P2AJ2_AMOJI
ID P2AJ2_AMOJI Reviewed; 71 AA.
AC G3F828;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Palustrin-2AJ2 {ECO:0000303|PubMed:21816202};
DE Flags: Precursor;
OS Amolops jingdongensis (Chinese torrent frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Amolops.
OX NCBI_TaxID=1077530;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AEM77058.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-71, SUBCELLULAR
RP LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Skin {ECO:0000312|EMBL:AEM77058.1}, and
RC Skin secretion {ECO:0000269|PubMed:21816202};
RX PubMed=21816202; DOI=10.1016/j.biochi.2011.07.021;
RA Chen Z., Yang X., Liu Z., Zeng L., Lee W., Zhang Y.;
RT "Two novel families of antimicrobial peptides from skin secretions of the
RT Chinese torrent frog, Amolops jingdongensis.";
RL Biochimie 94:328-334(2012).
CC -!- FUNCTION: Displays broad-spectrum antibacterial activity against a
CC range of Gram-positive and Gram-negative bacteria. Has low hemolytic
CC activity, low cytotoxicity and low antioxidant activity (By
CC similarity). {ECO:0000250|UniProtKB:G3ETQ3}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21816202}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:21816202}.
CC -!- MASS SPECTROMETRY: Mass=3064.8; Method=FAB;
CC Evidence={ECO:0000269|PubMed:21816202};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000255}.
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DR EMBL; JF489155; AEM77058.1; -; mRNA.
DR AlphaFoldDB; G3F828; -.
DR SMR; G3F828; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; ISS:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; ISS:UniProtKB.
DR InterPro; IPR012521; Antimicrobial_frog_2.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF08023; Antimicrobial_2; 1.
DR Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antibiotic; Antimicrobial; Antioxidant;
KW Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Hemolysis; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..40
FT /evidence="ECO:0000255, ECO:0000303|PubMed:21816202"
FT /id="PRO_0000415408"
FT PEPTIDE 43..71
FT /note="Palustrin-2AJ2"
FT /evidence="ECO:0000269|PubMed:21816202"
FT /id="PRO_0000415409"
FT DISULFID 65..71
FT /evidence="ECO:0000250|UniProtKB:A7WNV6"
SQ SEQUENCE 71 AA; 7815 MW; FB593E883B862A83 CRC64;
MFTLKKPLLV LLFLGTVSLS LCEQERAADD DEGEVIEEEV KRGFMDTAKQ VAKNVAVTLI
DKLRCKVTGG C