GenomeNet

Database: UniProt
Entry: Q76DT2
LinkDB: Q76DT2
Original site: Q76DT2 
ID   TX60A_ACTVL             Reviewed;         498 AA.
AC   Q76DT2;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   23-MAY-2018, entry version 46.
DE   RecName: Full=DELTA-thalatoxin-Avl2a {ECO:0000303|PubMed:22683676};
DE            Short=DELTA-TATX-Avl2a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Toxin AvTX-60A {ECO:0000303|PubMed:15019483};
DE            Short=Av60A {ECO:0000303|PubMed:15019483};
DE   Flags: Precursor;
OS   Actineria villosa (Okinawan sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Nynantheae; Aliciidae; Actineria.
OX   NCBI_TaxID=227975;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-63, AND FUNCTION.
RC   TISSUE=Nematoblast;
RX   PubMed=15019483; DOI=10.1016/j.toxicon.2003.11.017;
RA   Oshiro N., Kobayashi C., Iwanaga S., Nozaki M., Namikoshi M.,
RA   Spring J., Nagai H.;
RT   "A new membrane-attack complex/perforin (MACPF) domain lethal toxin
RT   from the nematocyst venom of the Okinawan sea anemone Actineria
RT   villosa.";
RL   Toxicon 43:225-228(2004).
RN   [2]
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).
CC   -!- FUNCTION: Is lethal to mice, and may cause hemolytic activity.
CC       {ECO:0000269|PubMed:15019483}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst
CC       {ECO:0000305}.
DR   EMBL; AB107916; BAD04943.1; -; mRNA.
DR   ProteinModelPortal; Q76DT2; -.
DR   TCDB; 1.C.39.10.1; the membrane attack complex/perforin (macpf) family.
DR   PRIDE; Q76DT2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
DR   InterPro; IPR020864; MACPF.
DR   Pfam; PF01823; MACPF; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS51412; MACPF_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytolysis; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Hemolysis; Nematocyst; Secreted; Signal; Toxin.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   PROPEP       23     35       {ECO:0000269|PubMed:15019483}.
FT                                /FTId=PRO_0000239811.
FT   CHAIN        36    498       DELTA-thalatoxin-Avl2a.
FT                                /FTId=PRO_0000239812.
FT   DOMAIN       23    359       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      410    422       EGF-like.
FT   COILED      135    159       {ECO:0000255}.
FT   DISULFID    389    402       {ECO:0000250}.
FT   DISULFID    396    410       {ECO:0000250}.
FT   DISULFID    412    422       {ECO:0000250}.
SQ   SEQUENCE   498 AA;  55463 MW;  515D5766108838C0 CRC64;
     MSPYFKLSSA LIFLAITMEA LCSPIENTST SNKDNDKETE HIEISAKPSG ISRGALGQGF
     EIHREDLLSK QFEATGEKIF EDLPMDECTV TTTLGTIERD DSFYNSTESL YQSVASSTKI
     SGSLKGAYTL GVSVAAVTNN IASSEEEVQG LSLNLKAYSM SSILKKNCVN TKPLSKDLVS
     DFEALDSEIT KPWKLSSWKK YKVLLEKYGS HIVKESISGS SIYQYVFAKS NQKFNHRSFT
     VKACVSLAGP KNASKVGFAG CTGVSQQEIE QSSSQSMIKK LVVRGGKTET RASLIGELDP
     DQINKFLIEA ETDPSPIQYK FEPIWTILKN RYVGTEHFAK AVNLEQFYKG FLHFGCSFLH
     TSNADNADVE IQKFDFAKTS DPDAPTYVCK VGPEGCQHHE DCHYRAAFWC ECGGPYDLAR
     TCLRYKTEKL NSGSTKRECY PNKESGFAWH GCQLHGLSCW CSAPNKNWEE TWSGEDTNNA
     LNDVHQVLME KKRRDQAK
//
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