ID   SPHE2_APTPA             Reviewed;          38 AA.
AC   P83430;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Spheniscin-2;
DE            Short=Sphe-2;
DE   AltName: Full=pBD-2;
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, MASS
RP   SPECTROMETRY, AND SYNTHESIS.
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 the
RT   king penguin, Aptenodytes patagonicus.";
RL   J. Biol. Chem. 278:51053-51058(2003).
RN   [2]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=15123713; DOI=10.1074/jbc.m401338200;
RA   Landon C., Thouzeau C., Labbe H., Bulet P., Vovelle F.;
RT   "Solution structure of spheniscin, a beta-defensin from the penguin
RT   stomach.";
RL   J. Biol. Chem. 279:30433-30439(2004).
CC   -!- FUNCTION: Has antifungal activity and antibacterial activity against
CC       Gram-positive and Gram-negative bacteria. Involved in the process of
CC       food preservation in the stomach during the incubation fast. May also
CC       be present during infection. {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=4501.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:14525994};
CC   -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR   PDB; 1UT3; NMR; -; A=1-38.
DR   PDBsum; 1UT3; -.
DR   AlphaFoldDB; P83430; -.
DR   SMR; P83430; -.
DR   EvolutionaryTrace; P83430; -.
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 another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR001855; Defensin_beta-typ.
DR   Pfam; PF00711; Defensin_beta; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Defensin;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Secreted.
FT   PEPTIDE         1..38
FT                   /note="Spheniscin-2"
FT                   /id="PRO_0000044729"
FT   DISULFID        5..33
FT                   /evidence="ECO:0000269|PubMed:15123713"
FT   DISULFID        12..27
FT                   /evidence="ECO:0000269|PubMed:15123713"
FT   DISULFID        17..34
FT                   /evidence="ECO:0000269|PubMed:15123713"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:1UT3"
FT   STRAND          11..16
FT                   /evidence="ECO:0007829|PDB:1UT3"
FT   STRAND          21..36
FT                   /evidence="ECO:0007829|PDB:1UT3"
SQ   SEQUENCE   38 AA;  4507 MW;  F4239C88C6187203 CRC64;
     SFGLCRLRRG FCARGRCRFP SIPIGRCSRF VQCCRRVW