CTCN2_ECHES
ID CTCN2_ECHES Reviewed; 121 AA.
AC A0A144LVL3;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Centrocin 2 {ECO:0000312|EMBL:AMT92375.1};
DE AltName: Full=EeCentrocin 2 {ECO:0000303|PubMed:27007817};
DE Contains:
DE RecName: Full=Centrocin 2, heavy chain {ECO:0000303|PubMed:27007817};
DE Contains:
DE RecName: Full=Centrocin 2, light chain {ECO:0000303|PubMed:27007817};
DE Flags: Precursor;
OS Echinus esculentus (Sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinidae; Echinus.
OX NCBI_TaxID=7648 {ECO:0000312|EMBL:AMT92375.1};
RN [1] {ECO:0000312|EMBL:AMT92375.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-82 AND 105-117,
RP FUNCTION, MASS SPECTROMETRY, BROMINATION AT TRP-51 AND TRP-59, AMIDATION AT
RP HIS-119, AND PYROGLUTAMATE FORMATION AT GLN-107.
RC TISSUE=Coelomocyte {ECO:0000303|PubMed:27007817};
RX PubMed=27007817; DOI=10.1371/journal.pone.0151820;
RA Solstad R.G., Li C., Isaksson J., Johansen J., Svenson J., Stensvag K.,
RA Haug T.;
RT "Novel Antimicrobial Peptides EeCentrocins 1, 2 and EeStrongylocin 2 from
RT the Edible Sea Urchin Echinus esculentus Have 6-Br-Trp Post-Translational
RT Modifications.";
RL PLoS ONE 11:E0151820-E0151820(2016).
CC -!- FUNCTION: [Centrocin 2, heavy chain]: Has antimicrobial activity
CC against Gram-negative bacteria, Gram-positive bacteria and against
CC fungi with minimum inhibitory concentration (MIC) between 0.78 uM and
CC 50 uM. Shows little hemolytic activity at concentrations up to 12.5 uM
CC but >50% lysis at 100 uM. {ECO:0000269|PubMed:27007817}.
CC -!- SUBUNIT: Heterodimer of a light and a heavy chain, probably disulfide-
CC linked. {ECO:0000269|PubMed:27007817}.
CC -!- MASS SPECTROMETRY: Mass=5019.37; Method=Electrospray; Note=The measured
CC ranges are 51-82, 107-119.; Evidence={ECO:0000269|PubMed:27007817};
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DR EMBL; KR494263; AMT92375.1; -; mRNA.
DR AlphaFoldDB; A0A144LVL3; -.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Bromination; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Fungicide; Hemolysis;
KW Pyrrolidone carboxylic acid; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..50
FT /evidence="ECO:0000305|PubMed:27007817"
FT /id="PRO_0000438842"
FT PEPTIDE 51..82
FT /note="Centrocin 2, heavy chain"
FT /evidence="ECO:0000269|PubMed:27007817"
FT /id="PRO_0000438843"
FT PROPEP 83..106
FT /evidence="ECO:0000305|PubMed:27007817"
FT /id="PRO_0000438844"
FT PEPTIDE 107..119
FT /note="Centrocin 2, light chain"
FT /evidence="ECO:0000269|PubMed:27007817"
FT /id="PRO_0000438845"
FT MOD_RES 51
FT /note="6'-bromotryptophan"
FT /evidence="ECO:0000269|PubMed:27007817"
FT MOD_RES 59
FT /note="6'-bromotryptophan"
FT /evidence="ECO:0000269|PubMed:27007817"
FT MOD_RES 107
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:27007817"
FT MOD_RES 119
FT /note="Histidine amide"
FT /evidence="ECO:0000269|PubMed:27007817"
FT DISULFID 77..112
FT /evidence="ECO:0000303|PubMed:27007817"
SQ SEQUENCE 121 AA; 13151 MW; E386FC153EFE6838 CRC64;
MMIKIAVVLC AVMATSMVFA NDVKEQELAD LLDLLISEEV SSPDDAVAES WGHKLRSSWN
KVKHAVKKGA GYASGACRVL GHSPQEARAK VLEAFPEMKE SDLDEEQVGK YCAVAHAIHG
R