ID PCH2_HUMAN Reviewed; 432 AA. AC Q15645; C9K0T3; D3DTC0; O15324; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 2. DT 23-MAY-2018, entry version 158. DE RecName: Full=Pachytene checkpoint protein 2 homolog; DE AltName: Full=Human papillomavirus type 16 E1 protein-binding protein; DE Short=16E1-BP; DE Short=HPV16 E1 protein-binding protein; DE AltName: Full=Thyroid hormone receptor interactor 13; DE AltName: Full=Thyroid receptor-interacting protein 13; DE Short=TR-interacting protein 13; DE Short=TRIP-13; GN Name=TRIP13; Synonyms=PCH2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HPV16 E1. RX PubMed=9223484; RA Yasugi T., Vidal M., Sakai H., Howley P.M., Benson J.D.; RT "Two classes of human papillomavirus type 16 E1 mutants suggest RT pleiotropic conformational constraints affecting E1 multimerization, RT E2 interaction, and interaction with cellular proteins."; RL J. Virol. 71:5942-5951(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-417 (ISOFORM 2), AND INTERACTION WITH RP THRA. RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974; RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.; RT "Two classes of proteins dependent on either the presence or absence RT of thyroid hormone for interaction with the thyroid hormone RT receptor."; RL Mol. Endocrinol. 9:243-254(1995). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [13] RP VARIANT MVA3 354-ARG--ILE-432 DEL, CHARACTERIZATION OF VARIANT MVA3 RP 354-ARG--ILE-432 DEL, AND FUNCTION. RX PubMed=28553959; DOI=10.1038/ng.3883; RA Yost S., de Wolf B., Hanks S., Zachariou A., Marcozzi C., Clarke M., RA de Voer R., Etemad B., Uijttewaal E., Ramsay E., Wylie H., Elliott A., RA Picton S., Smith A., Smithson S., Seal S., Ruark E., Houge G., RA Pines J., Kops G.J.P.L., Rahman N.; RT "Biallelic TRIP13 mutations predispose to Wilms tumor and chromosome RT missegregation."; RL Nat. Genet. 49:1148-1151(2017). CC -!- FUNCTION: Plays a key role in chromosome recombination and CC chromosome structure development during meiosis. Required at early CC steps in meiotic recombination that leads to non-crossovers CC pathways. Also needed for efficient completion of homologous CC synapsis by influencing crossover distribution along the CC chromosomes affecting both crossovers and non-crossovers pathways. CC Also required for development of higher-order chromosome CC structures and is needed for synaptonemal-complex formation. In CC males, required for efficient synapsis of the sex chromosomes and CC for sex body formation. Promotes early steps of the DNA double- CC strand breaks (DSBs) repair process upstream of the assembly of CC RAD51 complexes. Required for depletion of HORMAD1 and HORMAD2 CC from synapsed chromosomes (By similarity). Plays a role in mitotic CC spindle assembly checkpoint (SAC) activation (PubMed:28553959). CC {ECO:0000250|UniProtKB:Q3UA06, ECO:0000269|PubMed:28553959}. CC -!- SUBUNIT: Specifically interacts with the ligand binding domain of CC the thyroid receptor (TR). This interaction does not require the CC presence of thyroid hormone for its interaction. Interacts with CC HPV16 E1. {ECO:0000269|PubMed:7776974, CC ECO:0000269|PubMed:9223484}. CC -!