PYLAB_XENLA
ID PYLAB_XENLA Reviewed; 64 AA.
AC Q91826;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=PYLa/PGLa B;
DE Contains:
DE RecName: Full=PYLa {ECO:0000303|PubMed:6688991};
DE Contains:
DE RecName: Full=PGLa {ECO:0000303|PubMed:1717472, ECO:0000303|PubMed:3606567};
DE Contains:
DE RecName: Full=PGLa-H {ECO:0000303|PubMed:22014884};
DE Flags: Precursor;
GN Name=pgla-b; Synonyms=pyla {ECO:0000312|EMBL:AAA49940.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAA49940.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Skin {ECO:0000269|PubMed:6688991};
RX PubMed=6688991; DOI=10.1002/j.1460-2075.1983.tb01489.x;
RA Hoffmann W., Richter K., Kreil G.;
RT "A novel peptide designated PYLa and its precursor as predicted from cloned
RT mRNA of Xenopus laevis skin.";
RL EMBO J. 2:711-714(1983).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 39-59, SUBCELLULAR LOCATION, AND AMIDATION AT LEU-59.
RC TISSUE=Skin secretion {ECO:0000269|PubMed:3606567};
RX PubMed=3606567; DOI=10.1042/bj2430113;
RA Giovannini M.G., Poulter L., Gibson B.W., Williams D.H.;
RT "Biosynthesis and degradation of peptides derived from Xenopus laevis
RT prohormones.";
RL Biochem. J. 243:113-120(1987).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 39-59, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND AMIDATION AT LEU-59.
RC TISSUE=Stomach {ECO:0000269|PubMed:1717472};
RX PubMed=1717472; DOI=10.1016/s0021-9258(18)55069-9;
RA Moore K.S., Bevins C.L., Brasseur M.M., Tomassini N., Turner K., Eck H.,
RA Zasloff M.;
RT "Antimicrobial peptides in the stomach of Xenopus laevis.";
RL J. Biol. Chem. 266:19851-19857(1991).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 50-59, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion {ECO:0000269|PubMed:22014884};
RX PubMed=22014884; DOI=10.1016/j.ijantimicag.2011.07.012;
RA Hou F., Li J., Pan P., Xu J., Liu L., Liu W., Song B., Li N., Wan J.,
RA Gao H.;
RT "Isolation and characterisation of a new antimicrobial peptide from the
RT skin of Xenopus laevis.";
RL Int. J. Antimicrob. Agents 38:510-515(2011).
CC -!- FUNCTION: PGLa and PGLa-H display a broad-spectrum of antibacterial
CC activity against a range of Gram-positive and Gram-negative bacteria.
CC PGLa also displays antifungal activity against C.albicans ATCC 14053.
CC PGLa-H shows moderate antibacterial activity against the multidrug-
CC resistant methicillin-resistant S. aureus (MRSA) but exhibits very
CC little hemolytic activity. {ECO:0000269|PubMed:1717472,
CC ECO:0000269|PubMed:22014884}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1717472,
CC ECO:0000269|PubMed:22014884, ECO:0000269|PubMed:3606567,
CC ECO:0000269|PubMed:6688991}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands. Synthesized in the
CC stomach and stored in a novel granular multinucleated cell in the
CC gastric mucosa. Stored as active, processed peptides in large granules
CC within the granular gland secretions of the skin.
CC {ECO:0000269|PubMed:1717472, ECO:0000269|PubMed:22014884}.
CC -!- MASS SPECTROMETRY: [PGLa-H]: Mass=1053.727; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22014884};
CC -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family. Magainin
CC subfamily. {ECO:0000255}.
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DR EMBL; M12498; AAA49940.1; -; mRNA.
DR PIR; B26815; B26815.
DR RefSeq; NP_001081314.1; NM_001087845.1.
DR AlphaFoldDB; Q91826; -.
DR GeneID; 397770; -.
DR KEGG; xla:397770; -.
DR CTD; 397770; -.
DR Xenbase; XB-GENE-6252595; pgla.L.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 397770; Expressed in zone of skin and 13 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW Fungicide; Hemolysis; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255, ECO:0000312|EMBL:AAA49940.1"
FT PROPEP 21..35
FT /evidence="ECO:0000269|PubMed:6688991"
FT /id="PRO_0000415795"
FT PEPTIDE 36..59
FT /note="PYLa"
FT /evidence="ECO:0000269|PubMed:6688991"
FT /id="PRO_0000415796"
FT PEPTIDE 39..59
FT /note="PGLa"
FT /evidence="ECO:0000269|PubMed:1717472,
FT ECO:0000269|PubMed:3606567"
FT /id="PRO_0000415797"
FT PEPTIDE 50..59
FT /note="PGLa-H"
FT /evidence="ECO:0000269|PubMed:22014884"
FT /id="PRO_0000415798"
FT PROPEP 60..64
FT /evidence="ECO:0000269|PubMed:6688991"
FT /id="PRO_0000415799"
FT MOD_RES 59
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:1717472,
FT ECO:0000269|PubMed:3606567"
SQ SEQUENCE 64 AA; 6761 MW; 6BA7A49205AD7BF0 CRC64;
MYKQIFLCLI IAALCATIMA EASALADADD DDDKRYVRGM ASKAGAIAGK IAKVALKALG
RRDS
