ID   LAPP_HAEOF              Reviewed;         147 AA.
AC   Q01747;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Anti-platelet protein;
DE   Flags: Precursor;
GN   Name=LAPP;
OS   Haementeria officinalis (Mexican leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Haementeria.
OX   NCBI_TaxID=6410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 60-91 AND 123-139.
RC   TISSUE=Salivary gland;
RX   PubMed=1551898; DOI=10.1016/s0021-9258(19)50513-0;
RA   Keller P.M., Schultz L.D., Condra C., Karczewski J., Connolly T.M.;
RT   "An inhibitor of collagen-stimulated platelet activation from the salivary
RT   glands of the Haementeria officinalis leech. II. Cloning of the cDNA and
RT   expression.";
RL   J. Biol. Chem. 267:6899-6904(1992).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 58-147.
RX   PubMed=11468390; DOI=10.1107/s0907444901007405;
RA   Huizinga E.G., Schouten A., Connolly T.M., Kroon J., Sixma J.J., Gros P.;
RT   "The structure of leech anti-platelet protein, an inhibitor of
RT   haemostasis.";
RL   Acta Crystallogr. D 57:1071-1078(2001).
CC   -!- FUNCTION: An inhibitor of collagen-stimulated platelet aggregation,
CC       dense granule release and serotonin release.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; M81489; AAA29194.1; -; mRNA.
DR   PIR; A42435; A42435.
DR   PDB; 1I8N; X-ray; 2.20 A; A/B/C=22-147.
DR   PDBsum; 1I8N; -.
DR   AlphaFoldDB; Q01747; -.
DR   SMR; Q01747; -.
DR   EvolutionaryTrace; Q01747; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..147
FT                   /note="Anti-platelet protein"
FT                   /id="PRO_0000021578"
FT   REGION          21..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        67..145
FT   DISULFID        92..117
FT   DISULFID        96..105
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:1I8N"
FT   STRAND          63..72
FT                   /evidence="ECO:0007829|PDB:1I8N"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:1I8N"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:1I8N"
FT   HELIX           89..98
FT                   /evidence="ECO:0007829|PDB:1I8N"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:1I8N"
FT   STRAND          107..111
FT                   /evidence="ECO:0007829|PDB:1I8N"
FT   TURN            112..114
FT                   /evidence="ECO:0007829|PDB:1I8N"
FT   STRAND          117..120
FT                   /evidence="ECO:0007829|PDB:1I8N"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:1I8N"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:1I8N"
FT   STRAND          137..144
FT                   /evidence="ECO:0007829|PDB:1I8N"
SQ   SEQUENCE   147 AA;  15908 MW;  75A5511374A4E42E CRC64;
     MNSFLFSLAC SLLVAIPAIS AQDEDAGGAG DETSEGEDTT GSDETPSTGG GGDGGNEETI
     TAGNEDCWSK RPGWKLPDNL LTKTEFTSVD ECRKMCEESA VEPSCYILQI NTETNECYRN
     NEGDVTWSSL QYDQPNVVQW HLHACSK