VCO3_NAJKA
ID VCO3_NAJKA Reviewed; 1642 AA.
AC Q91132; Q6PQH3; Q6RHR7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cobra venom factor;
DE Short=CVF;
DE Short=CVFk;
DE AltName: Full=Complement C3 homolog;
DE Contains:
DE RecName: Full=Cobra venom factor alpha chain;
DE Contains:
DE RecName: Full=Cobra venom factor gamma chain;
DE Contains:
DE RecName: Full=Cobra venom factor beta chain;
DE Flags: Precursor;
OS Naja kaouthia (Monocled cobra) (Naja siamensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=7809120; DOI=10.1073/pnas.91.26.12775;
RA Fritzinger D.C., Bredehorst R., Vogel C.-W.;
RT "Molecular cloning and derived primary structure of cobra venom factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12775-12779(1994).
RN [2]
RP ERRATUM OF PUBMED:7809120.
RX PubMed=7638237; DOI=10.1073/pnas.92.16.7605-b;
RA Fritzinger D.C., Bredehorst R., Vogel C.-W.;
RL Proc. Natl. Acad. Sci. U.S.A. 92:7605-7605(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24 AND 1608-1642.
RC TISSUE=Liver;
RA Bammert H., Kunze B., Li Y., Fritzinger D.C., Bredehorst R., Vogel C.-W.;
RT "Genomic structure of cobra venom factor (CVF).";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP REVIEW.
RX PubMed=20417224; DOI=10.1016/j.toxicon.2010.04.007;
RA Vogel C.-W., Fritzinger D.C.;
RT "Cobra venom factor: Structure, function, and humanization for therapeutic
RT complement depletion.";
RL Toxicon 56:1198-1222(2010).
RN [5]
RP GLYCOSYLATION.
RX PubMed=11320058; DOI=10.1093/glycob/11.3.195;
RA Gowda D.C., Glushka J., van Halbeek H., Thotakura R.N., Bredehorst R.,
RA Vogel C.-W.;
RT "N-linked oligosaccharides of cobra venom factor contain novel alpha(1-
RT 3)galactosylated Le(x) structures.";
RL Glycobiology 11:195-208(2001).
RN [6]
RP STRUCTURE.
RX PubMed=15131128; DOI=10.1074/jbc.m403196200;
RA Kock M.A., Hew B.E., Bammert H., Fritzinger D.C., Vogel C.-W.;
RT "Structure and function of recombinant cobra venom factor.";
RL J. Biol. Chem. 279:30836-30843(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 23-649; 733-984 AND 1264-1642 IN
RP COMPLEX WITH HUMAN COMPLEMENT FACTOR B, METAL-BINDING SITES, GLYCOSYLATION
RP AT ASN-209 AND ASN-1346, AND DISULFIDE BONDS.
RX PubMed=19574954; DOI=10.1038/emboj.2009.184;
RA Janssen B.J., Gomes L., Koning R.I., Svergun D.I., Koster A.J.,
RA Fritzinger D.C., Vogel C.-W., Gros P.;
RT "Insights into complement convertase formation based on the structure of
RT the factor B-cobra venom factor complex.";
RL EMBO J. 28:2469-2478(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 23-649; 733-984 AND 1264-1642,
RP METAL-BINDING SITES, AND DISULFIDE BONDS.
RX PubMed=19368894; DOI=10.1016/j.str.2009.01.015;
RA Krishnan V., Ponnuraj K., Xu Y., Macon K., Volanakis J.E., Narayana S.V.;
RT "The crystal structure of cobra venom factor, a cofactor for C3- and C5-
RT convertase CVFBb.";
RL Structure 17:611-619(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (4.30 ANGSTROMS) OF 23-1642 IN COMPLEX WITH HUMAN
RP COMPLEMENT C5, GLYCOSYLATION AT ASN-209 AND ASN-1346, AND DISULFIDE BONDS.
RX PubMed=21217642; DOI=10.1038/emboj.2010.341;
RA Laursen N.S., Andersen K.R., Braren I., Spillner E., Sottrup-Jensen L.,
RA Andersen G.R.;
RT "Substrate recognition by complement convertases revealed in the C5-cobra
RT venom factor complex.";
RL EMBO J. 30:606-616(2011).
