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Venom prothrombin activator pseutarin-C catalytic subunit (PCCS) (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Pseutarin-C catalytic subunit light chain; Pseutarin-C catalytic subunit heavy chain]

 FAXC_PSETE              Reviewed;         467 AA.
Q56VR3; A5X463; Q6IT09; Q6IT10;
31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 2.
02-JUN-2021, entry version 109.
RecName: Full=Venom prothrombin activator pseutarin-C catalytic subunit;
Short=PCCS;
Short=vPA;
EC=3.4.21.6 {ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:23869089};
AltName: Full=Venom coagulation factor Xa-like protease;
Contains:
RecName: Full=Pseutarin-C catalytic subunit light chain;
Contains:
RecName: Full=Pseutarin-C catalytic subunit heavy chain;
Flags: Precursor;
Pseudonaja textilis (Eastern brown snake).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
NCBI_TaxID=8673;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 41-70;
77-119; 142-177; 210-242 AND 271-281, TOXIC DOSE, GLYCOSYLATION AT SER-92
AND ASN-254, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Venom gland;
PubMed=15351847; DOI=10.1160/th04-03-0144;
Rao V.S., Swarup S., Kini R.M.;
"The catalytic subunit of pseutarin C, a group C prothrombin activator from
the venom of Pseudonaja textilis, is structurally similar to mammalian
blood coagulation factor Xa.";
Thromb. Haemost. 92:509-521(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=16197456; DOI=10.1111/j.1365-2141.2005.05744.x;
Filippovich I., Sorokina N., St Pierre L., Flight S., de Jersey J.,
Perry N., Masci P.P., Lavin M.F.;
"Cloning and functional expression of venom prothrombin activator protease
from Pseudonaja textilis with whole blood procoagulant activity.";
Br. J. Haematol. 131:237-246(2005).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
PubMed=17239167; DOI=10.1111/j.1538-7836.2006.02266.x;
Reza M.A., Swarup S., Kini R.M.;
"Structure of two genes encoding parallel prothrombin activators in
Tropidechis carinatus snake: gene duplication and recruitment of factor X
gene to the venom gland.";
J. Thromb. Haemost. 5:117-126(2007).
[4]
PROTEIN SEQUENCE OF 41-70 AND 210-246, FUNCTION, CATALYTIC ACTIVITY,
ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47; GLU-54; GLU-56; GLU-59; GLU-60;
GLU-65 AND GLU-66.
TISSUE=Venom;
PubMed=12362232; DOI=10.1267/th02100611;
Rao V.S., Kini R.M.;
"Pseutarin C, a prothrombin activator from Pseudonaja textilis venom: its
structural and functional similarity to mammalian coagulation factor Xa-Va
complex.";
Thromb. Haemost. 88:611-619(2002).
[5]
TOXIC DOSE, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=Pseudonaja textilis textilis; TISSUE=Venom;
PubMed=3075905;
Masci P.P., Whitaker A.N., de Jersey J.;
"Purification and characterization of a prothrombin activator from the
venom of the Australian brown snake, Pseudonaja textilis textilis.";
Biochem. Int. 17:825-835(1988).
[6]
NOMENCLATURE.
PubMed=11522026;
Manjunatha Kini R., Morita T., Rosing J.;
"Classification and nomenclature of prothrombin activators isolated from
snake venoms.";
Thromb. Haemost. 86:710-711(2001).
[7]
PHARMACEUTICAL.
PubMed=21184772; DOI=10.1016/j.toxicon.2010.12.010;
Earl S.T., Masci P.P., de Jersey J., Lavin M.F., Dixon J.;
"Drug development from Australian elapid snake venoms and the Venomics
pipeline of candidates for haemostasis: Textilinin-1 (Q8008), Haempatch
(Q8009) and CoVase (V0801).";
Toxicon 59:456-463(2012).
[8] {ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW}
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 41-463 IN COMPLEX WITH
PSEUTARIN-C NON-CATALYTIC SUBUNIT, DISULFIDE BONDS, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=23869089; DOI=10.1182/blood-2013-06-511733;
Lechtenberg B.C., Murray-Rust T.A., Johnson D.J., Adams T.E.,
Krishnaswamy S., Camire R.M., Huntington J.A.;
"Crystal structure of the prothrombinase complex from the venom of
Pseudonaja textilis.";
Blood 122:2777-2783(2013).
