EMDB-67147: Structure of mouse cytoplasmic lattice (CPL) repeating unit

Basic information

Entry

Database: EMDB / ID: EMD-67147

• Title: Structure of mouse cytoplasmic lattice (CPL) repeating unit

Sample

• Complex: mouse cytoplasmic lattice
  • Protein or peptide: x 16 types
• Ligand: x 4 types

• Keywords: cytoplasmic lattice / maternal effect protein / proteostasis / protein storage / CYTOSOLIC PROTEIN

Function / homology

Function:

regulation of translation by machinery localization / Prolactin receptor signaling / Signaling by BMP / subcortical maternal complex / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / Sealing of the nuclear envelope (NE) by ESCRT-III / establishment of organelle localization / Chromatin modifying enzymes / protein storage / structural constituent of cytoplasmic lattice / cytoplasmic lattice / cortical granule exocytosis / embryonic process involved in female pregnancy / endoplasmic reticulum localization / ooplasm / Carboxyterminal post-translational modifications of tubulin / Intraflagellar transport / establishment or maintenance of apical/basal cell polarity / SCF-beta-TrCP mediated degradation of Emi1 / COPI-independent Golgi-to-ER retrograde traffic / E3 ubiquitin ligases ubiquitinate target proteins / Downregulation of SMAD2/3:SMAD4 transcriptional activity / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / cytoplasm organization / Regulation of BACH1 activity / histone H3K18 ubiquitin ligase activity / histone H3K14 ubiquitin ligase activity / histone H3 ubiquitin ligase activity / PINK1-PRKN Mediated Mitophagy / Inactivation of CSF3 (G-CSF) signaling / SCF(Skp2)-mediated degradation of p27/p21 / histone H3K23 ubiquitin ligase activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / COPI-mediated anterograde transport / spermatogonial cell division / Regulation of TNFR1 signaling / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Kinesins / histone H3 reader activity / Regulation of RUNX2 expression and activity / cortical granule / Degradation of GLI1 by the proteasome / Cyclin D associated events in G1 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Orc1 removal from chromatin / IKK complex recruitment mediated by RIP1 / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Dectin-1 mediated noncanonical NF-kB signaling / NIK-->noncanonical NF-kB signaling / PKR-mediated signaling / Aggrephagy / RHO GTPases activate IQGAPs / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / Degradation of beta-catenin by the destruction complex / Activation of NF-kappaB in B cells / Recycling pathway of L1 / Iron uptake and transport / The role of GTSE1 in G2/M progression after G2 checkpoint / COPI-dependent Golgi-to-ER retrograde traffic / apical cortex / positive regulation of meiotic nuclear division / regulation of RNA stability / positive regulation of embryonic development / chromosomal DNA methylation maintenance following DNA replication / FCERI mediated NF-kB activation / axonemal microtubule / CLEC7A (Dectin-1) signaling / Interleukin-1 signaling / Hedgehog 'off' state / RHO GTPases Activate Formins / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / F-box domain binding / organelle transport along microtubule / Anchoring of the basal body to the plasma membrane / Separation of Sister Chromatids / Downstream TCR signaling / Recruitment of NuMA to mitotic centrosomes / AURKA Activation by TPX2 / hemi-methylated DNA-binding / regulation of establishment of protein localization / forebrain morphogenesis / Peroxisomal protein import / GLI3 is processed to GLI3R by the proteasome / PcG protein complex / cerebellar cortex morphogenesis / Regulation of PLK1 Activity at G2/M Transition / Neddylation / glial cell differentiation / neuron projection arborization / dentate gyrus development / embryonic pattern specification / (E3-independent) E2 ubiquitin-conjugating enzyme / mitochondrion localization / establishment of spindle localization

Domain/homology:

