LCTA_LATTR
ID LCTA_LATTR Reviewed; 1413 AA.
AC Q9XZC0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Alpha-latrocrustotoxin-Lt1a {ECO:0000305};
DE Short=Alpha-LCT-Lt1a {ECO:0000305};
DE AltName: Full=Alpha-latrocrustotoxin {ECO:0000303|PubMed:34845192};
DE Short=Alpha-LCT {ECO:0000303|PubMed:34845192};
DE AltName: Full=Crusta1;
DE Flags: Precursor; Fragment;
OS Latrodectus tredecimguttatus (Mediterranean black widow spider)
OS (Latrodectus mactans tredecimguttatus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Araneoidea; Theridiidae; Latrodectus.
OX NCBI_TaxID=6925;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10563207;
RA Danilevich V.N., Luk'ianov S.A., Grishin E.V.;
RT "Cloning and structure of gene encoded alpha-latrocrustoxin from the Black
RT widow spider venom.";
RL Bioorg. Khim. 25:537-547(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11195592; DOI=10.1023/a:1026666606311;
RA Danilevich V.N., Grishin E.V.;
RT "The chromosomal genes for black widow spider neurotoxins do not contain
RT introns.";
RL Bioorg. Khim. 26:933-939(2000).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=10234443;
RA Volynskii K.E., Volkova T.M., Galkina T.G., Krasnoperov V.G.,
RA Pluzhnikov K.A., Khvoshchev M.V., Grishin E.V.;
RT "Molecular cloning and primary structure of cDNA fragment for alpha-
RT latrocrustatoxin from black widow spider venom.";
RL Bioorg. Khim. 25:25-30(1999).
RN [4]
RP TOXIC DOSE.
RX PubMed=9792186; DOI=10.1016/s0041-0101(98)00162-7;
RA Grishin E.V.;
RT "Black widow spider toxins: the present and the future.";
RL Toxicon 36:1693-1701(1998).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.03 ANGSTROMS) OF 48-1066 IN MONOMERIC
RP FORM, FUNCTION, RECOMBINANT EXPRESSION, AND SUBUNIT.
RX PubMed=34845192; DOI=10.1038/s41467-021-26562-8;
RA Chen M., Blum D., Engelhard L., Raunser S., Wagner R., Gatsogiannis C.;
RT "Molecular architecture of black widow spider neurotoxins.";
RL Nat. Commun. 12:6956-6956(2021).
CC -!- FUNCTION: Crustacean-selective presynaptic neurotoxin that induces
CC neurotransmitter exocytosis. May bind to crustacean neurexin-1 homolog,
CC adhesion G protein-coupled receptor L1 homolog, and receptor-type
CC tyrosine-protein phosphatase S homolog, and induces neurotransmitter
CC exocytosis both by forming tetrameric pores in membranes and signaling
CC via G protein-coupled receptor (By similarity) (PubMed:34845192). This
CC recombinant protein form channels in artificial membrane bilayers, that
CC are stabilized by calcium ions and allow calcium flux at negative
CC membrane potentials (PubMed:34845192). {ECO:0000250|UniProtKB:P23631,
CC ECO:0000269|PubMed:34845192}.
CC -!- SUBUNIT: Homotetramer in membranes. {ECO:0000269|PubMed:34845192}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:10234443}. Target
CC cell membrane {ECO:0000269|PubMed:34845192}. Note=Forms a membrane
CC channel in the prey. {ECO:0000269|PubMed:34845192}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10234443}.
CC -!- DOMAIN: The H8 helix is predicted to insert into membranes and form
CC pores by assembling into tetramers. The helix is contained within a
CC helical bundle domain that undergoes significant conformational changes
CC during pore formation to allow exposure of the H8 transmembrane helix
CC and transition of the toxin from a soluble monomer to a transmembrane
CC tetramer. {ECO:0000269|PubMed:34845192}.
CC -!- TOXIC DOSE: LD(50) is 100 ug/kg to the crayfish Procambarus cubensis.
CC {ECO:0000269|PubMed:9792186}.
CC -!- SIMILARITY: Belongs to the cationic peptide 01 (latrotoxin) family. 01
CC (alpha-latrocrustotoxin) subfamily. {ECO:0000305}.
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DR EMBL; AF134162; AAD33043.1; -; Genomic_DNA.
DR PDB; 7PTX; EM; 4.03 A; A=16-1211.
DR PDBsum; 7PTX; -.
DR AlphaFoldDB; Q9XZC0; -.
DR SMR; Q9XZC0; -.
DR ArachnoServer; AS000061; alpha-Latrocrustotoxin-Lt1a.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 5.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 6.
DR Pfam; PF13606; Ank_3; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 20.
DR SUPFAM; SSF48403; SSF48403; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 12.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Cleavage on pair of basic residues; Exocytosis;
KW Membrane; Neurotoxin; Presynaptic neurotoxin; Repeat; Secreted;
KW Target cell membrane; Target membrane; Toxin; Transmembrane.
