HIR18_POEMA
ID HIR18_POEMA Reviewed; 62 AA.
AC P26631;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Hirullin-P18;
DE AltName: Full=Hirudin-P18;
DE AltName: Full=Thrombin inhibitor hirullin P18;
OS Poecilobdella manillensis (Mexican medical leech) (Hirudinaria
OS manillensis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Poecilobdella.
OX NCBI_TaxID=1348078;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2401369; DOI=10.1016/0014-5793(90)81208-6;
RA Krstenansky J.L., Owen T.J., Yates M.T., Mao S.J.T.;
RT "The C-terminal binding domain of hirullin P18. Antithrombin activity and
RT comparison to hirudin peptides.";
RL FEBS Lett. 269:425-429(1990).
RN [2]
RP ERRATUM OF PUBMED:2401369, AND SEQUENCE REVISION.
RA Krstenansky J.L., Owen T.J., Yates M.T., Mao S.J.T.;
RL FEBS Lett. 276:232-232(1990).
RN [3]
RP PROTEIN SEQUENCE, GLYCOSYLATION AT THR-46, LACK OF GLYCOSYLATION AT THR-41,
RP AND STRUCTURE OF CARBOHYDRATE.
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 50-62.
RX PubMed=8499567; DOI=10.1097/00001721-199304000-00012;
RA Tulinsky A., Qiu X.;
RT "Active site and exosite binding of alpha-thrombin.";
RL Blood Coagul. Fibrinolysis 4:305-312(1993).
CC -!- FUNCTION: Inhibits thrombin, thereby abolishing its ability to cleave
CC fibrinogen.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: O-linked glycan consists of Fuc-Gal-GalNAc trisaccharide.
CC {ECO:0000269|PubMed:1540584}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I14 (hirudin) family.
CC {ECO:0000305}.
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DR PIR; S11341; HULXLM.
DR PDB; 1THR; X-ray; 2.30 A; I=50-62.
DR PDBsum; 1THR; -.
DR AlphaFoldDB; P26631; -.
DR SMR; P26631; -.
DR MEROPS; I14.001; -.
DR GlyConnect; 222; 2 O-Linked glycans (1 site).
DR EvolutionaryTrace; P26631; -.
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.
FT CHAIN 1..62
FT /note="Hirullin-P18"
FT /id="PRO_0000195653"
FT REGION 1..3
FT /note="Interaction with thrombin active site"
FT /evidence="ECO:0000250"
FT REGION 37..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..62
FT /note="Interaction with fibrinogen-binding exosite of
FT thrombin"
FT SITE 41
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:1540584"
FT CARBOHYD 46
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1540584"
FT /id="CAR_000144"
FT DISULFID 6..13
FT /evidence="ECO:0000250"
FT DISULFID 15..26
FT /evidence="ECO:0000250"
FT DISULFID 20..35
FT /evidence="ECO:0000250"
SQ SEQUENCE 62 AA; 6693 MW; C2E82BDAC8FEAB84 CRC64;
VSYTDCTSGQ NYCLCGGNFC GDGKHCEMDG SENKCVDGEG TPKRQTSGPS DFEEFSLDDI
EQ
