CEP1_CAEEL
ID CEP1_CAEEL Reviewed; 644 AA.
AC Q20646; Q564Z1; Q95V13;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Transcription factor cep-1 {ECO:0000305};
DE AltName: Full=C.elegans p53-like protein 1 {ECO:0000312|WormBase:F52B5.5a};
GN Name=cep-1 {ECO:0000312|WormBase:F52B5.5a};
GN ORFNames=F52B5.5 {ECO:0000312|WormBase:F52B5.5a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL28139.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11696333; DOI=10.1016/s0960-9822(01)00534-6;
RA Schumacher B., Hofmann K., Boulton S.J., Gartner A.;
RT "The C. elegans homolog of the p53 tumor suppressor is required for DNA
RT damage-induced apoptosis.";
RL Curr. Biol. 11:1722-1727(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA99857.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=11557844; DOI=10.1126/science.1065486;
RA Derry W.B., Putzke A.P., Rothman J.H.;
RT "Caenorhabditis elegans p53: role in apoptosis, meiosis, and stress
RT resistance.";
RL Science 294:591-595(2001).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=12445383; DOI=10.1016/s0960-9822(02)01262-9;
RA Hofmann E.R., Milstein S., Boulton S.J., Ye M., Hofmann J.J., Stergiou L.,
RA Gartner A., Vidal M., Hengartner M.O.;
RT "Caenorhabditis elegans HUS-1 is a DNA damage checkpoint protein required
RT for genome stability and EGL-1-mediated apoptosis.";
RL Curr. Biol. 12:1908-1918(2002).
RN [5]
RP FUNCTION, INTERACTION WITH APE-1, AND DISRUPTION PHENOTYPE.
RX PubMed=12524540; DOI=10.1038/ng1070;
RA Bergamaschi D., Samuels Y., O'Neil N.J., Trigiante G., Crook T.,
RA Hsieh J.-K., O'Connor D.J., Zhong S., Campargue I., Tomlinson M.L.,
RA Kuwabara P.E., Lu X.;
RT "iASPP oncoprotein is a key inhibitor of p53 conserved from worm to
RT human.";
RL Nat. Genet. 33:162-167(2003).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15273685; DOI=10.1038/ng1396;
RA Deng X., Hofmann E.R., Villanueva A., Hobert O., Capodieci P., Veach D.R.,
RA Yin X., Campodonico L., Glekas A., Cordon-Cardo C., Clarkson B.,
RA Bornmann W.G., Fuks Z., Hengartner M.O., Kolesnick R.;
RT "Caenorhabditis elegans ABL-1 antagonizes p53-mediated germline apoptosis
RT after ionizing irradiation.";
RL Nat. Genet. 36:906-912(2004).
RN [7] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15707894; DOI=10.1016/j.cell.2004.12.009;
RA Schumacher B., Hanazawa M., Lee M.-H., Nayak S., Volkmann K., Hofmann E.R.,
RA Hengartner M.O., Schedl T., Gartner A.;
RT "Translational repression of C. elegans p53 by GLD-1 regulates DNA damage-
RT induced apoptosis.";
RL Cell 120:357-368(2005).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=15605074; DOI=10.1038/sj.cdd.4401539;
RA Schumacher B., Schertel C., Wittenburg N., Tuck S., Mitani S., Gartner A.,
RA Conradt B., Shaham S.;
RT "C. elegans ced-13 can promote apoptosis and is induced in response to DNA
RT damage.";
RL Cell Death Differ. 12:153-161(2005).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=16319925; DOI=10.1038/sj.emboj.7600896;
RA Garcia-Muse T., Boulton S.J.;
RT "Distinct modes of ATR activation after replication stress and DNA double-
RT strand breaks in Caenorhabditis elegans.";
RL EMBO J. 24:4345-4355(2005).
RN [10] {ECO:0000305}
RP FUNCTION, INDUCTION, AND PHOSPHORYLATION.