- INTERACTION: CC Self; NbExp=5; IntAct=EBI-358993, EBI-358993; CC Q96EJ4:-; NbExp=3; IntAct=EBI-358993, EBI-750454; CC Q9Y303:AMDHD2; NbExp=3; IntAct=EBI-358993, EBI-2798672; CC Q969Q4:ARL11; NbExp=3; IntAct=EBI-358993, EBI-751892; CC P15289:ARSA; NbExp=12; IntAct=EBI-358993, EBI-2117357; CC Q9H0W9:C11orf54; NbExp=3; IntAct=EBI-358993, EBI-740204; CC Q8N1A6:C4orf33; NbExp=5; IntAct=EBI-358993, EBI-10264911; CC A0A0S2Z515:CFP; NbExp=3; IntAct=EBI-358993, EBI-16434710; CC P21964:COMT; NbExp=3; IntAct=EBI-358993, EBI-372265; CC P21964-2:COMT; NbExp=3; IntAct=EBI-358993, EBI-10200977; CC P53672:CRYBA2; NbExp=4; IntAct=EBI-358993, EBI-750444; CC Q6BCY4:CYB5R2; NbExp=4; IntAct=EBI-358993, EBI-744761; CC O95865:DDAH2; NbExp=5; IntAct=EBI-358993, EBI-749139; CC Q14689:DIP2A; NbExp=3; IntAct=EBI-358993, EBI-2564275; CC Q14689-6:DIP2A; NbExp=3; IntAct=EBI-358993, EBI-10233719; CC O14531:DPYSL4; NbExp=3; IntAct=EBI-358993, EBI-719542; CC Q96A09:FAM46B; NbExp=4; IntAct=EBI-358993, EBI-752030; CC Q9UBX5:FBLN5; NbExp=3; IntAct=EBI-358993, EBI-947897; CC A0A0S2Z576:FBXO8; NbExp=3; IntAct=EBI-358993, EBI-16434722; CC Q53EP0-3:FNDC3B; NbExp=7; IntAct=EBI-358993, EBI-10242151; CC A0A0S2Z4I0:GALT; NbExp=3; IntAct=EBI-358993, EBI-16434744; CC P07902:GALT; NbExp=4; IntAct=EBI-358993, EBI-750827; CC Q8IVS8:GLYCTK; NbExp=8; IntAct=EBI-358993, EBI-748515; CC Q9BSH5:HDHD3; NbExp=7; IntAct=EBI-358993, EBI-745201; CC P59990:KRTAP12-1; NbExp=5; IntAct=EBI-358993, EBI-10210845; CC P59991:KRTAP12-2; NbExp=3; IntAct=EBI-358993, EBI-10176379; CC Q6PEX3:KRTAP26-1; NbExp=3; IntAct=EBI-358993, EBI-3957672; CC Q16773:KYAT1; NbExp=3; IntAct=EBI-358993, EBI-10238309; CC Q14847:LASP1; NbExp=7; IntAct=EBI-358993, EBI-742828; CC Q8TBB1:LNX1; NbExp=6; IntAct=EBI-358993, EBI-739832; CC Q96JB6:LOXL4; NbExp=6; IntAct=EBI-358993, EBI-749562; CC Q96L50:LRR1; NbExp=3; IntAct=EBI-358993, EBI-2510106; CC Q8TC57:M1AP; NbExp=3; IntAct=EBI-358993, EBI-748182; CC Q15013:MAD2L1BP; NbExp=7; IntAct=EBI-358993, EBI-712181; CC A6NJ78-4:METTL15; NbExp=5; IntAct=EBI-358993, EBI-10174029; CC Q6PF18:MORN3; NbExp=3; IntAct=EBI-358993, EBI-9675802; CC Q15777:MPPED2; NbExp=7; IntAct=EBI-358993, EBI-2350461; CC Q9GZT8:NIF3L1; NbExp=3; IntAct=EBI-358993, EBI-740897; CC O00746:NME4; NbExp=3; IntAct=EBI-358993, EBI-744871; CC P55771:PAX9; NbExp=4; IntAct=EBI-358993, EBI-12111000; CC P30039:PBLD; NbExp=4; IntAct=EBI-358993, EBI-750589; CC Q6PIM4:PCMTD2; NbExp=3; IntAct=EBI-358993, EBI-10253759; CC Q96FA3:PELI1; NbExp=3; IntAct=EBI-358993, EBI-448369; CC Q9NRY6:PLSCR3; NbExp=6; IntAct=EBI-358993, EBI-750734; CC Q9NRQ2:PLSCR4; NbExp=3; IntAct=EBI-358993, EBI-769257; CC P67775:PPP2CA; NbExp=5; IntAct=EBI-358993, EBI-712311; CC O60260:PRKN; NbExp=3; IntAct=EBI-358993, EBI-716346; CC P47897:QARS; NbExp=5; IntAct=EBI-358993, EBI-347462; CC P47897-2:QARS; NbExp=3; IntAct=EBI-358993, EBI-10209725; CC Q9BQY4:RHOXF2; NbExp=7; IntAct=EBI-358993, EBI-372094; CC P22307:SCP2; NbExp=4; IntAct=EBI-358993, EBI-1050999; CC Q13228:SELENBP1; NbExp=3; IntAct=EBI-358993, EBI-711619; CC Q9NTN9:SEMA4G; NbExp=3; IntAct=EBI-358993, EBI-6447340; CC Q9NTN9-3:SEMA4G; NbExp=3; IntAct=EBI-358993, EBI-9089805; CC O15389:SIGLEC5; NbExp=4; IntAct=EBI-358993, EBI-750381; CC Q5W111:SPRYD7; NbExp=3; IntAct=EBI-358993, EBI-10248098; CC Q96LM6:TEX37; NbExp=6; IntAct=EBI-358993, EBI-743976; CC Q9GZM7:TINAGL1; NbExp=5; IntAct=EBI-358993, EBI-715869; CC Q9GZM7-3:TINAGL1; NbExp=3; IntAct=EBI-358993, EBI-10303636; CC Q6P9B6:TLDC1; NbExp=3; IntAct=EBI-358993, EBI-746504; CC Q8NDV7:TNRC6A; NbExp=3; IntAct=EBI-358993, EBI-2269715; CC P13693:TPT1; NbExp=3; IntAct=EBI-358993, EBI-1783169; CC P11473:VDR; NbExp=3; IntAct=EBI-358993, EBI-286357; CC Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-358993, EBI-741158; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q15645-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15645-2; Sequence=VSP_016957; CC Note=No experimental confirmation available.; CC -!