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