STYD_STYCL
ID STYD_STYCL Reviewed; 81 AA.
AC O18495;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Styelin-D;
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).
RN [2]
RP PROTEIN SEQUENCE OF 55-81, BROMINATION AT TRP-24, HYDROXYLATION AT ARG-26;
RP LYS-27; LYS-30; LYS-34; TYR-36; TYR-37; LYS-38; LYS-40; TYR-41; TYR-42 AND
RP LYS-44, AMIDATION AT LEU-54, AND ANTIBACTERIAL ACTIVITY.
RC TISSUE=Hemocyte;
RX PubMed=10978343; DOI=10.1074/jbc.m006762200;
RA Taylor S.W., Craig A.G., Fischer W.H., Park M., Lehrer R.I.;
RT "Styelin D, an extensively modified antimicrobial peptide from ascidian
RT hemocytes.";
RL J. Biol. Chem. 275:38417-38426(2000).
CC -!- FUNCTION: Bactericidal against several Gram-positive and Gram-negative
CC bacteria. Plays a significant role in the innate immune mechanisms of
CC S.clava.
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; Y13269; CAA73718.1; -; mRNA.
DR AlphaFoldDB; O18495; -.
DR TCDB; 1.C.17.2.1; the cecropin (cecropin) family.
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 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Bromination;
KW Direct protein sequencing; Hydroxylation; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PEPTIDE 23..54
FT /note="Styelin-D"
FT /evidence="ECO:0000269|PubMed:10978343"
FT /id="PRO_0000022436"
FT PROPEP 56..81
FT /note="Removed in mature form"
FT /id="PRO_0000022437"
FT MOD_RES 24
FT /note="6'-bromotryptophan"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 26
FT /note="3,4-dihydroxyarginine"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 27
FT /note="4,5-dihydroxylysine"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 30
FT /note="4,5-dihydroxylysine"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 34
FT /note="4,5-dihydroxylysine"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 36
FT /note="3',4'-dihydroxyphenylalanine"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 37
FT /note="3',4'-dihydroxyphenylalanine"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 38
FT /note="4,5-dihydroxylysine"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 40
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 41
FT /note="3',4'-dihydroxyphenylalanine"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 42
FT /note="3',4'-dihydroxyphenylalanine"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 44
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:10978343"
FT MOD_RES 54
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:10978343"
SQ SEQUENCE 81 AA; 9560 MW; E2F71DD39287D443 CRC64;
MQMKATILIV LVALFMIQQS EAGWLRKAAK SVGKFYYKHK YYIKAAWQIG KHALGDMTDE
EFQDFMKEVE QAREEELQSR Q