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BR1SC_LITSH
ID   BR1SC_LITSH             Reviewed;          24 AA.
AC   P82906;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Brevinin-1Sc;
OS   Lithobates sphenocephalus (Southern leopard frog) (Rana sphenocephala).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=146672;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion;
RX   PubMed=10604597; DOI=10.1034/j.1399-3011.1999.00123.x;
RA   Conlon J.M., Halverson T., Dulka J., Platz J.E., Knoop F.C.;
RT   "Peptides with antimicrobial activity of the brevinin-1 family isolated
RT   from skin secretions of the southern leopard frog, Rana sphenocephala.";
RL   J. Pept. Res. 54:522-527(1999).
CC   -!- FUNCTION: Antibacterial activity against Gram-negative bacterium
CC       E.coli. {ECO:0000269|PubMed:10604597}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- MASS SPECTROMETRY: Mass=2612; Mass_error=0.02; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10604597};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P82906; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR012520; Antimicrobial_frog_1.
DR   Pfam; PF08018; Antimicrobial_1; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Disulfide bond; Secreted.
FT   PEPTIDE         1..24
FT                   /note="Brevinin-1Sc"
FT                   /id="PRO_0000043548"
FT   DISULFID        18..24
SQ   SEQUENCE   24 AA;  2614 MW;  435347E4371C4515 CRC64;
     FFPIVAGVAG QVLKKIYCTI SKKC
 
 
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