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 NOTE=Ref.1. CC -!- SIMILARITY: Belongs to the beta-defensin family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- KW Antibiotic; Direct protein sequencing; Fungicide. 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 //