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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)DescriptionActionsGraphical viewLength
Sitei51 – 52Reactive bond2
Sitei106 – 107Reactive bond2

GO - Molecular functioni

GO - Biological processi

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 172 PublicationsAdd BLAST17
ChainiPRO_000000170018 – 136AntistasinAdd BLAST119

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei18Pyrrolidone carboxylic acid1
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

1136
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 28Combined sources4
Turni38 – 40Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi66 – 70Combined sources5
Helixi81 – 83Combined sources3
Turni92 – 94Combined sources3
Beta strandi95 – 97Combined sources3
Beta strandi99 – 101Combined sources3
Beta strandi113 – 115Combined sources3
Beta strandi121 – 125Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP15358.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 70Antistasin-like 1PROSITE-ProRule annotationAdd BLAST26
Domaini100 – 125Antistasin-like 2PROSITE-ProRule annotationAdd BLAST26

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni114 – 117Heparin-bindingSequence analysis4
Regioni128 – 135Heparin-bindingSequence analysis8

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)DescriptionActionsGraphical viewLength
Natural varianti22G → R in isoform B. 1
Natural varianti47G → E.1
Natural varianti52M → V.1
Natural varianti71R → I.1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SKZX-ray1.90A20-136[»]
ProteinModelPortaliP15358.
SMRiP15358.
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...

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: November 2, 2016
This is version 102 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

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 one 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.