TX9A1_ANEVI
ID TX9A1_ANEVI Reviewed; 159 AA.
AC P0DMZ8;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=U-actitoxin-Avd13a/b {ECO:0000303|PubMed:22683676};
DE Short=U-AITX-Avd13a/b {ECO:0000303|PubMed:22683676};
DE AltName: Full=Peptide toxin AV-1 {ECO:0000303|PubMed:21281459};
DE Contains:
DE RecName: Full=U-actitoxin-Avd13b {ECO:0000303|PubMed:22683676};
DE Short=U-AITX-Avd13b {ECO:0000303|PubMed:22683676};
DE AltName: Full=AnmTX Avi 9a-1 {ECO:0000303|PubMed:23801332};
DE Contains:
DE RecName: Full=U-actitoxin-Avd13a {ECO:0000303|PubMed:22683676};
DE Short=U-AITX-Avd13a {ECO:0000303|PubMed:22683676};
DE AltName: Full=AnmTX Avi 9a-2 {ECO:0000303|PubMed:23801332};
DE Flags: Precursor;
OS Anemonia viridis (Snakelocks anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Anemonia.
OX NCBI_TaxID=51769;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=19627569; DOI=10.1186/1471-2164-10-333;
RA Sabourault C., Ganot P., Deleury E., Allemand D., Furla P.;
RT "Comprehensive EST analysis of the symbiotic sea anemone, Anemonia
RT viridis.";
RL BMC Genomics 10:333-333(2009).
RN [2]
RP NOMENCLATURE.
RX PubMed=21281459; DOI=10.1186/1471-2164-12-88;
RA Kozlov S., Grishin E.;
RT "The mining of toxin-like polypeptides from EST database by single residue
RT distribution analysis.";
RL BMC Genomics 12:88-88(2011).
RN [3]
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).
RN [4]
RP NOMENCLATURE.
RX PubMed=23801332; DOI=10.1074/jbc.m113.485516;
RA Osmakov D.I., Kozlov S.A., Andreev Y.A., Koshelev S.G., Sanamyan N.P.,
RA Sanamyan K.E., Dyachenko I.A., Bondarenko D.A., Murashev A.N., Mineev K.S.,
RA Arseniev A.S., Grishin E.V.;
RT "Sea anemone peptide with uncommon beta-hairpin structure inhibits acid-
RT sensing ion channel 3 (ASIC3) and reveals analgesic activity.";
RL J. Biol. Chem. 288:23116-23127(2013).
CC -!- FUNCTION: Inhibits ion channels. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sea anemone structural class 9a family.
CC {ECO:0000305|PubMed:23801332}.
CC -!- CAUTION: Opinions are divided on whether Anemonia viridis (Forsskal,
CC 1775) and Anemonia sulcata (Pennant, 1777) are separate species.
CC {ECO:0000305}.
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DR EMBL; FK719982; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DMZ8; -.
DR SMR; P0DMZ8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Nematocyst; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..26
FT /evidence="ECO:0000305|PubMed:21281459"
FT /id="PRO_0000433714"
FT PEPTIDE 27..55
FT /note="U-actitoxin-Avd13b"
FT /id="PRO_0000433715"
FT PROPEP 59..60
FT /evidence="ECO:0000305|PubMed:21281459"
FT /id="PRO_0000433716"
FT PEPTIDE 61..89
FT /note="U-actitoxin-Avd13b"
FT /id="PRO_0000433717"
FT PROPEP 93..94
FT /evidence="ECO:0000305|PubMed:21281459"
FT /id="PRO_0000433718"
FT PEPTIDE 95..123
FT /note="U-actitoxin-Avd13b"
FT /id="PRO_0000433719"
FT PROPEP 127..128
FT /evidence="ECO:0000305|PubMed:21281459"
FT /id="PRO_0000433720"
FT PEPTIDE 129..157
FT /note="U-actitoxin-Avd13a"
FT /id="PRO_0000433721"
FT DISULFID 33..45
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 36..52
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 67..79
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 70..86
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 101..113
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 104..120
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 135..147
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 138..154
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
SQ SEQUENCE 159 AA; 17758 MW; 14A64EF0B3B0A695 CRC64;
MKSIFLVFFA VCLVKAEAGK GRKREPNIIN PPCRECYVQD SSGNCVYDKW GCGGARKREP
NIINPPCREC YVQDSSGNCV YDKWGCGGAR KREPNIINPP CRECYVQDSS GNCVYDKWGC
GGARKREPNI INPPCRECYV QDSSGNCVYH KWGCGGARK
