ID   SHE1_APTPA     STANDARD;      PRT;    38 AA.
AC   P83429;
DT   10-OCT-2003 (Rel. 42, Created)
DT   10-OCT-2003 (Rel. 42, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Spheniscin 1 (Sphe-1) (pBD-1).
OS   Aptenodytes patagonicus (King penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9234;
RN   [1]
RP   SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Stomach;
RX   PubMed=14525994; DOI=10.1074/jbc.M306839200;
RA   Thouzeau C., Le Maho Y., Froget G., Sabatier L., Le Bohec C.,
RA   Hoffmann J.A., Bulet P.;
RT   "Spheniscins, avian beta-defensins in preserved stomach contents of
RT   the king penguin, Aptenodytes patagonicus.";
RL   J. Biol. Chem. 278:51053-51058(2003).
CC   -!- FUNCTION: Has antifungal activity and antibacterial activity
CC       against Gram-positive and Gram-negative bacteria. Involved in the
CC       process of food preservation in the stomach during the incubation
CC       fast. May also be present during infection.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Secreted into the stomach cavity.
CC   -!- MASS SPECTROMETRY: MW=4482.8; METHOD=MALDI; RANGE=1-38.
CC   -!- SIMILARITY: Belongs to the beta-defensin family.
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KW   Antibiotic; Fungicide; Direct protein sequencing.
FT   DISULFID      5     33       By similarity.
FT   DISULFID     12     27
FT   DISULFID     17     34       By similarity.
SQ   SEQUENCE   38 AA;  4488 MW;  EF822688C6187203 CRC64;
     SFGLCRLRRG FCAHGRCRFP SIPIGRCSRF VQCCRRVW
//