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Antistasin (ATS) (Blood coagulation factor Xa/proclotting enzyme inhibitor)

 ANTA_HAEOF              Reviewed;         136 AA.
P15358; Q9TWQ8; Q9TX45;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
10-MAY-2017, entry version 105.
RecName: Full=Antistasin;
Short=ATS;
AltName: Full=Blood coagulation factor Xa/proclotting enzyme inhibitor;
Flags: Precursor;
Haementeria officinalis (Mexican leech).
Eukaryota; Metazoa; Lophotrochozoa; Annelida; Clitellata; Hirudinea;
Rhynchobdellida; Glossiphoniidae; Haementeria.
NCBI_TaxID=6410;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2470652; DOI=10.1016/0378-1119(89)90382-X;
Han J.H., Law S.W., Keller P.M., Kniskern P.J., Silberklang M.,
Tung J.S., Gasic T.B., Gasic G.J., Friedman P.A., Ellis R.W.;
"Cloning and expression of cDNA encoding antistasin, a leech-derived
protein having anti-coagulant and anti-metastatic properties.";
Gene 75:47-57(1989).
[2]
PROTEIN SEQUENCE OF 18-136.
TISSUE=Saliva;
PubMed=3164720;
Nutt E., Gasic T., Rodkey J., Gasic G.J., Jacobs J.W., Friedman P.A.,
Simpson E.;
"The amino acid sequence of antistasin. A potent inhibitor of factor
Xa reveals a repeated internal structure.";
J. Biol. Chem. 263:10162-10167(1988).
[3]
PROTEIN SEQUENCE OF 18-136.
TISSUE=Saliva;
PubMed=8271959; DOI=10.1016/0076-6879(93)23052-O;
Dunwiddie C.T., Waxman L., Vlasuk G.P., Friedman P.A.;
"Purification and characterization of inhibitors of blood coagulation
factor Xa from hematophagous organisms.";
Methods Enzymol. 223:291-312(1993).
[4]
REACTIVE SITE.
PubMed=2777803;
Dunwiddie C., Thornberry N.A., Bull H.G., Sardana M., Friedman P.A.,
Jacobs J.W., Simpson E.;
"Antistasin, a leech-derived inhibitor of factor Xa. Kinetic analysis
of enzyme inhibition and identification of the reactive site.";
J. Biol. Chem. 264:16694-16699(1989).
[5]
SULFATIDE-BINDING.
PubMed=2745433;
Holt G.D., Krivan H.C., Gasic G.J., Ginsburg V.;
"Antistasin, an inhibitor of coagulation and metastasis, binds to
sulfatide (Gal(3-SO4) beta 1-1Cer) and has a sequence homology with
other proteins that bind sulfated glycoconjugates.";
J. Biol. Chem. 264:12138-12140(1989).
[6]
MUTAGENESIS.
PubMed=1445252; DOI=10.1042/bj2870943;
Hofmann K.J., Nutt E.M., Dunwiddie C.;
"Site-directed mutagenesis of the leech-derived factor Xa inhibitor
antistasin. Probing of the reactive site.";
Biochem. J. 287:943-949(1992).
[7]
MUTAGENESIS.
PubMed=8073407; DOI=10.1016/0049-3848(94)90138-4;
Theunissen H.J., Dijkema R., Swinkels J.C., de Poorter T.L.,
Vink P.M., van Dinther T.G.;
"Mutational analysis of antistasin, an inhibitor of blood coagulation
factor Xa derived from the Mexican leech Haementeria officinalis.";
Thromb. Res. 75:41-50(1994).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-127.
PubMed=9311976; DOI=10.1093/emboj/16.17.5151;
Lapatto R., Krengel U., Schreuder H.A., Arkema A., de Boer B.,
Kalk K.H., Hol W.G.J., Grootenhuis P.D.J., Mulders J.W.M., Dijkema R.,
Theunissen H.J.M., Dijkstra B.W.;
"X-ray structure of antistasin at 1.9-A resolution and its modelled
complex with blood coagulation factor Xa.";
EMBO J. 16:5151-5161(1997).
