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Protein

Antistasin

Gene
N/A
Organism
Haementeria officinalis (Mexican leech)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei51 – 522Reactive bond
Sitei106 – 1072Reactive bond

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  1. blood coagulation Source: UniProtKB-KW
  2. negative regulation of coagulation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Heparin-binding

Protein family/group databases

MEROPSiI15.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Antistasin
Short name:
ATS
Alternative name(s):
Blood coagulation factor Xa/proclotting enzyme inhibitor
OrganismiHaementeria officinalis (Mexican leech)
Taxonomic identifieri6410 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaRhynchobdellidaGlossiphoniidaeHaementeria

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17172 PublicationsAdd
BLAST
Chaini18 – 136119AntistasinPRO_0000001700Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Pyrrolidone carboxylic acid
Disulfide bondi25 ↔ 36
Disulfide bondi30 ↔ 43
Disulfide bondi45 ↔ 65
Disulfide bondi50 ↔ 68
Disulfide bondi54 ↔ 70
Disulfide bondi79 ↔ 90
Disulfide bondi84 ↔ 97
Disulfide bondi99 ↔ 120
Disulfide bondi105 ↔ 123
Disulfide bondi109 ↔ 125

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1
136
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 284Combined sources
Turni38 – 403Combined sources
Beta strandi58 – 603Combined sources
Beta strandi66 – 705Combined sources
Helixi81 – 833Combined sources
Turni92 – 943Combined sources
Beta strandi95 – 973Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi121 – 1255Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SKZX-ray1.90A20-136[»]
ProteinModelPortaliP15358.
SMRiP15358. Positions 24-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15358.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 7026Antistasin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini100 – 12526Antistasin-like 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni114 – 1174Heparin-bindingSequence Analysis
Regioni128 – 1358Heparin-bindingSequence Analysis

Sequence similaritiesi

Contains 2 antistasin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.10.22.10. 2 hits.
InterProiIPR004094. Antistasin-like.
IPR011061. Hirudin/antistatin.
IPR008086. Prot_inh_I15_antistasin_leech.
[Graphical view]
PfamiPF02822. Antistasin. 1 hit.
[Graphical view]
PRINTSiPR01706. ANTISTASIN.
SUPFAMiSSF57262. SSF57262. 2 hits.
PROSITEiPS51252. ANTISTASIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15358-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKLAILLLF TVAIVRCQGP FGPGCEEAGC PEGSACNIIT DRCTCSGVRC
60 70 80 90 100
RMHCPHGFQR SRYGCEFCKC RLEPMKATCD ISECPEGMMC SRLTNKCDCK
110 120 130
IDINCRKTCP NGLKRDKLGC EYCECRPKRK LIPRLS
Length:136
Mass (Da):15,225
Last modified:February 1, 1991 - v2
Checksum:i582AF009ED9A0291
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221G → R in isoform B.
Natural varianti47 – 471G → E.
Natural varianti52 – 521M → V.
Natural varianti71 – 711R → I.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24422 mRNA. Translation: AAA29192.1.
M24423 mRNA. Translation: AAA29193.1.
PIRiA28806.
A34398.
JS0209.
S13904.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24422 mRNA. Translation: AAA29192.1.
M24423 mRNA. Translation: AAA29193.1.
PIRiA28806.
A34398.
JS0209.
S13904.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SKZX-ray1.90A20-136[»]
ProteinModelPortaliP15358.
SMRiP15358. Positions 24-127.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiI15.007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP15358.

Family and domain databases

Gene3Di2.10.22.10. 2 hits.
InterProiIPR004094. Antistasin-like.
IPR011061. Hirudin/antistatin.
IPR008086. Prot_inh_I15_antistasin_leech.
[Graphical view]
PfamiPF02822. Antistasin. 1 hit.
[Graphical view]
PRINTSiPR01706. ANTISTASIN.
SUPFAMiSSF57262. SSF57262. 2 hits.
PROSITEiPS51252. ANTISTASIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1988) [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(1987) [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(1992) [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(1988) [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(1988) [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(1991) [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(1993) [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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-127.

Entry informationi

Entry nameiANTA_HAEOF
AccessioniPrimary (citable) accession number: P15358
Secondary accession number(s): Q9TWQ8, Q9TX45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1991
Last modified: January 7, 2015
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.