ID   CAMP_BUNFA              Reviewed;         191 AA.
AC   B6D434;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Cathelicidin-related antimicrobial peptide Bf-CRAMP;
DE   AltName: Full=Cathelicidin-BF {ECO:0000303|PubMed:18795096};
DE   AltName: Full=Vipericidin {ECO:0000250|UniProtKB:U5KJM4};
DE   Flags: Precursor;
OS   Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 162-191, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CIRCULAR DICHROISM, MASS
RP   SPECTROMETRY, AND SYNTHESIS OF 157-171 AND 162-191.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=18795096; DOI=10.1371/journal.pone.0003217;
RA   Wang Y., Hong J., Liu X., Yang H., Liu R., Wu J., Wang A., Lin D., Lai R.;
RT   "Snake cathelicidin from Bungarus fasciatus is a potent peptide
RT   antibiotics.";
RL   PLoS ONE 3:E3217-E3217(2008).
RN   [2]
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
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:0000269|PubMed:18795096}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18795096}. Target
CC       cell membrane {ECO:0000269|PubMed:18795096}. Note=Forms a helical
CC       membrane channel in the prey.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland, stomach, trachea,
CC       skin, muscle, heart, kidney, lung, brain, intestine, spleen, liver, and
CC       ovary. {ECO:0000269|PubMed:18795096}.
CC   -!- MASS SPECTROMETRY: Mass=3638.0; Mass_error=0.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18795096};
CC   -!- SIMILARITY: Belongs to the cathelicidin family.
CC       {ECO:0000305|PubMed:18795096}.
CC   -!- CAUTION: A predicted cleavage site is located at position Val-157-158-
CC       Lys, giving a peptide of 34 residues instead of the 30 residues found
CC       for the purified protein. The 30 residues cathelicidin-BF could result
CC       from a further processing. {ECO:0000305|PubMed:18795096}.
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DR   EMBL; EU753183; ACI22652.1; -; mRNA.
DR   EMBL; EU622893; ACF21001.1; -; mRNA.
DR   AlphaFoldDB; B6D434; -.
DR   SMR; B6D434; -.
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; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR   InterPro; IPR001894; Cathelicidin-like.
DR   InterPro; IPR046350; Cystatin_sf.
DR   PANTHER; PTHR10206; PTHR10206; 1.
DR   SUPFAM; SSF54403; SSF54403; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Membrane; Secreted;
KW   Signal; Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..161
FT                   /evidence="ECO:0000269|PubMed:18795096"
FT                   /id="PRO_0000410956"
FT   PEPTIDE         162..191
FT                   /note="Cathelicidin-related antimicrobial peptide Bf-CRAMP"
FT                   /evidence="ECO:0000269|PubMed:18795096"
FT                   /id="PRO_0000410957"
FT   REGION          126..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..149
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;  21870 MW;  A8D667E4D6ACBE9A CRC64;
     MEGFFWKTLL VVGALAIAGT SSLPHKPLIY EEAVDLAVSI YNSKSGEDSL YRLLEAVSPP
     KWDPLSESNQ ELNFTMKETV CLVAEERSLE ECDFQEDGVV MGCTGYYFFG ESPPVVVLTC
     KPVGEEGEQK QEEGNEEEKE VEEEEQEEDE KDQPRRVKRF KKFFRKLKKS VKKRAKEFFK
     KPRVIGVSIP F