- DISEASE: Mosaic variegated aneuploidy syndrome 3 (MVA3) CC [MIM:617598]: A form of mosaic variegated aneuploidy syndrome, a CC severe disorder characterized by mosaic aneuploidies, CC predominantly trisomies and monosomies, involving multiple CC different chromosomes and tissues. Affected individuals typically CC present with severe intrauterine growth retardation and CC microcephaly. Eye anomalies, mild dysmorphism, variable CC developmental delay, and a broad spectrum of additional congenital CC abnormalities and medical conditions may also occur. The risk of CC malignancy is high, with rhabdomyosarcoma, Wilms tumor and CC leukemia reported in several cases. MVA3 inheritance is autosomal CC recessive. {ECO:0000269|PubMed:28553959}. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC MVA3 is caused by biallelic mutations in the TRIP13 gene. CC -!- SIMILARITY: Belongs to the AAA ATPase family. PCH2 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC41732.1; Type=Frameshift; Positions=1, 5; Evidence={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; U96131; AAB64095.1; -; mRNA. DR EMBL; CR456744; CAG33025.1; -; mRNA. DR EMBL; AC122719; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471102; EAX08185.1; -; Genomic_DNA. DR EMBL; CH471102; EAX08186.1; -; Genomic_DNA. DR EMBL; BC000404; AAH00404.1; -; mRNA. DR EMBL; BC019294; AAH19294.1; -; mRNA. DR EMBL; L40384; AAC41732.1; ALT_FRAME; mRNA. DR CCDS; CCDS3858.1; -. [Q15645-1] DR RefSeq; NP_004228.1; NM_004237.3. [Q15645-1] DR RefSeq; XP_011512465.1; XM_011514163.2. [Q15645-1] DR UniGene; Hs.436187; -. DR PDB; 5VQ9; X-ray; 3.02 A; D=1-432. DR PDB; 5VQA; X-ray; 2.54 A; A=1-432. DR PDBsum; 5VQ9; -. DR PDBsum; 5VQA; -. DR ProteinModelPortal; Q15645; -. DR SMR; Q15645; -. DR BioGrid; 114730; 127. DR DIP; DIP-34493N; -. DR IntAct; Q15645; 122. DR MINT; Q15645; -. DR STRING; 9606.ENSP00000166345; -. DR iPTMnet; Q15645; -. DR PhosphoSitePlus; Q15645; -. DR SwissPalm; Q15645; -. DR BioMuta; TRIP13; -. DR DMDM; 85541056; -. DR EPD; Q15645; -. DR MaxQB; Q15645; -. DR PaxDb; Q15645; -. DR PeptideAtlas; Q15645; -. DR PRIDE; Q15645; -. DR DNASU; 9319; -. DR Ensembl; ENST00000166345; ENSP00000166345; ENSG00000071539. [Q15645-1] DR GeneID; 9319; -. DR KEGG; hsa:9319; -. DR UCSC; uc003jbr.4; human. [Q15645-1] DR CTD; 9319; -. DR DisGeNET; 9319; -. DR EuPathDB; HostDB:ENSG00000071539.13; -. DR GeneCards; TRIP13; -. DR HGNC; HGNC:12307; TRIP13. DR HPA; HPA005727; -. DR HPA; HPA053093; -. DR MalaCards; TRIP13; -. DR MIM; 604507; gene. DR MIM; 617598; phenotype. DR neXtProt; NX_Q15645; -. DR OpenTargets; ENSG00000071539; -. DR PharmGKB; PA36986; -. DR eggNOG; KOG0744; Eukaryota. DR eggNOG; COG0464; LUCA. DR GeneTree; ENSGT00390000017432; -. DR HOGENOM; HOG000234557; -. DR HOVERGEN; HBG052830; -. DR InParanoid; Q15645; -. DR KO; K22399; -. DR OMA; HLNEEGP; -. DR OrthoDB; EOG091G0D83; -. DR PhylomeDB; Q15645; -. DR TreeFam; TF313507; -. DR GeneWiki; TRIP13; -. DR GenomeRNAi; 9319; -. DR