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Rhesus theta defensin-1/3 subunit A (RTD-1 subunit A) (RTD-1a) (Demidefensin-2) (RTD-3)

 RTD1A_MACMU             Reviewed;          76 AA.
P82270; Q9TU01;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
30-AUG-2017, entry version 74.
RecName: Full=Rhesus theta defensin-1/3 subunit A;
Short=RTD-1 subunit A;
Short=RTD-1a;
AltName: Full=Demidefensin-2;
AltName: Full=RTD-3;
Flags: Precursor;
Name=RTD1A;
Macaca mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 65-73,
SYNTHESIS OF 65-73, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
DISULFIDE BONDS.
TISSUE=Bone marrow {ECO:0000269|PubMed:10521339}, and
Leukocyte {ECO:0000269|PubMed:10521339};
PubMed=10521339; DOI=10.1126/science.286.5439.498;
Tang Y.-Q., Yuan J., Oesapay G., Oesapay K., Tran D., Miller C.J.,
Ouellette A.J., Selsted M.E.;
"A cyclic antimicrobial peptide produced in primate leukocytes by the
ligation of two truncated alpha-defensins.";
Science 286:498-502(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF RTD-1 AND RTD-3, AND MASS
SPECTROMETRY.
TISSUE=Bone marrow;
PubMed=11527997;
Leonova L., Kokryakov V.N., Aleshina G., Hong T., Nguyen T., Zhao C.,
Waring A.J., Lehrer R.I.;
"Circular minidefensins and posttranslational generation of molecular
diversity.";
J. Leukoc. Biol. 70:461-464(2001).
[3]
PROTEIN SEQUENCE OF 65-73, SYNTHESIS OF RTD-3, FUNCTION OF RTD-1 AND
RTD-3, AND MASS SPECTROMETRY.
TISSUE=Leukocyte;
PubMed=11675394; DOI=10.1074/jbc.M109117200;
Tran D., Tran P.A., Tang Y.-Q., Yuan J., Cole T., Selsted M.E.;
"Homodimeric theta-defensins from rhesus macaque leukocytes:
isolation, synthesis, antimicrobial activities, and bacterial binding
properties of the cyclic peptides.";
J. Biol. Chem. 277:3079-3084(2002).
-!- FUNCTION: RTD-1 and RTD-3 have similar antimicrobial activities
against the Gram-positive bacteria S.aureus 502A and
L.monocytogenes, the Gram-negative bacteria S.typhimurium and
E.coli ML35, and the fungi C.albicans 16820 and C.neoformans 271A.
{ECO:0000269|PubMed:11675394}.
-!- SUBUNIT: RTD-1 is a cyclic heterodimer composed of subunits A and
B; disulfide-linked. RTD-3 is a cyclic homodimer composed of two
subunits A; disulfide-linked. {ECO:0000269|PubMed:10521339}.
-!- TISSUE SPECIFICITY: RTD-1 is expressed in bone marrow. Detected in
promyelocytes, myelocytes and mature neutrophils and monocytes.
{ECO:0000269|PubMed:10521339}.
-!- DEVELOPMENTAL STAGE: RTD-1 expression begins early during
granulocyte myelopoiesis. {ECO:0000269|PubMed:10521339}.
-!- PTM: Forms a cyclic peptide with subunit A (RTD-3) or with subunit
B (RTD-1). An additional intersubunit disulfide bond is formed.
-!- MASS SPECTROMETRY: Mass=2083.0; Method=MALDI; Range=65-73;
Note=RTD-1, heterodimer, cyclized and oxidized.;
Evidence={ECO:0000269|PubMed:11675394};
-!- MASS SPECTROMETRY: Mass=2076.0; Method=MALDI; Range=65-73;
Note=RTD-3, homodimer, cyclized and oxidized.;
Evidence={ECO:0000269|PubMed:11675394};
-!- MASS SPECTROMETRY: Mass=2087.70; Method=MALDI; Range=65-73;
Note=RTD-1, heterodimer and reduced.;
Evidence={ECO:0000269|PubMed:11527997};
-!- MASS SPECTROMETRY: Mass=2080.48; Method=MALDI; Range=65-73;
Note=RTD-3, homodimer and reduced.;
Evidence={ECO:0000269|PubMed:11527997};
-!- MISCELLANEOUS: RTD-1 is 10-fold more present in cells than RTD-3.
-!- SIMILARITY: Belongs to the alpha-defensin family. Theta subfamily.
{ECO:0000305}.
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EMBL; AF191100; AAF04389.1; -; mRNA.
EMBL; AF191102; AAF04391.1; -; Genomic_DNA.
EMBL; AF184157; AAF07924.1; -; mRNA.
PIR; A59089; A59089.
RefSeq; NP_001027989.1; NM_001032817.2.
UniGene; Mmu.3480; -.
STRING; 9544.ENSMMUP00000023400; -.
TCDB; 1.C.19.1.6; the defensin (defensin) family.
GeneID; 574122; -.
KEGG; mcc:574122; -.
CTD; 574122; -.
HOGENOM; HOG000233351; -.
HOVERGEN; HBG079156; -.
InParanoid; P82270; -.
KO; K05230; -.
Proteomes; UP000006718; Unplaced.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0031640; P:killing of cells of other organism; IEA:UniProtKB-KW.
InterPro; IPR016327; Alpha-defensin_pro.
InterPro; IPR002366; Defensin_propep.
PANTHER; PTHR11876; PTHR11876; 1.
Pfam; PF00879; Defensin_propep; 1.
PIRSF; PIRSF001875; Alpha-defensin; 1.
1: Evidence at protein level;
Antibiotic; Antimicrobial; Complete proteome; Defensin;
Direct protein sequencing; Disulfide bond; Fungicide;
Reference proteome; Signal.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 64 {ECO:0000255,
ECO:0000269|PubMed:10521339}.
/FTId=PRO_0000006871.
PEPTIDE 65 73 Rhesus theta defensin-1/3 subunit A.
/FTId=PRO_0000006872.
PROPEP 74 76 {ECO:0000269|PubMed:10521339}.
/FTId=PRO_0000006873.
DISULFID 66 66 Interchain (with C-66 in subunit A); in
form RTD-3.
{ECO:0000269|PubMed:10521339}.
DISULFID 66 66 Interchain (with C-66 in subunit B); in
form RTD-1.
{ECO:0000269|PubMed:10521339}.
DISULFID 68 73 {ECO:0000269|PubMed:10521339}.
CROSSLNK 65 65 Cyclopeptide (Arg-Cys) (interchain with
C-73 in subunit A); in form RTD-3.
CROSSLNK 65 65 Cyclopeptide (Arg-Cys) (interchain with
C-73 in subunit B); in form RTD-1.
CROSSLNK 73 73 Cyclopeptide (Cys-Arg) (interchain with
R-65 in subunit A); in form RTD-3.
CROSSLNK 73 73 Cyclopeptide (Cys-Arg) (interchain with
R-65 in subunit B); in form RTD-1.
CONFLICT 38 38 T -> A (in Ref. 2; AAF07924).
{ECO:0000305}.
CONFLICT 49 49 W -> R (in Ref. 2; published sequence).
{ECO:0000305}.
SEQUENCE 76 AA; 8242 MW; BEA207932A030590 CRC64;
MRTFALLTAM LLLVALHAQA EARQARADEA AAQQQPGTDD QGMAHSFTWP ENAALPLSES
AKGLRCICTR GFCRLL


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