ID   CAMP_BOTAT              Reviewed;         189 AA.
AC   U5KJC9;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Batroxicidin {ECO:0000303|PubMed:25100358, ECO:0000303|PubMed:28246023};
DE            Short=BatxC {ECO:0000303|PubMed:28246023};
DE   AltName: Full=Cathelicidin-related antimicrobial peptide {ECO:0000303|PubMed:25100358};
DE            Short=CRAMP {ECO:0000303|PubMed:25100358};
DE   AltName: Full=Vipericidin {ECO:0000303|PubMed:25100358};
DE   Flags: Precursor;
OS   Bothrops atrox (Barba amarilla) (Fer-de-lance).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 156-189, AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=25100358; DOI=10.1007/s00726-014-1801-4;
RA   Falcao C.B., de La Torre B.G., Perez-Peinado C., Barron A.E., Andreu D.,
RA   Radis-Baptista G.;
RT   "Vipericidins: a novel family of cathelicidin-related peptides from the
RT   venom gland of South American pit vipers.";
RL   Amino Acids 46:2561-2571(2014).
RN   [2]
RP   FUNCTION, SYNTHESIS OF 156-189, AND PHARMACEUTICAL.
RX   PubMed=28246023; DOI=10.1016/j.toxicon.2017.02.031;
RA   Mello C.P., Lima D.B., Menezes R.R., Bandeira I.C., Tessarolo L.D.,
RA   Sampaio T.L., Falcao C.B., Radis-Baptista G., Martins A.M.;
RT   "Evaluation of the antichagasic activity of batroxicidin, a cathelicidin-
RT   related antimicrobial peptide found in Bothrops atrox venom gland.";
RL   Toxicon 130:56-62(2017).
CC   -!- FUNCTION: Potent antimicrobial peptide against Gram-negative (MIC=0.25
CC       ug/ml against E.coli ATCC 25922, MIC=1 ug/ml against P.aeruginosa) and
CC       Gram-positive bacteria (MIC=32 ug/ml against E.faecalis, MIC=32 ug/ml
CC       against S.aureus) (PubMed:25100358). Adopts an amphipathic alpha
CC       helical conformation, that may allow to partition into the target
CC       membrane (By similarity). Low hemolytic activities have been observed
CC       on mammalian cells (PubMed:25100358). In addition, when tested in vitro
CC       on the parasite Trypanosoma cruzi (responsible of the Chagas disease),
CC       is able to reduce the number of the three forms (epimastigote,
CC       trypomastigote and amastigote) by inducing cell death through necrosis
CC       (PubMed:28246023). {ECO:0000250|UniProtKB:B6D434,
CC       ECO:0000269|PubMed:25100358}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:B6D434}. Target
CC       cell membrane {ECO:0000250|UniProtKB:B6D434}. Note=Forms a helical
CC       membrane channel in the prey. {ECO:0000250|UniProtKB:B6D434}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:25100358}.
CC   -!- PHARMACEUTICAL: Promising drug candidate or lead for the development of
CC       new drugs to treat Chagas disease (also called American
CC       Trypanosomiasis). Shows a high selectivity index (SI) of 315.5 to the
CC       trypomastigote forms. {ECO:0000305|PubMed:28246023}.
CC   -!- MISCELLANEOUS: The putative mature sequence has been predicted by AMPA,
CC       a predictive algorithm for identification of peptide stretches with
CC       antimicrobial properties. {ECO:0000305|PubMed:25100358}.
CC   -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR   EMBL; JX948111; AGS36140.1; -; mRNA.
DR   AlphaFoldDB; U5KJC9; -.
DR   SMR; U5KJC9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR001894; Cathelicidin-like.
DR   InterPro; IPR046350; Cystatin_sf.
DR   PANTHER; PTHR10206; PTHR10206; 1.
DR   SUPFAM; SSF54403; SSF54403; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Disulfide bond; Membrane; Pharmaceutical; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..155
FT                   /evidence="ECO:0000305|PubMed:25100358"
FT                   /id="PRO_0000432131"
FT   PEPTIDE         156..189
FT                   /note="Batroxicidin"
FT                   /evidence="ECO:0000305|PubMed:25100358"
FT                   /id="PRO_0000432132"
FT   REGION          125..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..144
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        79..90
FT                   /evidence="ECO:0000250"
FT   DISULFID        101..118
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   189 AA;  21811 MW;  BA15856C1AE66E28 CRC64;
     MQGFFWKTWL VVALCGTSSS LAHRPLSYGE ALELALSIYN SKAGEESLFR LLEAVPQPEW
     DPLSEGSQQL NFTIKETVCQ VEEERPLEEC GFQEDGVVLE CTGYYFFGET PPVVVLTCVP
     VGGVEEEEED EEEQKAEVEK DEEKEDEEKD RPKRVKRFKK FFKKLKNSVK KRVKKFFRKP
     RVIGVTFPF