LCRP_PETMA
ID LCRP_PETMA Reviewed; 19 AA.
AC Q10996;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Corticostatin-related peptide LCRP;
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757;
RN [1]
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Skin;
RX PubMed=8759287; DOI=10.1016/0305-0491(95)02132-9;
RA Conlon J.M., Sower S.A.;
RT "Isolation of a peptide structurally related to mammalian corticostatins
RT from the lamprey Petromyzon marinus.";
RL Comp. Biochem. Physiol. 114B:133-137(1996).
CC -!- FUNCTION: May have microbicidal activities. May inhibit corticotropin
CC (ACTH) stimulated steroidogenesis and the microbial actions of the
CC corticostatins.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MASS SPECTROMETRY: Mass=2201; Mass_error=0.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8759287};
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR AlphaFoldDB; Q10996; -.
DR Ensembl; ENSPMAT00000011096; ENSPMAP00000011050; ENSPMAG00000010069.
DR HOGENOM; CLU_3430684_0_0_1; -.
DR Proteomes; UP000245300; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Defensin; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted.
FT PEPTIDE 1..19
FT /note="Corticostatin-related peptide LCRP"
FT /id="PRO_0000043635"
FT DISULFID 1..18
FT /evidence="ECO:0000250"
FT DISULFID 3..9
FT /evidence="ECO:0000250"
FT DISULFID 8..17
FT /evidence="ECO:0000250"
SQ SEQUENCE 19 AA; 2209 MW; 8D9CEDC71A199AE5 CRC64;
CPCGRRRCCV RGLNVYCCF