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P15358

- ANTA_HAEOF

UniProt

P15358 - ANTA_HAEOF

Protein

Antistasin

Gene
N/A
Organism
Haementeria officinalis (Mexican leech)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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 – 284
    Turni38 – 403
    Beta strandi58 – 603
    Beta strandi66 – 705
    Helixi81 – 833
    Turni92 – 943
    Beta strandi95 – 973
    Beta strandi99 – 1013
    Beta strandi113 – 1153
    Beta strandi121 – 1255

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MIKLAILLLF TVAIVRCQGP FGPGCEEAGC PEGSACNIIT DRCTCSGVRC    50
    RMHCPHGFQR SRYGCEFCKC RLEPMKATCD ISECPEGMMC SRLTNKCDCK 100
    IDINCRKTCP NGLKRDKLGC EYCECRPKRK LIPRLS 136
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24422 mRNA. Translation: AAA29192.1.
    M24423 mRNA. Translation: AAA29193.1.
    PIRiA28806.
    A34398.
    JS0209.
    S13904.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24422 mRNA. Translation: AAA29192.1 .
    M24423 mRNA. Translation: AAA29193.1 .
    PIRi A28806.
    A34398.
    JS0209.
    S13904.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SKZ X-ray 1.90 A 20-136 [» ]
    ProteinModelPortali P15358.
    SMRi P15358. Positions 24-127.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi I15.007.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P15358.

    Family and domain databases

    Gene3Di 2.10.22.10. 2 hits.
    InterProi IPR004094. Antistasin-like.
    IPR011061. Hirudin/antistatin.
    IPR008086. Prot_inh_I15_antistasin_leech.
    [Graphical view ]
    Pfami PF02822. Antistasin. 1 hit.
    [Graphical view ]
    PRINTSi PR01706. ANTISTASIN.
    SUPFAMi SSF57262. SSF57262. 2 hits.
    PROSITEi PS51252. ANTISTASIN. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    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(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.

    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: October 1, 2014
    This is version 94 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