-!- FUNCTION: This highly disulfide-bonded protein is a potent
inhibitor of factor Xa. May have therapeutic utility as an
anticoagulant. Also exhibits a strong metastatic activity.
-!- SUBCELLULAR LOCATION: Secreted.
-!- MISCELLANEOUS: Binds to heparin-agarose, binds to sulfated
glycoconjugates.
-!- MISCELLANEOUS: At least four isoforms of antistasin have been
identified in leech salivary gland extracts, which differ by 1 or
2 amino-acid residues.
-!- SIMILARITY: Belongs to the protease inhibitor I15 (antistasin)
family. {ECO:0000305}.
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EMBL; M24422; AAA29192.1; -; mRNA.
EMBL; M24423; AAA29193.1; -; mRNA.
PIR; A28806; A28806.
PIR; A34398; A34398.
PIR; JS0209; JS0209.
PIR; S13904; S13904.
PDB; 1SKZ; X-ray; 1.90 A; A=20-136.
PDBsum; 1SKZ; -.
ProteinModelPortal; P15358; -.
SMR; P15358; -.
MEROPS; I15.007; -.
EvolutionaryTrace; P15358; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0050819; P:negative regulation of coagulation; IEA:InterPro.
InterPro; IPR004094; Antistasin-like.
InterPro; IPR011061; Hirudin/antistatin.
InterPro; IPR008086; Prot_inh_I15_antistasin_leech.
Pfam; PF02822; Antistasin; 1.
PRINTS; PR01706; ANTISTASIN.
SUPFAM; SSF57262; SSF57262; 2.
PROSITE; PS51252; ANTISTASIN; 2.
1: Evidence at protein level;
3D-structure; Blood coagulation; Direct protein sequencing;
Disulfide bond; Hemostasis; Heparin-binding; Protease inhibitor;
Pyrrolidone carboxylic acid; Repeat; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 17 {ECO:0000269|PubMed:3164720,
ECO:0000269|PubMed:8271959}.
CHAIN 18 136 Antistasin.
/FTId=PRO_0000001700.
DOMAIN 45 70 Antistasin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00582}.
DOMAIN 100 125 Antistasin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00582}.
REGION 114 117 Heparin-binding. {ECO:0000255}.
REGION 128 135 Heparin-binding. {ECO:0000255}.
SITE 51 52 Reactive bond.
SITE 106 107 Reactive bond.
MOD_RES 18 18 Pyrrolidone carboxylic acid.
DISULFID 25 36
DISULFID 30 43
DISULFID 45 65
DISULFID 50 68
DISULFID 54 70
DISULFID 79 90
DISULFID 84 97
DISULFID 99 120
DISULFID 105 123
DISULFID 109 125
VARIANT 22 22 G -> R (in isoform B).
VARIANT 47 47 G -> E.
VARIANT 52 52 M -> V.
VARIANT 71 71 R -> I.
HELIX 25 28 {ECO:0000244|PDB:1SKZ}.
TURN 38 40 {ECO:0000244|PDB:1SKZ}.
STRAND 58 60 {ECO:0000244|PDB:1SKZ}.
STRAND 66 70 {ECO:0000244|PDB:1SKZ}.
HELIX 81 83 {ECO:0000244|PDB:1SKZ}.
TURN 92 94 {ECO:0000244|PDB:1SKZ}.
STRAND 95 97 {ECO:0000244|PDB:1SKZ}.
STRAND 99 101 {ECO:0000244|PDB:1SKZ}.
STRAND 113 115 {ECO:0000244|PDB:1SKZ}.
STRAND 121 125 {ECO:0000244|PDB:1SKZ}.
SEQUENCE 136 AA; 15225 MW; 582AF009ED9A0291 CRC64;
MIKLAILLLF TVAIVRCQGP FGPGCEEAGC PEGSACNIIT DRCTCSGVRC RMHCPHGFQR
SRYGCEFCKC RLEPMKATCD ISECPEGMMC SRLTNKCDCK IDINCRKTCP NGLKRDKLGC
EYCECRPKRK LIPRLS


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