ID   CAMP_CRODC              Reviewed;         194 AA.
AC   U5KJJ0;
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 isoform 3;
DE   AltName: Full=Cathelicidin-related antimicrobial peptide;
DE            Short=CRAMP {ECO:0000303|PubMed:25100358};
DE   AltName: Full=Vipericidin {ECO:0000303|PubMed:25100358};
DE   Flags: Precursor;
OS   Crotalus durissus cascavella (Northeastern Brazilian rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=184540;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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 and Gram-
CC       positive bacteria. Adopts an amphipathic alpha helical conformation,
CC       that may allow to partition into the target membrane. Low hemolytic
CC       activities have been observed on mammalian cells.
CC   -!- SUBCELLULAR LOCATION: Secreted. Target cell membrane
CC       {ECO:0000250|UniProtKB:B6D434}. Note=Forms a helical membrane channel
CC       in the prey. {ECO:0000250|UniProtKB:B6D434}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|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}.
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DR   EMBL; JX948110; AGS36139.1; -; mRNA.
DR   AlphaFoldDB; U5KJJ0; -.
DR   SMR; U5KJJ0; -.
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; Secreted; Signal; Target cell membrane;
KW   Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..164
FT                   /evidence="ECO:0000305|PubMed:25100358"
FT                   /id="PRO_0000432133"
FT   PEPTIDE         161..194
FT                   /note="Cathelicidin-related peptide isoform 3"
FT                   /evidence="ECO:0000305|PubMed:25100358"
FT                   /id="PRO_0000432134"
FT   REGION          125..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..149
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   194 AA;  22006 MW;  E2BBE720F1C3960C CRC64;
     MQGFFWKTWL VLAVCGTPAS LAHRPLSYGE ALELAVSVYN GKAGEASLYR LLEAVPQPEW
     DPSSEGSQQL NFTLKETACQ VEEERSLEEC GFQEDGVVLE CTGYYFFGET PPVVVLSCVP
     VGGVEEEEEE EEEEQKAEAE NDEEVEKEKG DEEKDQPKRV KRFKKFFKKV KKSVKKRLKK
     IFKKPMVIGV TIPF