-!- FUNCTION: Snake prothrombin activator that attacks the hemostatic
system of prey. This non-catalytic subunit is functionally similar to
blood coagulation factor V (PubMed:12362232, PubMed:23869089). It
serves as a critical cofactor for the prothrombinase activity of the
catalytic subunit, which is similar to the blood coagulation factor X
(PubMed:12362232, PubMed:23869089). The complex converts prothrombin to
thrombin by sequential cleavage at two positions, Arg-320 followed by
Arg-271 (PubMed:23869089). Cleavage at Arg-320 produces an active
intermediate known as meizothrombin (PubMed:23869089). Meizothrombin is
the 'second' substrate for prothrombinase, and it docks in an altered
manner to present the second cleavage site (271) (PubMed:23869089).
Cleavage at Arg-271 releases active thrombin from its pro-fragment
(PubMed:23869089). This order of events is reversed if the protease
component of prothrombinase is used on its own, suggesting that the 271
site is inherently more accessible to proteolysis (PubMed:23869089).
The complex converts prothrombin to thrombin in presence but also in
the absence of membrane (PubMed:23869089).
{ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:23869089}.
-!- CATALYTIC ACTIVITY:
Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in
prothrombin to form thrombin.; EC=3.4.21.6;
Evidence={ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:23869089};
-!- ACTIVITY REGULATION: Activated by calcium and negatively charged
phospholipids. {ECO:0000269|PubMed:12362232,
ECO:0000269|PubMed:23869089}.
-!- SUBUNIT: Heterodimer of a light and a heavy chains; disulfide-linked.
Is associated with pseutarin-C non-catalytic subunit (AC Q7SZN0) in a
non-covalent manner. {ECO:0000269|PubMed:12362232,
ECO:0000269|PubMed:23869089, ECO:0000269|PubMed:3075905}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12362232,
ECO:0000269|PubMed:3075905}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:3075905}.
-!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent
carboxylation. These residues are essential for the binding of calcium.
{ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12362232}.
-!- TOXIC DOSE: Intravenous injection (23 ug/kg bodyweight) of the group C
prothrombin activator causes death in rats through disseminated
intravascular coagulopathy (PubMed:3075905), whereas pseutarin-C is not
lethal even at 10 mg/kg in mice when injected intraperitoneally
(PubMed:15351847). {ECO:0000269|PubMed:15351847,
ECO:0000269|PubMed:3075905}.
-!- PHARMACEUTICAL: Is under preclinical trial by the Australian
biopharmaceutical company QRxPharma Ltd, its subsidiary Venomics Pty
Ltd (VPL) and the University of Queensland (UQ) under the name
Haempatch (Q8009). Tested as a topical hemostatic agent to reduce blood
loss resulting from surgery or trauma.
-!- MISCELLANEOUS: Is classified in the group C of snake venom prothrombin
activators, since it does not require the mammalian factor Va for the
cleavage of prothrombin as the venom contains its own non-catalytic
factor Va-like molecule. {ECO:0000305|PubMed:21184772}.
-!- MISCELLANEOUS: In contrast to blood coagulation factors that circulate
as inactive zymogen in plasma, venom prothrombin activators are always
found in the active form in the venom. Hence, catalytic and non-
catalytic subunits are found naturally in venom as stable complexes.
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; AY260939; AAP86642.1; -; mRNA.
EMBL; AY631239; AAT42491.1; -; mRNA.
EMBL; DQ533835; ABG02407.1; -; Genomic_DNA.
EMBL; AY631238; AAT42490.1; -; mRNA.
PDB; 4BXS; X-ray; 3.32 A; A=41-463.
PDB; 4BXW; X-ray; 2.71 A; A/B=41-463.
PDBsum; 4BXS; -.
PDBsum; 4BXW; -.
SMR; Q56VR3; -.
MEROPS; S01.446; -.
iPTMnet; Q56VR3; -.
BRENDA; 3.4.21.60; 6821.
Proteomes; UP000472273; Unplaced.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; IEA:InterPro.
GO; GO:0044469; P:envenomation resulting in positive regulation of blood coagulation in other organism; IDA:UniProtKB.