Zinc finger BED domain-containing protein 2/3 / : / BED zinc finger / KH-like RNA-binding domain / : / KH-like RNA-binding domain / Groucho/transducin-like enhancer / : / UHRF1, tandem tudor domain / Tandem tudor domain within UHRF1 / UHRF1/2-like / Protein-arginine deiminase / Protein-arginine deiminase, C-terminal / Protein-arginine deiminase (PAD), N-terminal / Protein-arginine deiminase (PAD), central domain / Protein-arginine deiminase, central domain superfamily / PAD, N-terminal domain superfamily / Protein-arginine deiminase (PAD) / Protein-arginine deiminase (PAD) N-terminal domain / Protein-arginine deiminase (PAD) middle domain / SRA-YDG / SRA-YDG superfamily / SAD/SRA domain / YDG domain profile. / SET and RING finger associated domain. Domain of unknown function in SET domain containing proteins and in Deinococcus radiodurans DRA1533. / : / NACHT, LRR and PYD domains-containing protein, helical domain HD2 / NLRC4 helical domain HD2 / A Receptor for Ubiquitination Targets / NOD2, winged helix domain / NOD2 winged helix domain / F-box domain profile. / NACHT nucleoside triphosphatase / NACHT domain / NACHT-NTPase domain profile. / F-box-like / DAPIN domain / PAAD/DAPIN/Pyrin domain / F-box-like domain superfamily / PAAD/DAPIN/Pyrin domain / SKP1 component, dimerisation / S-phase kinase-associated protein 1 / SKP1-like, dimerisation domain superfamily / Skp1 family, dimerisation domain / F-box domain / Leucine rich repeat, ribonuclease inhibitor type / Leucine Rich repeat / K Homology domain, type 1 superfamily / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / PUA-like superfamily / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme/RWD-like / PHD-finger / Alpha tubulin / Tubulin-beta mRNA autoregulation signal. / Beta tubulin, autoregulation binding site / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Beta tubulin / Death-like domain superfamily / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Zinc finger C2H2 superfamily / Zinc finger PHD-type signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / SKP1/BTB/POZ domain superfamily / Ring finger / Cupredoxin / Zinc finger PHD-type profile. / Leucine-rich repeat / Zinc finger, PHD-finger / Zinc finger, PHD-type / PHD zinc finger / Zinc finger, FYVE/PHD-type / Leucine-rich repeat domain superfamily / Zinc finger RING-type profile. / Zinc finger, RING-type / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Zinc finger, RING/FYVE/PHD-type

Component:

NLR family, pyrin domain containing 4F / Ubiquitin-conjugating enzyme E2 D3 / Tubulin alpha-1A chain / Tubulin beta-4B chain / Expressed sequence C85627 / NACHT, LRR and PYD domains-containing protein 14 / F-box and WD-40 domain protein 21 / F-box and WD-40 domain protein 19 / Inactive protein-arginine deiminase type-6 / E3 ubiquitin-protein ligase UHRF1 / Oocyte-expressed protein homolog / KH domain-containing protein 3 / Zinc finger BED domain-containing protein 3 / NACHT, LRR and PYD domains-containing protein 5 / S-phase kinase-associated protein 1 / Transducin-like enhancer protein 6

• Biological species: Mus musculus (house mouse)
• Method: single particle reconstruction / cryo EM / Resolution: 3.74 Å
• Authors: Chi PL / Wang X / Li JL / Deng D

Funding support

China, 1 items

Organization	Grant number	Country
National Natural Science Foundation of China (NSFC)	31971132	China

• Citation: Journal: Nature / Year: 2026; Title: Structure of the mouse cytoplasmic lattice.; Authors: Pengliang Chi / Xiang Wang / Jialu Li / Jingrui Huang / Sicheng Ju / Sibei Liu / Li Yan / Yuechao Lu / Zihan Zhang / Zhuo Han / Jinhong Li / Qianqian Qi / Qingting Liu / Yiren Zeng / Li Guo / Xiaofeng Zhang / Long Gui / Dong Deng / ; Abstract: The fertilized egg relies almost entirely on maternal stores in the oocyte to ensure the successful initiation of development. The cytoplasmic lattices (CPLs) in mammalian oocytes store maternal-expressed proteins and have an essential role in embryogenesis. Impairing multiple CPL members leads to early embryonic arrest, resulting in infertility in mammals. However, the mechanism underlying the assembly and storage of CPLs remains largely unknown. Here we report the cryo-electron microscopy structure of a native mouse CPL repeating unit (approximately 4 MDa) at 3.74 Å resolution. This repeating unit exhibits a tripartite architecture comprising a framework, extended linkers and a CPL core. The external framework is built from PADI6 decamers and the subcortical maternal complexes. Two linkers formed by NLRP4F polymerize the frameworks into an extended filament. In the CPL core, the epigenetic regulator UHRF1 is trapped by PADI6, UBE2D and NLRP14 in a compact, autoinhibited conformation that prevents nuclear entry and ubiquitin ligase activity. Moreover, the CPL core stores GTP-bound α/β-tubulin heterodimers and inactive SCF E3-ubiquitin ligase components (FBXW-SKP1 complex) in a poised but restrained state. These features establish CPLs as a dynamic regulatory pool that enables rapid microtubule assembly and tightly controlled ubiquitination during the oocyte-to-embryo transition. Together, this semi-in situ structure illuminates CPL assembly and storage-module organization, and establishes CPLs as specialized proteostasis organelles for maternal regulation in oocytes and early embryonic development.

