HIRP6_POEMA
ID HIRP6_POEMA Reviewed; 63 AA.
AC P28512;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Hirudin-P6;
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, 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; 221; 3 O-Linked glycans (1 site).
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-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 37..56
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