GO; GO:0035807; P:positive regulation of blood coagulation in other organism; IDA:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 2.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR012224; Pept_S1A_FX.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00008; EGF; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001143; Factor_X; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00069; GLA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57184; SSF57184; 1.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Blood coagulation cascade activating toxin; Calcium;
Cleavage on pair of basic residues; Direct protein sequencing;
Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
Hemostasis impairing toxin; Hydrolase; Pharmaceutical; Protease;
Prothrombin activator; Reference proteome; Repeat; Secreted;
Serine protease; Signal; Toxin.
SIGNAL 1..22
/evidence="ECO:0000255"
PROPEP 23..40
/evidence="ECO:0000269|PubMed:12362232,
ECO:0000269|PubMed:15351847"
/id="PRO_0000408523"
CHAIN 41..181
/note="Pseutarin-C catalytic subunit light chain"
/id="PRO_5000090539"
PROPEP 182..209
/note="Activation peptide"
/evidence="ECO:0000250"
/id="PRO_0000408525"
CHAIN 210..467
/note="Pseutarin-C catalytic subunit heavy chain"
/id="PRO_0000408526"
DOMAIN 41..86
/note="Gla"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
DOMAIN 86..122
/note="EGF-like 1; calcium-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 129..164
/note="EGF-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 210..454
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
ACT_SITE 251
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 309
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 406
/note="Charge relay system"
/evidence="ECO:0000250"
SITE 75
/note="Not modified"
/evidence="ECO:0000305"
SITE 103
/note="Not modified"
SITE 209..210
/note="Cleavage"
MOD_RES 46
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12362232"
MOD_RES 47
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12362232"
MOD_RES 54
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12362232"
MOD_RES 56
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12362232"
MOD_RES 59
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12362232"
MOD_RES 60
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12362232"
MOD_RES 65
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12362232"
MOD_RES 66
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:12362232"
MOD_RES 69
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 72
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
CARBOHYD 92
/note="O-linked (Hex...) serine"
/evidence="ECO:0000269|PubMed:15351847"
CARBOHYD 254
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15351847"
DISULFID 57..62
/evidence="ECO:0000250"
DISULFID 90..101
/evidence="ECO:0000250|UniProtKB:P00742"
DISULFID 95..110
/evidence="ECO:0000250|UniProtKB:P00742"
DISULFID 112..121
/evidence="ECO:0000250|UniProtKB:P00742"
DISULFID 129..140
/evidence="ECO:0000269|PubMed:23869089,
ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
DISULFID 136..149
/evidence="ECO:0000269|PubMed:23869089,
ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
DISULFID 151..164
/evidence="ECO:0000269|PubMed:23869089,
ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
DISULFID 172..329
/note="Interchain (between light and heavy chains)"
/evidence="ECO:0000269|PubMed:23869089,
ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
DISULFID 216..221
/evidence="ECO:0000269|PubMed:23869089,
ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
DISULFID 236..252
/evidence="ECO:0000269|PubMed:23869089,
ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
DISULFID 377..391
/evidence="ECO:0000269|PubMed:23869089,
ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
DISULFID 402..430
/evidence="ECO:0000269|PubMed:23869089,
ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
