ID   HIRP6_HIRMN             Reviewed;          63 AA.
AC   P28512;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   04-NOV-2026, entry version 100.
DE   RecName: Full=Hirudin-P6;
OS   Hirudinaria manillensis (Asian medical leech) (Poecilobdella manillensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudinaria.
OX   NCBI_TaxID=1348078;
RN   [1]
RP   PROTEIN SEQUENCE, STRUCTURE OF CARBOHYDRATE, SULFATION AT TYR-61, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=1540584; DOI=10.1021/bi00123a012;
RA   Steiner V., Knecht R., Boernsen O., Gassmann E., Stone S.R., Raschdorf F.,
RA   Schlaeppi J.-M., Maschler R.;
RT   "Primary structure and function of novel O-glycosylated hirudins from the
RT   leech Hirudinaria manillensis.";
RL   Biochemistry 31:2294-2298(1992).
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   -!- PTM: O-linked glycan consists of Fuc-Gal-GalNAc trisaccharide.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I14 (hirudin) family.
CC       {ECO:0000305}.
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DR   PIR; A42207; A42207.
DR   AlphaFoldDB; P28512; -.
DR   SMR; P28512; -.
DR   MEROPS; I14.001; -.
DR   GlyConnect; P28512; 3 O-Linked glycans (1 site).
DR   GlyCosmos; P28512; 1 site, 5 glycans.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 2.70.10.10; Thrombin Inhibitor (Hirudin), subunit I; 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; Leech antihemostatic proteins; 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-P6"
FT                   /id="PRO_0000195652"
FT   REGION          1..3
FT                   /note="Interaction with thrombin active site"
FT                   /evidence="ECO:0000250"
FT   REGION          35..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..63
FT                   /note="Interaction with fibrinogen-binding exosite of
FT                   thrombin"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        35..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         61
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:1540584"
FT   CARBOHYD        43
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /id="CAR_000143"
FT   DISULFID        6..14
FT                   /evidence="ECO:0000250"
FT   DISULFID        16..28
FT                   /evidence="ECO:0000250"
FT   DISULFID        22..37
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   63 AA;  6977 MW;  149A7369CC75A192 CRC64;
     MRYTACTESG QNQCICEGND VCGQGRNCQF DSSGKKCVEG EGTRKPQNEG QHDFDPIPEE
     YLS
//