BTDA_PAPAN
ID BTDA_PAPAN Reviewed; 76 AA.
AC B6ULW4; P86031;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Theta defensin subunit A;
DE Short=BTD-a {ECO:0000303|PubMed:18852242};
DE AltName: Full=BTD-1 subunit 1;
DE AltName: Full=BTD-3;
DE AltName: Full=BTD-4 subunit 1;
DE AltName: Full=BTD-7 subunit 1;
DE Flags: Precursor;
GN Name=BTDA;
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:ACJ12913.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 65-73, IDENTIFICATION OF
RP BTD-1; BTD-3; BTD-4 AND BTD-7, SYNTHESIS OF BTD-1; BTD-3; BTD-4 AND BTD-7,
RP 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-1, BTD-3, BTD-4 and BTD-7 have antimicrobial activity
CC against the Gram-negative bacterium E.coli ML35, the Gram-positive
CC bacterium S.aureus 502a, and the fungus C.albicans 16820. BTD-3 is more
CC effective against E.coli than BTD-1, BTD-4 and BTD-7.
CC {ECO:0000269|PubMed:18852242}.
CC -!- SUBUNIT: BTD-1 is a cyclic heterodimer composed of subunits A and B;
CC disulfide-linked. BTD-3 is a cyclic homodimer composed of two subunits
CC A; disulfide-linked. BTD-4 is a cyclic heterodimer composed of subunits
CC A and C; disulfide-linked. BTD-7 is a cyclic heterodimer composed of
CC subunits A and D; disulfide-linked. {ECO:0000269|PubMed:18852242}.
CC -!- PTM: Forms a cyclic peptide with subunit B (BTD-1), subunit A (BTD-3),
CC subunit C (BTD-4), or subunit D (BTD-7). An additional intersubunit
CC disulfide bond is formed. {ECO:0000269|PubMed:18852242}.
CC -!- MASS SPECTROMETRY: Mass=2055.69; Method=MALDI; Note=BTD-1, heterodimer,
CC cyclized.; Evidence={ECO:0000269|PubMed:18852242};
CC -!- MASS SPECTROMETRY: Mass=2048.38; Method=MALDI; Note=BTD-3, homodimer,
CC cyclized.; Evidence={ECO:0000269|PubMed:18852242};
CC -!- MASS SPECTROMETRY: Mass=1996.57; Method=MALDI; Note=BTD-4, heterodimer,
CC cyclized.; Evidence={ECO:0000269|PubMed:18852242};
CC -!- MASS SPECTROMETRY: Mass=2103.70; Method=MALDI; Note=BTD-7, 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; FJ030939; ACJ12913.1; -; mRNA.
DR RefSeq; NP_001135411.1; NM_001141939.1.
DR AlphaFoldDB; B6ULW4; -.
DR Ensembl; ENSPANT00000068787; ENSPANP00000060929; ENSPANG00000049195.
DR GeneID; 100196940; -.
DR KEGG; panu:100196940; -.
DR CTD; 100196940; -.
DR eggNOG; ENOG502TEA8; Eukaryota.
DR GeneTree; ENSGT00940000153268; -.
DR HOGENOM; CLU_160803_2_0_1; -.
DR OMA; IRVHENF; -.
DR OrthoDB; 1641414at2759; -.
DR Proteomes; UP000028761; Chromosome 8.
DR Bgee; ENSPANG00000033107; Expressed in bone marrow and 14 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_0000364007"
FT PEPTIDE 65..73
FT /note="Theta defensin subunit A"
FT /id="PRO_0000364008"
FT PROPEP 74..76
FT /evidence="ECO:0000269|PubMed:18852242"
FT /id="PRO_0000364009"
FT REGION 25..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 66
FT /note="Interchain (with C-66 in subunit A); in form BTD-3"
FT /evidence="ECO:0000250|UniProtKB:P82270"
FT DISULFID 66
FT /note="Interchain (with C-66 in subunit B); in form BTD-1"
FT /evidence="ECO:0000250|UniProtKB:P82270"
FT DISULFID 66
FT /note="Interchain (with C-66 in subunit C); in form BTD-4"
FT /evidence="ECO:0000250|UniProtKB:P82270"
FT DISULFID 66
FT /note="Interchain (with C-66 in subunit D); in form BTD-7"
FT /evidence="ECO:0000250|UniProtKB:P82270"
FT DISULFID 68..73
FT /evidence="ECO:0000250|UniProtKB:P82270"
FT CROSSLNK 65
FT /note="Cyclopeptide (Arg-Cys) (interchain with C-73 in
FT subunit A); in form BTD-3"
FT CROSSLNK 65
FT /note="Cyclopeptide (Arg-Cys) (interchain with C-73 in
FT subunit B); in form BTD-1"
FT CROSSLNK 65
FT /note="Cyclopeptide (Arg-Cys) (interchain with C-73 in
FT subunit C); in form BTD-4"
FT CROSSLNK 65
FT /note="Cyclopeptide (Arg-Cys) (interchain with C-73 in
FT subunit D); in form BTD-7"
FT CROSSLNK 73
FT /note="Cyclopeptide (Cys-Arg) (interchain with R-65 in
FT subunit A); in form BTD-3"
FT CROSSLNK 73
FT /note="Cyclopeptide (Cys-Arg) (interchain with R-65 in
FT subunit B); in form BTD-1"
FT CROSSLNK 73
FT /note="Cyclopeptide (Cys-Arg) (interchain with R-65 in
FT subunit C); in form BTD-4"
FT CROSSLNK 73
FT /note="Cyclopeptide (Cys-Arg) (interchain with R-65 in
FT subunit D); in form BTD-7"
SQ SEQUENCE 76 AA; 8198 MW; 1EABA4932A031826 CRC64;
MRTFALLTAM LLLVALHAQA EARQARADEA AAQQQPGADD QGMAHSFTWP ENAALPLSES
AKGLRCVCTR GFCRLL
