ID CO3_BOVIN Reviewed; 1661 AA.
AC Q2UVX4; Q2KIZ4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Complement C3;
DE Contains:
DE RecName: Full=Complement C3 beta chain;
DE Contains:
DE RecName: Full=Complement C3 alpha chain;
DE Contains:
DE RecName: Full=C3a anaphylatoxin;
DE Contains:
DE RecName: Full=C3-beta-c;
DE Short=C3bc;
DE Contains:
DE RecName: Full=Acylation stimulating protein;
DE Short=ASP;
DE AltName: Full=C3adesArg;
DE Contains:
DE RecName: Full=Complement C3b alpha' chain;
DE Contains:
DE RecName: Full=Complement C3c alpha' chain fragment 1;
DE Contains:
DE RecName: Full=Complement C3dg fragment;
DE Contains:
DE RecName: Full=Complement C3g fragment;
DE Contains:
DE RecName: Full=Complement C3d fragment;
DE Contains:
DE RecName: Full=Complement C3f fragment;
DE Contains:
DE RecName: Full=Complement C3c alpha' chain fragment 2;
DE Flags: Precursor;
GN Name=C3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (3.0
RP ANGSTROMS) OF C3.
RX PubMed=16831446; DOI=10.1016/j.jmb.2006.06.009;
RA Fredslund F., Jenner L., Husted L.B., Nyborg J., Andersen G.R.,
RA Sottrup-Jensen L.;
RT "The structure of bovine complement component 3 reveals the basis for
RT thioester function.";
RL J. Mol. Biol. 361:115-127(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH BHV-1 GLYCOPROTEIN C (MICROBIAL INFECTION).
RX PubMed=8390825; DOI=10.1007/bf01309666;
RA Huemer H.P., Larcher C., van Drunen Littel-van den Hurk S., Babiuk L.A.;
RT "Species selective interaction of Alphaherpesvirinae with the 'unspecific'
RT immune system of the host.";
RL Arch. Virol. 130:353-364(1993).
CC -!- FUNCTION: C3 plays a central role in the activation of the complement
CC system. Its processing by C3 convertase is the central reaction in both
CC classical and alternative complement pathways. After activation C3b can
CC bind covalently, via its reactive thioester, to cell surface
CC carbohydrates or immune aggregates (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Derived from proteolytic degradation of complement C3, C3a
CC anaphylatoxin is a mediator of local inflammatory process. It induces
CC the contraction of smooth muscle, increases vascular permeability and
CC causes histamine release from mast cells and basophilic leukocytes. In
CC chronic inflammation, acts as a chemoattractant for neutrophils (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: [C3-beta-c]: Acts as a chemoattractant for neutrophils in
CC chronic inflammation. {ECO:0000250}.
CC -!- FUNCTION: [Acylation stimulating protein]: Adipogenic hormone that
CC stimulates triglyceride (TG) synthesis and glucose transport in
CC adipocytes, regulating fat storage and playing a role in postprandial
CC TG clearance. Appears to stimulate TG synthesis via activation of the
CC PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the
CC phosphorylation, ARRB2-internalization and recycling of C5AR2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: C3 precursor is first processed by the removal of 4 Arg
CC residues, forming two chains, beta and alpha, linked by a disulfide
CC bond. C3 convertase activates C3 by cleaving the alpha chain, releasing
CC C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). Forms
CC the pro-C3-convertase enzyme complex by binding to Complement factor B
CC Bb fragment (Bb), which is then stabilized by binding CFP, allowing the
CC complex to become active (By similarity). The interaction with Bb is
CC dependent on Mg2+ (By similarity). C3b interacts with CR1 (via Sushi 8
CC and Sushi 9 domains). C3b interacts with CFH. C3d interacts with CFH.
CC C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2).
CC During pregnancy, C3dg exists as a complex (probably a 2:2:2
CC heterohexamer) with AGT and the proform of PRG2. Interacts with VSIG4.
CC Interacts with S.aureus immunoglobulin-binding protein sbi, this
CC prevents interaction between C3dg and CR2. Interacts with S.aureus fib.
CC Interacts (both C3a and ASP) with C5AR2; the interaction occurs with
CC higher affinity for ASP, enhancing the phosphorylation and activation
CC of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of
CC GRP77. {ECO:0000250|UniProtKB:P01024}.
CC -!- SUBUNIT: (Microbial infection) Interacts with BHV-1 GLYCOPROTEIN C.
