PLS5_PITHY
ID PLS5_PITHY Reviewed; 66 AA.
AC P84572; Q0VZ42;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Phylloseptin-H5 {ECO:0000303|PubMed:18644413};
DE Short=PLS-H5 {ECO:0000303|PubMed:18644413};
DE AltName: Full=Phylloseptin-7 {ECO:0000303|PubMed:16713656, ECO:0000303|PubMed:16963159, ECO:0000303|Ref.3};
DE Short=PS-7 {ECO:0000303|PubMed:16713656, ECO:0000303|PubMed:16963159, ECO:0000303|Ref.3};
DE Flags: Precursor;
GN Name=psn7; Synonyms=psn-7;
OS Pithecopus hypochondrialis (Orange-legged leaf frog) (Phyllomedusa
OS hypochondrialis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Pithecopus.
OX NCBI_TaxID=317381;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAJ76134.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-65, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND AMIDATION AT PHE-65.
RC TISSUE=Skin {ECO:0000312|EMBL:CAJ76134.1}, and
RC Skin secretion {ECO:0000269|PubMed:16713656};
RX PubMed=16713656; DOI=10.1016/j.peptides.2006.04.006;
RA Chen T., Zhou M., Gagliardo R., Walker B., Shaw C.;
RT "Elements of the granular gland peptidome and transcriptome persist in air-
RT dried skin of the South American orange-legged leaf frog, Phyllomedusa
RT hypocondrialis.";
RL Peptides 27:2129-2136(2006).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 47-65, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND AMIDATION AT PHE-65.
RC TISSUE=Skin secretion {ECO:0000269|PubMed:16963159};
RX PubMed=16963159; DOI=10.1016/j.peptides.2006.08.005;
RA Conceicao K., Konno K., Richardson M., Antoniazzi M.M., Jared C.,
RA Daffre S., de Camargo A.C.M., Pimenta D.C.;
RT "Isolation and biochemical characterization of peptides presenting
RT antimicrobial activity from the skin of Phyllomedusa hypochondrialis.";
RL Peptides 27:3092-3099(2006).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 47-65, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, AND AMIDATION AT PHE-65.
RC TISSUE=Skin secretion {ECO:0000269|Ref.3};
RA Silva L.P., Brand G.D., Bloch C. Jr.;
RT "High-throughput imaging co-localization of peptides and proteins.";
RL Submitted (AUG-2006) to UniProtKB.
RN [4]
RP NOMENCLATURE.
RX PubMed=18644413; DOI=10.1016/j.peptides.2008.06.017;
RA Amiche M., Ladram A., Nicolas P.;
RT "A consistent nomenclature of antimicrobial peptides isolated from frogs of
RT the subfamily Phyllomedusinae.";
RL Peptides 29:2074-2082(2008).
CC -!- FUNCTION: Has antibacterial activity against the Gram-negative bacteria
CC E.coli and P.aeruginosa, and the Gram-positive bacterium S.aureus. No
CC hemolytic activity. {ECO:0000269|PubMed:16963159}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16713656,
CC ECO:0000269|PubMed:16963159, ECO:0000269|Ref.3}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:16713656, ECO:0000269|PubMed:16963159,
CC ECO:0000269|Ref.3}.
CC -!- MASS SPECTROMETRY: Mass=2047.25; Mass_error=0.01; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16713656, ECO:0000269|Ref.3};
CC -!- MASS SPECTROMETRY: Mass=2049.46; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16713656, ECO:0000269|Ref.3};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Phylloseptin subfamily. {ECO:0000255}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=00762";
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DR EMBL; AM229010; CAJ76134.1; -; mRNA.
DR AlphaFoldDB; P84572; -.
DR TCDB; 1.C.52.1.12; the dermaseptin (dermaseptin) 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; IPR004275; Frog_antimicrobial_propeptide.
DR InterPro; IPR016322; FSAP.
DR Pfam; PF03032; FSAP_sig_propep; 1.
DR PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Direct protein sequencing; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..44
FT /evidence="ECO:0000269|PubMed:16713656,
FT ECO:0000269|PubMed:16963159, ECO:0000269|Ref.3"
FT /id="PRO_0000291607"
FT PEPTIDE 47..65
FT /note="Phylloseptin-H5"
FT /evidence="ECO:0000269|PubMed:16713656,
FT ECO:0000269|PubMed:16963159, ECO:0000269|Ref.3"
FT /id="PRO_0000250600"
FT REGION 24..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16713656,
FT ECO:0000269|PubMed:16963159, ECO:0000269|Ref.3"
SQ SEQUENCE 66 AA; 7554 MW; F6AD02D9B00C53AF CRC64;
MAFLKKSLFL VLFLGLVSLS ICEEEKRETE EEENEQEDDD KSEEKRFLSL IPHAINAVSA
IAKHFG