PRO; PR:Q15645; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000071539; -. DR CleanEx; HS_TRIP13; -. DR ExpressionAtlas; Q15645; baseline and differential. DR Genevisible; Q15645; HS. DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc. DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB. DR GO; GO:0007144; P:female meiosis I; IEA:Ensembl. DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl. DR GO; GO:0007094; P:mitotic spindle assembly checkpoint; IMP:UniProtKB. DR GO; GO:0001556; P:oocyte maturation; IEA:Ensembl. DR GO; GO:0048477; P:oogenesis; ISS:UniProtKB. DR GO; GO:0007131; P:reciprocal meiotic recombination; ISS:UniProtKB. DR GO; GO:0007286; P:spermatid development; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR GO; GO:0007130; P:synaptonemal complex assembly; ISS:UniProtKB. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00004; AAA; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00674; AAA; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Complete proteome; Differentiation; Disease mutation; Meiosis; KW Nucleotide-binding; Oogenesis; Reference proteome; Spermatogenesis. FT CHAIN 1 432 Pachytene checkpoint protein 2 homolog. FT /FTId=PRO_0000084782. FT NP_BIND 179 186 ATP. {ECO:0000255}. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:22223895}. FT VAR_SEQ 171 406 Missing (in isoform 2). FT {ECO:0000303|PubMed:7776974}. FT /FTId=VSP_016957. FT VARIANT 354 432 Missing (in MVA3; loss of protein FT expression; impairment of spindle FT assembly checkpoint). FT {ECO:0000269|PubMed:28553959}. FT /FTId=VAR_079275. FT STRAND 21 27 {ECO:0000244|PDB:5VQA}. FT HELIX 35 49 {ECO:0000244|PDB:5VQA}. FT STRAND 57 59 {ECO:0000244|PDB:5VQA}. FT HELIX 64 69 {ECO:0000244|PDB:5VQA}. FT STRAND 70 76 {ECO:0000244|PDB:5VQA}. FT STRAND 95 100 {ECO:0000244|PDB:5VQA}. FT STRAND 122 129 {ECO:0000244|PDB:5VQA}. FT HELIX 130 132 {ECO:0000244|PDB:5VQA}. FT HELIX 135 138 {ECO:0000244|PDB:5VQA}. FT HELIX 145 162 {ECO:0000244|PDB:5VQA}. FT TURN 166 168 {ECO:0000244|PDB:5VQA}. FT STRAND 173 178 {ECO:0000244|PDB:5VQA}. FT HELIX 185 199 {ECO:0000244|PDB:5VQA}. FT TURN 200 203 {ECO:0000244|PDB:5VQA}. FT STRAND 205 212 {ECO:0000244|PDB:5VQA}. FT HELIX 228 240 {ECO:0000244|PDB:5VQA}. FT STRAND 245 252 {ECO:0000244|PDB:5VQA}. FT HELIX 255 259 {ECO:0000244|PDB:5VQA}. FT HELIX 273 287 {ECO:0000244|PDB:5VQA}. FT STRAND 293 300 {ECO:0000244|PDB:5VQA}. FT STRAND 302 304 {ECO:0000244|PDB:5VQA}. FT TURN 307 312 {ECO:0000244|PDB:5VQA}. FT STRAND 314 318 {ECO:0000244|PDB:5VQA}. FT HELIX 324 340 {ECO:0000244|PDB:5VQA}. FT HELIX 353 358 {ECO:0000244|PDB:5VQA}. FT TURN 359 361 {ECO:0000244|PDB:5VQA}. FT TURN 365 367 {ECO:0000244|PDB:5VQA}. FT HELIX 368 379 {ECO:0000244|PDB:5VQA}. FT TURN 380 382 {ECO:0000244|PDB:5VQA}. FT HELIX 385 399 {ECO:0000244|PDB:5VQA}. FT HELIX 407 429 {ECO:0000244|PDB:5VQA}. SQ SEQUENCE 432 AA; 48551 MW; DFB0B37462D1D581 CRC64; MDEAVGDLKQ ALPCVAESPT VHVEVHQRGS STAKKEDINL SVRKLLNRHN IVFGDYTWTE FDEPFLTRNV QSVSIIDTEL KVKDSQPIDL SACTVALHIF QLNEDGPSSE NLEEETENII AANHWVLPAA EFHGLWDSLV YDVEVKSHLL DYVMTTLLFS DKNVNSNLIT WNRVVLLHGP PGTGKTSLCK ALAQKLTIRL SSRYRYGQLI EINSHSLFSK WFSESGKLVT KMFQKIQDLI DDKDALVFVL IDEVESLTAA RNACRAGTEP SDAIRVVNAV LTQIDQIKRH SNVVILTTSN ITEKIDVAFV DRADIKQYIG PPSAAAIFKI YLSCLEELMK CQIIYPRQQL LTLRELEMIG FIENNVSKLS LLLNDISRKS EGLSGRVLRK LPFLAHALYV QAPTVTIEGF LQALSLAVDK QFEERKKLAA YI //