DRS1_PITHY
ID DRS1_PITHY Reviewed; 76 AA.
AC P84597; Q0VZ37;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 2.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Dermaseptin-H1 {ECO:0000303|PubMed:16713656};
DE Short=DRS-H1 {ECO:0000305};
DE AltName: Full=DShypo 02 {ECO:0000303|PubMed:16844081};
DE AltName: Full=Dermaseptin-H4 {ECO:0000303|PubMed:18644413};
DE Short=DRS-H4 {ECO:0000303|PubMed:18644413};
DE Flags: Precursor;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT GLN-73.
RC TISSUE=Skin;
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]
RP PROTEIN SEQUENCE OF 46-73, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MASS SPECTROMETRY.
RC TISSUE=Skin secretion;
RX PubMed=16844081; DOI=10.1016/j.bbrc.2006.06.168;
RA Brand G.D., Leite J.R.S.A., de Sa Mandel S.M., Mesquita D.A., Silva L.P.,
RA Prates M.V., Barbosa E.A., Vinecky F., Martins G.R., Galasso J.H.,
RA Kuckelhaus S.A.S., Sampaio R.N.R., Furtado J.R. Jr., Andrade A.C.,
RA Bloch C. Jr.;
RT "Novel dermaseptins from Phyllomedusa hypochondrialis (Amphibia).";
RL Biochem. Biophys. Res. Commun. 347:739-746(2006).
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).
CC -!- FUNCTION: Has antimicrobial activity. {ECO:0000250|UniProtKB:P83639}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16844081}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:16844081}.
CC -!- MASS SPECTROMETRY: Mass=2868.36; Mass_error=0.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16844081};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Dermaseptin subfamily. {ECO:0000255}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=0942";
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DR EMBL; AM229015; CAJ76139.1; -; mRNA.
DR AlphaFoldDB; P84597; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR InterPro; IPR022731; Dermaseptin.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR InterPro; IPR016322; FSAP.
DR Pfam; PF12121; DD_K; 1.
DR Pfam; PF03032; FSAP_sig_propep; 1.
DR PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; 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..45
FT /evidence="ECO:0000269|PubMed:16844081"
FT /id="PRO_0000449575"
FT PEPTIDE 46..73
FT /note="Dermaseptin-H1"
FT /evidence="ECO:0000269|PubMed:16844081"
FT /id="PRO_0000248494"
FT PROPEP 75..76
FT /evidence="ECO:0000305|PubMed:16713656"
FT /id="PRO_0000449576"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Glutamine amide"
FT /evidence="ECO:0000305|PubMed:16713656"
SQ SEQUENCE 76 AA; 8540 MW; 070358B158EB596B CRC64;
MDILKKSLFI VLFLGLVSLS ICEEEKRENE DEEEQEDDEQ SEEKRGLWKS LLKNVGVAAG
KAALNAVTDM VNQGEQ
