ID   HIRUD_POEVI             Reviewed;          63 AA.
AC   P84590;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Hirudin;
OS   Poecilobdella viridis (Indian freshwater leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Poecilobdella.
OX   NCBI_TaxID=335439;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Saliva {ECO:0000269|Ref.1};
RA   Vankhede G.N., Gomase V.S., Deshmukh S.V., Chikhale N.J.;
RT   "Prediction of antigenic epitope of hirudin from Poecilobdella viridis.";
RL   J. Comp. Toxicol. Physiol. 2:110-118(2005).
CC   -!- FUNCTION: Hirudin is a potent thrombin-specific protease inhibitor. It
CC       forms a stable non-covalent complex with alpha-thrombin, thereby
CC       abolishing its ability to cleave fibrinogen. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I14 (hirudin) family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P84590; -.
DR   SMR; P84590; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.10.10; -; 1.
DR   InterPro; IPR024793; Hirudin.
DR   InterPro; IPR011061; Hirudin/antistatin.
DR   InterPro; IPR000429; Prot_inh_hirudin.
DR   Pfam; PF00713; Hirudin; 1.
DR   PIRSF; PIRSF001640; Hirudin; 1.
DR   PRINTS; PR00777; HIRUDIN.
DR   SUPFAM; SSF57262; SSF57262; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Secreted; Serine protease inhibitor; Sulfation.
FT   CHAIN           1..63
FT                   /note="Hirudin"
FT                   /id="PRO_0000195654"
FT   REGION          1..3
FT                   /note="Interaction with thrombin active site"
FT                   /evidence="ECO:0000250"
FT   REGION          39..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..63
FT                   /note="Interaction with fibrinogen-binding exosite of
FT                   thrombin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         62
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P01050"
FT   CARBOHYD        45
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        6..14
FT                   /evidence="ECO:0000250|UniProtKB:P01050"
FT   DISULFID        16..28
FT                   /evidence="ECO:0000250|UniProtKB:P01050"
FT   DISULFID        22..39
FT                   /evidence="ECO:0000250|UniProtKB:P01050"
SQ   SEQUENCE   63 AA;  6657 MW;  50516E218ECFAE56 CRC64;
     VVYTDCTESG QNLCLCEGSN VCGQGNKCIL GSDGEKNQCV TGEGTPGPQS HNDGDFEEPE
     EYL