Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein C activator

Gene
N/A
Organism
Agkistrodon contortrix contortrix (Southern copperhead)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Snake venom serine protease that selectively cleaves the heavy chain of protein C (PROC). This activation is thrombomodulin-independent.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei40Charge relay system1 Publication1
Active sitei85Charge relay system1 Publication1
Active sitei177Charge relay system1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade inhibiting toxin, Hemostasis impairing toxin, Hydrolase, Protease, Serine protease, Toxin

Protein family/group databases

MEROPSiS01.466.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein C activator (EC:3.4.21.-)
Alternative name(s):
ACC-C
Snake venom serine protease
Short name:
SVSP
OrganismiAgkistrodon contortrix contortrix (Southern copperhead)
Taxonomic identifieri8713 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeAgkistrodon

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

Is used in diagnostic practice for the determination of disorders in the PC pathway. Functional assays are either clotting assays or based on determinations using chromogenic assays. Sold under the name Protac by Pentapharm.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000887261 – 231Protein C activatorAdd BLAST231

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi7 ↔ 138PROSITE-ProRule annotation1 Publication
Glycosylationi21N-linked (GlcNAc...)2 Publications1
Disulfide bondi25 ↔ 41PROSITE-ProRule annotation1 Publication
Disulfide bondi73 ↔ 229PROSITE-ProRule annotation1 Publication
Glycosylationi78N-linked (GlcNAc...)2 Publications1
Disulfide bondi117 ↔ 183PROSITE-ProRule annotation1 Publication
Glycosylationi129N-linked (GlcNAc...)2 Publications1
Disulfide bondi149 ↔ 162PROSITE-ProRule annotation1 Publication
Disulfide bondi173 ↔ 198PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 20Combined sources6
Beta strandi23 – 29Combined sources7
Beta strandi31 – 37Combined sources7
Helixi39 – 41Combined sources3
Beta strandi47 – 51Combined sources5
Beta strandi63 – 65Combined sources3
Beta strandi67 – 71Combined sources5
Beta strandi78 – 80Combined sources3
Turni81 – 84Combined sources4
Beta strandi87 – 93Combined sources7
Beta strandi116 – 123Combined sources8
Beta strandi125 – 129Combined sources5
Beta strandi137 – 144Combined sources8
Helixi146 – 152Combined sources7
Beta strandi158 – 164Combined sources7
Beta strandi180 – 183Combined sources4
Beta strandi186 – 194Combined sources9
Beta strandi205 – 209Combined sources5
Helixi210 – 213Combined sources4
Helixi214 – 222Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AIPX-ray1.65A1-231[»]
2AIQX-ray1.54A1-231[»]
ProteinModelPortaliP09872.
SMRiP09872.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09872.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 222Peptidase S1PROSITE-ProRule annotationAdd BLAST222

Sequence similaritiesi

Belongs to the peptidase S1 family. Snake venom subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG013304.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09872-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VIGGDECNIN EHRFLALVYA NGSLCGGTLI NQEWVLTARH CDRGNMRIYL
60 70 80 90 100
GMHNLKVLNK DALRRFPKEK YFCLNTRNDT IWDKDIMLIR LNRPVRNSAH
110 120 130 140 150
IAPLSLPSNP PSVGSVCRIM GWGTITSPNA TLPDVPHCAN INILDYAVCQ
160 170 180 190 200
AAYKGLAATT LCAGILEGGK DTCKGDSGGP LICNGQFQGI LSVGGNPCAQ
210 220 230
PRKPGIYTKV FDYTDWIQSI ISGNTDATCP P
Length:231
Mass (Da):25,106
Last modified:February 1, 1994 - v2
Checksum:iDC3D7CBE601EC52B
GO

Sequence databases

PIRiA60468.

Cross-referencesi

Sequence databases

PIRiA60468.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AIPX-ray1.65A1-231[»]
2AIQX-ray1.54A1-231[»]
ProteinModelPortaliP09872.
SMRiP09872.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.466.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG013304.

Miscellaneous databases

EvolutionaryTraceiP09872.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVSPCA_AGKCO
AccessioniPrimary (citable) accession number: P09872
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1994
Last modified: November 2, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.