FAXC_PSETE
ID FAXC_PSETE Reviewed; 467 AA.
AC Q56VR3; A5X463; Q6IT09; Q6IT10;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Venom prothrombin activator pseutarin-C catalytic subunit;
DE Short=PCCS;
DE Short=vPA;
DE EC=3.4.21.6 {ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:23869089};
DE AltName: Full=Venom coagulation factor Xa-like protease;
DE Contains:
DE RecName: Full=Pseutarin-C catalytic subunit light chain;
DE Contains:
DE RecName: Full=Pseutarin-C catalytic subunit heavy chain;
DE Flags: Precursor;
OS Pseudonaja textilis (Eastern brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX NCBI_TaxID=8673;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 41-70;
RP 77-119; 142-177; 210-242 AND 271-281, TOXIC DOSE, GLYCOSYLATION AT SER-92
RP AND ASN-254, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom gland;
RX PubMed=15351847; DOI=10.1160/th04-03-0144;
RA Rao V.S., Swarup S., Kini R.M.;
RT "The catalytic subunit of pseutarin C, a group C prothrombin activator from
RT the venom of Pseudonaja textilis, is structurally similar to mammalian
RT blood coagulation factor Xa.";
RL Thromb. Haemost. 92:509-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16197456; DOI=10.1111/j.1365-2141.2005.05744.x;
RA Filippovich I., Sorokina N., St Pierre L., Flight S., de Jersey J.,
RA Perry N., Masci P.P., Lavin M.F.;
RT "Cloning and functional expression of venom prothrombin activator protease
RT from Pseudonaja textilis with whole blood procoagulant activity.";
RL Br. J. Haematol. 131:237-246(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RX PubMed=17239167; DOI=10.1111/j.1538-7836.2006.02266.x;
RA Reza M.A., Swarup S., Kini R.M.;
RT "Structure of two genes encoding parallel prothrombin activators in
RT Tropidechis carinatus snake: gene duplication and recruitment of factor X
RT gene to the venom gland.";
RL J. Thromb. Haemost. 5:117-126(2007).
RN [4]
RP PROTEIN SEQUENCE OF 41-70 AND 210-246, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47; GLU-54; GLU-56; GLU-59; GLU-60;
RP GLU-65 AND GLU-66.
RC TISSUE=Venom;
RX PubMed=12362232; DOI=10.1267/th02100611;
RA Rao V.S., Kini R.M.;
RT "Pseutarin C, a prothrombin activator from Pseudonaja textilis venom: its
RT structural and functional similarity to mammalian coagulation factor Xa-Va
RT complex.";
RL Thromb. Haemost. 88:611-619(2002).
RN [5]
RP TOXIC DOSE, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Pseudonaja textilis textilis; TISSUE=Venom;
RX PubMed=3075905;
RA Masci P.P., Whitaker A.N., de Jersey J.;
RT "Purification and characterization of a prothrombin activator from the
RT venom of the Australian brown snake, Pseudonaja textilis textilis.";
RL Biochem. Int. 17:825-835(1988).
RN [6]
RP NOMENCLATURE.
RX PubMed=11522026;
RA Manjunatha Kini R., Morita T., Rosing J.;
RT "Classification and nomenclature of prothrombin activators isolated from
RT snake venoms.";
RL Thromb. Haemost. 86:710-711(2001).
RN [7]
RP PHARMACEUTICAL.
RX PubMed=21184772; DOI=10.1016/j.toxicon.2010.12.010;
RA Earl S.T., Masci P.P., de Jersey J., Lavin M.F., Dixon J.;
RT "Drug development from Australian elapid snake venoms and the Venomics
RT pipeline of candidates for haemostasis: Textilinin-1 (Q8008), Haempatch
RT (Q8009) and CoVase (V0801).";
RL Toxicon 59:456-463(2012).
RN [8] {ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 41-463 IN COMPLEX WITH
RP PSEUTARIN-C NON-CATALYTIC SUBUNIT, DISULFIDE BONDS, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=23869089; DOI=10.1182/blood-2013-06-511733;
RA Lechtenberg B.C., Murray-Rust T.A., Johnson D.J., Adams T.E.,
RA Krishnaswamy S., Camire R.M., Huntington J.A.;
RT "Crystal structure of the prothrombinase complex from the venom of
RT Pseudonaja textilis.";
RL Blood 122:2777-2783(2013).