CC -!- FUNCTION: Complement-activating protein in cobra venom. It is a
CC structural and functional analog of complement component C3b, the
CC activated form of C3. It binds factor B (CFB), which is subsequently
CC cleaved by factor D (CFD) to form the bimolecular complex CVF/Bb.
CC CVF/Bb is a C3/C5 convertase that cleaves both complement components C3
CC and C5. Structurally, it resembles the C3b degradation product C3c,
CC which is not able to form a C3/C5 convertase. Unlike C3b/Bb, CVF/Bb is
CC a stable complex and completely resistant to the actions of complement
CC regulatory factors H (CFH) and I (CFI). Therefore, CVF continuously
CC activates complement resulting in the depletion of complement activity.
CC -!- SUBUNIT: Heterotrimer of alpha, beta and gamma chains; disulfide-
CC linked. Is active with factor B in the presence of factor D.
CC {ECO:0000269|PubMed:19368894, ECO:0000269|PubMed:19574954,
CC ECO:0000269|PubMed:21217642}.
CC -!- INTERACTION:
CC Q91132; P01031: C5; Xeno; NbExp=2; IntAct=EBI-7081824, EBI-8558308;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: First processed by the removal of 4 Arg residues by furin-type
CC protease, forming two chains, alpha and gamma/beta precursor, linked by
CC a disulfide bond. Probably, the cobrin cleaves the C3a-like domain and
CC then the C3d-like domain, generating the mature cobra venom factor
CC (CVF). This mature CVF is composed of three chains: alpha, gamma and
CC beta.
CC -!- PTM: Contains 3 N-linked oligosaccharide chains, two in the alpha-chain
CC and one in the beta-chain. Glycosylation is not required for the
CC biological activity. However, it contributes to the immunogenicity of
CC CVF. The carbohydrate content is 7.4. The major oligosaccharide is a
CC symmetric fucosylated biantennary complex-type chain with an unusual
CC alpha-galactosylated Le(x) structure at its non-reducing end.
CC {ECO:0000269|PubMed:11320058, ECO:0000269|PubMed:19574954,
CC ECO:0000269|PubMed:21217642}.
CC -!- MISCELLANEOUS: CVF has been used to study the complement pathways and
CC to investigate the role of complement in disease pathophysiology. It
CC has also been used to consume complement to prevent the hyperactive
CC rejection of organs in xenotransplantation and for targeted complement-
CC mediated cell killing. CVF can be safely administered to laboratory
CC animals for temporary depletion of complement activity. Interestingly,
CC it is able to deplete complement in serum from all vertebrates tested,
CC except cobras. The only side effect from massive activation of
CC complement in vivo by CVF has been an acute and fleeting inflammatory
CC injury of the lungs (PubMed:20417224). {ECO:0000305|PubMed:20417224}.
CC -!- SIMILARITY: Belongs to the venom complement C3 homolog family.
CC {ECO:0000305}.
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DR EMBL; U09969; AAA68989.1; -; mRNA.
DR EMBL; AY497579; AAR89520.1; -; Genomic_DNA.
DR EMBL; AY586272; AAS97956.1; -; Genomic_DNA.
DR PDB; 3FRP; X-ray; 2.61 A; A=23-649, B=1264-1642, G=733-984.
DR PDB; 3HRZ; X-ray; 2.20 A; A=23-649, B=733-984, C=1264-1642.
DR PDB; 3HS0; X-ray; 3.00 A; A/F=23-649, B/G=733-984, C/H=1264-1642.
DR PDB; 3PRX; X-ray; 4.30 A; B/D=1-1642.
DR PDB; 3PVM; X-ray; 4.30 A; B/D=1-1642.
DR PDB; 6I2X; EM; 3.35 A; B=1-1642.
DR PDBsum; 3FRP; -.
DR PDBsum; 3HRZ; -.
DR PDBsum; 3HS0; -.
DR PDBsum; 3PRX; -.
DR PDBsum; 3PVM; -.
DR PDBsum; 6I2X; -.
DR AlphaFoldDB; Q91132; -.
DR SASBDB; Q91132; -.
DR SMR; Q91132; -.
DR IntAct; Q91132; 3.
DR MINT; Q91132; -.
DR BindingDB; Q91132; -.
DR MEROPS; I39.950; -.
DR GlyConnect; 105; 23 N-Linked glycans.
DR iPTMnet; Q91132; -.
DR PRIDE; Q91132; -.
DR TopDownProteomics; Q91132; -.