History

Deposition	Nov 19, 2025	-
Header (metadata) release	Mar 18, 2026	-
Map release	Mar 18, 2026	-
Update	Apr 15, 2026	-
Current status	Apr 15, 2026	Processing site: PDBc / Status: Released

Map

• File: Download / File: emd_67147.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
• Voxel size: X=Y=Z: 1.194 Å

Density

Contour Level	By AUTHOR: 0.02
Minimum - Maximum	-0.061872337 - 0.16451812
Average (Standard dev.)	0.00013773498 (±0.0066687856)

• Symmetry: Space group: 1

Details

EMDB XML:

Map geometry	Axis order X Y Z Origin 0 0 0 Dimensions 512 512 512 Spacing 512 512 512
Cell	A=B=C: 611.328 Å α=β=γ: 90.0 °

Supplemental data

Additional map: Local map of SCMC-1

• File: emd_67147_additional_1.map
• Annotation: Local map of SCMC-1

Additional map: Local map of NLRP14-2

• File: emd_67147_additional_10.map
• Annotation: Local map of NLRP14-2

Additional map: Local map of SCMC-2

• File: emd_67147_additional_2.map
• Annotation: Local map of SCMC-2

Additional map: Local map of PADI6-1

• File: emd_67147_additional_3.map
• Annotation: Local map of PADI6-1

Additional map: Local map of PADI6-2

• File: emd_67147_additional_4.map
• Annotation: Local map of PADI6-2

Additional map: Local map of NLRP4F-2

• File: emd_67147_additional_5.map
• Annotation: Local map of NLRP4F-2

Additional map: Local map of NLRP14-1

• File: emd_67147_additional_6.map
• Annotation: Local map of NLRP14-1

Additional map: Local map of TTD

• File: emd_67147_additional_7.map
• Annotation: Local map of TTD

Additional map: Local map of NLRP4F-1

• File: emd_67147_additional_8.map
• Annotation: Local map of NLRP4F-1

Additional map: Local map of NLRP14-3

• File: emd_67147_additional_9.map
• Annotation: Local map of NLRP14-3

Half map: #2

• File: emd_67147_half_map_1.map

Half map: #1

• File: emd_67147_half_map_2.map

Sample components

Entire : mouse cytoplasmic lattice

• Entire: Name: mouse cytoplasmic lattice

Components

• Complex: mouse cytoplasmic lattice
  • Protein or peptide: Zinc finger BED domain-containing protein 3
  • Protein or peptide: KH domain-containing protein 3
  • Protein or peptide: F-box and WD-40 domain protein 21
  • Protein or peptide: S-phase kinase-associated protein 1
  • Protein or peptide: Transducin-like enhancer protein 6
  • Protein or peptide: NLR family, pyrin domain containing 4F
  • Protein or peptide: Inactive protein-arginine deiminase type-6
  • Protein or peptide: Expressed sequence C85627
  • Protein or peptide: Tubulin beta-4B chain
  • Protein or peptide: Oocyte-expressed protein homolog
  • Protein or peptide: NACHT, LRR and PYD domains-containing protein 5
  • Protein or peptide: Tubulin alpha-1A chain
  • Protein or peptide: NACHT, LRR and PYD domains-containing protein 14
  • Protein or peptide: Ubiquitin-conjugating enzyme E2 D3
  • Protein or peptide: E3 ubiquitin-protein ligase UHRF1
  • Protein or peptide: F-box and WD-40 domain protein 19
• Ligand: ZINC ION
• Ligand: GUANOSINE-5'-TRIPHOSPHATE
• Ligand: MAGNESIUM ION
• Ligand: ADENOSINE-5'-DIPHOSPHATE

Supramolecule #1: mouse cytoplasmic lattice

• Supramolecule: Name: mouse cytoplasmic lattice / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7, #9-#10, #8, #11-#16
• Source (natural): Organism: Mus musculus (house mouse)

Macromolecule #1: Zinc finger BED domain-containing protein 3

• Macromolecule: Name: Zinc finger BED domain-containing protein 3 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 25.643373 KDa

Sequence

String:

MKSKKPLKIT MEDSRRLNDP AEQGGLCPAP VGPSYSEAWG YFHLDPAQPR HRMMSAWATC RLCGLQVGGL PNFQMWTRAL CQHLSDVHL PELKKSAAPS SPTTMPCPPP PSPTMAAEGD WARLLEQMGE LAMRGSQREL ELERREAALM QAELELERKR Q ALKQEAQS VEQERHQLQV EREALSKWIK KQSPGAQVPE PPSPLPLLPK EDPDIHDNNS DNDMVTKVLL

UniProtKB: Zinc finger BED domain-containing protein 3

Macromolecule #2: KH domain-containing protein 3

• Macromolecule: Name: KH domain-containing protein 3 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 48.055301 KDa

Sequence

String:

MASLKRFQTL VPLDHKQGTL FEIIGEPKLP KWFHVECLED PKRLYVEPRL LEIMFGKDGE HIPHLESMLH TLIHVNVWGP ERRAEIWIF GPPPFRRDVD RMLTDLAHYC RMKLMEIEAL EAGVERRRMA AHKAATQPAP VKVREAAPRP ASVKVPETAT Q PAPVKVRE AAPQPAPVQE VREAAPQQAS VQEEVREAAT EQAPVQEVRE AATEQAPVQE VSEAATEQAP VQEVNEAATE QA SVQAVRE AATRPAPGKV RKAATQPAPV QVCQEATQLA PVKVREAATQ PASGKVREAA TQLAPVKVRK AATQLAPVKV HEA ATQPAP GKVSDAATQS ASVQVREAAT QLSPVEATDT SQLAQVKADE AFAQHTSGEA HQVANGQSPI EVCETATGQH SLDV SRALS QKCPEVFEWE TQSCLDGSYV IVQPPRDAWE SFIIL

