DEF1_RABIT
ID DEF1_RABIT Reviewed; 93 AA.
AC P07469;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Corticostatin 1;
DE AltName: Full=Antiadrenocorticotropin peptide I;
DE AltName: Full=Corticostatin I;
DE Short=CS-I;
DE AltName: Full=Microbicidal peptide NP-3A;
DE AltName: Full=Neutrophil antibiotic peptide NP-3A;
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 [GENOMIC DNA / MRNA].
RX PubMed=8477861; DOI=10.1016/0014-5793(93)80122-b;
RA Linzmeier R., Michaelson D., Liu L., Ganz T.;
RT "The structure of neutrophil defensin genes.";
RL FEBS Lett. 321:267-273(1993).
RN [2]
RP PROTEIN SEQUENCE OF 60-93.
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 [3]
RP PROTEIN SEQUENCE OF 60-93.
RC TISSUE=Lung;
RX PubMed=2829194; DOI=10.1073/pnas.85.2.592;
RA Zhu Q., Hu J., Esch F., Shimasaki S., Solomon S.;
RT "Isolation and structure of corticostatin peptides from rabbit fetal and
RT adult lung.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:592-596(1988).
RN [4]
RP PROTEIN SEQUENCE OF 60-93.
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).
CC -!- FUNCTION: Microbicidal activity and inhibits corticotropin (ACTH)
CC stimulated corticosterone production.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR EMBL; M64599; AAA31236.1; -; Genomic_DNA.
DR EMBL; M64600; AAA31237.1; -; mRNA.
DR PIR; S32553; S32553.
DR RefSeq; NP_001075767.1; NM_001082298.1.
DR AlphaFoldDB; P07469; -.
DR SMR; P07469; -.
DR GeneID; 100009134; -.
DR KEGG; ocu:100009134; -.
DR OrthoDB; 1610714at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; 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; Defensin; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..59
FT /evidence="ECO:0000269|PubMed:1311240,
FT ECO:0000269|PubMed:2829194, ECO:0000269|PubMed:3988726"
FT /id="PRO_0000006807"
FT PEPTIDE 60..93
FT /note="Corticostatin 1"
FT /id="PRO_0000006808"
FT DISULFID 62..90
FT /evidence="ECO:0000250"
FT DISULFID 64..79
FT /evidence="ECO:0000250"
FT DISULFID 69..89
FT /evidence="ECO:0000250"
SQ SEQUENCE 93 AA; 10344 MW; 7E1598C48A28F37C CRC64;
MRTLILLAAI LLAALQAQAE LFSVNVDEVL DQQQPGSDQD LVIHLTGEES SALQVPDTKG
ICACRRRFCP NSERFSGYCR VNGARYVRCC SRR