RX PubMed=17276923; DOI=10.1016/j.cub.2006.12.038;
RA Quevedo C., Kaplan D.R., Derry W.B.;
RT "AKT-1 regulates DNA-damage-induced germline apoptosis in C. elegans.";
RL Curr. Biol. 17:286-292(2007).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=17186023; DOI=10.1038/sj.cdd.4402075;
RA Derry W.B., Bierings R., van Iersel M., Satkunendran T., Reinke V.,
RA Rothman J.H.;
RT "Regulation of developmental rate and germ cell proliferation in
RT Caenorhabditis elegans by the p53 gene network.";
RL Cell Death Differ. 14:662-670(2007).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=17347667; DOI=10.1038/sj.cdd.4402115;
RA Stergiou L., Doukoumetzidis K., Sendoel A., Hengartner M.O.;
RT "The nucleotide excision repair pathway is required for UV-C-induced
RT apoptosis in Caenorhabditis elegans.";
RL Cell Death Differ. 14:1129-1138(2007).
RN [13] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17895432; DOI=10.1093/gerona/62.9.951;
RA Arum O., Johnson T.E.;
RT "Reduced expression of the Caenorhabditis elegans p53 ortholog cep-1
RT results in increased longevity.";
RL J. Gerontol. 62:951-959(2007).
RN [14] {ECO:0000305}
RP FUNCTION.
RX PubMed=18627611; DOI=10.1186/1471-2164-9-334;
RA Greiss S., Schumacher B., Grandien K., Rothblatt J., Gartner A.;
RT "Transcriptional profiling in C. elegans suggests DNA damage dependent
RT apoptosis as an ancient function of the p53 family.";
RL BMC Genomics 9:334-334(2008).
RN [15] {ECO:0000305}
RP FUNCTION.
RX PubMed=18836529; DOI=10.1371/journal.pone.0003354;
RA Masse I., Molin L., Mouchiroud L., Vanhems P., Palladino F., Billaud M.,
RA Solari F.;
RT "A novel role for the SMG-1 kinase in lifespan and oxidative stress
RT resistance in Caenorhabditis elegans.";
RL PLoS ONE 3:E3354-E3354(2008).
RN [16] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19015549; DOI=10.1534/genetics.107.080515;
RA Luo J., Shah S., Riabowol K., Mains P.E.;
RT "The Caenorhabditis elegans ing-3 gene regulates ionizing radiation-induced
RT germ-cell apoptosis in a p53-associated pathway.";
RL Genetics 181:473-482(2009).
RN [17]
RP FUNCTION, INTERACTION WITH PRMT-5 AND CBP-1, AND DISRUPTION PHENOTYPE.
RX PubMed=19521535; DOI=10.1371/journal.pgen.1000514;
RA Yang M., Sun J., Sun X., Shen Q., Gao Z., Yang C.;
RT "Caenorhabditis elegans protein arginine methyltransferase PRMT-5
RT negatively regulates DNA damage-induced apoptosis.";
RL PLoS Genet. 5:E1000514-E1000514(2009).
RN [18] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=21901106; DOI=10.1371/journal.pgen.1002238;
RA Rutkowski R., Dickinson R., Stewart G., Craig A., Schimpl M., Keyse S.M.,
RA Gartner A.;
RT "Regulation of Caenorhabditis elegans p53/CEP-1-dependent germ cell
RT apoptosis by Ras/MAPK signaling.";
RL PLoS Genet. 7:E1002238-E1002238(2011).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26598553; DOI=10.1242/jcs.174201;
RA Min H., Shim Y.H., Kawasaki I.;
RT "Loss of PGL-1 and PGL-3, members of a family of constitutive germ-granule
RT components, promotes germline apoptosis in C. elegans.";
RL J. Cell Sci. 129:341-353(2016).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, AND DNA-BINDING.
RX PubMed=15242600; DOI=10.1016/j.str.2004.05.007;
RA Huyen Y., Jeffrey P.D., Derry W.B., Rothman J.H., Pavletich N.P.,
RA Stavridi E.S., Halazonetis T.D.;
RT "Structural differences in the DNA binding domains of human p53 and its C.
RT elegans ortholog Cep-1.";
RL Structure 12:1237-1243(2004).
RN [21]
RP STRUCTURE BY NMR OF 514-644, DIMERIZATION, MUTAGENESIS OF LYS-544; ARG-551
RP AND GLU-552, AND ZINC-BINDING SITES.