CONFLICT 39
/note="K -> E (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 70
/note="V -> A (in Ref. 1; AAP86642)"
/evidence="ECO:0000305"
CONFLICT 142
/note="S -> H (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 185
/note="S -> N (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 193
/note="H -> Q (in Ref. 1; AAP86642 and 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 196
/note="T -> P (in Ref. 1; AAP86642)"
/evidence="ECO:0000305"
CONFLICT 200
/note="K -> I (in Ref. 1; AAP86642)"
/evidence="ECO:0000305"
CONFLICT 230..232
/note="DKK -> EKE (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 268..271
/note="RSRA -> KSRI (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 282
/note="V -> I (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 292..305
/note="KKSQEFYEKFDLVS -> QKAYKFDLAA (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 353..360
/note="GIFERGPN -> RIVEKGPK (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 379..388
/note="LSSNFPITPT -> VSSETPITPN (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 399
/note="Q -> R (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 411..413
/note="ITA -> TTV (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 426
/note="W -> S (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 433..438
/note="KGRYGI -> NGKYGN (in Ref. 8; AAT42490)"
/evidence="ECO:0000305"
CONFLICT 450..467
/note="Missing (in Ref. 1; AAP86642)"
/evidence="ECO:0000305"
TURN 128..132
/evidence="ECO:0007829|PDB:4BXS"
HELIX 133..135
/evidence="ECO:0007829|PDB:4BXW"
STRAND 137..141
/evidence="ECO:0007829|PDB:4BXW"
STRAND 144..146
/evidence="ECO:0007829|PDB:4BXS"
STRAND 148..150
/evidence="ECO:0007829|PDB:4BXW"
STRAND 155..157
/evidence="ECO:0007829|PDB:4BXW"
STRAND 164..168
/evidence="ECO:0007829|PDB:4BXW"
TURN 218..220
/evidence="ECO:0007829|PDB:4BXS"
STRAND 224..229
/evidence="ECO:0007829|PDB:4BXW"
TURN 230..232
/evidence="ECO:0007829|PDB:4BXW"
STRAND 233..240
/evidence="ECO:0007829|PDB:4BXW"
STRAND 242..248
/evidence="ECO:0007829|PDB:4BXW"
HELIX 250..252
/evidence="ECO:0007829|PDB:4BXW"
STRAND 253..257
/evidence="ECO:0007829|PDB:4BXW"
STRAND 260..264
/evidence="ECO:0007829|PDB:4BXW"
HELIX 268..273
/evidence="ECO:0007829|PDB:4BXW"
STRAND 279..285
/evidence="ECO:0007829|PDB:4BXW"
HELIX 291..295
/evidence="ECO:0007829|PDB:4BXW"
TURN 305..308
/evidence="ECO:0007829|PDB:4BXW"
STRAND 311..317
/evidence="ECO:0007829|PDB:4BXW"
HELIX 333..338
/evidence="ECO:0007829|PDB:4BXW"
HELIX 340..342
/evidence="ECO:0007829|PDB:4BXW"
STRAND 343..351
/evidence="ECO:0007829|PDB:4BXW"
STRAND 353..355
/evidence="ECO:0007829|PDB:4BXW"
STRAND 365..371
/evidence="ECO:0007829|PDB:4BXW"
HELIX 374..378
/evidence="ECO:0007829|PDB:4BXW"
STRAND 389..392
/evidence="ECO:0007829|PDB:4BXW"
STRAND 395..398
/evidence="ECO:0007829|PDB:4BXW"
STRAND 409..414
/evidence="ECO:0007829|PDB:4BXW"
STRAND 417..426
/evidence="ECO:0007829|PDB:4BXW"
STRAND 428..431
/evidence="ECO:0007829|PDB:4BXW"
STRAND 437..440
/evidence="ECO:0007829|PDB:4BXW"
HELIX 442..444
/evidence="ECO:0007829|PDB:4BXW"
HELIX 446..452
/evidence="ECO:0007829|PDB:4BXW"
SEQUENCE 467 AA; 52215 MW; C773D41DB08F9844 CRC64;
MAPQLLLCLI LTFLWSLPEA ESNVFLKSKV ANRFLQRTKR ANSLVEEFKS GNIERECIEE
RCSKEEAREV FEDDEKTETF WNVYVDGDQC SSNPCHYRGI CKDGIGSYTC TCLSGYEGKN
CERVLYKSCR VDNGNCWHFC KSVQNDIQCS CAEGYLLGED GHSCVAGGNF SCGRNIKTRN
KREASLPDFV QSHNATLLKK SDNPSPDIRI VNGMDCKLGE CPWQAALVDD KKGVFCGGTI
LSPIYVLTAA HCINETETIS VVVGEIDRSR AETGPLLSVD KVYVHKKFVP PKKSQEFYEK
FDLVSYDYDI AIIQMKTPIQ FSENVVPACL PTADFANQVL MKQDFGIVSG FGGIFERGPN
SKTLKVLKVP YVDRHTCMLS SNFPITPTMF CAGYDTLPQD ACQGDSGGPH ITAYRDTHFI
TGIVSWGEGC ARKGRYGIYT KLSKFIPWIK RIMRQKLPST ESSTGRL


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EIAAB31926 Calcineurin, testis-specific catalytic subunit,Calmodulin-dependent calcineurin A subunit gamma isoform,CALNA3,CAM-PRP catalytic subunit,CNA3,Homo sapiens,Human,PPP3CC,Serine_threonine-protein phospha
