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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