CTXA_SCOPL
ID CTXA_SCOPL Reviewed; 702 AA.
AC A0A2P1BRQ0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Cytolytic toxin-alpha {ECO:0000312|EMBL:AVI44916.1};
DE Short=Sp-CTx-alpha {ECO:0000303|PubMed:30181739};
OS Scorpaena plumieri (Spotted scorpionfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Scorpaenoidei; Scorpaenidae; Scorpaeninae;
OC Scorpaena.
OX NCBI_TaxID=274700;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom gland;
RX PubMed=30181739; DOI=10.1186/s40409-018-0158-7;
RA Costa F.L.S., De Lima M.E., Figueiredo S.G., Ferreira R.S., Prates N.S.,
RA Sakamoto T., Salas C.E.;
RT "Sequence analysis of the cDNA encoding for SpCTx: a lethal factor from
RT scorpionfish venom (Scorpaena plumieri).";
RL J. Venom. Anim. Toxins Incl. Trop. Dis. 24:24-24(2018).
RN [2]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=23933196; DOI=10.1016/j.toxicon.2013.07.023;
RA Gomes H.L., Andrich F., Fortes-Dias C.L., Perales J., Teixeira-Ferreira A.,
RA Vassallo D.V., Cruz J.S., Figueiredo S.G.;
RT "Molecular and biochemical characterization of a cytolysin from the
RT Scorpaena plumieri (scorpionfish) venom: evidence of pore formation on
RT erythrocyte cell membrane.";
RL Toxicon 74:92-100(2013).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND GLYCOSYLATION.
RC TISSUE=Venom;
RX PubMed=20493199; DOI=10.1016/j.toxicon.2010.05.003;
RA Andrich F., Carnielli J.B., Cassoli J.S., Lautner R.Q., Santos R.A.,
RA Pimenta A.M., de Lima M.E., Figueiredo S.G.;
RT "A potent vasoactive cytolysin isolated from Scorpaena plumieri
RT scorpionfish venom.";
RL Toxicon 56:487-496(2010).
CC -!- FUNCTION: This heterodimer induces potent hemolytic activities (when
CC tested on rabbit erythrocytes, EC(50)=25-56 ng/mL) due to its ability
CC to form pores in the cell membrane (PubMed:23933196, PubMed:20493199).
CC The pore may be composed of 10 alpha/beta heterodimers (By similarity).
CC The toxin shows cardiovascular effects that include a vasorelaxant
CC action that may involve the L-arginine-nitric oxid synthase pathway
CC (PubMed:20493199). In addition, it displays edema-inducing activities,
CC increases vascular permeability (By similarity). It also shows myotoxic
CC activities and interferes irreversibly with neuromuscular function (By
CC similarity). It also induces irreversible platelet aggregation in
CC rabbit or rat (but not in human or mouse) whole blood (By similarity).
CC In addition, it has been observed to increase spontaneous quantal
CC acetylcholine release from isolated frog cutaneous pectoris motor
CC endings (By similarity). {ECO:0000250|UniProtKB:Q98989,
CC ECO:0000269|PubMed:20493199, ECO:0000269|PubMed:23933196}.
CC -!- SUBUNIT: Heterodimer of alpha and beta subunits (PubMed:20493199); non-
CC covalently linked. Also associates into tetramers or even higher
CC aggregates (PubMed:23933196, PubMed:20493199).
CC {ECO:0000269|PubMed:20493199, ECO:0000269|PubMed:23933196}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20493199,
CC ECO:0000269|PubMed:23933196}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:20493199, ECO:0000305|PubMed:23933196}.
CC -!- DOMAIN: The first domain (residues 2-265) is structurally homologous to
CC the membrane attack complex-ferforin/cholesterol-dependent cytolysin
CC (MACPF/CDC) pore-forming domain. It makes numerous contacts with the
CC FAT domain and comprise essentially the core pore-forming machinery.
CC {ECO:0000250|UniProtKB:Q98989}.