RX PubMed=17581633; DOI=10.1038/sj.emboj.7601764;
RA Ou H.D., Loehr F., Vogel V., Maentele W., Doetsch V.;
RT "Structural evolution of C-terminal domains in the p53 family.";
RL EMBO J. 26:3463-3473(2007).
CC -!- FUNCTION: Transcriptional activator that binds the same DNA consensus
CC sequence as p53 (PubMed:11696333, PubMed:15242600). Has a role in
CC normal development to ensure proper meiotic chromosome segregation
CC (PubMed:11557844, PubMed:12445383). Promotes apoptosis under conditions
CC of cellular and genotoxic stress in response to DNA damage, hypoxia, or
CC starvation (PubMed:11696333, PubMed:11557844, PubMed:12445383,
CC PubMed:15273685, PubMed:17186023, PubMed:18836529, PubMed:21901106).
CC Regulates germline apoptosis in response to DNA damage
CC (PubMed:11696333, PubMed:15273685, PubMed:15707894, PubMed:16319925,
CC PubMed:17276923, PubMed:17186023, PubMed:17347667, PubMed:19015549,
CC PubMed:26598553). Its pro-apoptotic activity is inhibited when bound to
CC ape-1 in vitro (PubMed:12524540). Plays a role in cell cycle arrest in
CC the germline in response to DNA damage by UV-C light (PubMed:17347667).
CC However, not required for survival in response to DNA damage induced by
CC UV-C light, indicating that it is unlikely to be involved in DNA repair
CC (PubMed:17347667). Required for induction of ced-13 in response to DNA
CC damage (PubMed:15605074). Regulates DNA damage-induced apoptosis by
CC inducing transcription of the programmed cell death activator egl-1
CC (PubMed:12445383, PubMed:19521535). Regulates germline proliferation by
CC activating phg-1 (PubMed:17186023). Negatively regulates lifespan
CC (PubMed:17895432, PubMed:18836529). {ECO:0000269|PubMed:11557844,
CC ECO:0000269|PubMed:11696333, ECO:0000269|PubMed:12445383,
CC ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:15242600,
CC ECO:0000269|PubMed:15273685, ECO:0000269|PubMed:15605074,
CC ECO:0000269|PubMed:15707894, ECO:0000269|PubMed:16319925,
CC ECO:0000269|PubMed:17186023, ECO:0000269|PubMed:17276923,
CC ECO:0000269|PubMed:17347667, ECO:0000269|PubMed:17895432,
CC ECO:0000269|PubMed:18627611, ECO:0000269|PubMed:18836529,
CC ECO:0000269|PubMed:19015549, ECO:0000269|PubMed:19521535,
CC ECO:0000269|PubMed:21901106, ECO:0000269|PubMed:26598553}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17581633};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17581633};
CC -!- SUBUNIT: Homodimer (PubMed:15707894). Interacts (via C-terminus domain)
CC with prmt-5; not methylated by prmt-5 (PubMed:19521535). Interacts with
CC cbp-1 (via HAT domain); cep-1 transcriptional activity may be inhibited
CC by interaction with methylated cbp-1 (PubMed:19521535). Component of a
CC complex that contains prmt-5 and cbp-1 (PubMed:19521535). Interacts
CC with ape-1; the interaction inhibits pro-apoptotic activity of cep-1
CC (PubMed:12524540). {ECO:0000269|PubMed:12524540,
CC ECO:0000269|PubMed:15707894, ECO:0000269|PubMed:19521535,
CC ECO:0000303|PubMed:19521535}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11557844}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000303|PubMed:11696333, ECO:0000312|WormBase:F52B5.5a};
CC IsoId=Q20646-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F52B5.5b};
CC IsoId=Q20646-2; Sequence=VSP_053085;
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal muscle and neurons.
CC {ECO:0000269|PubMed:11557844}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and larvae (PubMed:11557844,
CC PubMed:15707894). Expressed in the distal zone of mitotic germline and
CC in late pachytene, diplotene and diakinesis stages of meiotic germline
CC (PubMed:11557844, PubMed:15707894, PubMed:21901106).
CC {ECO:0000269|PubMed:11557844, ECO:0000269|PubMed:15707894,
CC ECO:0000269|PubMed:21901106}.
