GenomeNet

Database: UniProt
Entry: Q58L94
LinkDB: Q58L94
Original site: Q58L94 
ID   FAXD2_NOTSC             Reviewed;         453 AA.
AC   Q58L94;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   05-DEC-2018, entry version 101.
DE   RecName: Full=Venom prothrombin activator notecarin-D2;
DE            Short=vPA;
DE            EC=3.4.21.6;
DE   AltName: Full=Venom coagulation factor Xa-like protease;
DE   Contains:
DE     RecName: Full=Notecarin-D2 light chain;
DE   Contains:
DE     RecName: Full=Notecarin-D2 heavy chain;
DE   Flags: Precursor;
OS   Notechis scutatus scutatus (Mainland tiger snake) (Common tiger
OS   snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC   Toxicofera; Serpentes; Colubroidea; Elapidae; Acanthophiinae;
OC   Notechis.
OX   NCBI_TaxID=70142;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15930152; DOI=10.1093/molbev/msi181;
RA   St Pierre L., Masci P.P., Filippovich I., Sorokina N., Marsh N.,
RA   Miller D.J., Lavin M.F.;
RT   "Comparative analysis of prothrombin activators from the venom of
RT   Australian elapids.";
RL   Mol. Biol. Evol. 22:1853-1864(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 41-76 AND 210-235, FUNCTION, SUBUNIT, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, GAMMA-CARBOXYGLUTAMATION AT GLU-46;
RP   GLU-47; GLU-54; GLU-56; GLU-59; GLU-60; GLU-65; GLU-66; GLU-69; GLU-72
RP   AND GLU-75, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=12403650; DOI=10.1042/BJ20020889;
RA   Rao V.S., Joseph J.S., Kini R.M.;
RT   "Group D prothrombin activators from snake venom are structural
RT   homologues of mammalian blood coagulation factor Xa.";
RL   Biochem. J. 369:635-642(2003).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=11522026;
RA   Manjunatha Kini R., Morita T., Rosing J.;
RT   "Classification and nomenclature of prothrombin activators isolated
RT   from snake venoms.";
RL   Thromb. Haemost. 86:710-711(2001).
CC   -!- FUNCTION: Snake prothrombin activator that attacks the hemostatic
CC       system of prey. This protein is functionally similar to blood
CC       coagulation factor Xa. {ECO:0000269|PubMed:12403650}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds
CC         in prothrombin to form thrombin.; EC=3.4.21.6;
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain;
CC       disulfide-linked. {ECO:0000269|PubMed:12403650}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12403650}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:12403650}.
CC   -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K
CC       dependent carboxylation. These residues are essential for the
CC       binding of calcium. {ECO:0000255|PROSITE-ProRule:PRU00463,
CC       ECO:0000269|PubMed:12403650}.
CC   -!- MISCELLANEOUS: Is classified in the group D of snake venom
CC       prothrombin activators, since it requires the mammalian factor Va
CC       for maximal activity for the cleavage of prothrombin. The venom of
CC       this species does not contains its own coagulation factor V-like.
CC   -!- MISCELLANEOUS: PubMed:12403650 describes 2 isoforms of notecarin D
CC       (D1 and D2). We chose to name this protein D1 according to the
CC       masses indicated in the paper.
CC   -!- MISCELLANEOUS: In contrast to blood coagulation factors that
CC       circulate as inactive zymogen in plasma, venom prothrombin
CC       activators are always found in the active form in the venom.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; AY940206; AAX37262.1; -; mRNA.
DR   ProteinModelPortal; Q58L94; -.
DR   SMR; Q58L94; -.
DR   MEROPS; S01.425; -.
DR   HOVERGEN; HBG013304; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR   GO; GO:0044469; P:envenomation resulting in positive regulation of blood coagulation in other organism; IDA:UniProtKB.
DR   GO; GO:0035807; P:positive regulation of blood coagulation in other organism; IDA:UniProtKB.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Calcium;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid;
KW   Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease;
KW   Prothrombin activator; Repeat; Secreted; Serine protease; Signal;
KW   Toxin.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   PROPEP       21     40       {ECO:0000250}.
FT                                /FTId=PRO_0000409893.
FT   CHAIN        41    181       Notecarin-D2 light chain.
FT                                /FTId=PRO_5000095352.
FT   PROPEP      182    209       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_5000095353.
FT   CHAIN       210    453       Notecarin-D2 heavy chain.
FT                                /FTId=PRO_5000095354.
FT   DOMAIN       41     86       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       86    122       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      129    164       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      210    451       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    251    251       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    306    306       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    403    403       Charge relay system. {ECO:0000250}.
FT   MOD_RES      46     46       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      47     47       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      54     54       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      56     56       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      59     59       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      60     60       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      65     65       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      66     66       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      69     69       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      72     72       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      75     75       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   CARBOHYD     92     92       O-linked (Hex...) serine. {ECO:0000250}.
FT   CARBOHYD    254    254       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     57     62       {ECO:0000250}.
FT   DISULFID     90    101       {ECO:0000250}.
FT   DISULFID     95    110       {ECO:0000250}.
FT   DISULFID    112    121       {ECO:0000250}.
FT   DISULFID    129    140       {ECO:0000250}.
FT   DISULFID    136    149       {ECO:0000250}.
FT   DISULFID    151    164       {ECO:0000250}.
FT   DISULFID    172    326       Interchain (between light and heavy
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274, ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DISULFID    216    221       {ECO:0000250}.
FT   DISULFID    236    252       {ECO:0000250}.
FT   DISULFID    374    388       {ECO:0000250}.
FT   DISULFID    399    427       {ECO:0000250}.
SQ   SEQUENCE   453 AA;  50872 MW;  6AEF16F233F64EED CRC64;
     MAPQLLLCLI LTFLWSLPEA ESNVFLKSKV ANRFLQRTKR SNSLFEEIRP GNIERECIEE
     KCSKEEAREV FEDNEKTETF WNVYVDGDQC SSNPCHYRGT CKDGIGSYTC TCLPNYEGKN
     CEKVLFKSCR AFNGNCWHFC KRVQSETQCS CAESYLLGVD GHSCVAEGDF SCGRNIKARN
     KREASLPDFV QSQKATVLKK SDNPSPDIRI VNGMDCKLGE CPWQAVLINE KGEVFCGGTI
     LSPIHVLTAA HCINQTKSVS VIVGEIDISR KETRRLLSVD KIYVHKKFVP PNSYYQNIDR
     FAYDYDIAII RMKTPIQFSE NVVPACLPTA DFAKEVLMKQ DSGIVSGFGR TQSIGYTSNI
     LKVITVPYVD RHTCMLSSNF RITQNMFCAG YDTLPQDACQ GDSGGPHITA YGDTHFVTGI
     ISWGEGCARK GKYGVYTKVS NFIPWIKKIM SLK
//
DBGET integrated database retrieval system