CTXB_SCOPL
ID CTXB_SCOPL Reviewed; 702 AA.
AC A0A2P1BRP3;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Cytolytic toxin-beta {ECO:0000312|EMBL:AVI44917.1};
DE Short=Sp-CTx-beta {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:Q91453}.
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:Q91453}.
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:Q91453}.
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:Q91453}.
CC -!- PTM: Intrachain disulfide bonds may be present in the heterodimer.
CC {ECO:0000250|UniProtKB:Q91453}.
CC -!- SIMILARITY: Belongs to the SNTX/VTX toxin family. {ECO:0000305}.
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DR EMBL; MG053104; AVI44917.1; -; mRNA.
DR AlphaFoldDB; A0A2P1BRP3; -.
DR SMR; A0A2P1BRP3; -.
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; IPR003877; SPRY_dom.
DR InterPro; IPR040581; Thioredoxin_11.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF18078; Thioredoxin_11; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 1: Evidence at protein level;
KW Cytolysis; Disulfide bond; Glycoprotein; Hemolysis; Myotoxin; Neurotoxin;
KW Secreted; Toxin.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q91453"
FT CHAIN 2..702
FT /note="Cytolytic toxin-beta"
FT /id="PRO_0000451468"
FT DOMAIN 504..702
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 2..264
FT /note="Structural MACPF/CDC pore-forming domain"
FT /evidence="ECO:0000250|UniProtKB:Q98989"
FT REGION 265..387
FT /note="Structural FAT domain"
FT /evidence="ECO:0000250|UniProtKB:Q98989"
FT REGION 388..515
FT /note="Thioredoxin (THX) domain"
FT /evidence="ECO:0000250|UniProtKB:Q98989"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 702 AA; 80127 MW; 88E55C4968807B54 CRC64;
MPSDILVVAA LGRPFTLGAL YDARKDKLYP GFTLWEHEVL EESTVESDQP SSTFEITASD
SIDDKSSLMD IEASLKASFL GGLIEVGGSA KYLNDTKKFK NQSRVTLQYK ATTSFKQLMT
NLETKHVEYS EYFQNIEATH VVIGILYGAN AFFVFDSDKV DSSNVQDIQG SMEAVIKKIP
SVEISGQGSV QLTSEESDIT NSFSCKFHGD FHLPSNPTTF EDAVKTYQQL PQMMGKETAV
PMTVWLVPMT NFYSEAPQLM ADSSTPILRK VRNTLEAMRQ LDMRCNDSLE RRHSEAGFHC
LKKKLKTFQK HYERLHVNPF RKNHFPETFS PSGKGTKMKL QCLPTFRNKL RSPSNINSLN
MWMDCAEREI NVLRSCIDII EEAKHKVVLS KSQMARELDD SEVKHAVCYV FTYVTDYDPF
LNALSDFSKS IKPKKYSPSK KDYWYTSDDV PEMMREKAHH FYNLAKDMEN RCVRFLVASI
VNPKEEGAAI HYYREGIQII NDFSNPRIPP VETIQDQESY SGMTVSSPWK ETAHPALHLS
EGNKKAMSGK PQPSDNNPKR FDHYQQVLCN KGLSKRHYWE VEWCGYVRAG ITYKGIQRKT
FASECSLGHT DMSWVFDYYP KSGYHHIYNN KKVRVKVASP GFDRLGVYLD WPAGTLSFYM
VTSTWVTHLH TFSIRFNEAV YPAFLIGHGQ KNANGQIKLK GE
