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NDB48_SCOTI
ID   NDB48_SCOTI             Reviewed;          74 AA.
AC   P0DJO3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Amphipathic peptide CT1 {ECO:0000303|PubMed:19854232};
DE            Short=StCT1 {ECO:0000303|PubMed:19854232};
DE   AltName: Full=Non-disulfide-bridged peptide 4.8 {ECO:0000303|PubMed:24184590};
DE            Short=NDBP-4.8 {ECO:0000303|PubMed:24184590};
DE   AltName: Full=Non-disulfide-bridged peptide 5.16 {ECO:0000303|PubMed:23624072};
DE            Short=NDBP-5.16 {ECO:0000303|PubMed:23624072};
DE   Flags: Precursor;
OS   Scorpiops tibetanus (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Chactoidea; Euscorpiidae; Scorpiopinae; Scorpiopini;
OC   Scorpiops.
OX   NCBI_TaxID=500600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT VAL-37, AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=19854232; DOI=10.1016/j.peptides.2009.10.008;
RA   Yuan W., Cao L., Ma Y., Mao P., Wang W., Zhao R., Wu Y., Cao Z., Li W.;
RT   "Cloning and functional characterization of a new antimicrobial peptide
RT   gene StCT1 from the venom of the scorpion Scorpiops tibetanus.";
RL   Peptides 31:22-26(2010).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=23624072; DOI=10.1016/j.peptides.2013.03.026;
RA   Zeng X.C., Zhou L., Shi W., Luo X., Zhang L., Nie Y., Wang J., Wu S.,
RA   Cao B., Cao H.;
RT   "Three new antimicrobial peptides from the scorpion Pandinus imperator.";
RL   Peptides 45:28-34(2013).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=24184590; DOI=10.1016/j.peptides.2013.10.021;
RA   Almaaytah A., Albalas Q.;
RT   "Scorpion venom peptides with no disulfide bridges: a review.";
RL   Peptides 51:35-45(2014).
CC   -!- FUNCTION: Antimicrobial peptide that is rapidly bactericidal against
CC       Gram-positive bacteria (MIC=12.5 ug/ml against S.aureus, and MIC=100
CC       ug/ml against M.luteus). Is also active against clinical antibiotics-
CC       resistant bacterial strains. {ECO:0000269|PubMed:19854232}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Target cell membrane
CC       {ECO:0000250}. Note=Forms a helical membrane channel in the prey.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Is highly capable of inhibiting antibiotic-resistant
CC       pathogen growth, including methicillin-resistant S.aureus. In vivo,
CC       shows high antimicrobial activity on a S.aureus-infected mouse model
CC       (PubMed:19854232). {ECO:0000305|PubMed:19854232}.
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   EMBL; FD664386; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DJO3; -.
DR   SMR; P0DJO3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Cytolysis; Hemolysis; Membrane; Secreted; Signal; Target cell membrane;
KW   Target membrane; Transmembrane.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         24..37
FT                   /note="Amphipathic peptide CT1"
FT                   /id="PRO_0000418785"
FT   PROPEP          41..74
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000418786"
FT   MOD_RES         37
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:19854232"
SQ   SEQUENCE   74 AA;  8561 MW;  B340C3D1E89DB002 CRC64;
     MKTQIVILFI SMIMLQMFVQ IEGGFWGSLW EGVKSVVGKR GLRNLDDLDD LDLDHLFDSD
     VSDADLRLLK QMFR
 
 
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