FT PROPEP <1..28
FT /evidence="ECO:0000305"
FT /id="PRO_0000391353"
FT CHAIN 29..1192
FT /note="Alpha-latrocrustotoxin-Lt1a"
FT /evidence="ECO:0000305"
FT /id="PRO_0000067053"
FT PROPEP 1193..1413
FT /evidence="ECO:0000305"
FT /id="PRO_0000391354"
FT REPEAT 457..490
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 494..524
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 528..557
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 562..592
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 596..625
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 629..658
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 664..694
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 699..729
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT REPEAT 733..762
FT /note="ANK 9"
FT /evidence="ECO:0000255"
FT REPEAT 766..795
FT /note="ANK 10"
FT /evidence="ECO:0000255"
FT REPEAT 799..828
FT /note="ANK 11"
FT /evidence="ECO:0000255"
FT REPEAT 832..861
FT /note="ANK 12"
FT /evidence="ECO:0000255"
FT REPEAT 866..895
FT /note="ANK 13"
FT /evidence="ECO:0000255"
FT REPEAT 899..928
FT /note="ANK 14"
FT /evidence="ECO:0000255"
FT REPEAT 965..995
FT /note="ANK 15"
FT /evidence="ECO:0000255"
FT REPEAT 996..1026
FT /note="ANK 16"
FT /evidence="ECO:0000255"
FT REPEAT 1031..1072
FT /note="ANK 17"
FT /evidence="ECO:0000255"
FT REPEAT 1077..1106
FT /note="ANK 18"
FT /evidence="ECO:0000255"
FT REPEAT 1109..1139
FT /note="ANK 19"
FT /evidence="ECO:0000255"
FT REPEAT 1143..1172
FT /note="ANK 20"
FT /evidence="ECO:0000255"
FT REGION 238..257
FT /note="Helix H8 is the probable transmembrane region of the
FT tetrameric pore inserted in the target cell membrane"
FT /evidence="ECO:0000305|PubMed:34845192"
FT NON_TER 1
SQ SEQUENCE 1413 AA; 158223 MW; 98E263D6CE982EC8 CRC64;
VSIFIFHFSA NILVRNSEMK GKRVISKREM SKADQCTFLS YQSVAYGTLG DVAGDVSSIE
GADLVATPIA AGGHLAKGAT DAAMIAMDCS SIPFDEIKQQ LNQRFNEVDK KLQKGAEALE
NVTELAEKTY SSVEKMRVEM REGFNHVIAT IENANTKQII TGINQIIQYF NDERENINNR
QKEDYVAKLQ EPASGNFLLY LRKSRTSEDG SLHSLLFKII NQELAIPNNA ADNNAIRALF
ALFYGTQTFI SIMFYLVKQY SYLADYHYQN GNLAEFNSNF DHMKTVFQDF KFTLIGINTS
NSKPLVNTVL SIIEDVKNKR FIRNLRSNLY QKIIKSTKSL LDLREKITKM DLPIIEDTPK
SSVLINFREK SSSVPRIETP ILKWTPGTVV KYAIQYEQDG KYSKISKWSN PITVQRLANP
YITIDKDRRN RLVFRQFGNE KPELISILDS SQNEFRDIHR DLYNAAQMPY KETALGICRK
LIDSGAQVGA SFEMGRKSIH ASATAGNDDV ARLLLAKNNG LLNVPDKNGY TPLHIASERK
NNDFVKFLLE KGADVNVRTF ANELTPLHLA ARQDFTIIVK TLMEKRGIDV NAKERAGFTP
LHLSITSNSR AARTLINETP AGINIKSNSG LTPLHLAVLQ NNLSAAKVLV KSNKKVKLNE
MDNNGMTPLH YASMLGNLEF VKYFTSEQGI DVNAKTKVKN WTPLHLAILF KKFDVAQSLL
QVRNIDISTR ADQAITPLHL AAATGNSQIV KTILNSGAVV DQETANGFTA LHLAIMNPNT
ETPQFLIAKG ANINAKTNDG STPLHFAAAL GKTNIFQLLM DKGANIKAEN LINQMPIHEA
VVNGHLAIVK MLIEQDSSLM NAKNMRDEYP FYLAAEKRYK DVFNYLESKG ADVNEKNNDG
NTLLHLFSIN GEVEVVQFLI QNGADFRLRN KERKSFFDLA VEFGHAGIVG YAIEENKVDL
QEPYRGKTIL YHAICDSVKY DRIEVVRYFV ETLNEDQCSP LQEAAAYAHL DLVKYFVQER
GINPTAFNND NQVSPLCIAI VGAPCGFVKS CDTPERLDVV EYLVDKTPDI NKECDTQQST
PVSSAVYGNK VSILNYLIRN GADPNKKVRG DPPLFIAAMI GQYDIVKSLV EQHKIDVNTR
NKEQFTPLHA AASNDHIDVV KYLIQKGADV NAKGDENLKP IDLAGEKSKA YLRSLGRRFF
RNESPSKSFE IDKFNAIMPE VSMSGKVSHD SNFIQHISSG TRSKSNFNSA KNKMYAENSH
VRSIDVNGAL LLLDFMVRVF SNRKMNYAAS ISGIKSRSNS EAQAEALILT ERFEHLLNAL
IADQSIDSLD FSNVHSRIYK AIINGNPNGI SEMLCSYAKE YSELDPEKIE KLLQEFETLT
FTKSSEIQIN EKFSHALFET CGLNRPTNVL QIK