CC {ECO:0000269|PubMed:8390825}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: C3b is rapidly split in two positions by factor I and a cofactor
CC to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is
CC slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha'
CC chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other
CC proteases produce other fragments such as C3d or C3g. C3a is further
CC processed by carboxypeptidases to release the C-terminal arginine
CC residue generating the acylation stimulating protein (ASP). Levels of
CC ASP are increased in adipocytes in the postprandial period and by
CC dietary chylomicrons (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P01024}.
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DR EMBL; AM086793; CAJ31249.1; -; Genomic_DNA.
DR EMBL; BC112452; AAI12453.1; -; mRNA.
DR RefSeq; NP_001035559.2; NM_001040469.2.
DR RefSeq; XP_010805188.1; XM_010806886.2.
DR PDB; 8CEM; X-ray; 3.00 A; A/B=1-1661.
DR PDBsum; 8CEM; -.
DR AlphaFoldDB; Q2UVX4; -.
DR SMR; Q2UVX4; -.
DR STRING; 9913.ENSBTAP00000022979; -.
DR MEROPS; I39.950; -.
DR GlyCosmos; Q2UVX4; 2 sites, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000022979; -.
DR PeptideAtlas; Q2UVX4; -.
DR Ensembl; ENSBTAT00000022979.5; ENSBTAP00000022979.5; ENSBTAG00000017280.5.
DR GeneID; 280677; -.
DR KEGG; bta:280677; -.
DR CTD; 718; -.
DR VEuPathDB; HostDB:ENSBTAG00000017280; -.
DR VGNC; VGNC:26638; C3.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000154063; -.
DR InParanoid; Q2UVX4; -.
DR OMA; QATNTMQ; -.
DR OrthoDB; 4033541at2759; -.
DR Reactome; R-BTA-173736; Alternative complement activation.
DR Reactome; R-BTA-174577; Activation of C3 and C5.
DR Reactome; R-BTA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-BTA-977606; Regulation of Complement cascade.
DR EvolutionaryTrace; Q2UVX4; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000017280; Expressed in liver and 104 other cell types or tissues.
DR ExpressionAtlas; Q2UVX4; baseline.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0031715; F:C5L2 anaphylatoxin chemotactic receptor binding; ISS:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0097242; P:amyloid-beta clearance; IEA:Ensembl.
DR GO; GO:0006956; P:complement activation; IBA:GO_Central.
DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0097278; P:complement-dependent cytotoxicity; IEA:Ensembl.
DR GO; GO:0150062; P:complement-mediated synapse pruning; IEA:Ensembl.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0016322; P:neuron remodeling; IEA:Ensembl.
DR GO; GO:0035846; P:oviduct epithelium development; IEA:Ensembl.
DR GO; GO:0001970; P:positive regulation of activation of membrane attack complex; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:2000427; P:positive regulation of apoptotic cell clearance; IEA:Ensembl.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0010884; P:positive regulation of lipid storage; ISS:UniProtKB.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0001798; P:positive regulation of type IIa hypersensitivity; IEA:Ensembl.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IEA:Ensembl.
DR GO; GO:0010866; P:regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0150064; P:vertebrate eye-specific patterning; IEA:Ensembl.
DR CDD; cd00017; ANATO; 1.
DR CDD; cd02896; complement_C3_C4_C5; 1.
DR CDD; cd03583; NTR_complement_C3; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 3.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 6.20.50.160; -; 1.
DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 1.20.91.20; Anaphylotoxins (complement system); 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
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; IPR049466; C3_CUB1.
DR InterPro; IPR048848; C3_CUB2.
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; COMPLEMENT C3; 1.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 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; PF21406; C3_CUB1; 1.
DR Pfam; PF21308; C3_CUB2; 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 SFLD; SFLDG01179; Complement_C3/C4_Like; 1.
