FA5V_PSETE
ID FA5V_PSETE Reviewed; 1460 AA.
AC Q7SZN0;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Venom prothrombin activator pseutarin-C non-catalytic subunit;
DE Short=PCNS;
DE Short=vPA;
DE AltName: Full=Venom coagulation factor Va-like protein;
DE Contains:
DE RecName: Full=Pseutarin-C non-catalytic subunit heavy chain;
DE Contains:
DE RecName: Full=Pseutarin-C non-catalytic subunit light 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 [MRNA], PROTEIN SEQUENCE OF 31-54; 58-124; 141-160;
RP 309-317; 331-340; 352-372; 378-392; 430-454; 477-499; 507-530; 559-567;
RP 821-840; 851-866; 868-886; 896-922; 926-949; 968-996; 1037-1059; 1078-1089;
RP 1119-1134; 1149-1175; 1266-1279; 1327-1368; 1396-1405; 1413-1425; 1429-1435
RP AND 1443-1451, LACK OF GLYCOSYLATION AT ASN-385 AND ASN-1397, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=12730119; DOI=10.1182/blood-2002-12-3839;
RA Rao V.S., Swarup S., Kini R.M.;
RT "The nonenzymatic subunit of pseutarin C, a prothrombin activator from
RT eastern brown snake (Pseudonaja textilis) venom, shows structural
RT similarity to mammalian coagulation factor V.";
RL Blood 102:1347-1354(2003).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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 [3]
RP PROTEIN SEQUENCE OF 852-861, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=16284125; DOI=10.1074/mcp.m500270-mcp200;
RA Birrell G.W., Earl S., Masci P.P., de Jersey J., Wallis T.P., Gorman J.J.,
RA Lavin M.F.;
RT "Molecular diversity in venom from the Australian Brown snake, Pseudonaja
RT textilis.";
RL Mol. Cell. Proteomics 5:379-389(2006).
RN [4]
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 [5]
RP TISSUE SPECIFICITY.
RC TISSUE=Venom gland;
RX PubMed=15735790; DOI=10.1160/th04-11-0707;
RA Minh Le T.N., Reza M.A., Swarup S., Kini R.M.;
RT "Gene duplication of coagulation factor V and origin of venom prothrombin
RT activator in Pseudonaja textilis snake.";
RL Thromb. Haemost. 93:420-429(2005).
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (3.32 ANGSTROMS) OF 31-1460 IN COMPLEX WITH
RP PSEUTARIN-C CATALYTIC SUBUNIT AND CALCIUM, GLYCOSYLATION AT ASN-156;
RP ASN-242; ASN-406; ASN-944 AND ASN-1180, DISULFIDE BOND, AND FUNCTION.
RC TISSUE=Venom;
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 -!- SUBUNIT: Heterodimer of a light and a heavy chains; non-disulfide-
CC linked. The interaction between the two chains is calcium-dependent (By
CC similarity). Found in its active form associated with pseutarin-C
CC catalytic subunit (AC Q56VR3). {ECO:0000250,
CC ECO:0000269|PubMed:12362232}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12362232,
CC ECO:0000269|PubMed:12730119}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:15735790}.
CC -!- PTM: In physiological conditions, blood coagulation factor V and factor
CC Va are inactivated by activated protein C (APC) through proteolytic
CC degradation of the heavy chain. However, pseutarin-C non-catalytic
CC subunit (factor V-like protein) retains its full activity even at high
CC concentration of APC. This has two explanations: this protein has only
CC one of the three cleavage sites present in factor V that are targeted
CC by the APC for inactivation, and the binding with the catalytic subunit
CC protect the cleavage site from inactivation.
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 CoVase
CC (V0801). Tested as a procoagulant cofactor that may have application as
CC a systemic anti-bleeding agent in the treatment of internal bleeding
CC and non-compressible hemorrhage. {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 multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AY168281; AAO38805.1; -; mRNA.
DR PDB; 4BXS; X-ray; 3.32 A; V=31-1460.
DR PDBsum; 4BXS; -.
DR AlphaFoldDB; Q7SZN0; -.
DR SMR; Q7SZN0; -.
DR iPTMnet; Q7SZN0; -.
DR PRIDE; Q7SZN0; -.
