Vipera russelli

034 Vipera russelli proteinase RVV-V alpha (Factor V-activating proteinase alpha) (Snake venom factor V activator alpha)

No.034
LOCUS    P18964
DEFINITION Vipera russelli proteinase RVV-V alpha (Factor V-activating proteinase alpha) (Snake venom factor V activator alpha).
SOURCE Daboia russellii siamensis
COMMENT
[FUNCTION] RVV-V induces the coagulation of mammalian plasma. It activates factor V in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule.
[CATALYTIC ACTIVITY] Fully activates human clotting factor V by a single cleavage at the 1545-Trp-Tyr-Leu-Arg-|-Ser-Asn-Asn-Gly-1552 bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO(2).
[SUBCELLULAR LOCATION] Secreted protein.
[TISSUE SPECIFICITY] Expressed by the venom gland.
[MISCELLANEOUS] There are three isoproteins of RVV-V, designated RVV-V alpha, V-beta, and V-gamma.
[SIMILARITY] Belongs to the peptidase S1 family. Snake venom subfamily.
[SIMILARITY] Contains 1 peptidase S1 domain.
FEATURES EC_number="3.4.21.95"
ORIGIN
001 vvggdecnin ehpflvalyt stsstihcgg alinrewvlt aahcdrrnir iklgmhskni
061 rnedeqirvp rgkyfclntk fpngldkdim lirlrrpvty sthiapvslp srsrgvgsrc
121 rimgwgkist tedtypdvph ctnifivkhk wceplypwvp adsrtlcagi lkggrdtchg
181 dsggplicng qiqgivaggs epcgqhlkpa vytkvfdynn wiqniiagnr tvtcpp
LENGTH 236 aa
MOLECULAR WEIGHT 26182 Da

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035 Vipera russelli proteinase RVV-V gamma (Factor V-activating proteinase gamma) (Snake venom factor V activator gamma)

No.035
LOCUS    P18965
DEFINITION Vipera russelli proteinase RVV-V gamma (Factor V-activating proteinase gamma) (Snake venom factor V activator gamma).
SOURCE Daboia russellii siamensis
COMMENT
[FUNCTION] RVV-V induce the coagulation of mammalian plasma. It activates factor V in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule.
[CATALYTIC ACTIVITY] Fully activates human clotting factor V by a single cleavage at the 1545-Trp-Tyr-Leu-Arg-|-Ser-Asn-Asn-Gly-1552 bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO(2).
[SUBCELLULAR LOCATION] Secreted protein.
[TISSUE SPECIFICITY] Expressed by the venom gland.
[MISCELLANEOUS] There are three isoproteins of RVV-V, designated RVV-V alpha, V-beta, and V-gamma.
[SIMILARITY] Belongs to the peptidase S1 family. Snake venom subfamily.
[SIMILARITY] Contains 1 peptidase S1 domain.
FEATURES EC_number="3.4.21.95"
ORIGIN
001 vvggdecnin ehpflvalyt sasstihcag alinrewvlt aahcdrrnir iklgmhskni
061 rnedeqirvp rgkyfclntk fpngldkdim lirlrrpvty sthiapvslp srsrgvgsrc
121 rimgwgkist tedtypdvph ctnifivkhk wceplypwvp adsrtlcagi lkggrdtchg
181 dsggplicng emhgivaggs epcgqhlkpa vytkvfdynn wiqsiiagnr tvtcpp
LENGTH 236 aa
MOLECULAR WEIGHT 26167 Da

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036 Coagulation factor X-activating enzyme light chain 1 precursor (RVV-X light chain 1) (Coagulation factor X-activating enzyme gamma-chain) (C-type lectin-like protein subunit 2)

No.036
LOCUS     Q4PRD1
DEFINITION Coagulation factor X-activating enzyme light chain 1 precursor (RVV-X light chain 1) (Coagulation factor X-activating enzyme gamma-chain) (C-type lectin-like protein subunit 2).
SOURCE Daboia russellii siamensis
COMMENT
[FUNCTION] Regulatory subunit of coagulation factor X-activating enzyme, a zinc-protease enzyme that acts in hemorrhage. The enzyme activates coagulation factor X by cleaving the Arg-Ile bond at position 234 and is also able to activate coagulation factor IX and protein C by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X in a calcium-dependent manner.
[SUBUNIT] Heterotrimer; disulfide-linked. The heterotrimer consists of 1 heavy chain and 2 light chains: LC1 and LC2.
[SUBCELLULAR LOCATION] Secreted protein.
[TISSUE SPECIFICITY] Expressed by the venom gland.
[PTM] N-glycosylated; probably required for conformation. Removal of easily accessible sugars does not change its functional capacity, but removal of the core sugars with N-glycanase causes a virtually complete loss of enzyme activity, apparently as a result of major conformational changes in the molecule. Not O-glycosylated.
[MISCELLANEOUS] Calcium is required for ligand binding.
[SIMILARITY] Contains 1 C-type lectin domain.
ORIGIN
001 mgrfisvsfg wlvvflslsg teavldcpsg wlsyeqhcyk gfndlknwtd aekfcteqkk
061 gshlvslhsr eeekfvvnli senleypatw iglgnmwkdc rmewsdrgnv kykalaeesy
121 climithekv wksmtcnfia pvvckf
LENGTH 146 aa
MOLECULAR WEIGHT 16923 Da

