA_ANESU Reviewed; 48 AA.
AC P16895;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=PI-actitoxin-Avd5a {ECO:0000303|PubMed:22683676};
DE Short=PI-AITX-Avd5a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Non-classical Kazal-type elastase inhibitor {ECO:0000303|PubMed:2892502};
OS Anemonia sulcata (Mediterranean snakelocks sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Anemonia.
OX NCBI_TaxID=6108;
RN [1]
RP PROTEIN SEQUENCE, AND DISULFIDE BOND.
RX PubMed=2892502; DOI=10.1515/bchm3.1987.368.2.1297;
RA Tschesche H., Kolkenbrock H., Bode W.;
RT "The covalent structure of the elastase inhibitor from Anemonia sulcata
RT -- a 'non-classical' Kazal-type protein.";
RL Biol. Chem. Hoppe-Seyler 368:1297-1304(1987).
RN [2]
RP NOMENCLATURE.
RX PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA Oliveira J.S., Fuentes-Silva D., King G.F.;
RT "Development of a rational nomenclature for naming peptide and protein
RT toxins from sea anemones.";
RL Toxicon 60:539-550(2012).
RN [3]
RP STRUCTURE BY NMR, DISULFIDE BONDS, SYNTHESIS, AND FUNCTION.
RX PubMed=16008348; DOI=10.1021/bi0472806;
RA Hemmi H., Kumazaki T., Yoshizawa-Kumagaye K., Nishiuchi Y., Yoshida T.,
RA Ohkubo T., Kobayashi Y.;
RT "Structural and functional study of an Anemonia elastase inhibitor, a
RT 'nonclassical' Kazal-type inhibitor from Anemonia sulcata.";
RL Biochemistry 44:9626-9636(2005).
CC -!- FUNCTION: Exhibits strong inhibition toward Streptomyces griseus
CC protease B (SGPB) (AC P00777). {ECO:0000269|PubMed:16008348}.
CC -!- CAUTION: Opinions are divided on whether Anemonia viridis (Forsskal,
CC 1775) and Anemonia sulcata (Pennant, 1777) are separate species.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S00130; S00130.
DR PDB; 1Y1B; NMR; -; A=1-48.
DR PDB; 1Y1C; NMR; -; A=1-48.
DR PDBsum; 1Y1B; -.
DR PDBsum; 1Y1C; -.
DR AlphaFoldDB; P16895; -.
DR SMR; P16895; -.
DR MEROPS; I01.018; -.
DR EvolutionaryTrace; P16895; -.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001239; Prot_inh_Kazal-m.
DR Pfam; PF00050; Kazal_1; 1.
DR PRINTS; PR00290; KAZALINHBTR.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Serine protease inhibitor.
FT CHAIN 1..48
FT /note="PI-actitoxin-Avd5a"
FT /evidence="ECO:0000269|PubMed:2892502"
FT /id="PRO_0000073199"
FT DOMAIN 1..48
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 10..11
FT /note="Reactive bond"
FT DISULFID 4..34
FT /evidence="ECO:0000269|PubMed:16008348,
FT ECO:0000269|PubMed:2892502"
FT DISULFID 8..27
FT /evidence="ECO:0000269|PubMed:16008348,
FT ECO:0000269|PubMed:2892502"
FT DISULFID 16..48
FT /evidence="ECO:0000269|PubMed:16008348,
FT ECO:0000269|PubMed:2892502"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:1Y1B"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:1Y1B"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:1Y1B"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1Y1B"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1Y1B"
SQ SEQUENCE 48 AA; 5134 MW; 40FBC2AC936AA78F CRC64;
KPDCPLICTM QYDPVCGSDG ITYGNACMLL GASCRSDTPI ELVHKGRC
