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ACTPA_OULOR
ID   ACTPA_OULOR             Reviewed;         165 AA.
AC   Q5I4B8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=DELTA-actitoxin-Oor1a {ECO:0000303|PubMed:22683676};
DE            Short=DELTA-AITX-Oor1a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Actinoporin Or-A {ECO:0000303|PubMed:15787212, ECO:0000303|PubMed:16119454};
DE   AltName: Full=Cytolysin Or-A {ECO:0000303|PubMed:15787212};
OS   Oulactis orientalis (Japan anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Oulactis.
OX   NCBI_TaxID=308032;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16119454;
RA   Il'ina A.P., Monastyrnaia M.M., Isaeva M.P., Guzev K.V., Rasskazov V.A.,
RA   Kozlovskaya E.P.;
RT   "Primary structures of actinoporins from sea anemone Oulactis orientalis.";
RL   Bioorg. Khim. 31:357-362(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-8.
RX   PubMed=15787212;
RA   Il'ina A.P., Monastyrnaia M.M., Sokotun I.N., Egorov T.A., Nazarenko I.A.,
RA   Likhatskaia G.N., Kozlovskaya E.P.;
RT   "Actinoporins from the Sea of Japan anemone Oulactis orientalis: isolation
RT   and partial characterization.";
RL   Bioorg. Khim. 31:39-48(2005).
RN   [3]
RP   3D-STRUCTURE MODELING.
RX   PubMed=20692277; DOI=10.1016/j.toxicon.2010.07.011;
RA   Monastyrnaya M., Leychenko E., Isaeva M., Likhatskaya G., Zelepuga E.,
RA   Kostina E., Trifonov E., Nurminski E., Kozlovskaya E.;
RT   "Actinoporins from the sea anemones, tropical Radianthus macrodactylus and
RT   northern Oulactis orientalis: comparative analysis of structure-function
RT   relationships.";
RL   Toxicon 56:1299-1314(2010).
RN   [4]
RP   REVIEW.
RX   PubMed=19268680; DOI=10.1016/j.toxicon.2009.02.026;
RA   Kristan K.C., Viero G., Dalla Serra M., Macek P., Anderluh G.;
RT   "Molecular mechanism of pore formation by actinoporins.";
RL   Toxicon 54:1125-1134(2009).
RN   [5]
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).
CC   -!- FUNCTION: Pore-forming protein that forms cations-selective hydrophilic
CC       pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore
CC       formation is a multi-step process that involves specific recognition of
CC       membrane sphingomyelin (but neither cholesterol nor
CC       phosphatidylcholine) using aromatic rich region and adjacent
CC       phosphocholine (POC) binding site, firm binding to the membrane (mainly
CC       driven by hydrophobic interactions) accompanied by the transfer of the
CC       N-terminal region to the lipid-water interface and finally pore
CC       formation after oligomerization of monomers. Cytolytic effects include
CC       red blood cells hemolysis, platelet aggregation and lysis, cytotoxic
CC       and cytostatic effects on fibroblasts. Lethality in mammals has been
CC       ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia,
CC       and inotropic effects. {ECO:0000250}.
CC   -!- SUBUNIT: Tetramer in the presence of a lipidic interface. Monomer, in
CC       soluble state (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Nematocyst. Target cell membrane
CC       {ECO:0000250}. Note=Forms an alpha-helical membrane channel in the
CC       prey. {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal region, before the pore is formed, is bound to
CC       the lipid membrane. It partitions into the lipid-water interface and
CC       stabilizes the monomeric molecule on the membrane. Finally, it
CC       traverses the bilayer, thus forming the transmembrane pore.
CC       {ECO:0000250|UniProtKB:P61914}.
CC   -!- SIMILARITY: Belongs to the actinoporin family. Sea anemone subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY856481; AAW48528.1; -; mRNA.
DR   AlphaFoldDB; Q5I4B8; -.
DR   SMR; Q5I4B8; -.
DR   TCDB; 1.C.38.1.4; the pore-forming equinatoxin (equinatoxin) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0046930; C:pore complex; IEA:InterPro.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006812; P:cation transport; IEA:InterPro.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0046931; P:pore complex assembly; IEA:InterPro.
DR   Gene3D; 2.60.270.20; -; 1.
DR   InterPro; IPR009104; Anemon_actinoporin-like.
DR   InterPro; IPR015926; Cytolysin/lectin.
DR   Pfam; PF06369; Anemone_cytotox; 1.
DR   SUPFAM; SSF63724; SSF63724; 1.
PE   1: Evidence at protein level;
KW   Cytolysis; Direct protein sequencing; Hemolysis; Ion transport; Membrane;
KW   Nematocyst; Secreted; Target cell membrane; Target membrane; Toxin;
KW   Transmembrane; Transport.
FT   CHAIN           1..165
FT                   /note="DELTA-actitoxin-Oor1a"
FT                   /id="PRO_0000239261"
FT   REGION          1..17
FT                   /note="N-terminal region"
FT                   /evidence="ECO:0000250"
FT   REGION          92..107
FT                   /note="Trp-rich region, which is important for the binding
FT                   to lipid membrane"
FT                   /evidence="ECO:0000250|UniProtKB:P61914"
FT   BINDING         41
FT                   /ligand="phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:295975"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:295975"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:295975"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:295975"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:295975"
FT                   /evidence="ECO:0000250"
FT   SITE            100
FT                   /note="Important in the initial contact with the lipid
FT                   membrane"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   165 AA;  17886 MW;  2066C005AB9A9F1E CRC64;
     ATFRVLAKVL AELGKVSRKI AVGVDNESGG SWTALNAYFR SGTTDVILPD LVPNQKALLY
     RGGKDTGPVA TGVVGVLAYA MSDGNTLAIL FSVPYDYNLY SNWWNVKVYS GKRRADQGMS
     EDLSYGNPYG GDNGWHARKL AYGLKERGFM KSSAQSILEI HATKA
 
 
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