UniProtKB: KH domain-containing protein 3

Macromolecule #3: F-box and WD-40 domain protein 21

• Macromolecule: Name: F-box and WD-40 domain protein 21 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 54.517043 KDa

Sequence

String:

MEIHLPRLPL MEIFSYLDAY SLLQVAQVNK NWNELASSDV LWRKLCQKRW FYCNMVTQQL LGKETWKEFF IYRTWQEHAK SRAKPEDFI YKEIPAEYGI QAYACYISEH GLTRNGQGRS VICMATSMNR ISTWDIHEGV LTWVSPEQPA SIKLLTTLPE M YIAVTVDM ESTIKLWDCH NSEALATNSL ISPCQSLKAV ITKDGPIVLI GDTLGNLNIF RIPDLYHITR LKVFPYGISE LY CSPQKKW IFLNRKHPHI LPKVFYMSSL LRTSEFSAPV STDLKFSLCQ RAFWTPRRED RITLMSIHGP KKIKKFITFD MEL EKIGNK ITVKEHFFAS FSLQNYEERP EWYGVSDKDV IVCSTRFSLL LFDINGHCLQ AFQYCPEQIL RLWVDPLHVI VSCN DGFLD VYAWEERSQQ LNKCYRLQYS KHLPSSGLIN KTLSDDVSII QVITIRTTPC FLMAFILKSA LEN

UniProtKB: F-box and WD-40 domain protein 21

Macromolecule #4: S-phase kinase-associated protein 1

• Macromolecule: Name: S-phase kinase-associated protein 1 / type: protein_or_peptide / ID: 4 / Number of copies: 5 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 18.693992 KDa

Sequence

String:

MPTIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV NAAILKKVIQ WCTHHKDDPP PPEDDENKEK RTDDIPVWD QEFLKVDQGT LFELILAANY LDIKGLLDVT CKTVANMIKG KTPEEIRKTF NIKNDFTEEE EAQVRKENQW C EEK

UniProtKB: S-phase kinase-associated protein 1

Macromolecule #5: Transducin-like enhancer protein 6

• Macromolecule: Name: Transducin-like enhancer protein 6 / type: protein_or_peptide / ID: 5 / Number of copies: 6 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 65.187332 KDa

Sequence

String:

MTSHRQSSDT FGGILPSTLS SRYLSIVNQL PEEFSSVVSE MMVHLENIFS LAENFFQAIE RFSRTPDLLE RNKMSIGVGA EGDSWPCHV SHEAPMGSAQ TTENSAKEED KQVPESAALQ HPKFKSTPGP QLPTRRRFLS ESDELQDPQP VWDAEPQFCQ G FLIQGLWE LFMDSRQKNQ QEHGGEDSSQ ESKDSGLCDF KPEPQPRHRN SLSDSADPFL IKSPSALLDY YQEDVSRPQP ET QESSGRA DKFLKPLSWG SEVLESSCNQ PSTALWQLER FTVPQALQKV RVLKHQELLL VVAVSSFTRH VFTCSQSGIK VWN LVNQVA EDRDPESHLK CSVQDNKVYL RTCLLSSNSR TLFAGGYNLP GVIVWDLAAP SLYEKCQLPC EGLSCQALAN TKEN MALAG FTDGTVRIWD LRTQEIVRNL KGPTNSARNL VVKDDNIWTG GLDACLRCWD LRMAKVSLEH LFQSQIMSLA HSPTE DWLL LGLANGQHCL FNSRKRDQVL TVDTKDNTIL GLKFSPNGKW WASVGMGNFI TVHSMPTGAK LFQVPEVGPV RCFDMT ENG RLIITGSRDC ASVYHIKY

UniProtKB: Transducin-like enhancer protein 6

Macromolecule #6: NLR family, pyrin domain containing 4F

• Macromolecule: Name: NLR family, pyrin domain containing 4F / type: protein_or_peptide / ID: 6 / Number of copies: 4 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 108.001281 KDa

Sequence

String:

MASFISDFGL IWYLRELNKK EFMKFKDFLI QEILELKLKQ VSSTKVKKAS REDLANLLLK CGENQAWDMT FRILQKINRK DLTERATGA IVGNPNLYRD HLKKKLTHDC PKKFNVRIQD FIKETFIQND YDAFENLLIS KGTERKPHMV FLKGMAGVGK T LMLKNLML AWSKGLVFQN KFSYAFYFCC QDVKQLKTAS LAELISREWP SPSAPIEEIL SQPEKLLFII DSLEGMEWDL TK QESELCD DCMEKQPVST LLSSLLRRKM LPESSLLLST TPETFEKMED RIQCTDVKTA TAFDERSMKI YFHRLFQDRK RAQ EAFSLV RENKQLFTIC QVPLLCWMVA TCLKEEIEKG GDPVSLCRRT TSLYTTHIFS LFIPQSAQYP SKKSQDQLQG LCSL AAEGM WTDTFVFGKE ALRRNGIFDS DIPTLLDIGM LGKIREFENS YIFLHPSVQE VCAAIFYMLK RHVEHPSQDV KNIET VLFM FLKKVKTQWI FLGCFIFGLL QKSEQEKLGV FFGHRLSKNI HHKLYQCLET LSGNAELQEQ IDGMRLFSCL FEMEDE AFL VKAMNCMQQI NFVAKNYSDF IVAAYCLKHC STLKKLSFST ENVLNEGDQS YMEELLICWN NMCSVFVRSK DIQELRI KD TNFNEPAIRV LYESLKYPSF TLNKLVANNV SFGDNHVLFE LIQNSSLQYL DLSCSFLSHN EVKLLCDILN QAECNIEK L MIAHCKLSPD DCKIFGSILM SSKSLKVLNL ASNNLNQGIS SLCKALCHPH CTLEYLVLSN CSLSEQCWDY LSEVLRQNK TLSHLDISSN DLKDEGLKIL CRSLILPYCV LESLCLSCCG ITERGCQDLA EVLKNNQNLK YLHVSYNKLK DTGVMLLCDA IKHPNCHLK DLQLEACEIT DASNEELCYA FMQCETLQTL NLMGNAFEVS RMVFFPRF

UniProtKB: NLR family, pyrin domain containing 4F

Macromolecule #7: Inactive protein-arginine deiminase type-6

• Macromolecule: Name: Inactive protein-arginine deiminase type-6 / type: protein_or_peptide / ID: 7 / Number of copies: 20 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 76.854109 KDa

Sequence

String:

MSFQNSLSLS LVNPTHALCM VGMEITLDIS KCAPDKCKSF TIRGSPRILI HISSSVIAGK EDTVVWRSMN HPTVALVRMV APSPTVDED KVLVSYFCPD QEVPTATAVL FLTGIEISLE ADIYRDGQLD MPSDKQAKKK WMWGMNGWGA ILLVNCSPNA V GQPDEQSF QEGPREIQNL SQMNVTVEGP TSILQNYQLI LHTSEEEAKK TRVYWSQRGS SAYELVVGPN KPVYLLPTFE NR RKEAFYV EATEFPSPSF SGLISLSLSL VEKAHDECIP EIPLYKDTVM FRVAPYIFMP STQMPLEVYL CRELQLQGFV DSV TKLSEK SKVQVVKVYE DPNRQSKWLQ DEMAFCYTQA PHKTVSLILD TPRVSKLEDF PMKYTLTPGS GYLIRQTEDH RVAS LDSIG NLMVSPPVKA QGKDYPLGRV LIGGSFYPSS EGRDMNKGLR EFVYAQQVQA PVELFSDWLM TGHMDQFMCF VPTND KNND QKDFRLLLAS PSACFELFEQ KQKEGYGNVT LFEDIGAEQL LSNGRESKTI SQILADKSFR EQNTYVEKCI SLNRTL LKT ELGLEDKDII LIPQLFCLEQ LTNVPSNQQS TKLFARPYFP DMLQIIVLGK NLGIPKPFGP KINGTCCLEE KVCGLLE PL GLKCTFIDDF DCYLANIGDV CASAIINRVP FAFKWWKMTP

UniProtKB: Inactive protein-arginine deiminase type-6

Macromolecule #8: Oocyte-expressed protein homolog

• Macromolecule: Name: Oocyte-expressed protein homolog / type: protein_or_peptide / ID: 8 / Number of copies: 6 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 18.481295 KDa

Sequence

String:

MASHTADADA KPDSDSQKLL NVLPVSLRLR TRPWWFPIQE VSNPLVLYME AWVAERVIGT DQAEISEIEW MCQALLTVDS VNSGNLAEI TIFGQPSAQT RMKNILLNMA AWHKENELQR AVKVKEVEEF LKIRASSILS KLSKKGLKLA GFPLPLEGRE T QMES

UniProtKB: Oocyte-expressed protein homolog

Macromolecule #9: Expressed sequence C85627

• Macromolecule: Name: Expressed sequence C85627 / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 54.205703 KDa

Sequence

String:

METHLPSLPS LPMMKILSYL DAYSLLQVAQ VNKNWNALAS SDVLWRKLCQ KRWLYCDTVI LQLHDKETWK QFFVNRTYQE HTKTRAKPE DFTYKEICAE TGIWAYACYI SGRGLTRNGQ GTSVVCMLTS MTKISTWDIH EGVMTWVSPV QPTTIKLLNT L PEMHIAVT VDIHSTIKLW DCNSSDALAT NNLFFPCQTL KSVFTKDAAI VLVSDTLGNL YIFRIPDLHL ISTINVFPYG IN ELYCSPQ KKWVFLSRKH PHILPKVFYM NSLLRRSEFS APVSTVLNFS LCDKAFWTPR KEDRITLMSI SAPYKVTKFV TFD MKLEEI GNQIIVTGYL IASFSLTDYE GRLECFGVSD KDVIVCSTGS SLLLFSIYGV CLQTFDYCSE EILRLWVDPF HVIV TFIDG SLDVYAWEER CQQLSKCYRL QNRRRLPRQS CFEKTLCDEV SIIRMVRNGR NPCYLMTYTL NIHS

UniProtKB: Expressed sequence C85627

Macromolecule #10: Tubulin beta-4B chain

• Macromolecule: Name: Tubulin beta-4B chain / type: protein_or_peptide / ID: 10 / Number of copies: 3 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 49.877824 KDa

Sequence

String:

MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGKYV PRAVLVDLEP GTMDSVRSGP FGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELVDSVLDV VRKEAESCDC LQGFQLTHSL GGGTGSGMGT LLISKIREEY P DRIMNTFS VVPSPKVSDT VVEPYNATLS VHQLVENTDE TYCIDNEALY DICFRTLKLT TPTYGDLNHL VSATMSGVTT CL RFPGQLN ADLRKLAVNM VPFPRLHFFM PGFAPLTSRG SQQYRALTVP ELTQQMFDAK NMMAACDPRH GRYLTVAAVF RGR MSMKEV DEQMLNVQNK NSSYFVEWIP NNVKTAVCDI PPRGLKMSAT FIGNSTAIQE LFKRISEQFT AMFRRKAFLH WYTG EGMDE MEFTEAESNM NDLVSEYQQY QDATAEEEGE FEEEAEEEVA

UniProtKB: Tubulin beta-4B chain

Macromolecule #11: NACHT, LRR and PYD domains-containing protein 5

• Macromolecule: Name: NACHT, LRR and PYD domains-containing protein 5 / type: protein_or_peptide / ID: 11 / Number of copies: 6 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 119.819859 KDa

Sequence

String:

MGPPEKDSKA ILKARGLEEE QKSESTMSPS ENVSRAILKD SGSEEVEQAS ERKMTSPEND SKSIQKDQGP EQEQTSETLQ SKEEDEVTE ADKDNGGDLQ DYKAHVIAKF DTSVDLHYDS PEMKLLSDAF KPYQKTFQPH TIILHGRPGV GKSALARSIV L GWAQGKLF QKMSFVIFFS VREIKWTEKS SLAQLIAKEC PDSWDLVTKI MSQPERLLFV IDGLDDMDSV LQHDDMTLSR DW KDEQPIY ILMYSLLRKA LLPQSFLIIT TRNTGLEKLK SMVVSPLYIL VEGLSASRRS QLVLENISNE SDRIQVFHSL IEN HQLFDQ CQAPSVCSLV CEALQLQKKL GKRCTLPCQT LTGLYATLVF HQLTLKRPSQ SALSQEEQIT LVGLCMMAAE GVWT MRSVF YDDDLKNYSL KESEILALFH MNILLQVGHN SEQCYVFSHL SLQDFFAALY YVLEGLEEWN QHFCFIENQR SIMEV KRTD DTRLLGMKRF LFGLMNKDIL KTLEVLFEYP VIPTVEQKLQ HWVSLIAQQV NGTSPMDTLD AFYCLFESQD EEFVGG ALK RFQEVWLLIN QKMDLKVSSY CLKHCQNLKA IRVDIRDLLS VDNTLELCPV VTVQETQCKP LLMEWWGNFC SVLGSLR NL KELDLGDSIL SQRAMKILCL ELRNQSCRIQ KLTFKSAEVV SGLKHLWKLL FSNQNLKYLN LGNTPMKDDD MKLACEAL K HPKCSVETLR LDSCELTIIG YEMISTLLIS TTRLKCLSLA KNRVGVKSMI SLGNALSSSM CLLQKLILDN CGLTPASCH LLVSALFSNQ NLTHLCLSNN SLGTEGVQQL CQFLRNPECA LQRLILNHCN IVDDAYGFLA MRLANNTKLT HLSLTMNPVG DGAMKLLCE ALKEPTCYLQ ELELVDCQLT QNCCEDLACM ITTTKHLKSL DLGNNALGDK GVITLCEGLK QSSSSLRRLG L GACKLTSN CCEALSLAIS CNPHLNSLNL VKNDFSTSGM LKLCSAFQCP VSNLGIIGLW KQEYYARVRR QLEEVEFVKP HV VIDGDWY ASDEDDRNWW KN

