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AUR12_RANRN
ID   AUR12_RANRN             Reviewed;          13 AA.
AC   P82387;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-JUN-2021, entry version 53.
DE   RecName: Full=Aurein-1.2;
OS   Ranoidea raniformis (Southern bell frog) (Litoria raniformis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=116057;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT PHE-13, FUNCTION, AND STRUCTURE BY NMR.
RC   TISSUE=Skin secretion;
RX   PubMed=10951191; DOI=10.1046/j.1432-1327.2000.01536.x;
RA   Rozek T., Wegener K.L., Bowie J.H., Olver I.N., Carver J.A., Wallace J.C.,
RA   Tyler M.J.;
RT   "The antibiotic and anticancer active aurein peptides from the australian
RT   bell frogs Litoria aurea and Litoria raniformis the solution structure of
RT   aurein 1.2.";
RL   Eur. J. Biochem. 267:5330-5341(2000).
CC   -!- FUNCTION: Antimicrobial activity against B.cereus, L.lactis, L.innocua,
CC       M.luteus, P.multocida, S.aureus, S.epidermidis and S.uberis. Probably
CC       acts by disturbing membrane functions with its amphipathic structure.
CC       Shows anticancer activity. {ECO:0000269|PubMed:10951191}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Aurein subfamily. {ECO:0000305}.
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DR   PDB; 1VM5; NMR; -; A=1-13.
DR   PDBsum; 1VM5; -.
DR   PCDDB; P82387; -.
DR   SMR; P82387; -.
DR   TCDB; 1.C.76.1.3; the pore-forming maculatin peptide (maculatin) family.
DR   EvolutionaryTrace; P82387; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR013157; Aurein_antimicrobial_peptide.
DR   Pfam; PF08256; Antimicrobial20; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW   Antimicrobial; Direct protein sequencing; Secreted.
FT   PEPTIDE         1..13
FT                   /note="Aurein-1.2"
FT                   /id="PRO_0000043719"
FT   MOD_RES         13
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:10951191"
FT   HELIX           3..12
FT                   /evidence="ECO:0007829|PDB:1VM5"
SQ   SEQUENCE   13 AA;  1481 MW;  1EACB99DFBC83330 CRC64;
     GLFDIIKKIA ESF
 
 
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