ID   HIR2P_HIRME             Reviewed;          65 AA.
AC   P28505;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Hirudin-2';
DE   AltName: Full=Hirudin II';
OS   Hirudo medicinalis (Medicinal leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudo.
OX   NCBI_TaxID=6421;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2792365; DOI=10.1016/0014-5793(89)81070-1;
RA   Scharf M., Engels J., Tripier D.;
RT   "Primary structures of new 'iso-hirudins'.";
RL   FEBS Lett. 255:105-110(1989).
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.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I14 (hirudin) family.
CC       {ECO:0000305}.
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DR   PIR; S05679; S05679.
DR   PDB; 1HAG; X-ray; 2.00 A; I=55-64.
DR   PDB; 1TBZ; X-ray; 2.30 A; I=54-64.
DR   PDBsum; 1HAG; -.
DR   PDBsum; 1TBZ; -.
DR   AlphaFoldDB; P28505; -.
DR   SMR; P28505; -.
DR   Allergome; 9843; Hir me Hirudin.
DR   EvolutionaryTrace; P28505; -.
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   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Secreted; Serine protease inhibitor; Sulfation.
FT   CHAIN           1..65
FT                   /note="Hirudin-2'"
FT                   /id="PRO_0000195645"
FT   REGION          1..3
FT                   /note="Interaction with thrombin active site"
FT                   /evidence="ECO:0000250"
FT   REGION          39..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..65
FT                   /note="Interaction with fibrinogen-binding exosite of
FT                   thrombin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         63
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        45
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        6..14
FT                   /evidence="ECO:0000250"
FT   DISULFID        16..28
FT                   /evidence="ECO:0000250"
FT   DISULFID        22..39
FT                   /evidence="ECO:0000250"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:1HAG"
SQ   SEQUENCE   65 AA;  6987 MW;  AE1EEAE55EA69ADC CRC64;
     ITYTDCTESG QDLCLCEGSD VCGKGNKCIL GSNGEENQCV TGEGTPKPQS HNDGDFEEIP
     EEYLQ