CDC4_YEAST
ID CDC4_YEAST Reviewed; 779 AA.
AC P07834; D6VTM1;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Cell division control protein 4;
DE AltName: Full=E3 ubiquitin ligase complex SCF subunit CDC4;
DE AltName: Full=F-box protein CDC4;
GN Name=CDC4; OrderedLocusNames=YFL009W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3309335; DOI=10.1016/0022-2836(87)90646-2;
RA Yochem J., Byers B.;
RT "Structural comparison of the yeast cell division cycle gene CDC4 and a
RT related pseudogene.";
RL J. Mol. Biol. 195:233-245(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-579.
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Barrell B.G., Churcher C., Rajandream M.A.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=7813440; DOI=10.1002/j.1460-2075.1994.tb06948.x;
RA Kornitzer D., Raboy B., Kulka R.G., Fink G.R.;
RT "Regulated degradation of the transcription factor Gcn4.";
RL EMBO J. 13:6021-6030(1994).
RN [6]
RP INTERACTION WITH SKP1/CBF3D.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8706131; DOI=10.1016/s0092-8674(00)80098-7;
RA Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.W., Elledge S.J.;
RT "SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery
RT through a novel motif, the F-box.";
RL Cell 86:263-274(1996).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9346238; DOI=10.1016/s0092-8674(00)80403-1;
RA Skowyra D., Craig K.L., Tyers M., Elledge S.J., Harper J.W.;
RT "F-box proteins are receptors that recruit phosphorylated substrates to the
RT SCF ubiquitin-ligase complex.";
RL Cell 91:209-219(1997).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9346239; DOI=10.1016/s0092-8674(00)80404-3;
RA Feldman R.M., Correll C.C., Kaplan K.B., Deshaies R.J.;
RT "A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of
RT the phosphorylated CDK inhibitor Sic1p.";
RL Cell 91:221-230(1997).
RN [9]
RP FUNCTION, AND INTERACTION WITH SKP1.
RX PubMed=9312022; DOI=10.1093/emboj/16.18.5629;
RA Li F.N., Johnston M.;
RT "Grr1 of Saccharomyces cerevisiae is connected to the ubiquitin proteolysis
RT machinery through Skp1: coupling glucose sensing to gene expression and the
RT cell cycle.";
RL EMBO J. 16:5629-5638(1997).
RN [10]
RP FUNCTION, AND INTERACTION WITH CDC6.
RX PubMed=9312054; DOI=10.1093/emboj/16.19.5966;
RA Drury L.S., Perkins G., Diffley J.F.;
RT "The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast.";
RL EMBO J. 16:5966-5976(1997).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9736614; DOI=10.1093/emboj/17.18.5360;
RA Jaquenoud M., Gulli M.P., Peter K., Peter M.;
RT "The Cdc42p effector Gic2p is targeted for ubiquitin-dependent degradation
RT by the SCFGrr1 complex.";
RL EMBO J. 17:5360-5373(1998).
RN [12]
RP INTERACTION WITH CDC53.
RX PubMed=9499404; DOI=10.1101/gad.12.5.692;
RA Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L.,
RA Tyers M.;
RT "Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein
RT complexes that regulate cell division and methionine biosynthesis in
RT yeast.";
RL Genes Dev. 12:692-705(1998).
RN [13]
RP INTERACTION WITH HRT1.
RX PubMed=10385629; DOI=10.1101/gad.13.12.1614;
RA Seol J.H., Feldman R.M.R., Zachariae W., Shevchenko A., Correll C.C.,
RA Lyapina S., Chi Y., Galova M., Claypool J., Sandmeyer S., Nasmyth K.,
RA Shevchenko A., Deshaies R.J.;
RT "Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a
RT ubiquitin ligase module that activates the E2 enzyme Cdc34.";
RL Genes Dev. 13:1614-1626(1999).
RN [14]
RP FUNCTION.
RX PubMed=10409741; DOI=10.1128/mcb.19.8.5512;
RA Goh P.Y., Surana U.;
RT "Cdc4, a protein required for the onset of S phase, serves an essential
RT function during G(2)/M transition in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 19:5512-5522(1999).
RN [15]
RP FUNCTION, AND RECONSTITUTION OF THE SKF(GRR1)COMPLEX.
RX PubMed=10213692; DOI=10.1126/science.284.5414.662;
RA Skowyra D., Koepp D.M., Kamura T., Conrad M.N., Conaway R.C., Conaway J.W.,
RA Elledge S.J., Harper J.W.;
RT "Reconstitution of G1 cyclin ubiquitination with complexes containing
RT SCFGrr1 and Rbx1.";
RL Science 284:662-665(1999).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 82-LYS-ARG-83 AND
RP LYS-85.
RX PubMed=11080155; DOI=10.1093/emboj/19.22.6085;
RA Blondel M., Galan J.M., Chi Y., Lafourcade C., Longaretti C.,
RA Deshaies R.J., Peter M.;
RT "Nuclear-specific degradation of Far1 is controlled by the localization of
RT the F-box protein Cdc4.";
RL EMBO J. 19:6085-6097(2000).
