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AMP2_MELGA
ID   AMP2_MELGA              Reviewed;          64 AA.
AC   P80392; O93506;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Antimicrobial peptide THP2;
DE   AltName: Full=Turkey heterophil peptide 2;
DE   Flags: Precursor;
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=9745666; DOI=10.1046/j.1365-2052.1998.00338.x;
RA   Brockus C.W., Harmon B.G., Jackwood M.W.;
RT   "Characterization of beta-defensin prepropeptide mRNA from chicken and
RT   turkey bone marrow.";
RL   Anim. Genet. 29:283-289(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 29-48, AND FUNCTION.
RC   TISSUE=Granulocyte;
RX   PubMed=7964174; DOI=10.1002/jlb.56.5.661;
RA   Evans E.W., Beach G.G., Wunderlich J., Harmon B.G.;
RT   "Isolation of antimicrobial peptides from avian heterophils.";
RL   J. Leukoc. Biol. 56:661-665(1994).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC   TISSUE=Bone marrow, and Granulocyte;
RX   PubMed=19151352; DOI=10.3382/ps.2008-00366;
RA   Kannan L., Rath N.C., Liyanage R., Lay J.O. Jr.;
RT   "Direct screening identifies mature beta-defensin 2 in avian heterophils.";
RL   Poult. Sci. 88:372-379(2009).
CC   -!- FUNCTION: Antibacterial activity against the Gram-positive bacterium
CC       Staphylococcus aureus. Lacks antibacterial activity against the Gram-
CC       negative bacterium E.coli K-12. {ECO:0000269|PubMed:7964174}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in circulating heterophil granulocytes
CC       and bone marrow (at protein level). {ECO:0000269|PubMed:19151352}.
CC   -!- MASS SPECTROMETRY: Mass=4129.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19151352};
CC   -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR   EMBL; AF033338; AAC36054.1; -; mRNA.
DR   AlphaFoldDB; P80392; -.
DR   SMR; P80392; -.
DR   Proteomes; UP000001645; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR001855; Defensin_beta-typ.
DR   Pfam; PF00711; Defensin_beta; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Defensin; Direct protein sequencing;
KW   Disulfide bond; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:7964174"
FT   PEPTIDE         29..64
FT                   /note="Antimicrobial peptide THP2"
FT                   /id="PRO_0000007018"
FT   DISULFID        31..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        36..51
FT                   /evidence="ECO:0000250"
FT   DISULFID        41..58
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   64 AA;  7327 MW;  7E597FEE4FCA4995 CRC64;
     MRILYLLFSL LFLALQVSPG LSSPKRDMLF CKRGTCHFGR CPSHLIKVGS CFGFRSCCKW
     PWDA
 
 
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