NDB4T_CHATC
ID NDB4T_CHATC Reviewed; 75 AA.
AC P0DME3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Peptide Ctri10036 {ECO:0000303|PubMed:22791717, ECO:0000303|PubMed:23415044};
DE Flags: Precursor;
OS Chaerilus tricostatus (Scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Chaerilida; Chaeriloidea; Chaerilidae; Chaerilus.
OX NCBI_TaxID=1055734;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SYNTHESIS OF 23-41.
RC TISSUE=Venom gland;
RX PubMed=23415044; DOI=10.1016/j.biomaterials.2013.01.075;
RA Hong W., Zhang R., Di Z., He Y., Zhao Z., Hu J., Wu Y., Li W., Cao Z.;
RT "Design of histidine-rich peptides with enhanced bioavailability and
RT inhibitory activity against hepatitis C virus.";
RL Biomaterials 34:3511-3522(2013).
RN [2]
RP SYNTHESIS OF 24-41.
RX PubMed=22791717; DOI=10.1074/jbc.m112.370312;
RA Zhao Z., Hong W., Zeng Z., Wu Y., Hu K., Tian X., Li W., Cao Z.;
RT "Mucroporin-M1 inhibits hepatitis B virus replication by activating the
RT mitogen-activated protein kinase (MAPK) pathway and down-regulating
RT HNF4alpha in vitro and in vivo.";
RL J. Biol. Chem. 287:30181-30190(2012).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- MISCELLANEOUS: Shows a low ability to inhibit hepatitis C virus (HCV)
CC infection in Huh7.5.1 cells (PubMed:23415044), and no ability to
CC inhibit hepatitis B virus in HepG2.2.15 cells (PubMed:22791717).
CC {ECO:0000305|PubMed:22791717, ECO:0000305|PubMed:23415044}.
CC -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC superfamily. Short antimicrobial peptide (group 4) family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P0DME3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Amidation; Antimicrobial; Antiviral protein; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PEPTIDE 23..41
FT /note="Peptide Ctri10036"
FT /id="PRO_0000428679"
FT PROPEP 47..75
FT /evidence="ECO:0000250"
FT /id="PRO_0000428680"
FT MOD_RES 41
FT /note="Lysine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 75 AA; 8894 MW; 1EF169E8FAD5314C CRC64;
MNSKYLFVFL ILNVIFIDLC QGFLWSLIPS AISAVTSLIK KGRRRRELGS QYDYLQDFRK
RELDLDDLLS KFPDY