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 SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF47686; Anaphylotoxins (complement system); 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR SUPFAM; SSF50242; TIMP-like; 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 alternate pathway; Complement pathway; Disulfide bond;
KW Fatty acid metabolism; Glycoprotein; Immunity; Inflammatory response;
KW Innate immunity; Lipid metabolism; Phosphoprotein; Reference proteome;
KW Secreted; Signal; Thioester bond.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT CHAIN 23..1661
FT /note="Complement C3"
FT /id="PRO_0000236227"
FT CHAIN 23..665
FT /note="Complement C3 beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000236228"
FT CHAIN 567..665
FT /note="C3-beta-c"
FT /evidence="ECO:0000250"
FT /id="PRO_0000430428"
FT CHAIN 670..1661
FT /note="Complement C3 alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000236229"
FT CHAIN 670..746
FT /note="C3a anaphylatoxin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000236230"
FT CHAIN 670..745
FT /note="Acylation stimulating protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000419934"
FT CHAIN 747..1661
FT /note="Complement C3b alpha' chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000236231"
FT CHAIN 747..953
FT /note="Complement C3c alpha' chain fragment 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000273938"
FT CHAIN 954..1302
FT /note="Complement C3dg fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000273939"
FT CHAIN 954..1000
FT /note="Complement C3g fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000273940"
FT CHAIN 1001..1302
FT /note="Complement C3d fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000236232"
FT PEPTIDE 1303..1319
FT /note="Complement C3f fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000273941"
FT CHAIN 1320..1661
FT /note="Complement C3c alpha' chain fragment 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000273942"
FT DOMAIN 691..726
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 1516..1659
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 1632..1657
FT /note="Interaction with CFP/properdin"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT SITE 745..746
FT /note="Cleavage; by carboxypeptidases"
FT /evidence="ECO:0000250"
FT SITE 746..747
FT /note="Cleavage; by C3 convertase"
FT /evidence="ECO:0000250"
FT SITE 953..954
FT /note="Cleavage; by factor I"
FT /evidence="ECO:0000250"
FT SITE 1302..1303
FT /note="Cleavage; by factor I"
FT /evidence="ECO:0000250"
FT SITE 1319..1320
FT /note="Cleavage; by factor I"
FT /evidence="ECO:0000250"
FT SITE 1661
FT /note="Coordinates Mg2+ for interaction with Complement
FT factor B Bb fragment"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 1320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 1571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 557..815
FT /note="Interchain (between beta and alpha chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022,
FT ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 625..660
FT /evidence="ECO:0000250"
FT DISULFID 691..718
FT /evidence="ECO:0000250"
FT DISULFID 692..725
FT /evidence="ECO:0000250"
FT DISULFID 705..726
FT /evidence="ECO:0000250"
FT DISULFID 872..1511
FT /evidence="ECO:0000250"
FT DISULFID 1100..1157
FT /evidence="ECO:0000250"
FT DISULFID 1357..1487
FT /evidence="ECO:0000250"
FT DISULFID 1388..1456
FT /evidence="ECO:0000250"
FT DISULFID 1504..1509
FT /evidence="ECO:0000250"
FT DISULFID 1516..1588
FT /evidence="ECO:0000250"
FT DISULFID 1535..1659
FT /evidence="ECO:0000250"
FT DISULFID 1635..1644
FT /evidence="ECO:0000250"
FT CROSSLNK 1009..1012
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
FT CONFLICT 533
FT /note="Y -> N (in Ref. 2; AAI12453)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="S -> I (in Ref. 2; AAI12453)"
FT /evidence="ECO:0000305"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 181..185
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 212..223
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 418..424
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 453..457
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 468..476
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 495..505
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 527..533
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 545..551
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 578..585
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 598..601
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 605..607
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 611..618
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 632..639
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 672..682
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 688..694
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 705..708
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 709..711
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 716..736
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 756..758
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 769..774
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 786..793
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 799..805
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 810..812
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 813..815
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 820..823
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 827..833
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 838..841
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 843..852
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 859..865
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 882..887
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 892..901
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 905..920
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 922..931