RN [17]
RP INTERACTION WITH CIC1.
RX PubMed=11500370; DOI=10.1093/emboj/20.16.4423;
RA Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.;
RT "Cic1, an adaptor protein specifically linking the 26S proteasome to its
RT substrate, the SCF component Cdc4.";
RL EMBO J. 20:4423-4431(2001).
RN [18]
RP INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(CDC4) COMPLEX.
RX PubMed=14747994; DOI=10.1002/prot.10620;
RA Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.;
RT "Functional interaction of 13 yeast SCF complexes with a set of yeast E2
RT enzymes in vitro.";
RL Proteins 54:455-467(2004).
RN [19]
RP HOMODIMERIZATION, AND INTERACTION WITH SIC1.
RX PubMed=17434132; DOI=10.1016/j.molcel.2007.02.022;
RA Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P.;
RT "Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated
RT substrate recognition by SCF ubiquitin ligases.";
RL Mol. Cell 26:131-143(2007).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Recognizes and binds to phosphorylated target proteins.
CC Directs ubiquitination of the phosphorylated CDK inhibitor SIC1.
CC Involved in the degradation of CDC6 together with CDC34/UBC3 and CDC53,
CC and in restricting the degradation of FAR1 to the nucleus. Is essential
CC for initiation of DNA replication and separation of the spindle pole
CC bodies to form the poles of the mitotic spindle. It also plays a role
CC in bud development, fusion of zygotic nuclei after conjugation and
CC various aspects of sporulation. Required for HTA1-HTB1 locus
CC transcription activation. Required for G1/S and G2/M transition.
CC {ECO:0000269|PubMed:10213692, ECO:0000269|PubMed:10409741,
CC ECO:0000269|PubMed:11080155, ECO:0000269|PubMed:7813440,
CC ECO:0000269|PubMed:9312022, ECO:0000269|PubMed:9312054,
CC ECO:0000269|PubMed:9346238, ECO:0000269|PubMed:9346239,
CC ECO:0000269|PubMed:9736614}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DCD53 and SKP1. Component of the SCF(CDC4)
CC complex containing CDC53, SKP1, RBX1 and CDC4. CDC34. Interacts with
CC CDC6 and CIC1. Interacts with SIC1; the interaction involves a SIC1
CC double phosphorylated motif (degron). Homodimerizes; the dimerization
CC increases SIC1 ubiquitination in vitro. {ECO:0000269|PubMed:10385629,
CC ECO:0000269|PubMed:11500370, ECO:0000269|PubMed:14747994,
CC ECO:0000269|PubMed:17434132, ECO:0000269|PubMed:8706131,
CC ECO:0000269|PubMed:9312022, ECO:0000269|PubMed:9312054,
CC ECO:0000269|PubMed:9346238, ECO:0000269|PubMed:9346239,
CC ECO:0000269|PubMed:9499404, ECO:0000269|PubMed:9736614}.
CC -!- INTERACTION:
CC P07834; Q12018: CDC53; NbExp=8; IntAct=EBI-4434, EBI-4321;
CC P07834; P38779: CIC1; NbExp=2; IntAct=EBI-4434, EBI-24538;
CC P07834; Q08273: HRT1; NbExp=3; IntAct=EBI-4434, EBI-31686;
CC P07834; P36054: RCN1; NbExp=4; IntAct=EBI-4434, EBI-14898;
CC P07834; P38634: SIC1; NbExp=5; IntAct=EBI-4434, EBI-17127;
CC P07834; P52286: SKP1; NbExp=14; IntAct=EBI-4434, EBI-4090;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11080155}.
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DR EMBL; X05625; CAA29113.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09229.1; -; Genomic_DNA.
DR EMBL; Z46255; CAA86341.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12431.1; -; Genomic_DNA.
DR PIR; S56245; S56245.
DR RefSeq; NP_116585.1; NM_001179957.1.
DR PDB; 1NEX; X-ray; 2.70 A; B/D=263-744.
DR PDB; 2P63; X-ray; 2.67 A; A/B/C/D=222-273.
DR PDB; 3MKS; X-ray; 2.60 A; B/D=263-744.
DR PDB; 3V7D; X-ray; 2.31 A; B/D=263-744.
DR PDBsum; 1NEX; -.
DR PDBsum; 2P63; -.
DR PDBsum; 3MKS; -.
DR PDBsum; 3V7D; -.
DR AlphaFoldDB; P07834; -.
DR SMR; P07834; -.
DR BioGRID; 31138; 614.
DR ComplexPortal; CPX-3234; SCF-Cdc4 ubiquitin ligase complex.
DR DIP; DIP-1625N; -.
DR IntAct; P07834; 14.
DR MINT; P07834; -.
DR STRING; 4932.YFL009W; -.
DR iPTMnet; P07834; -.
DR MaxQB; P07834; -.
DR PaxDb; P07834; -.
DR PRIDE; P07834; -.
