RTD1B_MACMU
ID RTD1B_MACMU Reviewed; 76 AA.
AC P82271;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Rhesus theta defensin-1/2 subunit B;
DE Short=RTD-1 subunit B;
DE Short=RTD-1b;
DE AltName: Full=Demidefensin-1;
DE AltName: Full=RTD-2;
DE Flags: Precursor;
GN Name=RTD1B;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 65-73,
RP SYNTHESIS OF 65-73, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISULFIDE
RP BONDS.
RC TISSUE=Bone marrow {ECO:0000269|PubMed:10521339}, and
RC Leukocyte {ECO:0000269|PubMed:10521339};
RX PubMed=10521339; DOI=10.1126/science.286.5439.498;
RA Tang Y.-Q., Yuan J., Oesapay G., Oesapay K., Tran D., Miller C.J.,
RA Ouellette A.J., Selsted M.E.;
RT "A cyclic antimicrobial peptide produced in primate leukocytes by the
RT ligation of two truncated alpha-defensins.";
RL Science 286:498-502(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SYNTHESIS OF RTD-1 AND RTD-2.
RC TISSUE=Bone marrow;
RX PubMed=11527997;
RA Leonova L., Kokryakov V.N., Aleshina G., Hong T., Nguyen T., Zhao C.,
RA Waring A.J., Lehrer R.I.;
RT "Circular minidefensins and posttranslational generation of molecular
RT diversity.";
RL J. Leukoc. Biol. 70:461-464(2001).
RN [3]
RP PROTEIN SEQUENCE OF 65-73, SYNTHESIS OF RTD-2, FUNCTION OF RTD-1 AND RTD-2,
RP AND MASS SPECTROMETRY.
RC TISSUE=Leukocyte;
RX PubMed=11675394; DOI=10.1074/jbc.m109117200;
RA Tran D., Tran P.A., Tang Y.-Q., Yuan J., Cole T., Selsted M.E.;
RT "Homodimeric theta-defensins from rhesus macaque leukocytes: isolation,
RT synthesis, antimicrobial activities, and bacterial binding properties of
RT the cyclic peptides.";
RL J. Biol. Chem. 277:3079-3084(2002).
RN [4]
RP STRUCTURE BY NMR OF 65-73, DISULFIDE BOND, SYNTHESIS OF RTD-1, 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: RTD-1 and RTD-2 have similar antimicrobial activities against
CC the Gram-positive bacteria S.aureus 502A and L.monocytogenes, the Gram-
CC negative bacterium S.typhimurium, and the fungi C.albicans 16820 and
CC C.neoformans 271A. RTD-2 is 2-3-fold less active than RTD-1 against
CC E.coli ML35. {ECO:0000269|PubMed:11675394}.
CC -!- SUBUNIT: RTD-1 is a cyclic heterodimer composed of subunits A and B;
CC disulfide-linked. RTD-2 is a cyclic homodimer composed of two subunits
CC B; disulfide-linked. {ECO:0000269|PubMed:10521339,
CC ECO:0000269|PubMed:23148585}.
CC -!- TISSUE SPECIFICITY: RTD-1 is expressed in bone marrow. Detected in
CC promyelocytes, myelocytes and mature neutrophils and monocytes.
CC {ECO:0000269|PubMed:10521339}.
CC -!- DEVELOPMENTAL STAGE: RTD-1 expression begins early during granulocyte
CC myelopoiesis. {ECO:0000269|PubMed:10521339}.
CC -!- PTM: Forms a cyclic peptide with 1 subunit B (RTD-2) or with 1 subunit
CC A (RTD-1). An additional intersubunit disulfide bond is formed.
CC {ECO:0000269|PubMed:10521339, ECO:0000269|PubMed:23148585}.
CC -!- MASS SPECTROMETRY: Mass=2083.0; Method=MALDI; Note=RTD-1, heterodimer,
CC cyclized and oxidized.; Evidence={ECO:0000269|PubMed:11675394};
CC -!- MASS SPECTROMETRY: Mass=2087.9; Method=MALDI; Note=RTD-2, homodimer,
CC cyclized and oxidized.; Evidence={ECO:0000269|PubMed:11675394};
CC -!- MASS SPECTROMETRY: Mass=2087.70; Method=MALDI; Note=RTD-1, heterodimer
CC and reduced.; Evidence={ECO:0000269|PubMed:11675394};
CC -!- MASS SPECTROMETRY: Mass=2094.89; Method=MALDI; Note=RTD-2, homodimer
CC and reduced.; Evidence={ECO:0000269|PubMed:11675394};
CC -!- MISCELLANEOUS: RTD-1 is 10-fold more present in cells than RTD-2.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. Theta subfamily.
CC {ECO:0000305}.
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DR EMBL; AF191101; AAF04390.1; -; mRNA.
DR EMBL; AF191103; AAF04392.1; -; Genomic_DNA.
DR EMBL; AF184156; AAF07923.1; -; mRNA.
DR PIR; B59089; B59089.
DR RefSeq; NP_001027990.1; NM_001032818.1.
DR PDB; 2LYF; NMR; -; A=65-73.
DR PDBsum; 2LYF; -.
DR AlphaFoldDB; P82271; -.
DR STRING; 9544.ENSMMUP00000024364; -.
DR GeneID; 574123; -.
DR KEGG; mcc:574123; -.
DR CTD; 574123; -.
DR eggNOG; ENOG502TEA8; Eukaryota.
DR HOGENOM; CLU_160803_2_0_1; -.
DR InParanoid; P82271; -.
DR OMA; MIISFTG; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0051673; P:membrane disruption in another organism; IBA:GO_Central.
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:0000255, ECO:0000269|PubMed:10521339"
FT /id="PRO_0000006874"
FT PEPTIDE 65..73
FT /note="Rhesus theta defensin-1/2 subunit B"
FT /id="PRO_0000006875"
FT PROPEP 74..76
FT /evidence="ECO:0000269|PubMed:10521339"
FT /id="PRO_0000006876"
FT REGION 25..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 RTD-1"
FT /evidence="ECO:0000269|PubMed:10521339,
FT ECO:0000269|PubMed:23148585"
FT DISULFID 66
FT /note="Interchain (with C-66 in subunit B); in form RTD-2"
FT /evidence="ECO:0000269|PubMed:10521339"
FT DISULFID 68..73
FT /evidence="ECO:0000269|PubMed:10521339,
FT ECO:0000269|PubMed:23148585"
FT CROSSLNK 65
FT /note="Cyclopeptide (Arg-Cys) (interchain with C-73 in
FT subunit A); in form RTD-1"
FT CROSSLNK 65
FT /note="Cyclopeptide (Arg-Cys) (interchain with C-73 in
FT subunit B); in form RTD-2"
FT CROSSLNK 73
FT /note="Cyclopeptide (Cys-Arg) (interchain with R-65 in
FT subunit A); in form RTD-1"
FT CROSSLNK 73
FT /note="Cyclopeptide (Cys-Arg) (interchain with R-65 in
FT subunit B); in form RTD-2"
SQ SEQUENCE 76 AA; 8189 MW; F0B754466156071E CRC64;
MRTFALLTAM LLLVALHAQA EARQARADEA AAQQQPGADD QGMAHSFTRP ENAALPLSES
ARGLRCLCRR GVCQLL
