ID   CAMP1_PSETE             Reviewed;         184 AA.
AC   U5KJJ1;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Cathelicidin-related peptide Pt_CRAMP1 {ECO:0000303|PubMed:25100358};
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   Pseudonaja textilis (Eastern brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX   NCBI_TaxID=8673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 151-184, FUNCTION, AND TISSUE
RP   SPECIFICITY.
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).
CC   -!- FUNCTION: Potent antimicrobial peptide against Gram-negative (MIC=2
CC       ug/ml against E.coli ATCC 25922, MIC=8 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). High hemolytic activities have been observed
CC       on mammalian cells (PubMed:25100358). {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:0000269|PubMed:25100358}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JX948115; AGS36144.1; -; mRNA.
DR   AlphaFoldDB; U5KJJ1; -.
DR   SMR; U5KJJ1; -.
DR   Proteomes; UP000472273; Unplaced.
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   GO; GO:0044179; P:hemolysis in another organism; 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; Cytolysis;
KW   Disulfide bond; Hemolysis; Membrane; Reference proteome; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..150
FT                   /evidence="ECO:0000305|PubMed:25100358"
FT                   /id="PRO_0000432139"
FT   PEPTIDE         151..184
FT                   /note="Cathelicidin-related peptide Pt_CRAMP1"
FT                   /evidence="ECO:0000305|PubMed:25100358"
FT                   /id="PRO_0000432140"
FT   REGION          125..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..141
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        81..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        103..120
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   184 AA;  21152 MW;  0CFCF9A239B4CC4B CRC64;
     MEGFFWKTWL VVAAFAIGGT SSLPHKPLTY EEAVDLAVST YNGKSGEESL YRLLEAVPPP
     KWDPLSESNQ ELNLTIKETV CLVAEERSLE ECDFQDDGAV MGCTGYFFFG ESPPVLVLTC
     EPLGEDEEQN QEEEEEEEKE EDEKDQPRRV KRFKKFFMKL KKSVKKRVMK FFKKPMVIGV
     TFPF