UniProtKB: NACHT, LRR and PYD domains-containing protein 5

Macromolecule #12: Tubulin alpha-1A chain

• Macromolecule: Name: Tubulin alpha-1A chain / type: protein_or_peptide / ID: 12 / Number of copies: 3 / Enantiomer: LEVO; EC number: Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 50.188441 KDa

Sequence

String:

MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHP EQLITGKEDA ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFLVFH SFGGGTGSGF TSLLMERLSV D YGKKSKLE FSIYPAPQVS TAVVEPYNSI LTTHTTLEHS DCAFMVDNEA IYDICRRNLD IERPTYTNLN RLIGQIVSSI TA SLRFDGA LNVDLTEFQT NLVPYPRIHF PLATYAPVIS AEKAYHEQLS VAEITNACFE PANQMVKCDP RHGKYMACCL LYR GDVVPK DVNAAIATIK TKRTIQFVDW CPTGFKVGIN YQPPTVVPGG DLAKVQRAVC MLSNTTAIAE AWARLDHKFD LMYA KRAFV HWYVGEGMEE GEFSEAREDM AALEKDYEEV GVDSVEGEGE EEGEEY

UniProtKB: Tubulin alpha-1A chain

Macromolecule #13: NACHT, LRR and PYD domains-containing protein 14

• Macromolecule: Name: NACHT, LRR and PYD domains-containing protein 14 / type: protein_or_peptide / ID: 13 / Number of copies: 3 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 113.527188 KDa

Sequence

String:

MKTEDDEMEY EASKEETVSE DKDFDDGIDY RTVIKENIFT MWYKTSLHGE FATLNCVITP KDQNLLQHIF DEDIQTSEAP QTVVLQGAA GIGKTTLLKK AVLEWADGNL YQQFTHVFYL NGKEISQVKE KSFAQLISKH WPSSEGPIEQ VLSKPSSLLF I IDSFDELD FSFEEPQFAL CKDWTQISPV SFLISSLLRK VMLPESYLLV ATRSTAWKRL VPLLQKPQRV KLSGLSKNAR MD YIHHLLK DKAWATSAIY SLRMNWRLFH MCHVCHMCQM ICAVLKGQVE KGGRVEETCK TSTALFTYYI CSLFPRIPVG CVT LPNETL LRSLCKAAVE GIWTMKHVLY QQNLRKHELT REDILLFLDA KVLQQDTEYE NCYMFTHLHV QEFFAALFYL LREN LEEQD YPSEPFENLY LLLESNHIHD PHLEQMKCFL FGLLNKDRVR QLEETFNLTI SMEVREELLA CLEGLEKDDS SLSQL RFQD LLHCIYETQD QEFITQALMY FQKIIVRVDE EPQLRIYSFC LKHCHTLKTM RLTARADLKN MLDTAEMCLE GAAVQV IHY WQDLFSVLHT NESLIEMDLY ESRLDESLMK ILNEELSHPK CKLQKLIFRA VDFLNGCQDF TFLASNKKVT HLDLKET DL GVNGLKTLCE ALKCKGCKLR VLRLASCDLN VARCQKLSNA LQTNRSLVFL NLSLNNLSND GVKSLCEVLE NPNSSLER L ALASCGLTKA GCKVLSSALT KSKRLTHLCL SDNVLEDEGI KLLSHTLKHP QCTLQSLVLR SCSFTPIGSE HLSTALLHN RSLVHLDLGQ NKLADNGVKL LCHSLQQPHC NLQELELMSC VLTSKACGDL ASVLVNNSNL WSLDLGHNIL DDAGLNILCD ALRNPNCHV QRLGLENCGL TPGCCQDLLG ILSNNKSVIQ MNLMKNALDH ESIKNLCKVL RSPTCKMEFL ALDKKEILKK K IKKFLVDV RINNPHLVIG PECPNTESGC WWNYF

UniProtKB: NACHT, LRR and PYD domains-containing protein 14

Macromolecule #14: Ubiquitin-conjugating enzyme E2 D3

• Macromolecule: Name: Ubiquitin-conjugating enzyme E2 D3 / type: protein_or_peptide / ID: 14 / Number of copies: 3 / Enantiomer: LEVO / EC number: E2 ubiquitin-conjugating enzyme
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 16.706133 KDa

Sequence

String:

MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDIL RSQWSPALTI SKVLLSICSL LCDPNPDDPL VPEIARIYKT DRDKYNRISR EWTQKYAM

UniProtKB: Ubiquitin-conjugating enzyme E2 D3

Macromolecule #15: E3 ubiquitin-protein ligase UHRF1

• Macromolecule: Name: E3 ubiquitin-protein ligase UHRF1 / type: protein_or_peptide / ID: 15 / Number of copies: 3 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 88.436805 KDa

Sequence

String:

MWIQVRTMDG KETHTVNSLS RLTKVQELRK KIEEVFHVEP QLQRLFYRGK QMEDGHTLFD YDVRLNDTIQ LLVRQSLALP LSTKERDSE LSDSDSGYGV GHSESDKSST HGEGAAEADD KTVWEDTDLG LYKVNEYVDV RDNIFGAWFE AQVVQVQKRA L SEDEPCSS SAVKTSEDDI MYHVKYDDYP EHGVDIVKAK NVRARARTVI PWENLEVGQV VMANYNVDYP RKRGFWYDVE IC RKRQTRT ARELYGNIRL LNDSQLNNCR IMFVDEVLMI ELPKERRPLI ASPSQPPPAL RNTGKSGPSC RFCKDDENKP CRK CACHVC GGREAPEKQL LCDECDMAFH LYCLKPPLTS VPPEPEWYCP SCRTDSSEVV QAGEKLKESK KKAKMASATS SSRR DWGKG MACVGRTTEC TIVPANHFGP IPGVPVGTMW RFRVQVSESG VHRPHVAGIH GRSNDGAYSL VLAGGYEDDV DNGNY FTYT GSGGRDLSGN KRTAGQSSDQ KLTNNNRALA LNCHSPINEK GAEAEDWRQG KPVRVVRNMK GGKHSKYAPA EGNRYD GIY KVVKYWPERG KSGFLVWRYL LRRDDTEPEP WTREGKDRTR QLGLTMQYPE GYLEALANKE KSRKRPAKAL EQGPSSS KT GKSKQKSTGP TLSSPRASKK SKLEPYTLSE QQANLIKEDK GNAKLWDDVL TSLQDGPYQI FLSKVKEAFQ CICCQELV F RPVTTVCQHN VCKDCLDRSF RAQVFSCPAC RFELDHSSPT RVNQPLQTIL NQLFPGYGSG R

UniProtKB: E3 ubiquitin-protein ligase UHRF1

Macromolecule #16: F-box and WD-40 domain protein 19

• Macromolecule: Name: F-box and WD-40 domain protein 19 / type: protein_or_peptide / ID: 16 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Mus musculus (house mouse)
• Molecular weight: Theoretical: 53.657457 KDa

Sequence

String:

MEIHLPSLPM MKILSYLDAY SLLQAAKVNK NWNELASSDV LWRKLCQKRW LYCDRVTLQL HGLETWKQFF ISRTWQEHAK TRAKPEDFN YKEIPVAFEF RAHPCYISRH GLIRNGQGKS AVCMVTSTNR ISTWDVHEGA MTWVSPVQPS YITRMTTLPE M HIAVTIDM QSNIKLWDCH NRKVLATTGL LSSCQLLQAV FTNDSPIVLV GDILGNLYIF RIPDLHLISK VNVFPYGIDE LH CSPQKKW VLLIGKQRHV LTKVFYMSSL LRTSEFSAPV STDLKFSLCQ RAFWTPRRED RITLMSSTIP PDPTKFATFD MKL EEIENK VTIQGHLVAS FSLQDCKERA EWMGVSDKDV IVCSTGSSLL LFDINGLRLQ TFQYCPEEIL RLCVDPVHVI VTCN NGSLD VYVWEERSPL LRRCYRLRKR GYLPLSGFII KTLCDESSII LVMTSSPIPC FLMAYTLKVC S

UniProtKB: F-box and WD-40 domain protein 19

Macromolecule #17: ZINC ION

• Macromolecule: Name: ZINC ION / type: ligand / ID: 17 / Number of copies: 13 / Formula: ZN
• Molecular weight: Theoretical: 65.409 Da

Macromolecule #18: GUANOSINE-5'-TRIPHOSPHATE

• Macromolecule: Name: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 18 / Number of copies: 5 / Formula: GTP
• Molecular weight: Theoretical: 523.18 Da

Chemical component information

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

Macromolecule #19: MAGNESIUM ION

• Macromolecule: Name: MAGNESIUM ION / type: ligand / ID: 19 / Number of copies: 4 / Formula: MG
• Molecular weight: Theoretical: 24.305 Da

Macromolecule #20: ADENOSINE-5'-DIPHOSPHATE

• Macromolecule: Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 20 / Number of copies: 3 / Formula: ADP
• Molecular weight: Theoretical: 427.201 Da

Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Experimental details

Structure determination

• Method: cryo EM
• Processing: single particle reconstruction
• Aggregation state: filament

Sample preparation

• Buffer: pH: 6.7
• Vitrification: Cryogen name: ETHANE

Electron microscopy

• Microscope: TFS KRIOS
• Image recording: Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 60.0 e/Ų
• Electron beam: Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
• Electron optics: Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm
• Experimental equipment: Model: Titan Krios / Image courtesy: FEI Company

Image processing

• CTF correction: Type: NONE
• Startup model: Type of model: NONE
• Final reconstruction: Resolution.type: BY AUTHOR / Resolution: 3.74 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 349408
• Initial angle assignment: Type: ANGULAR RECONSTITUTION
• Final angle assignment: Type: ANGULAR RECONSTITUTION