ID   STYE_STYCL              Reviewed;          81 AA.
AC   O18496;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Styelin-E;
DE   Flags: Precursor;
OS   Styela clava (Sea squirt).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC   Styelidae; Styela.
OX   NCBI_TaxID=7725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pharynx;
RX   PubMed=9257708; DOI=10.1016/s0014-5793(97)00769-2;
RA   Zhao C., Liaw L., Lee I.H., Lehrer R.I.;
RT   "cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from
RT   the tunicate, Styela clava.";
RL   FEBS Lett. 412:144-148(1997).
CC   -!- FUNCTION: Bactericidal against several Gram-positive and Gram-negative
CC       bacteria. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Hemocytes and pharyngeal tissues.
CC   -!- PTM: Contains L-DOPA (3',4'-dihydroxyphenylalanine).
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DR   EMBL; Y13270; CAA73719.1; -; mRNA.
DR   AlphaFoldDB; O18496; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR035578; Styelin.
DR   Pfam; PF17562; Styelin; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Antibiotic; Antimicrobial; Bromination; Hydroxylation; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..54
FT                   /note="Styelin-E"
FT                   /id="PRO_0000022438"
FT   PROPEP          56..81
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000022439"
FT   MOD_RES         24
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         26
FT                   /note="3,4-dihydroxyarginine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         27
FT                   /note="4,5-dihydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         30
FT                   /note="4,5-dihydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         34
FT                   /note="4,5-dihydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         36
FT                   /note="3',4'-dihydroxyphenylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="3',4'-dihydroxyphenylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         38
FT                   /note="4,5-dihydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         40
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         41
FT                   /note="3',4'-dihydroxyphenylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         42
FT                   /note="3',4'-dihydroxyphenylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         44
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         54
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   81 AA;  9588 MW;  36D3A2987287CCD2 CRC64;
     MQMKATILIV LVALFMIQQS EAGWLRKAAK SVGKFYYKHK YYIKAAWKIG RHALGDMTDE
     EFQDFMKEVE QAREEELQSR Q