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PYLAA_XENLA
ID   PYLAA_XENLA             Reviewed;          64 AA.
AC   Q99134; B7ZSG6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=PYLa/PGLa A;
DE   Contains:
DE     RecName: Full=PYLa;
DE   Contains:
DE     RecName: Full=PGLa;
DE   Contains:
DE     RecName: Full=PGLa-H;
DE   Flags: Precursor;
GN   Name=pgla-a; Synonyms=pyla;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
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]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2465151; DOI=10.1111/j.1432-1033.1989.tb14552.x;
RA   Kuchler K., Kreil G., Sures I.;
RT   "The genes for the frog skin peptides GLa, xenopsin, levitide and caerulein
RT   contain a homologous export exon encoding a signal sequence and part of an
RT   amphiphilic peptide.";
RL   Eur. J. Biochem. 179:281-285(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 39-59, SUBCELLULAR LOCATION, AND AMIDATION AT LEU-59.
RC   TISSUE=Skin secretion;
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   [5]
RP   PROTEIN SEQUENCE OF 39-59, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND AMIDATION AT LEU-59.
RC   TISSUE=Stomach;
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   [6]
RP   PROTEIN SEQUENCE OF 50-59, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion;
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   -!- 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:0000305}.
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DR   EMBL; M12602; AAA49942.1; -; mRNA.
DR   EMBL; X01824; CAA25963.1; -; mRNA.
DR   EMBL; X13389; CAA31761.1; -; Genomic_DNA.
DR   EMBL; X13390; CAA31762.1; -; Genomic_DNA.
DR   EMBL; BC170516; AAI70516.1; -; mRNA.
DR   EMBL; BC170517; AAI70517.1; -; mRNA.
DR   PIR; A26815; A26815.
DR   RefSeq; NP_001081314.1; NM_001087845.1.
DR   RefSeq; NP_001095268.1; NM_001101798.1.
DR   AlphaFoldDB; Q99134; -.
DR   TCDB; 1.C.16.1.5; the magainin (magainin) family.
DR   GeneID; 397770; -.
DR   GeneID; 779059; -.
DR   KEGG; xla:397770; -.
DR   CTD; 397770; -.
DR   CTD; 779059; -.
DR   Xenbase; XB-GENE-6252595; pgla.L.
DR   Xenbase; XB-GENE-6253101; pgla.S.
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"
FT   PROPEP          21..35
FT                   /id="PRO_0000010702"
FT   PEPTIDE         36..59
FT                   /note="PYLa"
FT                   /id="PRO_0000010703"
FT   PEPTIDE         39..59
FT                   /note="PGLa"
FT                   /id="PRO_0000010704"
FT   PEPTIDE         50..59
FT                   /note="PGLa-H"
FT                   /id="PRO_0000415794"
FT   PROPEP          60..64
FT                   /id="PRO_0000010705"
FT   MOD_RES         59
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:1717472,
FT                   ECO:0000269|PubMed:3606567"
SQ   SEQUENCE   64 AA;  6809 MW;  630527391F1D7BFE CRC64;
     MYKQIFLCLI IAALCATIMA EASAFADADE DDDKRYVRGM ASKAGAIAGK IAKVALKALG
     RRDS
 
 
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