Reviewed, UniProtKB/Swiss-Prot O18495 (STYD_STYCL)

Names and origin

Protein names	Recommended name:     Styelin-D
Organism	Styela clava (Sea squirt)
Taxonomic identifier	7725 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Urochordata › Ascidiacea › Stolidobranchia › Styelidae › Styela

Protein attributes

Sequence length	81 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Bactericidal against several Gram-positive and Gram-negative bacteria. Plays a significant role in the innate immune mechanisms of S.clava.
Subcellular location	Secreted.
Tissue specificity	Hemocytes and pharyngeal tissues.
Post-translational modification	Contains L-DOPA (3',4'-dihydroxyphenylalanine).

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Antibiotic Antimicrobial
PTM	Amidation Bromination Hydroxylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Peptide	23 – 54	32	Styelin-D		PRO_0000022436
	Propeptide	56 – 81	26	Removed in mature form		PRO_0000022437
Amino acid modifications
	Modified residue	24	1	6'-bromotryptophan
	Modified residue	26	1	3,4-dihydroxyarginine
	Modified residue	27	1	4,5-dihydroxylysine
	Modified residue	30	1	4,5-dihydroxylysine
	Modified residue	34	1	4,5-dihydroxylysine
	Modified residue	36	1	3',4'-dihydroxyphenylalanine
	Modified residue	37	1	3',4'-dihydroxyphenylalanine
	Modified residue	38	1	4,5-dihydroxylysine
	Modified residue	40	1	5-hydroxylysine
	Modified residue	41	1	3',4'-dihydroxyphenylalanine
	Modified residue	42	1	3',4'-dihydroxyphenylalanine
	Modified residue	44	1	5-hydroxylysine
	Modified residue	54	1	Leucine amide

Sequences

	Sequence		Length	Mass (Da)
	O18495-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: E2F71DD39287D443	FASTA	81	9,560
	10 20 30 40 50 60 MQMKATILIV LVALFMIQQS EAGWLRKAAK SVGKFYYKHK YYIKAAWQIG KHALGDMTDE 70 80 EFQDFMKEVE QAREEELQSR Q

References

[1]	"cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate, Styela clava." Zhao C., Liaw L., Lee I.H., Lehrer R.I. FEBS Lett. 412:144-148(1997) [PubMed: 9257708] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pharynx.
[2]	"Styelin D, an extensively modified antimicrobial peptide from ascidian hemocytes." Taylor S.W., Craig A.G., Fischer W.H., Park M., Lehrer R.I. J. Biol. Chem. 275:38417-38426(2000) [PubMed: 10978343] [Abstract] Cited for: PROTEIN SEQUENCE OF 55-81, POST-TRANSLATIONAL MODIFICATIONS, ANTIBACTERIAL ACTIVITY. Tissue: Hemocyte.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y13269 mRNA. Translation: CAA73718.1.
3D structure databases
ModBase	Search...
Protein family/group databases
TCDB	1.C.17.2.1. cecropin family.
Phylogenomic databases
HOVERGEN	O18495.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

STYD_STYCL

Accession

Primary (citable) accession number: O18495

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)