NDB4M_TITSE
ID NDB4M_TITSE Reviewed; 73 AA.
AC S6CWV8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=Antimicrobial peptide TsAP-1 {ECO:0000303|PubMed:23770440};
DE AltName: Full=Non-disulfide-bridged peptide 4.22 {ECO:0000303|PubMed:24184590};
DE Short=NDBP-4.22 {ECO:0000303|PubMed:24184590};
DE Flags: Precursor;
OS Tityus serrulatus (Brazilian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=6887;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SYNTHESIS OF 23-39, MUTAGENESIS OF
RP SER-29; 32-GLY--SER-34 AND SER-36, MASS SPECTROMETRY, AMIDATION AT LYS-39,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=23770440; DOI=10.1016/j.biochi.2013.06.003;
RA Guo X., Ma C., Du Q., Wei R., Wang L., Zhou M., Chen T., Shaw C.;
RT "Two peptides, TsAP-1 and TsAP-2, from the venom of the Brazilian yellow
RT scorpion, Tityus serrulatus: evaluation of their antimicrobial and
RT anticancer activities.";
RL Biochimie 95:1784-1794(2013).
RN [2]
RP NOMENCLATURE.
RX PubMed=24184590; DOI=10.1016/j.peptides.2013.10.021;
RA Almaaytah A., Albalas Q.;
RT "Scorpion venom peptides with no disulfide bridges: a review.";
RL Peptides 51:35-45(2014).
CC -!- FUNCTION: Has a low antimicrobial activity against S.aureus, E.coli,
CC and C.albicans (MICs 120-160 uM). Has a low hemolytic activity (4% at
CC 160 uM). Also inhibits the growth of two cancer cell lines (on a total
CC of five). {ECO:0000269|PubMed:23770440}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23770440}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:23770440}.
CC -!- MASS SPECTROMETRY: Mass=1735.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:23770440};
CC -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC superfamily. Short antimicrobial peptide (group 4) family.
CC {ECO:0000305}.
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DR EMBL; HF677516; CCQ98791.1; -; mRNA.
DR AlphaFoldDB; S6CWV8; -.
DR SMR; S6CWV8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Cytolysis; Fungicide; Hemolysis;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000305|PubMed:23770440"
FT PEPTIDE 23..39
FT /note="Antimicrobial peptide TsAP-1"
FT /evidence="ECO:0000269|PubMed:23770440"
FT /id="PRO_5001155561"
FT PROPEP 45..73
FT /evidence="ECO:0000305|PubMed:23770440"
FT /id="PRO_5001155560"
FT MOD_RES 39
FT /note="Lysine amide"
FT /evidence="ECO:0000269|PubMed:23770440"
FT MUTAGEN 29
FT /note="S->K: Important increase of antimicrobial and
FT hemolytic activities; when associated with 32-K--I-34, AND
FT K-36."
FT /evidence="ECO:0000269|PubMed:23770440"
FT MUTAGEN 32..34
FT /note="GGS->KKI: Important increase of antimicrobial and
FT hemolytic activities; when associated with K-29 AND K-36."
FT /evidence="ECO:0000269|PubMed:23770440"
FT MUTAGEN 36
FT /note="S->K: Important increase of antimicrobial and
FT hemolytic activities; when associated with K-29 AND 32-K--
FT I-34."
FT /evidence="ECO:0000269|PubMed:23770440"
SQ SEQUENCE 73 AA; 8410 MW; FE8F16AD9E74D3FA CRC64;
MQIKHLITLF FLVLIVADQC SAFLSLIPSL VGGSISAFKG RRKREISAQI EQYKDLQKRE
AELEELLDRL PMY
