HIRM2_POEMA
ID HIRM2_POEMA Reviewed; 84 AA.
AC P81492; Q07557;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Hirudin-HM2;
DE AltName: Full=Bufrudin;
DE AltName: Full=Hirudin-HV1;
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-84.
RX PubMed=7685281; DOI=10.1111/j.1432-1033.1993.tb17924.x;
RA Scacheri E., Nitti G., Valsasina B., Orsini G., Visco C., Ferrera M.,
RA Sawyer R.T., Sarmientos P.;
RT "Novel hirudin variants from the leech Hirudinaria manillensis. Amino acid
RT sequence, cDNA cloning and genomic organization.";
RL Eur. J. Biochem. 214:295-304(1993).
RN [2]
RP PROTEIN SEQUENCE OF 21-83.
RC TISSUE=Head;
RX PubMed=8397794; DOI=10.1007/bf01028198;
RA Electricwala A., Hartwell R., Scawen M.D., Atkinson T.;
RT "The complete amino acid sequence of a hirudin variant from the leech
RT Hirudinaria manillensis.";
RL J. Protein Chem. 12:365-370(1993).
RN [3]
RP STRUCTURE BY NMR OF 21-84, AND DISULFIDE BONDS.
RX PubMed=9128439;
RX DOI=10.1002/(sici)1097-0282(199706)41:7<731::aid-bip3>3.0.co;2-q;
RA Nicastro G., Baumer L., Bolis G., Tato M.;
RT "NMR solution structure of a novel hirudin variant HM2, N-terminal 1-47 and
RT N64-->V + G mutant.";
RL Biopolymers 41:731-749(1997).
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 EMBL; X72786; CAA51293.1; -; Genomic_DNA.
DR PIR; S33329; S33329.
DR AlphaFoldDB; P81492; -.
DR SMR; P81492; -.
DR MEROPS; I14.001; -.
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; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:7685281,
FT ECO:0000269|PubMed:8397794"
FT CHAIN 21..84
FT /note="Hirudin-HM2"
FT /id="PRO_0000013443"
FT REGION 21..23
FT /note="Interaction with thrombin active site"
FT /evidence="ECO:0000250"
FT REGION 53..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..84
FT /note="Interaction with fibrinogen-binding exosite of
FT thrombin"
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT DISULFID 26..34
FT /evidence="ECO:0000269|PubMed:9128439"
FT DISULFID 36..48
FT /evidence="ECO:0000269|PubMed:9128439"
FT DISULFID 42..57
FT /evidence="ECO:0000269|PubMed:9128439"
FT CONFLICT 83
FT /note="L -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 84 AA; 9004 MW; CCBA5D85E71B4F07 CRC64;
MFSLKLFVVF LAVCICVSQA VSYTDCTESG QNYCLCVGSN VCGEGKNCQL SSSGNQCVHG
EGTPKPKSQT EGDFEEIPDE DILN
