DEF4_RABIT
ID DEF4_RABIT Reviewed; 95 AA.
AC P01377;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Defensin alpha 4 {ECO:0000250|UniProtKB:P12838};
DE AltName: Full=Antiadrenocorticotropin peptide IV;
DE AltName: Full=Corticostatin IV;
DE Short=CS-IV;
DE AltName: Full=Corticostatin-4;
DE AltName: Full=Macrophage antibiotic peptide MCP-2;
DE Short=NP-2;
DE Flags: Precursor;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2745983;
RA Ganz T., Rayner J.R., Valore E.V., Tumolo A., Talmadge K., Fuller F.;
RT "The structure of the rabbit macrophage defensin genes and their organ-
RT specific expression.";
RL J. Immunol. 143:1358-1365(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8439302; DOI=10.1006/bbrc.1993.1149;
RA Sadro L.C., Tremblay A., Solomon S., Palfree R.G.E.;
RT "Differential expression of corticostatins/defensins: higher levels of CS-4
RT (NP-2) transcripts compared with CS-6 (NP-5) in rabbit lung.";
RL Biochem. Biophys. Res. Commun. 190:1009-1016(1993).
RN [3]
RP PROTEIN SEQUENCE OF 63-95.
RC TISSUE=Lung macrophage;
RX PubMed=6643497; DOI=10.1016/s0021-9258(17)43888-9;
RA Selsted M.E., Brown D.M., Delange R.J., Lehrer R.I.;
RT "Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of
RT rabbit lung macrophages.";
RL J. Biol. Chem. 258:14485-14489(1983).
RN [4]
RP PROTEIN SEQUENCE OF 63-95.
RC TISSUE=Peritoneal neutrophil;
RX PubMed=3988726; DOI=10.1016/s0021-9258(18)89110-4;
RA Selsted M.E., Brown D.M., Delange R.J., Harwig S.S.L., Lehrer R.I.;
RT "Primary structures of six antimicrobial peptides of rabbit peritoneal
RT neutrophils.";
RL J. Biol. Chem. 260:4579-4584(1985).
RN [5]
RP PROTEIN SEQUENCE OF 63-95, AND FUNCTION.
RC TISSUE=Lung;
RX PubMed=1311240; DOI=10.1210/endo.130.3.1311240;
RA Zhu Q., Solomon S.;
RT "Isolation and mode of action of rabbit corticostatic
RT (antiadrenocorticotropin) peptides.";
RL Endocrinology 130:1413-1423(1992).
RN [6]
RP STRUCTURE BY NMR OF 63-95.
RX PubMed=1445872; DOI=10.1021/bi00161a012;
RA Zhang X.-L., Selsted M.E., Pardi A.;
RT "NMR studies of defensin antimicrobial peptides. 1. Resonance assignment
RT and secondary structure determination of rabbit NP-2 and human HNP-1.";
RL Biochemistry 31:11348-11356(1992).
RN [7]
RP STRUCTURE BY NMR OF 63-95.
RX PubMed=1445873; DOI=10.1021/bi00161a013;
RA Pardi A., Zhang X.-L., Selsted M.E., Skalicky J.J., Yip P.F.;
RT "NMR studies of defensin antimicrobial peptides. 2. Three-dimensional
RT structures of rabbit NP-2 and human HNP-1.";
RL Biochemistry 31:11357-11364(1992).
CC -!- FUNCTION: Host-defense peptide that has antimicrobial activity (By
CC similarity). Inhibits corticotropin (ACTH)-stimulated corticosterone
CC production (in vitro) (PubMed:1311240). {ECO:0000250|UniProtKB:P28311,
CC ECO:0000269|PubMed:1311240}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01523}.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR EMBL; M28884; AAA31390.1; -; mRNA.
DR EMBL; S55582; AAB25449.2; -; mRNA.
DR EMBL; M28073; AAA31389.1; -; Genomic_DNA.
DR EMBL; L10841; AAA31424.1; -; mRNA.
DR PIR; B45811; WTRBM2.
DR RefSeq; NP_001164484.1; NM_001171013.1.
DR RefSeq; XP_008272399.1; XM_008274177.2.
DR AlphaFoldDB; P01377; -.
DR SMR; P01377; -.
DR Ensembl; ENSOCUT00000023530; ENSOCUP00000023567; ENSOCUG00000021307.
DR GeneID; 100009116; -.
DR KEGG; ocu:100009116; -.
DR CTD; 100009116; -.
DR GeneTree; ENSGT00940000153268; -.
DR OrthoDB; 1610714at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000021307; Expressed in lung and 18 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:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR InterPro; IPR016327; Alpha-defensin.
DR InterPro; IPR006081; Alpha-defensin_C.
DR InterPro; IPR002366; Alpha-defensin_propep.
DR InterPro; IPR006080; Defensin_beta/alpha.
DR PANTHER; PTHR11876; PTHR11876; 1.
DR Pfam; PF00323; Defensin_1; 1.
DR Pfam; PF00879; Defensin_propep; 1.
DR PIRSF; PIRSF001875; Alpha-defensin; 1.
DR SMART; SM00048; DEFSN; 1.
DR PROSITE; PS00269; DEFENSIN; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Antiviral defense; Defensin;
KW Direct protein sequencing; Disulfide bond; Fungicide; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..62
FT /evidence="ECO:0000269|PubMed:1311240,
FT ECO:0000269|PubMed:3988726, ECO:0000269|PubMed:6643497"
FT /id="PRO_0000006811"
FT PEPTIDE 63..95
FT /note="Defensin alpha 4"
FT /id="PRO_0000006812"
FT DISULFID 65..93
FT /evidence="ECO:0000250|UniProtKB:P28311"
FT DISULFID 67..82
FT /evidence="ECO:0000250|UniProtKB:P28311"
FT DISULFID 72..92
FT /evidence="ECO:0000250|UniProtKB:P28311"
SQ SEQUENCE 95 AA; 10431 MW; 58418C82B462F332 CRC64;
MRTLALLAAI LLVALQAQAE HISVSIDEVV DQQPPQAEDQ DVAIYVKEHE SSALEALGVK
AGVVCACRRA LCLPLERRAG FCRIRGRIHP LCCRR