CC -!- DOMAIN: The second domain is structurally homologous to the focal
CC adhesion-targeting (FAT) domain (266-385). It makes numerous in cis
CC contacts with the MACPF/CDC domain (first domain) and the thioredoxin
CC (THX) domain (third domain) as well as extensive in trans interactions
CC at the SNTX-alpha/beta interface. {ECO:0000250|UniProtKB:Q98989}.
CC -!- DOMAIN: The third domain corresponds to the thioredoxin (THX) domain.
CC It makes numerous contacts with the second domain (FAT domain). Since
CC it lacks the canonical catalytic residues, it may only play a purely
CC structural role. {ECO:0000250|UniProtKB:Q98989}.
CC -!- DOMAIN: The fourth domain corresponds to the B30.2/SPRY domain. This
CC domain would be responsible for initial interaction with the cell
CC surface through either lipid- or protein-mediated interactions.
CC {ECO:0000250|UniProtKB:Q98989}.
CC -!- PTM: Intrachain disulfide bonds may be present in the heterodimer.
CC {ECO:0000250|UniProtKB:Q98989}.
CC -!- SIMILARITY: Belongs to the SNTX/VTX toxin family. {ECO:0000305}.
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DR EMBL; MG053103; AVI44916.1; -; mRNA.
DR AlphaFoldDB; A0A2P1BRQ0; -.
DR SMR; A0A2P1BRQ0; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR040581; Thioredoxin_11.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF18078; Thioredoxin_11; 1.
DR SMART; SM00589; PRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 1: Evidence at protein level;
KW Cytolysis; Disulfide bond; Glycoprotein; Hemolysis;
KW Hemostasis impairing toxin; Myotoxin; Neurotoxin;
KW Platelet aggregation activating toxin; Secreted; Toxin.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q91453"
FT CHAIN 2..702
FT /note="Cytolytic toxin-alpha"
FT /evidence="ECO:0000305|PubMed:30181739"
FT /id="PRO_0000451467"
FT DOMAIN 505..702
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 2..265
FT /note="Structural MACPF/CDC pore-forming domain"
FT /evidence="ECO:0000250|UniProtKB:Q98989"
FT REGION 266..385
FT /note="Structural FAT domain"
FT /evidence="ECO:0000250|UniProtKB:Q98989"
FT REGION 386..513
FT /note="Thioredoxin (THX) domain"
FT /evidence="ECO:0000250|UniProtKB:Q98989"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 702 AA; 79801 MW; 7C641BB921332F7D CRC64;
MSSDIIMAGL GRPFTLGFLY DARREKLIPG FSLFGDETLQ KYATSTPQHS SDFQIVASDS
VESKSNVMDI EASLGVSFLG GLVEVGGSAK YLNNTKKYQN QSRVTLQYKV TTTFKQFKAP
PGKVNVQQTA ISDKNVATHV VTAILFGANA FFVFDSDKVE DSNLQDIQGK MEAVIKKIPS
VSIEGSGSVQ LTDEEKSLAS NLSCKFHGDF LLESLPTTFE EAVMTYQKLP ELVGEEASDG
VPMKVWLVPL TRFYSKADLL VRDISQGLVR KVHSILEDLH KLKRRANDSL EDDTVKLFPL
LEKKLKNFQK NYSDYMTTFR RTISQKLQSI RKGDEDETAM LQLFEDRLRS PFNIDSLNMW
MEITEREINV LRSCIDIIEE TKHKAVLSQS QMVKDLLDSE VMHAVCYVFT YVTDKDHYLD
ALRDYLKSPN SRPARVRPVV TWVASNTVLE TMREKAHLFR SLAKDMENRC VHFLVASIVN
LKVEGAAIHY YRESVLIEPN FKHPIISAVE KIVDRRDLLW YDCELTLDPN TSHPSLYLSE
GNKKAVTGTL RAFDNNPERF GLWQQVLCNK GLSRRHYWEV EWNGYVIVGV TYSSIGRKNI
DIQSFIGFSE TSWTLMFIPK NGVAVKGARR SVSYYFISDL AFPPLGLYHD CHASTLSFYK
VSDNVLNHFH TIEIKPKLSE PVYAIIRIGD EDRPYHGTVR LL
