位置:首页 > 蛋白库 > ACTPA_ACTFR
ACTPA_ACTFR
ID   ACTPA_ACTFR             Reviewed;          20 AA.
AC   P0DUW8;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   25-MAY-2022, entry version 3.
DE   RecName: Full=DELTA-actitoxin-Afr1b {ECO:0000305};
DE            Short=DELTA-AITX-Afr1b {ECO:0000305};
DE   AltName: Full=Alpha-helical pore-forming toxin {ECO:0000250|UniProtKB:B9W5G6};
DE            Short=PFT {ECO:0000250|UniProtKB:B9W5G6};
DE   AltName: Full=Cytolysin {ECO:0000250|UniProtKB:B9W5G6};
DE   AltName: Full=Fragaceatoxin A {ECO:0000303|PubMed:31295915};
DE            Short=fraA {ECO:0000303|PubMed:31295915};
DE   Flags: Fragment;
OS   Actinia fragacea (Strawberry anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Actinia.
OX   NCBI_TaxID=396334;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=31295915; DOI=10.3390/toxins11070401;
RA   Morante K., Bellomio A., Viguera A.R., Gonzalez-Manas J.M., Tsumoto K.,
RA   Caaveiro J.M.M.;
RT   "The isolation of new pore-forming toxins from the sea anemone Actinia
RT   fragacea provides insights into the mechanisms of actinoporin evolution.";
RL   Toxins 11:0-0(2019).
CC   -!- FUNCTION: Pore-forming toxin (PFT) that consists of a crown-shaped
CC       octamer or nonamer that forms cation-selective hydrophilic pores of
CC       about 1.5 nm (inside) and 13 nm (outside) (By similarity). It causes
CC       cardiac stimulation (By similarity). Also causes hemolysis (HC(50)=0.4
CC       nM) (PubMed:31295915). Interestingly, the Phe-16 is crucial for
CC       hemolysis (By similarity). Pore formation is a multi-step process that
CC       involves specific recognition of membrane sphingomyelin (but neither
CC       cholesterol nor phosphatidylcholine) using aromatic rich region and
CC       adjacent phosphocholine (POC) binding site, firm binding to the
CC       membrane (mainly driven by hydrophobic interactions) accompanied by the
CC       transfer of the N-terminal region to the lipid-water interface and
CC       finally pore formation after oligomerization of monomers (By
CC       similarity). It is probable that a dimeric form is an assembly
CC       intermediate before the complete oligomerization (By similarity). The
CC       formation of stable pores occurs only in vesicles composed of DOPC/SM
CC       (there is no oligomerization when the PFT is treated with vesicles of
CC       DOPC or SM alone) (By similarity). The transmembrane pore displays 8
CC       lateral perforations, one at each subunit-subunit interface, partially
CC       occupied by the acyl-chain region of a bridging lipid (By similarity).
CC       Each pore contains 24 lipid molecules, firmly bound to each subunit,
CC       that is, 3 lipids (L1, L2, L3, L4 and/or L5) are associated to each
CC       subunit (By similarity). Lipid L1 bridges 2 subunits, whereas lipids L2
CC       and L3 bind to sites at single subunit (By similarity).
CC       {ECO:0000250|UniProtKB:B9W5G6, ECO:0000269|PubMed:31295915}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Stable up to about 65 degrees Celsius. {ECO:0000269|PubMed:31295915};
CC   -!- SUBUNIT: Octamer or nonamer in membranes. Monomer in the soluble state.
CC       {ECO:0000250|UniProtKB:B9W5G6}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31295915}.
CC       Nematocyst {ECO:0000250|UniProtKB:P61914}. Target cell membrane
CC       {ECO:0000250|UniProtKB:B9W5G6}. Note=Forms an alpha-helical membrane
CC       channel in the prey. {ECO:0000250|UniProtKB:B9W5G6}.
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   -!- MASS SPECTROMETRY: Mass=19728; Mass_error=3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:31295915};
CC   -!- MISCELLANEOUS: This protein has been found to bind carbohydrates, since
CC       it shows a substantial delay in elution profile in size-exclusion
CC       chromatography. The carbohydrate pocket ovelaps with the lipid-binding
CC       module of actinoporins. {ECO:0000250|UniProtKB:B9W5G6}.
CC   -!- SIMILARITY: Belongs to the actinoporin family. Sea anemone subfamily.
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   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cytolysis; Direct protein sequencing; Hemolysis; Ion transport;
KW   Lipid-binding; Membrane; Nematocyst; Secreted; Target cell membrane;
KW   Target membrane; Toxin; Transmembrane; Transport.
FT   CHAIN           1..>20
FT                   /note="DELTA-actitoxin-Afr1b"
FT                   /evidence="ECO:0000269|PubMed:31295915"
FT                   /id="PRO_0000453822"
FT   SITE            16
FT                   /note="Part of the hydrophobic cavity (in subunit A) that
FT                   receives Val-60 from the adjacent subunit (B); essential in
FT                   hemolysis, since it is critical for pore formation in
FT                   cholesterol-rich membrane cells (such as red blood cells)"
FT                   /evidence="ECO:0000250|UniProtKB:B9W5G6"
FT   NON_TER         20
FT                   /evidence="ECO:0000305|PubMed:31295915"
SQ   SEQUENCE   20 AA;  2017 MW;  3935C151509FF5E8 CRC64;
     SAEVAGAVIE GAKLTFNVLQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024