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- EMDB-45301: mouse Seipin/Adig complex -

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Basic information

Entry
Database: EMDB / ID: EMD-45301
Titlemouse Seipin/Adig complex
Map dataSeipin/Adig complex
Sample
  • Complex: Seipin/Adig complex
    • Protein or peptide: Seipin
    • Protein or peptide: Adipogenin
Keywordsseipin / adipogenin / lipid droplets / adipose / MEMBRANE PROTEIN
Function / homology
Function and homology information


lipid droplet formation / white fat cell differentiation / positive regulation of fat cell differentiation / brown fat cell differentiation / lipid droplet / phospholipid binding / lipid metabolic process / spermatogenesis / endoplasmic reticulum membrane / nucleus ...lipid droplet formation / white fat cell differentiation / positive regulation of fat cell differentiation / brown fat cell differentiation / lipid droplet / phospholipid binding / lipid metabolic process / spermatogenesis / endoplasmic reticulum membrane / nucleus / membrane / cytoplasm
Similarity search - Function
Adipogenin / Adipogenin / Seipin family / Putative adipose-regulatory protein (Seipin)
Similarity search - Domain/homology
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.98 Å
AuthorsLi C / Han Y / Wynn RM / Chen Z / Scherer PE
Funding support United States, 5 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)RC2-DK118620 United States
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)R01- DK55758 United States
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)R01-DK099110 United States
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)R01-DK127274 United States
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)R01-DK131537 United States
CitationJournal: To Be Published
Title: Adipogenin Dictates Adipose Tissue Expansion by Facilitating the Assembly of a Dodecameric Seipin Complex
Authors: Li C / Sun X
History
DepositionJun 12, 2024-
Header (metadata) releaseAug 27, 2025-
Map releaseAug 27, 2025-
UpdateAug 27, 2025-
Current statusAug 27, 2025Processing site: RCSB / Status: Released

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Structure visualization

Downloads & links

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Map

FileDownload / File: emd_45301.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSeipin/Adig complex
Voxel sizeX=Y=Z: 0.8344 Å
Density
Contour LevelBy AUTHOR: 0.08
Minimum - Maximum-0.0018189892 - 1.9801874
Average (Standard dev.)0.001477541 (±0.026838925)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 320.4096 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Seipin/Adig complex

EntireName: Seipin/Adig complex
Components
  • Complex: Seipin/Adig complex
    • Protein or peptide: Seipin
    • Protein or peptide: Adipogenin

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Supramolecule #1: Seipin/Adig complex

SupramoleculeName: Seipin/Adig complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 700 KDa

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Macromolecule #1: Seipin

MacromoleculeName: Seipin / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 50.993406 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSGRWSHPQF EKIHQRREAG ARETCRDQIK GSDKDEEPSA ALSHGQGYRP CGRPARNSKP EAGARPPAVP IMVNDPPVPA LLWAQEVGH VLAGRARRLM LQFGVLFCTI LLLLWVSVFL YGSFYYSYMP TVSHLSPVHF HYRTDCDSST ASLCSFPVAN V SLAKSGRD ...String:
MSGRWSHPQF EKIHQRREAG ARETCRDQIK GSDKDEEPSA ALSHGQGYRP CGRPARNSKP EAGARPPAVP IMVNDPPVPA LLWAQEVGH VLAGRARRLM LQFGVLFCTI LLLLWVSVFL YGSFYYSYMP TVSHLSPVHF HYRTDCDSST ASLCSFPVAN V SLAKSGRD RVLMYGQPYR VTLELELPES PVNQDLGMFL VTVSCYTRGG RIISTSSRSV MLHYRSQLLQ VLDTLLFSSL LL FGFAEQK QLLEVELYSD YRENSYVPTT GAIIEIHSKR IQMYGAYLRI HAHFTGLRYL LYNFPMTCAF VGVASNFTFL SVI VLFSYM QWVWGAVWPR HRFSLQVNIR QRDNSHHGAP RRISRHQPGQ ESTQQSDVTE DGESPEDPSG TEGQLSEEEK PEKR PLNGE EEQEPEASDG SWEDAALLTE ANPPTSASAS ALAPETLGSL RQRPTCSSS

UniProtKB: Seipin

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Macromolecule #2: Adipogenin

MacromoleculeName: Adipogenin / type: protein_or_peptide / ID: 2 / Number of copies: 12 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 10.767105 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MKYPLVPLVS DLTLSFLVFW LCLPVALLLF LTIVWLHFLL SQESKEDDSD LCFNWEPWSK RPSECGCEET FPGEEDGLHW GGSGSGDYK DDDDK

UniProtKB: Adipogenin

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Support film - Material: GRAPHENE OXIDE / Support film - topology: CONTINUOUS
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionApplied symmetry - Point group: C12 (12 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 2.98 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 32123
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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