CC -!- INDUCTION: By DNA damage. {ECO:0000269|PubMed:17276923}.
CC -!- PTM: Phosphorylated in response to IR-induced DNA damage which is
CC thought to be mediated by akt-1. {ECO:0000269|PubMed:17276923}.
CC -!- DISRUPTION PHENOTYPE: Reduced numbers of germ cell corpses,
CC hypersensitive to the lethal effects of hypoxia, increase in production
CC of males (Him phenotype), decreased lifespan and in extreme cases
CC embryonic lethality (PubMed:11557844, PubMed:11696333, PubMed:15273685,
CC PubMed:17895432, PubMed:19015549, PubMed:26598553). In cep-1 and prmt-5
CC double mutants, germline cell death and up-regulation of egl-1 mRNA
CC induced by gamma irradiation is prevented (PubMed:19521535). Double
CC RNAi-mediated knockdown together with ape-1 abrogates the increased
CC number of apoptotic germ cells in the ape-1 knockdown model
CC (PubMed:12524540). {ECO:0000269|PubMed:11557844,
CC ECO:0000269|PubMed:11696333, ECO:0000269|PubMed:12524540,
CC ECO:0000269|PubMed:15273685, ECO:0000269|PubMed:17895432,
CC ECO:0000269|PubMed:19015549, ECO:0000269|PubMed:19521535,
CC ECO:0000269|PubMed:26598553}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
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DR EMBL; AF440800; AAL28139.1; -; mRNA.
DR EMBL; BX284601; CAA99857.2; -; Genomic_DNA.
DR EMBL; BX284601; CAI79201.1; -; Genomic_DNA.
DR PIR; T22495; T22495.
DR RefSeq; NP_001021478.1; NM_001026307.5. [Q20646-1]
DR RefSeq; NP_001021479.1; NM_001026308.4.
DR PDB; 1T4W; X-ray; 2.10 A; A=223-418.
DR PDB; 2RP5; NMR; -; A/B=514-644.
DR PDBsum; 1T4W; -.
DR PDBsum; 2RP5; -.
DR AlphaFoldDB; Q20646; -.
DR SMR; Q20646; -.
DR BioGRID; 38050; 6.
DR ComplexPortal; CPX-1131; Prmt-5-cep-1-cbp-1 complex.
DR IntAct; Q20646; 1.
DR MINT; Q20646; -.
DR STRING; 6239.F52B5.5a.2; -.
DR EPD; Q20646; -.
DR PaxDb; Q20646; -.
DR PeptideAtlas; Q20646; -.
DR PRIDE; Q20646; -.
DR EnsemblMetazoa; F52B5.5a.1; F52B5.5a.1; WBGene00000467. [Q20646-1]
DR EnsemblMetazoa; F52B5.5b.1; F52B5.5b.1; WBGene00000467. [Q20646-2]
DR EnsemblMetazoa; F52B5.5b.2; F52B5.5b.2; WBGene00000467. [Q20646-2]
DR EnsemblMetazoa; F52B5.5b.3; F52B5.5b.3; WBGene00000467. [Q20646-2]
DR EnsemblMetazoa; F52B5.5b.4; F52B5.5b.4; WBGene00000467. [Q20646-2]
DR GeneID; 172616; -.
DR KEGG; cel:CELE_F52B5.5; -.
DR UCSC; F52B5.5a.1; c. elegans.
DR CTD; 172616; -.
DR WormBase; F52B5.5a; CE29805; WBGene00000467; cep-1. [Q20646-1]
DR WormBase; F52B5.5b; CE38369; WBGene00000467; cep-1. [Q20646-2]
DR eggNOG; ENOG502TH76; Eukaryota.
DR HOGENOM; CLU_425295_0_0_1; -.
DR InParanoid; Q20646; -.
DR OMA; VAYPRRD; -.
DR OrthoDB; 1351862at2759; -.
DR SignaLink; Q20646; -.
DR EvolutionaryTrace; Q20646; -.
DR PRO; PR:Q20646; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000467; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005730; C:nucleolus; IDA:WormBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IDA:WormBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:ComplexPortal.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:UniProtKB.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IMP:WormBase.
DR GO; GO:0042770; P:signal transduction in response to DNA damage; IDA:UniProtKB.