CC -!- FUNCTION: Snake prothrombin activator that attacks the hemostatic
CC system of prey. This non-catalytic subunit is functionally similar to
CC blood coagulation factor V (PubMed:12362232, PubMed:23869089). It
CC serves as a critical cofactor for the prothrombinase activity of the
CC catalytic subunit, which is similar to the blood coagulation factor X
CC (PubMed:12362232, PubMed:23869089). The complex converts prothrombin to
CC thrombin by sequential cleavage at two positions, Arg-320 followed by
CC Arg-271 (PubMed:23869089). Cleavage at Arg-320 produces an active
CC intermediate known as meizothrombin (PubMed:23869089). Meizothrombin is
CC the 'second' substrate for prothrombinase, and it docks in an altered
CC manner to present the second cleavage site (271) (PubMed:23869089).
CC Cleavage at Arg-271 releases active thrombin from its pro-fragment
CC (PubMed:23869089). This order of events is reversed if the protease
CC component of prothrombinase is used on its own, suggesting that the 271
CC site is inherently more accessible to proteolysis (PubMed:23869089).
CC The complex converts prothrombin to thrombin in presence but also in
CC the absence of membrane (PubMed:23869089).
CC {ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:23869089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in
CC prothrombin to form thrombin.; EC=3.4.21.6;
CC Evidence={ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:23869089};
CC -!- ACTIVITY REGULATION: Activated by calcium and negatively charged
CC phospholipids. {ECO:0000269|PubMed:12362232,
CC ECO:0000269|PubMed:23869089}.
CC -!- SUBUNIT: Heterodimer of a light and a heavy chains; disulfide-linked.
CC Is associated with pseutarin-C non-catalytic subunit (AC Q7SZN0) in a
CC non-covalent manner. {ECO:0000269|PubMed:12362232,
CC ECO:0000269|PubMed:23869089, ECO:0000269|PubMed:3075905}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12362232,
CC ECO:0000269|PubMed:3075905}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:3075905}.
CC -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent
CC carboxylation. These residues are essential for the binding of calcium.
CC {ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12362232}.
CC -!- TOXIC DOSE: Intravenous injection (23 ug/kg bodyweight) of the group C
CC prothrombin activator causes death in rats through disseminated
CC intravascular coagulopathy (PubMed:3075905), whereas pseutarin-C is not
CC lethal even at 10 mg/kg in mice when injected intraperitoneally
CC (PubMed:15351847). {ECO:0000269|PubMed:15351847,
CC ECO:0000269|PubMed:3075905}.
CC -!- PHARMACEUTICAL: Is under preclinical trial by the Australian
CC biopharmaceutical company QRxPharma Ltd, its subsidiary Venomics Pty
CC Ltd (VPL) and the University of Queensland (UQ) under the name
CC Haempatch (Q8009). Tested as a topical hemostatic agent to reduce blood
CC loss resulting from surgery or trauma.
CC -!- MISCELLANEOUS: Is classified in the group C of snake venom prothrombin
CC activators, since it does not require the mammalian factor Va for the
CC cleavage of prothrombin as the venom contains its own non-catalytic
CC factor Va-like molecule. {ECO:0000305|PubMed:21184772}.
CC -!- MISCELLANEOUS: In contrast to blood coagulation factors that circulate
CC as inactive zymogen in plasma, venom prothrombin activators are always
CC found in the active form in the venom. Hence, catalytic and non-
CC catalytic subunits are found naturally in venom as stable complexes.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AY260939; AAP86642.1; -; mRNA.
DR EMBL; AY631239; AAT42491.1; -; mRNA.
DR EMBL; DQ533835; ABG02407.1; -; Genomic_DNA.
DR EMBL; AY631238; AAT42490.1; -; mRNA.
DR PDB; 4BXS; X-ray; 3.32 A; A=41-463.