DR EnsemblFungi; YFL009W_mRNA; YFL009W; YFL009W.
DR GeneID; 850539; -.
DR KEGG; sce:YFL009W; -.
DR SGD; S000001885; CDC4.
DR VEuPathDB; FungiDB:YFL009W; -.
DR eggNOG; KOG0274; Eukaryota.
DR GeneTree; ENSGT00940000174696; -.
DR HOGENOM; CLU_000288_103_3_1; -.
DR InParanoid; P07834; -.
DR OMA; CLQHDDE; -.
DR BioCyc; YEAST:G3O-30447-MON; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P07834; -.
DR PRO; PR:P07834; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P07834; protein.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IDA:SGD.
DR GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0050815; F:phosphoserine residue binding; IDA:SGD.
DR GO; GO:0034511; F:U3 snoRNA binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR031740; Cdc4_D.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF16856; CDC4_D; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Sporulation; Ubl conjugation pathway;
KW WD repeat.
FT CHAIN 1..779
FT /note="Cell division control protein 4"
FT /id="PRO_0000050899"
FT DOMAIN 272..319
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 380..408
FT /note="WD 1"
FT REPEAT 420..449
FT /note="WD 2"
FT REPEAT 461..493
FT /note="WD 3"
FT REPEAT 528..556
FT /note="WD 4"
FT REPEAT 568..598
FT /note="WD 5"
FT REPEAT 630..658
FT /note="WD 6"
FT REPEAT 669..698
FT /note="WD 7"
FT REGION 39..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 82..85
FT /note="Nuclear localization signal"
FT COMPBIAS 60..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 82
FT /note="K->A: Prevents nuclear localization; when associated
FT with A-83 and A-85."
FT MUTAGEN 83
FT /note="R->A: Prevents nuclear localization; when associated
FT with A-82 and A-85."
FT MUTAGEN 83
FT /note="R->G: Prevents nuclear localization."
FT MUTAGEN 85
FT /note="K->A: Prevents nuclear localization; when associated
FT with A-82 and A-83."
FT /evidence="ECO:0000269|PubMed:11080155"
FT CONFLICT 460
FT /note="K -> E (in Ref. 1; CAA29113)"
FT /evidence="ECO:0000305"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:2P63"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:2P63"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:2P63"
FT HELIX 256..271
FT /evidence="ECO:0007829|PDB:2P63"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 347..366
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:3MKS"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 450..453
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 466..476
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 478..484
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:3V7D"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 533..539
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 542..547
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 552..556
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 557..560
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 573..579
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 580..583
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 584..589
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 594..598
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 599..601
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 625..628
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 635..640
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 642..649
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 652..658
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 659..661
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 664..669
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 676..681
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 683..690
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 693..698
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 699..701
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 704..707
FT /evidence="ECO:0007829|PDB:3V7D"
FT TURN 709..712
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 714..722
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 725..732
FT /evidence="ECO:0007829|PDB:3V7D"
FT STRAND 735..742
FT /evidence="ECO:0007829|PDB:3V7D"
SQ SEQUENCE 779 AA; 86090 MW; 0348F2F8FA78F3BC CRC64;
MGSFPLAEFP LRDIPVPYSY RVSGGIASSG SVTALVTAAG THRNSSTAKT VETEDGEEDI
DEYQRKRAAG SGESTPERSD FKRVKHDNHK TLHPVNLQNT GAASVDNDGL HNLTDISNDA
EKLLMSVDDG SAAPSTLSVN MGVASHNVAA PTTVNAATIT GSDVSNNVNS ATINNPMEEG
ALPLSPTASS PGTTTPLAKT TKTINNNNNI ADLIESKDSI ISPEYLSDEI FSAINNNLPH
AYFKNLLFRL VANMDRSELS DLGTLIKDNL KRDLITSLPF EISLKIFNYL QFEDIINSLG
VSQNWNKIIR KSTSLWKKLL ISENFVSPKG FNSLNLKLSQ KYPKLSQQDR LRLSFLENIF
ILKNWYNPKF VPQRTTLRGH MTSVITCLQF EDNYVITGAD DKMIRVYDSI NKKFLLQLSG
HDGGVWALKY AHGGILVSGS TDRTVRVWDI KKGCCTHVFK GHNSTVRCLD IVEYKNIKYI
VTGSRDNTLH VWKLPKESSV PDHGEEHDYP LVFHTPEENP YFVGVLRGHM ASVRTVSGHG
NIVVSGSYDN TLIVWDVAQM KCLYILSGHT DRIYSTIYDH ERKRCISASM DTTIRIWDLE
NIWNNGECSY ATNSASPCAK ILGAMYTLQG HTALVGLLRL SDKFLVSAAA DGSIRGWDAN
DYSRKFSYHH TNLSAITTFY VSDNILVSGS ENQFNIYNLR SGKLVHANIL KDADQIWSVN
FKGKTLVAAV EKDGQSFLEI LDFSKASKIN YVSNPVNSSS SSLESISTSL GLTRTTIIP
