PLS2_PITHY
ID PLS2_PITHY Reviewed; 66 AA.
AC P84567; Q0VZ43;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Phylloseptin-H2 {ECO:0000303|PubMed:18644413};
DE Short=PLS-H2 {ECO:0000303|PubMed:18644413};
DE AltName: Full=Phylloseptin-2 {ECO:0000303|PubMed:15752569, ECO:0000303|PubMed:16713656};
DE Short=PS-2 {ECO:0000303|PubMed:15752569, ECO:0000303|PubMed:16713656};
DE Flags: Precursor;
GN Name=psn2; Synonyms=psn-2;
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:CAJ76133.1}
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:0000269|PubMed:16713656}, 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, MASS SPECTROMETRY, AND AMIDATION AT PHE-65.
RC TISSUE=Skin secretion {ECO:0000269|PubMed:15752569};
RX PubMed=15752569; DOI=10.1016/j.peptides.2004.11.002;
RA Leite J.R.S.A., Silva L.P., Rodrigues M.I.S., Prates M.V., Brand G.D.,
RA Lacava B.M., Azevedo R.B., Bocca A.L., Albuquerque S., Bloch C. Jr.;
RT "Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides
RT from the Phyllomedusa genus.";
RL Peptides 26:565-573(2005).
RN [3]
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).
RN [4]
RP STRUCTURE BY NMR OF 47-65, AND AMIDATION AT PHE-65.
RX PubMed=18656510; DOI=10.1016/j.peptides.2008.06.022;
RA Resende J.M., Moraes C.M., Prates M.V., Cesar A., Almeida F.C.,
RA Mundim N.C., Valente A.P., Bemquerer M.P., Pilo-Veloso D., Bechinger B.;
RT "Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2,
RT and -3 and biological activity: the role of charges and hydrogen bonding
RT interactions in stabilizing helix conformations.";
RL Peptides 29:1633-1644(2008).
CC -!- FUNCTION: Has antimicrobial activity. No hemolytic activity.
CC {ECO:0000250|UniProtKB:P84566, ECO:0000269|PubMed:15752569}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15752569,
CC ECO:0000269|PubMed:16713656}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:15752569, ECO:0000269|PubMed:16713656}.
CC -!- MASS SPECTROMETRY: Mass=2115.26; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15752569, ECO:0000269|PubMed:16713656};
CC -!- MASS SPECTROMETRY: Mass=2116.55; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15752569, ECO:0000269|PubMed:16713656};
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=00757";
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DR EMBL; AM229009; CAJ76133.1; -; mRNA.
DR PDB; 2JPY; NMR; -; A=47-65.
DR PDBsum; 2JPY; -.
DR AlphaFoldDB; P84567; -.
DR SMR; P84567; -.
DR EvolutionaryTrace; P84567; -.
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 3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW Antimicrobial; Cleavage on pair of basic residues;
KW Direct protein sequencing; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..44
FT /evidence="ECO:0000269|PubMed:15752569,
FT ECO:0000269|PubMed:16713656"
FT /id="PRO_0000343889"
FT PEPTIDE 47..65
FT /note="Phylloseptin-H2"
FT /evidence="ECO:0000269|PubMed:15752569,
FT ECO:0000269|PubMed:16713656"
FT /id="PRO_0000043823"
FT MOD_RES 65
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:15752569,
FT ECO:0000269|PubMed:16713656, ECO:0000269|PubMed:18656510"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:2JPY"
SQ SEQUENCE 66 AA; 7655 MW; 18FE8178EC5B2ED4 CRC64;
MAFLKKSLFL VLFLGLATLS ICEEEKRETE EEEYNQEEDD KSEEKRFLSL IPHAINAVST
LVHHFG