DR EvolutionaryTrace; Q91132; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006956; P:complement activation; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR CDD; cd00017; ANATO; 1.
DR CDD; cd03583; NTR_complement_C3; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
DR InterPro; IPR041425; C3/4/5_MG1.
DR InterPro; IPR035711; Complement_C3-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR035815; NTR_complement_C3.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF81; PTHR11412:SF81; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF17790; MG1; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF07678; TED_complement; 1.
DR PRINTS; PR00004; ANAPHYLATOXN.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00643; C345C; 1.
DR SUPFAM; SSF47686; SSF47686; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues;
KW Complement system impairing toxin; Disulfide bond; Glycoprotein;
KW Inflammatory response; Magnesium; Metal-binding; Secreted; Signal;
KW Thioester bond; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..1642
FT /note="Cobra venom factor"
FT /id="PRO_0000005928"
FT CHAIN 23..649
FT /note="Cobra venom factor alpha chain"
FT /id="PRO_0000005929"
FT PROPEP 650..732
FT /id="PRO_0000423372"
FT CHAIN 733..984
FT /note="Cobra venom factor gamma chain"
FT /id="PRO_0000005930"
FT PROPEP 985..1263
FT /id="PRO_0000423373"
FT CHAIN 1264..1642
FT /note="Cobra venom factor beta chain"
FT /id="PRO_0000005931"
FT DOMAIN 677..712
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 1497..1640
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 654..732
FT /note="C3a-like domain"
FT /evidence="ECO:0000250"
FT REGION 736..747
FT /note="Factor B binding site"
FT /evidence="ECO:0000250"
FT REGION 985..1263
FT /note="C3d-like domain"
FT /evidence="ECO:0000250"
FT REGION 1190..1253
FT /note="Factor H binding site"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19574954,
FT ECO:0000269|PubMed:21217642"
FT CARBOHYD 1346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19574954,
FT ECO:0000269|PubMed:21217642"
FT DISULFID 544..801
FT /note="Interchain (between alpha and gamma chains)"
FT DISULFID 609..644
FT DISULFID 677..704
FT /evidence="ECO:0000250"
FT DISULFID 678..711
FT /evidence="ECO:0000250"
FT DISULFID 691..712
FT /evidence="ECO:0000250"
FT DISULFID 857..1492
FT /note="Interchain (between gamma and beta chains)"
FT DISULFID 1340..1468
FT DISULFID 1368..1437
FT DISULFID 1485..1490
FT DISULFID 1497..1569
FT DISULFID 1516..1640
FT DISULFID 1616..1625
FT CROSSLNK 993..996
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
FT STRAND 24..35
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3HS0"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 223..236
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 243..251
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 259..269
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 328..342
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:6I2X"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:6I2X"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6I2X"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 407..415
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:3HS0"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 459..468
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 470..474
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 478..485
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 488..496
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 502..509
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 516..526
FT /evidence="ECO:0007829|PDB:3HRZ"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 530..539
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:6I2X"
FT STRAND 562..570
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 574..581
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 582..587
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:3HS0"
FT HELIX 595..604
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 617..623
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 626..630
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:6I2X"
FT HELIX 742..744
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 772..779
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 784..795
FT /evidence="ECO:0007829|PDB:3HRZ"
FT TURN 796..798
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 799..802
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 806..810
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 813..818
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 830..838
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 840..842
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 844..850
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 856..859
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 862..864
