BTDB_PAPAN
ID BTDB_PAPAN Reviewed; 76 AA.
AC B6ULW5; P86032;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Theta defensin subunit B;
DE Short=BTD-b {ECO:0000303|PubMed:18852242};
DE AltName: Full=BTD-1 subunit 2;
DE AltName: Full=BTD-2;
DE Flags: Precursor;
GN Name=BTDB;
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:ACJ12914.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 65-73, IDENTIFICATION OF
RP BTD-1 AND BTD-2, SYNTHESIS OF BTD-1 AND BTD-2, FUNCTION, SUBUNIT, AND MASS
RP 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).
RN [2]
RP STRUCTURE BY NMR OF 65-73, SYNTHESIS OF BTD-2, DISULFIDE BOND, AND SUBUNIT.
RX PubMed=23148585; DOI=10.1021/bi301363a;
RA Conibear A.C., Rosengren K.J., Harvey P.J., Craik D.J.;
RT "Structural characterization of the cyclic cystine ladder motif of theta-
RT defensins.";
RL Biochemistry 51:9718-9726(2012).
CC -!- FUNCTION: BTD-1 and BTD-2 have antimicrobial activity against the Gram-
CC negative bacterium E.coli ML35, the Gram-positive bacterium S.aureus
CC 502a, and the fungus C.albicans 16820. BTD-2 is more effective against
CC E.coli than BTD-1. {ECO:0000269|PubMed:18852242}.
CC -!- SUBUNIT: BTD-1 is a cyclic heterodimer composed of subunits A and B;
CC disulfide-linked. BTD-2 is a cyclic homodimer composed of two subunits
CC B; disulfide-linked. {ECO:0000269|PubMed:18852242,
CC ECO:0000269|PubMed:23148585}.
CC -!- PTM: Forms a cyclic peptide with subunit A (BTD-1), or subunit B (BTD-
CC 2). An additional intersubunit disulfide bond is formed.
CC {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=2062.72; Method=MALDI; Note=BTD-2, homodimer,
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; FJ030940; ACJ12914.1; -; mRNA.
DR RefSeq; NP_001135412.1; NM_001141940.1.
DR PDB; 2LYE; NMR; -; A=65-73.
DR PDBsum; 2LYE; -.
DR AlphaFoldDB; B6ULW5; -.
DR GeneID; 100196941; -.
DR KEGG; panu:100196941; -.
DR CTD; 100196941; -.
DR OrthoDB; 1644337at2759; -.
DR Proteomes; UP000028761; Unplaced.
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 3D-structure; Antibiotic; Antimicrobial; Defensin;
KW Direct protein sequencing; Disulfide bond; Fungicide; Reference proteome;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..64
FT /evidence="ECO:0000269|PubMed:18852242"
FT /id="PRO_0000364010"
FT PEPTIDE 65..73
FT /note="Theta defensin subunit B"
FT /id="PRO_0000364011"
FT PROPEP 74..76
FT /evidence="ECO:0000269|PubMed:18852242"
FT /id="PRO_0000364012"
FT REGION 24..54
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-1"
FT /evidence="ECO:0000250|UniProtKB:P82271"
FT DISULFID 66
FT /note="Interchain (with C-66 in subunit B); in form BTD-2"
FT /evidence="ECO:0000269|PubMed:23148585"
FT DISULFID 68..73
FT /evidence="ECO:0000269|PubMed:23148585"
FT CROSSLNK 65
FT /note="Cyclopeptide (Arg-Cys) (interchain with C-73 in
FT subunit A); in form BTD-1"
FT CROSSLNK 65
FT /note="Cyclopeptide (Arg-Cys) (interchain with C-73 in
FT subunit B); in form BTD-2"
FT CROSSLNK 73
FT /note="Cyclopeptide (Cys-Arg) (interchain with R-65 in
FT subunit A); in form BTD-1"
FT CROSSLNK 73
FT /note="Cyclopeptide (Cys-Arg) (interchain with R-65 in
FT subunit B); in form BTD-2"
SQ SEQUENCE 76 AA; 8164 MW; F0ABB74E7847103A CRC64;
MRTFALLTAM LLLVALQPQA EARQARADEA AAQQQPGADD QGMAHSFTRP ENAALPLSES
AKGLRCVCRR GVCQLL
