CTCN1_ECHES
ID CTCN1_ECHES Reviewed; 119 AA.
AC A0A144LUY5;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Centrocin 1 {ECO:0000312|EMBL:AMT92374.1};
DE AltName: Full=EeCentrocin 1 {ECO:0000303|PubMed:27007817};
DE Contains:
DE RecName: Full=Centrocin 1, heavy chain {ECO:0000303|PubMed:27007817};
DE Contains:
DE RecName: Full=Centrocin 1, 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:AMT92374.1};
RN [1] {ECO:0000312|EMBL:AMT92374.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-80 AND 105-117,
RP FUNCTION, MASS SPECTROMETRY, BROMINATION AT TRP-52 AND TRP-53, AND
RP AMIDATION AT ASN-117.
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 1, 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 even at a concentration of 100
CC uM. {ECO:0000269|PubMed:27007817}.
CC -!- FUNCTION: [Centrocin 1, light chain]: Has no antimicrobial activity.
CC Shows no hemolytic activity. {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=4830.2; Method=Electrospray; Note=The measured
CC ranges are 51-80, 105-117.; Evidence={ECO:0000269|PubMed:27007817};
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DR EMBL; KR494262; AMT92374.1; -; mRNA.
DR AlphaFoldDB; A0A144LUY5; -.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Bromination;
KW Direct protein sequencing; Disulfide bond; Fungicide; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..50
FT /evidence="ECO:0000305|PubMed:27007817"
FT /id="PRO_0000438838"
FT PEPTIDE 51..80
FT /note="Centrocin 1, heavy chain"
FT /evidence="ECO:0000269|PubMed:27007817"
FT /id="PRO_0000438839"
FT PROPEP 81..104
FT /evidence="ECO:0000269|PubMed:27007817"
FT /id="PRO_0000438840"
FT PEPTIDE 105..117
FT /note="Centrocin 1, light chain"
FT /evidence="ECO:0000269|PubMed:27007817"
FT /id="PRO_0000438841"
FT MOD_RES 52
FT /note="6'-bromotryptophan"
FT /evidence="ECO:0000269|PubMed:27007817"
FT MOD_RES 53
FT /note="6'-bromotryptophan"
FT /evidence="ECO:0000269|PubMed:27007817"
FT MOD_RES 117
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:27007817"
FT DISULFID 75..110
FT /evidence="ECO:0000303|PubMed:27007817"
SQ SEQUENCE 119 AA; 13040 MW; 660D6A37CDD45D89 CRC64;
MMIKIAVVLC AVMATTMVRA KYVEEQELAD LLDLLISEEV SSPDDAVALQ GWWRRTVDKV
RNAGRKVAGF ASKACGALGH SPQEARAKVL EAFPEMKEAD LDEEDIGKYC GYAHALNGR