FT /evidence="ECO:0007829|PDB:3HS0"
FT STRAND 866..872
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 876..886
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 888..900
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 906..916
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 918..930
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 932..935
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 937..945
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 959..967
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1274..1280
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1282..1286
FT /evidence="ECO:0007829|PDB:3FRP"
FT STRAND 1288..1293
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 1294..1296
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1301..1307
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1311..1318
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1321..1331
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1342..1351
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1363..1371
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1373..1375
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1377..1385
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1390..1393
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 1394..1401
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1406..1408
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1417..1419
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1421..1430
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1432..1434
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1436..1444
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1454..1460
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1469..1473
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1474..1476
FT /evidence="ECO:0007829|PDB:3FRP"
FT STRAND 1483..1486
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1489..1492
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 1508..1515
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1522..1534
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1537..1549
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 1556..1558
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1561..1566
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 1567..1569
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 1570..1573
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1580..1585
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 1587..1589
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1596..1600
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 1602..1604
FT /evidence="ECO:0007829|PDB:3HS0"
FT STRAND 1606..1610
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 1614..1617
FT /evidence="ECO:0007829|PDB:3HRZ"
FT TURN 1619..1621
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 1622..1638
FT /evidence="ECO:0007829|PDB:3HRZ"
SQ SEQUENCE 1642 AA; 184518 MW; 2A71B2BD61D612A3 CRC64;
MERMALYLVA ALLIGFPGSS HGALYTLITP AVLRTDTEEQ ILVEAHGDST PKQLDIFVHD
FPRKQKTLFQ TRVDMNPAGG MLVTPTIEIP AKEVSTDSRQ NQYVVVQVTG PQVRLEKVVL
LSYQSSFLFI QTDKGIYTPG SPVLYRVFSM DHNTSKMNKT VIVEFQTPEG ILVSSNSVDL
NFFWPYNLPD LVSLGTWRIV AKYEHSPENY TAYFDVRKYV LPSFEVRLQP SEKFFYIDGN
ENFHVSITAR YLYGEEVEGV AFVLFGVKID DAKKSIPDSL TRIPIIDGDG KATLKRDTFR
SRFPNLNELV GHTLYASVTV MTESGSDMVV TEQSGIHIVA SPYQIHFTKT PKYFKPGMPY
ELTVYVTNPD GSPAAHVPVV SEAFHSMGTT LSDGTAKLIL NIPLNAQSLP ITVRTNHGDL
PRERQATKSM TAIAYQTQGG SGNYLHVAIT STEIKPGDNL PVNFNVKGNA NSLKQIKYFT
YLILNKGKIF KVGRQPRRDG QNLVTMNLHI TPDLIPSFRF VAYYQVGNNE IVADSVWVDV
KDTCMGTLVV KGDNLIQMPG AAMKIKLEGD PGARVGLVAV DKAVYVLNDK YKISQAKIWD
TIEKSDFGCT AGSGQNNLGV FEDAGLALTT STNLNTKQRS AAKCPQPANR RRRSSVLLLD
SNASKAAEFQ DQDLRKCCED VMHENPMGYT CEKRAKYIQE GDACKAAFLE CCRYIKGVRD
ENQRESELFL ARDDNEDGFI ADSDIISRSD FPKSWLWLTK DLTEEPNSQG ISSKTMSFYL
RDSITTWVVL AVSFTPTKGI CVAEPYEIRV MKVFFIDLQM PYSVVKNEQV EIRAILHNYV
NEDIYVRVEL LYNPAFCSAS TKGQRYRQQF PIKALSSRAV PFVIVPLEQG LHDVEIKASV
QEALWSDGVR KKLKVVPEGV QKSIVTIVKL DPRAKGVGGT QLEVIKARKL DDRVPDTEIE
TKIIIQGDPV AQIIENSIDG SKLNHLIITP SGCGEQNMIR MAAPVIATYY LDTTEQWETL
GINRRTEAVN QIVTGYAQQM VYKKADHSYA AFTNRASSSW LTAYVVKVFA MAAKMVAGIS
HEIICGGVRW LILNRQQPDG AFKENAPVLS GTMQGGIQGA EEEVYLTAFI LVALLESKTI
CNDYVNSLDS SIKKATNYLL KKYEKLQRPY TTALTAYALA AADQLNDDRV LMAASTGRDH
WEEYNAHTHN IEGTSYALLA LLKMKKFDQT GPIVRWLTDQ NFYGETYGQT QATVMAFQAL
AEYEIQMPTH KDLNLDITIE LPDREVPIRY RINYENALLA RTVETKLNQD ITVTASGDGK
ATMTILTFYN AQLQEKANVC NKFHLNVSVE NIHLNAMGAK GALMLKICTR YLGEVDSTMT
IIDISMLTGF LPDAEDLTRL SKGVDRYISR YEVDNNMAQK VAVIIYLNKV SHSEDECLHF
KILKHFEVGF IQPGSVKVYS YYNLDEKCTK FYHPDKGTGL LNKICIGNVC RCAGETCSSL
NHQERIDVPL QIEKACETNV DYVYKTKLLR IEEQDGNDIY VMDVLEVIKQ GTDENPRAKT
HQYISQRKCQ EALNLKVNDD YLIWGSRSDL LPTKDKISYI ITKNTWIERW PHEDECQEEE
FQKLCDDFAQ FSYTLTEFGC PT
