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 27-MAR-2024, entry version 154. 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 FUNCTION. RX PubMed=28560849; DOI=10.1111/acel.12619; RA Chang H.W., Pisano S., Chaturbedi A., Chen J., Gordon S., Baruah A., RA Lee S.S.; RT "Transcription factors CEP-1/p53 and CEH-23 collaborate with AAK-2/AMPK to RT modulate longevity in Caenorhabditis elegans."; RL Aging Cell 16:814-824(2017). RN [21] 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 [22] 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, PubMed:28560849). CC Has a role in normal development to ensure proper meiotic chromosome CC segregation (PubMed:11557844, PubMed:12445383). Promotes apoptosis CC under conditions of cellular and genotoxic stress in response to DNA CC damage, hypoxia, or starvation (PubMed:11696333, PubMed:11557844, CC PubMed:12445383, PubMed:15273685, PubMed:17186023, PubMed:18836529, CC PubMed:21901106). Regulates germline apoptosis in response to DNA CC damage (PubMed:11696333, PubMed:15273685, PubMed:15707894, CC PubMed:16319925, PubMed:17276923, PubMed:17186023, PubMed:17347667, CC PubMed:19015549, PubMed:26598553). Its pro-apoptotic activity is CC inhibited when bound to ape-1 in vitro (PubMed:12524540). Plays a role CC in cell cycle arrest in the germline in response to DNA damage by UV-C CC light (PubMed:17347667). However, not required for survival in response CC to DNA damage induced by UV-C light, indicating that it is unlikely to CC be involved in DNA repair (PubMed:17347667). Required for induction of CC ced-13 in response to DNA damage (PubMed:15605074). Regulates DNA CC damage-induced apoptosis by inducing transcription of the programmed CC cell death activator egl-1 (PubMed:12445383, PubMed:19521535). CC Regulates germline proliferation by activating phg-1 (PubMed:17186023). CC Modulates lifespan (PubMed:17895432, PubMed:18836529, PubMed:28560849). CC {ECO:0000269|PubMed:11557844, ECO:0000269|PubMed:11696333, CC ECO:0000269|PubMed:12445383, ECO:0000269|PubMed:12524540, CC ECO:0000269|PubMed:15242600, ECO:0000269|PubMed:15273685, CC ECO:0000269|PubMed:15605074, ECO:0000269|PubMed:15707894, CC ECO:0000269|PubMed:16319925, ECO:0000269|PubMed:17186023, CC ECO:0000269|PubMed:17276923, ECO:0000269|PubMed:17347667, CC ECO:0000269|PubMed:17895432, ECO:0000269|PubMed:18627611, CC ECO:0000269|PubMed:18836529, ECO:0000269|PubMed:19015549, CC ECO:0000269|PubMed:19521535, ECO:0000269|PubMed:21901106, CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 6239-F52B5-5a-2; -. DR PeptideAtlas; 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 AGR; WB:WBGene00000467; -. 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; 2883888at2759; -. 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 cell types or 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: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 DNA-templated transcription; 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 Gene3D; 1.10.150.830; -; 1. DR Gene3D; 2.60.40.720; -; 1. DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf. DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf. DR InterPro; IPR015367; Trans_fact_CEP1_DNA-bd. DR Pfam; PF09287; CEP1-DNA_bind; 1. DR SUPFAM; SSF49417; p53-like transcription factors; 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 //