ID   CAMP_NAJAT              Reviewed;         191 AA.
AC   B6S2X0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Cathelicidin-related antimicrobial peptide Na_CRAMP;
DE   AltName: Full=Cathelicidin-NA antimicrobial peptide;
DE   AltName: Full=Vipericidin {ECO:0000250|UniProtKB:U5KJM4};
DE   Flags: Precursor;
OS   Naja atra (Chinese cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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).
CC   -!- FUNCTION: Potent antimicrobial peptide against most of Gram-negative
CC       bacteria, some Gram-positive bacteria (Bacillus) and some fungi. 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}. Target cell membrane
CC       {ECO:0000305}. Note=Forms a helical membrane channel in the prey.
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18620012}.
CC   -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR   EMBL; EU622892; ACF21000.1; -; mRNA.
DR   AlphaFoldDB; B6S2X0; -.
DR   SMR; B6S2X0; -.
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; Fungicide; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..161
FT                   /evidence="ECO:0000305|PubMed:18620012"
FT                   /id="PRO_0000410960"
FT   PEPTIDE         158..191
FT                   /note="Cathelicidin-related antimicrobial peptide Na_CRAMP"
FT                   /evidence="ECO:0000305|PubMed:18620012"
FT                   /id="PRO_0000410961"
FT   REGION          126..154
FT                   /note="Disordered"
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;  21835 MW;  2CA9FF4493538E7D CRC64;
     MEGFFWKTLL VVGALTISGT SSFPHKPLTY EEAVDLAVSV YNSKSGEDSL YRLLEAVPAL
     KWDALSESNQ ELNFSVKETV CQMAEERSLE ECDFQEAGAV MGCTGYYFFG ESPPVLVLTC
     KSVGNEEEQK QEEGNEEEKE VEKEEKEEDQ KDQPKRVKRF KKFFKKLKNS VKKRAKKFFK
     KPKVIGVTFP F