位置:首页 > 蛋白库 > RTD1A_MACMU
RTD1A_MACMU
ID   RTD1A_MACMU             Reviewed;          76 AA.
AC   P82270; Q9TU01;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Rhesus theta defensin-1/3 subunit A;
DE            Short=RTD-1 subunit A;
DE            Short=RTD-1a;
DE   AltName: Full=Demidefensin-2;
DE   AltName: Full=RTD-3;
DE   Flags: Precursor;
GN   Name=RTD1A;
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], SYNTHESIS OF RTD-1 AND RTD-3, AND MASS
RP   SPECTROMETRY.
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-3, FUNCTION OF RTD-1 AND RTD-3,
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-3 have similar antimicrobial activities against
CC       the Gram-positive bacteria S.aureus 502A and L.monocytogenes, the Gram-
CC       negative bacteria S.typhimurium and E.coli ML35, and the fungi
CC       C.albicans 16820 and C.neoformans 271A. {ECO:0000269|PubMed:11675394}.
CC   -!- SUBUNIT: RTD-1 is a cyclic heterodimer composed of subunits A and B;
CC       disulfide-linked (PubMed:23148585). RTD-3 is a cyclic homodimer
CC       composed of two subunits A; disulfide-linked.
CC       {ECO:0000269|PubMed:10521339, 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 subunit A (RTD-3) or with subunit B
CC       (RTD-1). An additional intersubunit disulfide bond is formed.
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=2076.0; Method=MALDI; Note=RTD-3, 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:11527997};
CC   -!- MASS SPECTROMETRY: Mass=2080.48; Method=MALDI; Note=RTD-3, homodimer
CC       and reduced.; Evidence={ECO:0000269|PubMed:11527997};
CC   -!- MISCELLANEOUS: RTD-1 is 10-fold more present in cells than RTD-3.
CC   -!- SIMILARITY: Belongs to the alpha-defensin family. Theta subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF191100; AAF04389.1; -; mRNA.
DR   EMBL; AF191102; AAF04391.1; -; Genomic_DNA.
DR   EMBL; AF184157; AAF07924.1; -; mRNA.
DR   PIR; A59089; A59089.
DR   RefSeq; NP_001027989.1; NM_001032817.2.
DR   PDB; 2LYF; NMR; -; A=65-73.
DR   PDBsum; 2LYF; -.
DR   AlphaFoldDB; P82270; -.
DR   STRING; 9544.ENSMMUP00000023400; -.
DR   TCDB; 1.C.19.1.6; the defensin (defensin) family.
DR   GeneID; 574122; -.
DR   KEGG; mcc:574122; -.
DR   CTD; 574122; -.
DR   eggNOG; ENOG502TEA8; Eukaryota.
DR   HOGENOM; CLU_160803_2_0_1; -.
DR   InParanoid; P82270; -.
DR   OrthoDB; 1634035at2759; -.
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_0000006871"
FT   PEPTIDE         65..73
FT                   /note="Rhesus theta defensin-1/3 subunit A"
FT                   /id="PRO_0000006872"
FT   PROPEP          74..76
FT                   /evidence="ECO:0000269|PubMed:10521339"
FT                   /id="PRO_0000006873"
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 RTD-3"
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-1"
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-3"
FT   CROSSLNK        65
FT                   /note="Cyclopeptide (Arg-Cys) (interchain with C-73 in
FT                   subunit B); in form RTD-1"
FT   CROSSLNK        73
FT                   /note="Cyclopeptide (Cys-Arg) (interchain with R-65 in
FT                   subunit A); in form RTD-3"
FT   CROSSLNK        73
FT                   /note="Cyclopeptide (Cys-Arg) (interchain with R-65 in
FT                   subunit B); in form RTD-1"
FT   CONFLICT        38
FT                   /note="T -> A (in Ref. 2; AAF07924)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="W -> R (in Ref. 2; published sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   76 AA;  8242 MW;  BEA207932A030590 CRC64;
     MRTFALLTAM LLLVALHAQA EARQARADEA AAQQQPGTDD QGMAHSFTWP ENAALPLSES
     AKGLRCICTR GFCRLL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024