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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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 CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; -; 5.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR024715; Factor_5/8-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR Pfam; PF07732; Cu-oxidase_3; 3.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR PIRSF; PIRSF000354; Factors_V_VIII; 1.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; SSF49503; 6.
DR SUPFAM; SSF49785; SSF49785; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation cascade activating toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Metal-binding; Pharmaceutical;
KW Prothrombin activator; Reference proteome; Repeat; Secreted; Signal; Toxin.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:12730119"
FT CHAIN 31..772
FT /note="Pseutarin-C non-catalytic subunit heavy chain"
FT /evidence="ECO:0000305"
FT /id="PRO_5000089286"
FT PROPEP 773..818
FT /note="Activation peptide (connecting region)"
FT /id="PRO_0000408521"
FT CHAIN 819..1460
FT /note="Pseutarin-C non-catalytic subunit light chain"
FT /id="PRO_0000408522"
FT DOMAIN 32..330
FT /note="F5/8 type A 1"
FT DOMAIN 32..196
FT /note="Plastocyanin-like 1"
FT DOMAIN 206..330
FT /note="Plastocyanin-like 2"
FT DOMAIN 351..685
FT /note="F5/8 type A 2"
FT DOMAIN 351..529
FT /note="Plastocyanin-like 3"
FT DOMAIN 539..685
FT /note="Plastocyanin-like 4"
FT DOMAIN 824..1143
FT /note="F5/8 type A 3"
FT DOMAIN 824..992
FT /note="Plastocyanin-like 5"
FT DOMAIN 1001..1143
FT /note="Plastocyanin-like 6"
FT DOMAIN 1147..1298
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 1303..1457
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 693..818
FT /note="B"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000312|PDB:4BXS"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000312|PDB:4BXS"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000312|PDB:4BXS"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000312|PDB:4BXS"
FT BINDING 920
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000312|PDB:4BXS"
FT BINDING 935
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000312|PDB:4BXS"
FT BINDING 938
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000312|PDB:4BXS"
FT BINDING 939
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000312|PDB:4BXS"
FT SITE 385
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:12730119"
FT SITE 772..773
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 818..819
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 1397
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:12730119"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT CARBOHYD 1001
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT DISULFID 170..196
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT DISULFID 251..332
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT DISULFID 503..529
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT DISULFID 672..1032
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT DISULFID 966..992
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT DISULFID 1147..1298
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT DISULFID 1303..1457
FT /evidence="ECO:0000269|PubMed:23869089,
FT ECO:0000312|PDB:4BXS"
FT CONFLICT 80..82
FT /note="EPR -> KPQ (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="I -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..124
FT /note="SAVYNK -> DAVKIG (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="P -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="N -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 350..363
FT /note="IKNWEYFIAAEEIT -> AQLWEYHIAAQKED (in Ref. 1; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 440..444
FT /note="NLASR -> DLAVQ (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 522..523
FT /note="LI -> IL (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 820..827
FT /note="INRGNKRR -> QNTGNKLY (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="S -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 876
FT /note="G -> GK (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="K -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 944
FT /note="N -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 981..995
FT /note="IHSGLIGPILICQKG -> VEPGLIGPLYSIAEEAV (in Ref. 1; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1041..1043
FT /note="SLH -> NLG (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1055..1058
FT /note="LQGL -> GK (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1166..1170
FT /note="SGHVG -> AGHVQ (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1274
FT /note="I -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1369
FT /note="I -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1400..1404
FT /note="WKPYL -> YKPYG (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1433..1434
FT /note="LS -> SL (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 100..111
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 211..221
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 355..366
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 392..404
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 433..440
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 483..489
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 502..509
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 514..519
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 562..569
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 581..587
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 639..643
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 674..677