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 933..946
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 948..951
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 953..955
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 957..961
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 967..969
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 976..984
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 987..993
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 996..998
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 999..1001
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1002..1005
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1012..1016
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1018..1030
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1033..1035
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1040..1056
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1075..1088
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 1089..1091
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1096..1109
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1140..1152
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 1153..1160
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1164..1178
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 1179..1181
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1185..1197
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1203..1212
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 1215..1217
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1225..1242
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 1245..1247
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1249..1257
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1268..1284
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1288..1290
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1296..1298
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1300..1304
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1310..1315
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1317..1321
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1329..1333
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1339..1349
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1358..1368
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1382..1391
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1393..1395
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1399..1405
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1410..1412
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1414..1422
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1423..1425
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1429..1439
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1441..1447
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1451..1453
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1455..1463
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1465..1469
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1473..1479
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1485..1491
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1506..1511
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 1512..1516
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 1529..1534
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1539..1551
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1554..1566
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1576..1578
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1581..1585
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 1586..1588
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1589..1592
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1599..1606
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1633..1636
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1639..1646
FT /evidence="ECO:0007829|PDB:8CEM"
FT HELIX 1647..1649
FT /evidence="ECO:0007829|PDB:8CEM"
FT TURN 1650..1653
FT /evidence="ECO:0007829|PDB:8CEM"
FT STRAND 1654..1656
FT /evidence="ECO:0007829|PDB:8CEM"
SQ SEQUENCE 1661 AA; 187253 MW; 3EBBE948F0638AD2 CRC64;
MKPTSGPSLL LLLLASLPMA LGNPMYSMIT PNILRLESEE TVVLEAHGGQ GTIQVSVTVH
DFPAKKQVLS NENTQLNSNN GYLSTVTIKI PASKELKSDK GHKFVTVVAT FGNVQVEKVV
LISLQSGYLF IQTDKTIYTP GSTVLYRVFT VDHKLLPVGQ TVFITIETPD GIPVKRDSKS
SQNQFGILTL SWNIPELVNM GVWKIKAYYE DSPQQVFSAE FEVKEYVLPS FEVQLEPEEK
FYYIDDPDGL KVNIIARFLY GEQVDGTAFV IFGVQDGDRR ISLTHSLTRV PINDGNGEAI
LKRQVLLNGV QPSRADALVG KSIYVSATVI LQSGSDMVEA ERTGIPIVTS PYQIHFTKTP
KFFKPAMPFD LMVYVTNPDG SPARHIPVVT QGSNVQSLTQ DDGVAKLSIN TQNKRDPLTI
TVRTKKDNIP EGRQATRTMQ ALPYNTQGNS NNYLHLSVPR VELKPGETLN VNFHLRTDPG
EQAKIRYYTY MIMNKGKLLK VGRQYREPGQ DLVVLPLTIT SDFIPSFRLV AYYTLINAKG
QREVVADSVW VDVKDSCMGT LVVKNGGKEE KHHRPGQQIT LKIEADQGAR VGLVAVDKGV
FVLNKKNKLT QRKIWDVVEK ADIGCTPGSG RNYAGVFTDA GLTLKTSQGL ETQQRADPQC
PQPATRRRRS VQLMEKRMDK AGQYSSDLRK CCEDGMRDNP MKFPCQRRAQ FILQGDACVK
AFLDCCEYIT QLRQQHSRDG ALELARSDLD DDIIPEEDII SRSQFPESWL WTVIEDLKQA
DKNGISTKLM NVFLKDSITT WEILAVSLSD KKGICVADPY EVTVMQDFFI DLRLPYSVVR
NEQVEIRAIL YNYREAENLK VRVELLYNPA FCSLATAKKR HQQTITIPAR SSVAVPYVIV
PLKIGLHEVE VKAAVYNHFI SDGVKKTLKV VPEGVRVNKT VAVRTLNPEH LGQGGVQREE
VPAADLSDQV PDTESETKIL LQGTPVAQMT EDAIDGERLK HLIQTPSGCG EQNMIGMTPT
VIAVHYLDST DQWEKFGLEK RQESLELIRK GYTQQLAFRQ KSSAYAAFQY RPPSTWLTAY
VVKVFALAAN LIAIDSKDLC ETVKWLILEK QKPDGIFQED GPVIHQEMIG GFRDTREKDV
SLTAFVLIAL HEAKDICEAQ VNSLGRSIAK AGDFLENHYR ELRRPYTVAI AAYALALLGK
LEGDRLTKFL NTAKEKNRWE EPNQKLYNVE ATSYALLALL ARKDYDTTPP VVRWLNEQRY
YGGGYGSTQA TFMVFQALAQ YQKDVPDHKE LNLDVSIQLP SRNSAVRHRI LWESASLLRS
EETKENERFT VKAEGKGQGT LSVVTVYHAK LKGKVSCKKF DLRVSIRPAP ETVKKPQDAK
GSMILDICTK YLGDQDATMS ILDISMMTGF SPDVEDLKTL STGVDRYISK YEMNRDSNKN
TLIIYLDKVS HTVEDCLSFK VHQYFNVGLI QPGAVKVYSY YNLDETCIRF YHPDKEDGML
SKLCHKDTCR CAEENCFMHH TEKEVTLEDR LDKACEPGVD YVYKTRLIQK KLEDDFDEYI
MVIENIIKSG SDEVQVKQER KFISHIKCRE ALKLKEGAHY LVWGVSSDLW GEKPKISYII
GKDTWVELWP EAEECQDEEN QKQCEDLANF TENMVVFGCP N
//