DR CDD; cd08367; P53; 1.
DR Gene3D; 2.60.40.720; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR InterPro; IPR011615; p53_DNA-bd.
DR InterPro; IPR015367; Trans_fact_CEP1_DNA-bd.
DR Pfam; PF09287; CEP1-DNA_bind; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Apoptosis; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor; Zinc.
FT CHAIN 1..644
FT /note="Transcription factor cep-1"
FT /id="PRO_0000371248"
FT DNA_BIND 223..418
FT /evidence="ECO:0000255"
FT REGION 528..555
FT /note="Required for tertiary structure stability of the
FT protein"
FT /evidence="ECO:0000269|PubMed:17581633"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17581633"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17581633"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17581633"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17581633"
FT VAR_SEQ 1..447
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053085"
FT MUTAGEN 544
FT /note="K->L: Disrupts homodimer formation."
FT /evidence="ECO:0000269|PubMed:17581633"
FT MUTAGEN 551
FT /note="R->L: Disrupts homodimer formation."
FT /evidence="ECO:0000269|PubMed:17581633"
FT MUTAGEN 552
FT /note="E->L: Disrupts homodimer formation."
FT /evidence="ECO:0000269|PubMed:17581633"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1T4W"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:1T4W"
FT TURN 271..275
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1T4W"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:1T4W"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 352..361
FT /evidence="ECO:0007829|PDB:1T4W"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1T4W"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 373..382
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 388..399
FT /evidence="ECO:0007829|PDB:1T4W"
FT HELIX 403..416
FT /evidence="ECO:0007829|PDB:1T4W"
FT STRAND 532..538
FT /evidence="ECO:0007829|PDB:2RP5"
FT HELIX 539..554
FT /evidence="ECO:0007829|PDB:2RP5"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:2RP5"
FT HELIX 563..566
FT /evidence="ECO:0007829|PDB:2RP5"
FT TURN 571..573
FT /evidence="ECO:0007829|PDB:2RP5"
FT HELIX 576..581
FT /evidence="ECO:0007829|PDB:2RP5"
FT TURN 585..587
FT /evidence="ECO:0007829|PDB:2RP5"
FT HELIX 588..594
FT /evidence="ECO:0007829|PDB:2RP5"
FT HELIX 601..608
FT /evidence="ECO:0007829|PDB:2RP5"
FT HELIX 612..616
FT /evidence="ECO:0007829|PDB:2RP5"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:2RP5"
FT HELIX 623..641
FT /evidence="ECO:0007829|PDB:2RP5"
SQ SEQUENCE 644 AA; 74569 MW; AED566E5461212B0 CRC64;
MEPDDSQLSD ILKDARIPDS QDIGVNLTQN LSFDTVQKMI DGVFTPIFSQ GTEDSLEKDI
LKTPGISTIY NGILGNGEET KKRTPKISDA FEPDLNTSGD VFDSDKSEDG LMNDESYLSN
TTLSQVVLDS QKYEYLRVRT EEEQQLVIEK RARERFIRKS MKIAEETALS YENDGSRELS
ETMTQKVTQM DFTETNVPFD GNDESSNLAV RVQSDMNLNE DCEKWMEIDV LKQKVAKSSD
MAFAISSEHE KYLWTKMGCL VPIQVKWKLD KRHFNSNLSL RIRFVKYDKK ENVEYAIRNP
RSDVMKCRSH TEREQHFPFD SFFYIRNSEH EFSYSAEKGS TFTLIMYPGA VQANFDIIFM
CQEKCLDLDD RRKTMCLAVF LDDENGNEIL HAYIKQVRIV AYPRRDWKNF CEREDAKQKD
FRFPELPAYK KASLESINIK QEVNLENMFN VTNTTAQMEP STSYSSPSNS NNRKRFLNEC
DSPNNDYTMM HRTPPVTGYA SRLHGCVPPI ETEHENCQSP SMKRSRCTNY SFRTLTLSTA
EYTKVVEFLA REAKVPRYTW VPTQVVSHIL PTEGLERFLT AIKAGHDSVL FNANGIYTMG
DMIREFEKHN DIFERIGIDS SKLSKYYEAF LSFYRIQEAM KLPK
