ID   CAMP_OPHHA              Reviewed;         191 AA.
AC   B6S2X2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Cathelicidin-related peptide Oh-Cath {ECO:0000303|PubMed:18620012};
DE   AltName: Full=Cathelicidin-related antimicrobial peptide {ECO:0000303|PubMed:25100358};
DE            Short=Oh_CRAMP {ECO:0000303|PubMed:25100358};
DE   AltName: Full=Vipericidin {ECO:0000303|PubMed:25100358};
DE   Flags: Precursor;
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 158-191, AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=18620012; DOI=10.1016/j.peptides.2008.06.008;
RA   Zhao H., Gan T.-X., Liu X.-D., Jin Y., Lee W.-H., Shen J.-H., Zhang Y.;
RT   "Identification and characterization of novel reptile cathelicidins from
RT   elapid snakes.";
RL   Peptides 29:1685-1691(2008).
RN   [2]
RP   SYNTHESIS OF 158-191, AND FUNCTION.
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=0.25
CC       ug/ml against E.coli ATCC 25922, MIC=0.5 ug/ml against P.aeruginosa)
CC       and Gram-positive bacteria (MIC=64 ug/ml against E.faecalis, MIC=64
CC       ug/ml 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). {ECO:0000250|UniProtKB:B6D434,
CC       ECO:0000269|PubMed:25100358}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:B6D434}. Target
CC       cell membrane {ECO:0000305}. Note=Forms a helical membrane channel in
CC       the prey. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MISCELLANEOUS: The peptide length (30 residues) shown here is
CC       propagated from the directly sequenced mature cathelicidin-BF. A longer
CC       peptide (34 residues) with predicted cleavage site located at position
CC       Val-157-158-Lys is proposed in PubMed:18620012. This 30 residues
CC       peptide could result from a further processing.
CC       {ECO:0000305|PubMed:18620012}.
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; EU622894; ACF21002.1; -; mRNA.
DR   AlphaFoldDB; B6S2X2; -.
DR   SMR; B6S2X2; -.
DR   PRIDE; B6S2X2; -.
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; ISS:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; ISS:UniProtKB.
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..161
FT                   /evidence="ECO:0000305|PubMed:18620012"
FT                   /id="PRO_0000410958"
FT   PEPTIDE         162..191
FT                   /note="Cathelicidin-related peptide Oh-Cath"
FT                   /evidence="ECO:0000305|PubMed:18620012"
FT                   /id="PRO_0000410959"
FT   REGION          125..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..145
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   191 AA;  21865 MW;  FF753E01F072A0E4 CRC64;
     MEGFFWKTLL VVGALAIGGT SSLPHKPLTY EEAVDLAVSI YNSKSGEDSL YRLLEAVPPP
     EWDPLSESNQ ELNFTIKETV CLVAEERSLE ECDFQEDGAI MGCTGYYFFG ESPPVLVLTC
     KPVGEEEEQK QEEGNEEEKE VEKEEKEEDE KDQPRRVKRF KKFFKKLKNS VKKRAKKFFK
     KPRVIGVSIP F