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037 Coagulation factor X-activating enzyme light chain 2 precursor (RVV-X light chain 1) (Coagulation factor X-activating enzyme beta-chain) (C-type lectin-like protein subunit 1)

No.037
LOCUS    Q4PRD2
DEFINITION Coagulation factor X-activating enzyme light chain 2 precursor (RVV-X light chain 1) (Coagulation factor X-activating enzyme beta-chain) (C-type lectin-like protein subunit 1).
SOURCE Daboia russellii siamensis
COMMENT
[FUNCTION] Regulatory subunit of coagulation factor X-activating enzyme, a zinc-protease enzyme that acts in hemorrhage. The enzyme activates coagulation factor X by cleaving the Arg-Ile bond at position 234 and is also able to activate coagulation factor IX and protein C by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X in a calcium-dependent manner.
[SUBUNIT] Heterotrimer; disulfide-linked. The heterotrimer consists of 1 heavy chain and 2 light chains: LC1 and LC2.
[SUBCELLULAR LOCATION] Secreted protein.
[TISSUE SPECIFICITY] Expressed by the venom gland.
[PTM] N-glycosylated; probably required for conformation. Removal of easily accessible sugars does not change its functional capacity, but removal of the core sugars with N-glycanase causes a virtually complete loss of enzyme activity, apparently as a result of major conformational changes in the molecule. Not O-glycosylated.
[MISCELLANEOUS] Calcium is required for ligand binding.
[SIMILARITY] Contains 1 C-type lectin domain.
ORIGIN
001 mgrfisvsfg llvvflslsg tgagldcppd sslyryfcyr vfkehktwea aerfcmehpn
061 nghlvsiesm eeaefvakll snttgkfith fwiglmikdk eqecssewsd gssvsydklg
121 kqefrkcfvl ekesgyrmwf nrnceerylf vckvppec
LENGTH 158 aa
MOLECULAR WEIGHT 18337 Da

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038 Phospholipase A2 [Daboia russellii]

No.038
LOCUS    CAA48456(CAA48457)(S29298)(S29299)
DEFINITION phospholipase a2 [Daboia russellii].
SOURCE Daboia russellii (Russell's viper)
[AUTHORS] Tsai,I.
[TITLE] Direct Submission
[JOURNAL] Submitted (14-SEP-1992) I. Tsai, Inst. of Biological Chemistry, Academia Sinica, P.O. Box 23-106, Taipei, Taiwan 10798, ROC
FEATURES EC_number="3.1.1.4"
ORIGIN
001 mrtlwivavc ligvegnlfq farmingklg afsvwnyisy gcycgwggqg tpkdatdrcc
061 fvhdccyggv kgcnpklaiy sysfqrgniv cgrnngclrt icecdrvaan cfhqnkntyn
121 keykflsssk crqrseqc
LENGTH 138 AA
MOLECULAR WEIGHT 15555 Da

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039 Venom nerve growth factor (v-NGF)

No.039
LOCUS    P30894(S28161)(AAA03282)
DEFINITION Venom nerve growth factor (v-NGF).
SOURCE Daboia russellii russellii
COMMENT
[FUNCTION] Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons as well as basal forebrain cholinergic neurons in the brain. Its relevance in the snake venom is not clear. It probably participates direcetly or indirectly in the toxic activity.
[SUBUNIT] Homodimer.
[SUBCELLULAR LOCATION] Secreted protein.
[TISSUE SPECIFICITY] Expressed by the venom gland.
[SIMILARITY] Belongs to the NGF-beta family.
ORIGIN
001 hpvhnqgefs vcdsvsvwva nkttatdmrg nvvtvmvdvn lnnnvykqyf fetkcknpnp
061 vpsgcrgida khwnsycttt dtfvraltme rnqaswrfir intacvcvis rkndnfg
LENGTH 117 aa
MOLECULAR WEIGHT 13283 Da

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