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BTDC_PAPAN
ID   BTDC_PAPAN              Reviewed;          76 AA.
AC   B6ULW6; P86033;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Theta defensin subunit C;
DE            Short=BTD-c {ECO:0000303|PubMed:18852242};
DE   AltName: Full=BTD-4 subunit 2;
DE   Flags: Precursor;
GN   Name=BTDC;
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ACJ12915.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 65-73, IDENTIFICATION OF
RP   BTD-4, SYNTHESIS OF BTD-4, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Bone marrow {ECO:0000269|PubMed:18852242}, and
RC   Leukocyte {ECO:0000269|PubMed:18852242};
RX   PubMed=18852242; DOI=10.1128/iai.01100-08;
RA   Garcia A.E., Oesapay G., Tran P.A., Yuan J., Selsted M.E.;
RT   "Isolation, synthesis, and antimicrobial activities of naturally occurring
RT   theta-defensin isoforms from baboon leukocytes.";
RL   Infect. Immun. 76:5883-5891(2008).
CC   -!- FUNCTION: BTD-4 has antimicrobial activity against the Gram-negative
CC       bacterium E.coli ML35, the Gram-positive bacterium S.aureus 502a, and
CC       the fungus C.albicans 16820. {ECO:0000269|PubMed:18852242}.
CC   -!- SUBUNIT: BTD-4 is a cyclic heterodimer composed of subunits A and C;
CC       disulfide-linked. {ECO:0000269|PubMed:18852242}.
CC   -!- PTM: Forms a cyclic peptide with subunit A (BTD-4). An additional
CC       intersubunit disulfide bond is formed. {ECO:0000269|PubMed:18852242}.
CC   -!- MASS SPECTROMETRY: Mass=1996.57; Method=MALDI; Note=BTD-4, heterodimer,
CC       cyclized.; Evidence={ECO:0000269|PubMed:18852242};
CC   -!- SIMILARITY: Belongs to the alpha-defensin family. Theta subfamily.
CC       {ECO:0000255}.
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DR   EMBL; FJ030941; ACJ12915.1; -; mRNA.
DR   RefSeq; NP_001135410.1; NM_001141938.1.
DR   AlphaFoldDB; B6ULW6; -.
DR   Ensembl; ENSPANT00000006616; ENSPANP00000012161; ENSPANG00000046278.
DR   GeneID; 100196939; -.
DR   KEGG; panu:100196939; -.
DR   CTD; 100196939; -.
DR   eggNOG; ENOG502TEA8; Eukaryota.
DR   GeneTree; ENSGT00940000153268; -.
DR   HOGENOM; CLU_160803_2_0_1; -.
DR   OMA; GESNAGM; -.
DR   Proteomes; UP000028761; Chromosome 8.
DR   Bgee; ENSPANG00000033219; Expressed in bone marrow and 30 other tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
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; IPR016327; Alpha-defensin.
DR   InterPro; IPR002366; Alpha-defensin_propep.
DR   PANTHER; PTHR11876; PTHR11876; 1.
DR   Pfam; PF00879; Defensin_propep; 1.
DR   PIRSF; PIRSF001875; Alpha-defensin; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Defensin; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..64
FT                   /evidence="ECO:0000269|PubMed:18852242"
FT                   /id="PRO_0000364013"
FT   PEPTIDE         65..73
FT                   /note="Theta defensin subunit C"
FT                   /id="PRO_0000364014"
FT   PROPEP          74..76
FT                   /evidence="ECO:0000269|PubMed:18852242"
FT                   /id="PRO_0000364015"
FT   DISULFID        66
FT                   /note="Interchain (with C-66 in subunit A); in form BTD-4"
FT                   /evidence="ECO:0000250|UniProtKB:P82271"
FT   DISULFID        68..73
FT                   /evidence="ECO:0000250|UniProtKB:P82271"
FT   CROSSLNK        65
FT                   /note="Cyclopeptide (Arg-Cys) (interchain with C-73 in
FT                   subunit A); in form BTD-4"
FT                   /evidence="ECO:0000269|PubMed:18852242"
FT   CROSSLNK        73
FT                   /note="Cyclopeptide (Cys-Arg) (interchain with R-65 in
FT                   subunit A); in form BTD-4"
FT                   /evidence="ECO:0000269|PubMed:18852242"
SQ   SEQUENCE   76 AA;  8299 MW;  32AA6F84C2482AD9 CRC64;
     MRTFAFLTAM LLLVALHAQA EARQARADEA AIQEQPGADD QGMAHSFTRN ESAVLPLSES
     ERGLRCICLL GICRLL
 
 
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