ID A0A3B4UNB3_SERDU Unreviewed; 711 AA.
AC A0A3B4UNB3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Neoverrucotoxin subunit beta-like {ECO:0000313|Ensembl:ENSSDUP00000019837.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000019837.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000019837.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the SNTX/VTX toxin family.
CC {ECO:0000256|ARBA:ARBA00006480}.
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DR AlphaFoldDB; A0A3B4UNB3; -.
DR STRING; 41447.ENSSDUP00000019837; -.
DR Ensembl; ENSSDUT00000020187.1; ENSSDUP00000019837.1; ENSSDUG00000014154.1.
DR GeneTree; ENSGT00390000014380; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR CDD; cd16040; SPRY_PRY_SNTX; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR048997; Stonustoxin-like_helical.
DR InterPro; IPR040581; Thioredoxin_11.
DR PANTHER; PTHR31594; AIG1-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR31594:SF16; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF21109; Stonustoxin_helical; 1.
DR Pfam; PF18078; Thioredoxin_11; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 3: Inferred from homology;
KW Cytolysis {ECO:0000256|ARBA:ARBA00022852};
KW Hemolysis {ECO:0000256|ARBA:ARBA00022735};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 688..710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 508..709
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
SQ SEQUENCE 711 AA; 80975 MW; D338DCBC143447AE CRC64;
MASDQMVVAA LGRPFTLGML YDAQKDQLIT AFPQWDKKTL QENSKKHLQQ TSAYEITASD
SFESKASLLD VEASLKASFL SGLVEVGGSA SYLNDKKKSN KQSRVTFQYK ATTVFEQLTM
THPEAKNMQE KEVHENCSAT HVVTGILYGA NAFFVFDSKK LDASDVQNIQ GSMEAMVKKI
PSFTFEGKVE IKLSDEEKAL TEKFSCKFYG DFILESNPVT FEDAVKTYQQ LPKLLGENGE
KTVPVKVWLT PLKKLVSSAS ELKREICVGL LRKVENALES MMEIQVRCND SLEDEVVKSF
PQITKKLSNF KDVCDDYTTK LRKTMKEKFP SIRAGNEVDS SVEKLFDNKE KSPFSHENLS
KWLNNEERKI NVIRSCVELE EIKIIQNKSE LDREVFDRHV DDVLCFVFTS LETAEPYLVQ
MSDYLHSHDP QCVGSIPPQT QDRWHFSQEV LNKMREKASY FHGLAKALKS SSRFRFLVAV
VPNEKYKGAT IYHYRNGMLV TEDFSKPAVP DVKTVTDRRD LLWYACDLNL DPDTASGYLS
LSEGNKKATC GTWQTYPDRR QRFDTRPQVL CREGLTGQHY WEVEWSEGCN NEVGVGVTYG
EIERKGKGAD TGLGSNSLSW YFGVKDKFEA WHNGHVWSKD LPPTGCRRVG VFLDCCAGSL
SFYNITHNTL SHLYSFKAQF IQPLHPGFYI YNTSNYAALL WYCFILNILI Y
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