ID   DFB1_EMYOR              Reviewed;          40 AA.
AC   P86253;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Beta-defensin 1 {ECO:0000303|PubMed:19253295};
DE            Short=TBD-1 {ECO:0000303|PubMed:19253295};
OS   Emys orbicularis (European pond turtle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Emydidae; Emys.
OX   NCBI_TaxID=82168;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, DISULFIDE BONDS, AND
RP   AMIDATION AT GLY-40.
RC   TISSUE=Leukocyte {ECO:0000269|PubMed:19253295};
RX   PubMed=19253295; DOI=10.1002/pmic.200800569;
RA   Stegemann C., Kolobov A. Jr., Leonova Y.F., Knappe D., Shamova O.,
RA   Ovchinnikova T.V., Kokryakov V.N., Hoffmann R.;
RT   "Isolation, purification and de novo sequencing of TBD-1, the first beta-
RT   defensin from leukocytes of reptiles.";
RL   Proteomics 9:1364-1373(2009).
CC   -!- FUNCTION: Has antimicrobial activity against the Gram-positive bacteria
CC       methicillin-resistant S.aureus ATCC 33591 and L.monocytogenes EGD, the
CC       Gram-negative bacterium E.coli ML53p and the yeast C.albicans 820. Has
CC       no hemolytic activity towards human erythrocytes.
CC       {ECO:0000269|PubMed:19253295}.
CC   -!- SUBUNIT: Monomer. Homodimer. {ECO:0000250|UniProtKB:P60022}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P60022}. Membrane
CC       {ECO:0000250|UniProtKB:P60022}. Note=Associates with tumor cell
CC       membrane-derived microvesicles. {ECO:0000250|UniProtKB:P60022}.
CC   -!- MASS SPECTROMETRY: Mass=4540.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19253295};
CC   -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000255}.
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DR   AlphaFoldDB; P86253; -.
DR   SMR; P86253; -.
DR   GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR   GO; GO:1990742; C:microvesicle; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR001855; Defensin_beta-typ.
DR   Pfam; PF00711; Defensin_beta; 1.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Defensin; Direct protein sequencing;
KW   Disulfide bond; Membrane; Secreted.
FT   PEPTIDE         1..40
FT                   /note="Beta-defensin 1"
FT                   /evidence="ECO:0000269|PubMed:19253295"
FT                   /id="PRO_0000371260"
FT   MOD_RES         40
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:19253295"
FT   DISULFID        7..35
FT                   /evidence="ECO:0000269|PubMed:19253295"
FT   DISULFID        14..29
FT                   /evidence="ECO:0000269|PubMed:19253295"
FT   DISULFID        19..36
FT                   /evidence="ECO:0000269|PubMed:19253295"
FT   UNSURE          37
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:19253295"
SQ   SEQUENCE   40 AA;  4550 MW;  C498CA4DF2BA865A CRC64;
     YDLSKNCRLR GGICYIGKCP RRFFRSGSCS RGNVCCLRFG