EIAAB32388 DNA-dependent protein kinase catalytic subunit,DNA-PK catalytic subunit,DNA-PKcs,Mouse,Mus musculus,p460,Prkdc,Xrcc7
EIAAB32387 DNA-dependent protein kinase catalytic subunit,DNA-PK catalytic subunit,DNA-PKcs,DNPK1,Homo sapiens,Human,HYRC,HYRC1,p460,PRKDC
EIAAB31922 Calmodulin-dependent calcineurin A subunit alpha isoform,CALNA,CAM-PRP catalytic subunit,CNA,Homo sapiens,Human,PPP3CA,Serine_threonine-protein phosphatase 2B catalytic subunit alpha isoform
EIAAB31923 Calmodulin-dependent calcineurin A subunit beta isoform,CALNA2,CALNB,CAM-PRP catalytic subunit,CNA2,Homo sapiens,Human,PPP3CB,Serine_threonine-protein phosphatase 2B catalytic subunit beta isoform
EIAAB31924 Calmodulin-dependent calcineurin A subunit beta isoform,Calnb,CAM-PRP catalytic subunit,Mouse,Mus musculus,Ppp3cb,Serine_threonine-protein phosphatase 2B catalytic subunit beta isoform
EIAAB31921 Calmodulin-dependent calcineurin A subunit alpha isoform,Calna,CAM-PRP catalytic subunit,Ppp3ca,Rat,Rattus norvegicus,Serine_threonine-protein phosphatase 2B catalytic subunit alpha isoform
EIAAB31920 Calmodulin-dependent calcineurin A subunit alpha isoform,Calna,CAM-PRP catalytic subunit,Mouse,Mus musculus,Ppp3ca,Serine_threonine-protein phosphatase 2B catalytic subunit alpha isoform
EIAAB31925 Calmodulin-dependent calcineurin A subunit beta isoform,CAM-PRP catalytic subunit,Ppp3cb,Rat,Rattus norvegicus,Serine_threonine-protein phosphatase 2B catalytic subunit beta isoform
EIAAB31919 Bos taurus,Bovine,Calmodulin-dependent calcineurin A subunit alpha isoform,CAM-PRP catalytic subunit,PPP3CA,Serine_threonine-protein phosphatase 2B catalytic subunit alpha isoform
EIAAB32386 Chicken,DNA-dependent protein kinase catalytic subunit,DNA-PK catalytic subunit,DNA-PKcs,Gallus gallus,PRKDC,XRCC7
EIAAB31889 Homo sapiens,Human,PP-1G,PPP1CC,Protein phosphatase 1C catalytic subunit,Serine_threonine-protein phosphatase PP1-gamma catalytic subunit
EIAAB32385 Canis familiaris,Canis lupus familiaris,DNA-dependent protein kinase catalytic subunit,DNA-PK catalytic subunit,DNA-PKcs,Dog,PRKDC
EIAAB11823 DNA polymerase alpha catalytic subunit,DNA polymerase alpha catalytic subunit p180,Homo sapiens,Human,POLA,POLA1
18-783-75678 RABBIT ANTI Cdk5 (C-TERMINAL) - EC 2.7.11.22; Cyclin-dependent kinase 5; Tau protein kinase II catalytic subunit; TPKII catalytic subunit; Serine_threonine-protein kinase PSSALRE Polyclonal 0.05 ml
EIAAB11824 DNA polymerase alpha catalytic subunit,DNA polymerase alpha catalytic subunit p180,Pola,Pola1,Rat,Rattus norvegicus
EIAAB31887 Mouse,Mus musculus,PP-1G,Ppp1cc,Protein phosphatase 1C catalytic subunit,Serine_threonine-protein phosphatase PP1-gamma catalytic subunit
EIAAB11822 DNA polymerase alpha catalytic subunit,DNA polymerase alpha catalytic subunit p180,Mouse,Mus musculus,Pola,Pola1
EIAAB31890 Bos taurus,Bovine,PP-1G,PPP1CC,Protein phosphatase 1C catalytic subunit,Serine_threonine-protein phosphatase PP1-gamma catalytic subunit
EIAAB31891 PP-1G,Ppp1cc,Protein phosphatase 1C catalytic subunit,Rat,Rattus norvegicus,Serine_threonine-protein phosphatase PP1-gamma catalytic subunit
E0739h ELISA CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Homo sapiens,Human,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
U0739h CLIA CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Homo sapiens,Human,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
E0739r ELISA Cdk5,Cdkn5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Rat,Rattus norvegicus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
U0739r CLIA Cdk5,Cdkn5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Rat,Rattus norvegicus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
Pathways :
WP1626: Benzoate degradation via CoA ligation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1634: Butanoate metabolism
WP688: Catalytic cycle of mammalian FMOs