DR PDB; 4BXW; X-ray; 2.71 A; A/B=41-463.
DR PDBsum; 4BXS; -.
DR PDBsum; 4BXW; -.
DR AlphaFoldDB; Q56VR3; -.
DR SMR; Q56VR3; -.
DR MEROPS; S01.446; -.
DR iPTMnet; Q56VR3; -.
DR BRENDA; 3.4.21.60; 6821.
DR Proteomes; UP000472273; Unplaced.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; 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 another organism; IDA:UniProtKB.
DR GO; GO:0035807; P:positive regulation of blood coagulation in another organism; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
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; 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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
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 3D-structure; 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; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Pharmaceutical; Protease;
KW Prothrombin activator; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..40
FT /evidence="ECO:0000269|PubMed:12362232,
FT ECO:0000269|PubMed:15351847"
FT /id="PRO_0000408523"
FT CHAIN 41..181
FT /note="Pseutarin-C catalytic subunit light chain"
FT /id="PRO_5000090539"
FT PROPEP 182..209
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000408525"
FT CHAIN 210..467
FT /note="Pseutarin-C catalytic subunit heavy chain"
FT /id="PRO_0000408526"
FT DOMAIN 41..86
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 86..122
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 129..164
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 210..454
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 251
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 309
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 406
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 75
FT /note="Not modified"
FT /evidence="ECO:0000305"
FT SITE 103
FT /note="Not modified"
FT SITE 209..210
FT /note="Cleavage"
FT MOD_RES 46
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12362232"
FT MOD_RES 47
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12362232"
FT MOD_RES 54
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12362232"
FT MOD_RES 56
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12362232"
FT MOD_RES 59
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12362232"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12362232"
FT MOD_RES 65
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12362232"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12362232"
FT MOD_RES 69
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT CARBOHYD 92
FT /note="O-linked (Hex...) serine"
FT /evidence="ECO:0000269|PubMed:15351847"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15351847"
FT DISULFID 57..62
FT /evidence="ECO:0000250"
FT DISULFID 90..101
FT /evidence="ECO:0000250|UniProtKB:P00742"
FT DISULFID 95..110
FT /evidence="ECO:0000250|UniProtKB:P00742"
FT DISULFID 112..121
FT /evidence="ECO:0000250|UniProtKB:P00742"
FT DISULFID 129..140
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
FT DISULFID 136..149
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
FT DISULFID 151..164
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
FT DISULFID 172..329
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
FT DISULFID 216..221
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
FT DISULFID 236..252
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
FT DISULFID 377..391
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
FT DISULFID 402..430
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0007744|PDB:4BXS, ECO:0007744|PDB:4BXW"
FT CONFLICT 39
FT /note="K -> E (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="V -> A (in Ref. 1; AAP86642)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="S -> H (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="S -> N (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="H -> Q (in Ref. 1; AAP86642 and 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="T -> P (in Ref. 1; AAP86642)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="K -> I (in Ref. 1; AAP86642)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..232
FT /note="DKK -> EKE (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..271
FT /note="RSRA -> KSRI (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="V -> I (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 292..305
FT /note="KKSQEFYEKFDLVS -> QKAYKFDLAA (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 353..360
FT /note="GIFERGPN -> RIVEKGPK (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 379..388
FT /note="LSSNFPITPT -> VSSETPITPN (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="Q -> R (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 411..413
FT /note="ITA -> TTV (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="W -> S (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 433..438
FT /note="KGRYGI -> NGKYGN (in Ref. 8; AAT42490)"
FT /evidence="ECO:0000305"
FT CONFLICT 450..467
FT /note="Missing (in Ref. 1; AAP86642)"
FT /evidence="ECO:0000305"
FT TURN 128..132
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:4BXW"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:4BXW"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:4BXW"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:4BXW"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:4BXW"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:4BXW"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:4BXW"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:4BXW"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 343..351
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:4BXW"
FT HELIX 374..378
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 417..426
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:4BXW"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:4BXW"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:4BXW"
FT HELIX 446..452
FT /evidence="ECO:0007829|PDB:4BXW"
SQ 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
