Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P15358 (ANTA_HAEOF) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Antistasin

Short name=ATS
Alternative name(s):
Blood coagulation factor Xa/proclotting enzyme inhibitor
OrganismHaementeria officinalis (Mexican leech)
Taxonomic identifier6410 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaRhynchobdellidaGlossiphoniidaeHaementeria

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

At least four isoforms of antistasin have been identified in leech salivary gland extracts, which differ by 1 or 2 amino-acid residues.

Sequence similarities

Belongs to the protease inhibitor I15 (antistasin) family. [View classification]

Contains 2 antistasin-like domains.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.2 Ref.3
Chain18 – 136119Antistasin
PRO_0000001700

Regions

Domain45 – 7026Antistasin-like 1
Domain100 – 12526Antistasin-like 2
Region114 – 1174Heparin-binding Potential
Region128 – 1358Heparin-binding Potential

Sites

Site51 – 522Reactive bond
Site106 – 1072Reactive bond

Amino acid modifications

Modified residue181Pyrrolidone carboxylic acid
Disulfide bond25 ↔ 36
Disulfide bond30 ↔ 43
Disulfide bond45 ↔ 65
Disulfide bond50 ↔ 68
Disulfide bond54 ↔ 70
Disulfide bond79 ↔ 90
Disulfide bond84 ↔ 97
Disulfide bond99 ↔ 120
Disulfide bond105 ↔ 123
Disulfide bond109 ↔ 125

Natural variations

Natural variant221G → R in isoform B.
Natural variant471G → E.
Natural variant521M → V.
Natural variant711R → I.

Secondary structure

.................... 136
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15358 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 582AF009ED9A0291

FASTA13615,225
        10         20         30         40         50         60 
MIKLAILLLF TVAIVRCQGP FGPGCEEAGC PEGSACNIIT DRCTCSGVRC RMHCPHGFQR 

        70         80         90        100        110        120 
SRYGCEFCKC RLEPMKATCD ISECPEGMMC SRLTNKCDCK IDINCRKTCP NGLKRDKLGC 

       130 
EYCECRPKRK LIPRLS 

« Hide

References

[1]"Cloning and expression of cDNA encoding antistasin, a leech-derived protein having anti-coagulant and anti-metastatic properties."
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.
Gene 75:47-57(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The amino acid sequence of antistasin. A potent inhibitor of factor Xa reveals a repeated internal structure."
Nutt E., Gasic T., Rodkey J., Gasic G.J., Jacobs J.W., Friedman P.A., Simpson E.
J. Biol. Chem. 263:10162-10167(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-136.
Tissue: Saliva.
[3]"Purification and characterization of inhibitors of blood coagulation factor Xa from hematophagous organisms."
Dunwiddie C.T., Waxman L., Vlasuk G.P., Friedman P.A.
Methods Enzymol. 223:291-312(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-136.
Tissue: Saliva.
[4]"Antistasin, a leech-derived inhibitor of factor Xa. Kinetic analysis of enzyme inhibition and identification of the reactive site."
Dunwiddie C., Thornberry N.A., Bull H.G., Sardana M., Friedman P.A., Jacobs J.W., Simpson E.
J. Biol. Chem. 264:16694-16699(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: REACTIVE SITE.
[5]"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."
Holt G.D., Krivan H.C., Gasic G.J., Ginsburg V.
J. Biol. Chem. 264:12138-12140(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATIDE-BINDING.
[6]"Site-directed mutagenesis of the leech-derived factor Xa inhibitor antistasin. Probing of the reactive site."
Hofmann K.J., Nutt E.M., Dunwiddie C.
Biochem. J. 287:943-949(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[7]"Mutational analysis of antistasin, an inhibitor of blood coagulation factor Xa derived from the Mexican leech Haementeria officinalis."
Theunissen H.J., Dijkema R., Swinkels J.C., de Poorter T.L., Vink P.M., van Dinther T.G.
Thromb. Res. 75:41-50(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[8]"X-ray structure of antistasin at 1.9-A resolution and its modelled complex with blood coagulation factor Xa."
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.
EMBO J. 16:5151-5161(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-127.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24422 mRNA. Translation: AAA29192.1.
M24423 mRNA. Translation: AAA29193.1.
PIRA28806.
A34398.
JS0209.
S13904.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SKZX-ray1.90A20-136[»]
ProteinModelPortalP15358.
SMRP15358. Positions 24-127.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSI15.007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.10.22.10. 2 hits.
InterProIPR004094. Antistasin-like.
IPR011061. Hirudin/antistatin.
IPR008086. Prot_inh_I15_antistasin_leech.
[Graphical view]
PfamPF02822. Antistasin. 1 hit.
[Graphical view]
PRINTSPR01706. ANTISTASIN.
SUPFAMSSF57262. SSF57262. 2 hits.
PROSITEPS51252. ANTISTASIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15358.

Entry information

Entry nameANTA_HAEOF
AccessionPrimary (citable) accession number: P15358
Secondary accession number(s): Q9TWQ8, Q9TX45
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references