DECO_MACDE
ID DECO_MACDE Reviewed; 39 AA.
AC P17350;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Decorsin;
OS Macrobdella decora (North American leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Macrobdella.
OX NCBI_TaxID=6405;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2351655; DOI=10.1016/s0021-9258(19)38791-5;
RA Seymour J.L., Henzel W.J., Nevins B., Stults J.T., Lazarus R.A.;
RT "Decorsin. A potent glycoprotein IIb-IIIa antagonist and platelet
RT aggregation inhibitor from the leech Macrobdella decora.";
RL J. Biol. Chem. 265:10143-10147(1990).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=8009227; DOI=10.1126/science.8009227;
RA Krezel A.M., Wagner G., Seymour-Ulmer J., Lazarus R.A.;
RT "Structure of the RGD protein decorsin: conserved motif and distinct
RT function in leech proteins that affect blood clotting.";
RL Science 264:1944-1947(1994).
CC -!- FUNCTION: Inhibits fibrinogen interaction with platelet receptors
CC expressed on glycoprotein IIb-IIIa complex. May prevent blood from
CC clotting during either feeding and/or storage of ingested blood.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the ornatin family. {ECO:0000305}.
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DR PIR; A36453; A36453.
DR PDB; 1DEC; NMR; -; A=1-39.
DR PDBsum; 1DEC; -.
DR AlphaFoldDB; P17350; -.
DR SMR; P17350; -.
DR EvolutionaryTrace; P17350; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR011061; Hirudin/antistatin.
DR SUPFAM; SSF57262; SSF57262; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Cell adhesion; Direct protein sequencing;
KW Hemostasis; Secreted.
FT PEPTIDE 1..39
FT /note="Decorsin"
FT /id="PRO_0000044770"
FT REGION 27..38
FT /note="High affinity binding domain"
FT /evidence="ECO:0000255"
FT MOTIF 31..33
FT /note="Cell attachment site"
FT VARIANT 1..3
FT /note="Missing (in N-3 isoform)"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1DEC"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1DEC"
SQ SEQUENCE 39 AA; 4384 MW; 3A3B35756FB70D36 CRC64;
APRLPQCQGD DQEKCLCNKD ECPPGQCRFP RGDADPYCE