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 678..684
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 692..698
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 834..839
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 855..859
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 870..872
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 878..880
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 889..892
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 896..899
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 905..907
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 912..917
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 933..935
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 936..938
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 949..952
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 955..957
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 966..972
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 974..976
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 977..981
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 982..984
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 987..992
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 999..1002
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1004..1017
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 1018..1020
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1021..1023
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1044..1048
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1051..1053
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1059..1064
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1066..1072
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1080..1084
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1100..1104
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1111..1113
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1120..1127
FT /evidence="ECO:0007829|PDB:4BXS"
FT HELIX 1129..1132
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1139..1143
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1152..1155
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 1160..1162
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1163..1166
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1169..1171
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1183..1185
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1200..1215
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1226..1232
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1235..1237
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1254..1256
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1259..1262
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1265..1267
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1273..1288
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1293..1298
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 1309..1311
FT /evidence="ECO:0007829|PDB:4BXS"
FT TURN 1316..1318
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1319..1322
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1343..1345
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1359..1362
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1368..1374
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1376..1378
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1383..1389
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1392..1394
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1396..1398
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1400..1402
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1408..1410
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1418..1421
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1426..1432
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1435..1438
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1441..1447
FT /evidence="ECO:0007829|PDB:4BXS"
FT STRAND 1452..1457
FT /evidence="ECO:0007829|PDB:4BXS"
SQ SEQUENCE 1460 AA; 165932 MW; 6AFB63E2D5D275A6 CRC64;
MGRYSVSPVP KCLLLMFLGW SGLKYYQVNA AQLREYHIAA QLEDWDYNPQ PEELSRLSES
DLTFKKIVYR EYELDFKQEE PRDALSGLLG PTLRGEVGDS LIIYFKNFAT QPVSIHPQSA
VYNKWSEGSS YSDGTSDVER LDDAVPPGQS FKYVWNITAE IGPKKADPPC LTYAYYSHVN
MVRDFNSGLI GALLICKEGS LNANGSQKFF NREYVLMFSV FDESKNWYRK PSLQYTINGF
ANGTLPDVQA CAYDHISWHL IGMSSSPEIF SVHFNGQTLE QNHYKVSTIN LVGGASVTAD
MSVSRTGKWL ISSLVAKHLQ AGMYGYLNIK DCGNPDTLTR KLSFRELMKI KNWEYFIAAE
EITWDYAPEI PSSVDRRYKA QYLDNFSNFI GKKYKKAVFR QYEDGNFTKP TYAIWPKERG
ILGPVIKAKV RDTVTIVFKN LASRPYSIYV HGVSVSKDAE GAIYPSDPKE NITHGKAVEP
GQVYTYKWTV LDTDEPTVKD SECITKLYHS AVDMTRDIAS GLIGPLLVCK HKALSVKGVQ
NKADVEQHAV FAVFDENKSW YLEDNIKKYC SNPSAVKKDD PKFYKSNVMY TLNGYASDRT
EVLRFHQSEV VQWHLTSVGT VDEIVPVHLS GHTFLSKGKH QDILNLFPMS GESATVTMDN
LGTWLLSSWG SCEMSNGMRL RFLDANYDDE DEGNEEEEED DGDIFADIFI PSEVVKKKEE
VPVNFVPDPE SDALAKELGL IDDEGNPIIQ PRREQTEDDE EQLMKASMLG LRSFKGSVAE
EELKHTALAL EEDAHASDPR IDSNSARNPD DIAGRYLRTI NRGNKRRYYI AAEEVLWDYS
PIGKSQVRSR AAKTTFKKAI FRSYLDDTFQ TPSTGGEYEK HLGILGPIIR AEVDDVIEIQ
FKNLASRPYS LHAHGLLYEK SSEGRSYDDK SPELFKKDDA IMPNGTYTYV WQVPPRSGPT
DNTEKCKSWA YYSGVNPEKD IHSGLIGPIL ICQKGMIDKY NRTIDIREFV LFFMVFDEEK
SWYFPKSDKS TCEEKLIGVQ SLHTFPAING IPYQLQGLTM YKDENVHWHL LNMGGPKDIH
VVNFHGQTFT EEGREDNQLG VLPLLPGTFA SIKMKPSKIG TWLLETEVGE NQERGMQALF
TVIDKDCKLP MGLASGIIQD SQISASGHVG YWEPKLARLN NTGKYNAWSI IKKEHEHPWI
QIDLQRQVVI TGIQTQGTVQ LLQHSYTVEY FVTYSEDGQN WITFKGRHSE TQMHFEGNSD
GTTVKENHID PPIIARYIRL HPTKFYNRPT FRIELLGCEV EGCSVPLGME SGAIKNSEIT
ASSYKKTWWS SWEPSLARLN LEGGTNAWQP EVNNKDQWLQ IDLQHLTKIT SIITQGATSM
TTSMYVKTFS IHYTDDNSTW KPYLDVRTSM EKVFTGNINS DGHVKHFFKP PILSRFIRII
PKTWNQYIAL RIELFGCEVF
