ID SPHE1_APTPA Reviewed; 38 AA. AC P83429; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2003, sequence version 1. DT 05-OCT-2016, entry version 46. DE RecName: Full=Spheniscin-1; DE Short=Sphe-1; DE AltName: Full=pBD-1; OS Aptenodytes patagonicus (King penguin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; OC Aptenodytes. OX NCBI_TaxID=9234; RN [1] RP PROTEIN 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 {ECO:0000269|PubMed:14525994}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14525994}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14525994}. CC -!- TISSUE SPECIFICITY: Secreted into the stomach cavity. CC -!- MASS SPECTROMETRY: Mass=4482.8; Method=MALDI; Range=1-38; CC Evidence={ECO:0000269|PubMed:14525994}; CC -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}. 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 --------------------------------------------------------------------------- DR ProteinModelPortal; P83429; -. DR HOVERGEN; HBG093983; -. 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:0031640; P:killing of cells of other organism; IEA:UniProtKB-KW. DR InterPro; IPR001855; Defensin_beta-typ. DR Pfam; PF00711; Defensin_beta; 1. PE 1: Evidence at protein level; KW Antibiotic; Antimicrobial; Defensin; Direct protein sequencing; KW Disulfide bond; Fungicide; Secreted. FT PEPTIDE 1 38 Spheniscin-1. FT /FTId=PRO_0000044728. FT DISULFID 5 33 {ECO:0000250}. FT DISULFID 12 27 FT DISULFID 17 34 {ECO:0000250}. SQ SEQUENCE 38 AA; 4488 MW; EF822688C6187203 CRC64; SFGLCRLRRG FCAHGRCRFP SIPIGRCSRF VQCCRRVW //