CAMP2_PSETE
ID CAMP2_PSETE Reviewed; 184 AA.
AC U5KJM6;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Cathelicidin-related peptide Pt_CRAMP2 {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].
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 most of Gram-negative
CC bacteria, some Gram-positive bacteria (Bacillus) and some fungi
CC (C.albicans, P.pastoris, A.terreus, A.nidulans, and C.globosum). Adopts
CC an amphipathic alpha helical conformation, that may allow to partition
CC into the target membrane. No hemolytic and cytotoxic activities have
CC been observed on mammalian cells. {ECO:0000250|UniProtKB:B6D434}.
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. {ECO:0000305}.
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; JX948114; AGS36143.1; -; mRNA.
DR AlphaFoldDB; U5KJM6; -.
DR SMR; U5KJM6; -.
DR PRIDE; U5KJM6; -.
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 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; 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_0000432142"
FT PEPTIDE 151..184
FT /note="Cathelicidin-related peptide Pt_CRAMP2"
FT /evidence="ECO:0000305|PubMed:25100358"
FT /id="PRO_0000432143"
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; 21117 MW; 44A676D5C7774E82 CRC64;
MDGFFWKTWL VVAALAIGGT SSLPHKPLTY EEAVDLAVST YNGKSGEESL YRLLEAVPPP
KWDPLSESNQ ELNLTIKETV CLVAEERSLE ECDFQDDGAV MGCTGYFFFG ESPPVLVLTC
EPLGEDEEQN QEEEEEEEKE EDEKDQPRRV KRFKKFFRKL KKSVKKRVKK FFKKPRVIGV
TIPF