WP1694: Pyrimidine metabolism
WP1574: Catalytic cycle of mammalian FMOs
WP1718: Vitamin B6 metabolism
WP1663: Homologous recombination
WP2292: Chemokine signaling pathway
WP1672: Mismatch repair
WP1693: Purine metabolism
WP1566: Citrate cycle (TCA cycle)
WP1711: Trinitrotoluene degradation
WP1644: DNA replication
WP1655: Geraniol degradation
WP2272: Pathogenic Escherichia coli infection
WP1671: Methane metabolism
WP1680: Oxidative phosphorylation
WP1002: Electron Transport Chain
WP111: Electron Transport Chain
WP1654: gamma-Hexachlorocyclohexane degradation
WP1665: Limonene and pinene degradation
WP1339: Electron Transport Chain
WP1673: Naphthalene and anthracene degradation
WP1633: Bisphenol A degradation

Related Genes :
[] Venom prothrombin activator pseutarin-C catalytic subunit (PCCS) (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Pseutarin-C catalytic subunit light chain; Pseutarin-C catalytic subunit heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Stuart-Prower factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[] Coagulation factor X-activating enzyme heavy chain (EC 3.4.24.58) (Coagulation factor X-activating enzyme chain alpha) (Snake venom metalloproteinase) (SVMP) (VL factor X activator) (VLFXA heavy chain) [Cleaved into: Coagulation factor X-activating enzyme heavy chain alternate form]
[F10 FX] Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Virus-activating protease) (VAP) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F2] Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Proconvertin) (Serum prothrombin conversion accelerator) (SPCA) (Eptacog alfa) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F9] Coagulation factor IX (EC 3.4.21.22) (Christmas factor) (Plasma thromboplastin component) (PTC) [Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F7 Cf7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[HABP2 HGFAL PHBP] Hyaluronan-binding protein 2 (EC 3.4.21.-) (Factor VII-activating protease) (Factor seven-activating protease) (FSAP) (Hepatocyte growth factor activator-like protein) (Plasma hyaluronan-binding protein) [Cleaved into: Hyaluronan-binding protein 2 50 kDa heavy chain; Hyaluronan-binding protein 2 50 kDa heavy chain alternate form; Hyaluronan-binding protein 2 27 kDa light chain; Hyaluronan-binding protein 2 27 kDa light chain alternate form]
[PROC] Vitamin K-dependent protein C (EC 3.4.21.69) (Anticoagulant protein C) (Autoprothrombin IIA) (Blood coagulation factor XIV) [Cleaved into: Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; Activation peptide]
[F10 TrFX] Coagulation factor X (EC 3.4.21.6) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[] Factor V activator (FVA) (VLFVA) (EC 3.4.21.95) (Lebetina viper venom FV activator) (LVV-V) (Snake venom serine protease) (SVSP)
[] Genome polyprotein [Cleaved into: Peptide 2k; Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease/Helicase NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[Tmprss11c] Transmembrane protease serine 11C (EC 3.4.21.-) (Neurobin) [Cleaved into: Transmembrane protease serine 11C non-catalytic chain; Transmembrane protease serine 11C catalytic chain]
[F5] Coagulation factor V (Activated protein C cofactor) (Proaccelerin, labile factor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[Cfi If] Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain]
[Masp1 Crarf Masp3] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[F12] Coagulation factor XII (EC 3.4.21.38) (Hageman factor) (HAF) [Cleaved into: Coagulation factor XIIa heavy chain; Beta-factor XIIa part 1; Coagulation factor XIIa light chain (Beta-factor XIIa part 2)]
[F11] Coagulation factor XI (FXI) (EC 3.4.21.27) (Plasma thromboplastin antecedent) (PTA) [Cleaved into: Coagulation factor XIa heavy chain; Coagulation factor XIa light chain]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

Bibliography :