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- PDB-9cfc: Cryo-EM structure of human kidney V-ATPase state 2 -

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Basic information

Entry
Database: PDB / ID: 9cfc
TitleCryo-EM structure of human kidney V-ATPase state 2
Components
  • (V-type proton ATPase ...) x 12
  • Renin receptor
  • Ribonuclease kappa
KeywordsMEMBRANE PROTEIN / human / kidney / V-ATPase
Function / homology
Function and homology information


proton-transporting two-sector ATPase complex / Ion channel transport / Regulation of MITF-M-dependent genes involved in lysosome biogenesis and autophagy / intracellular pH reduction / plasma membrane proton-transporting V-type ATPase complex / eye pigmentation / central nervous system maturation / ATPase-coupled ion transmembrane transporter activity / rostrocaudal neural tube patterning / positive regulation of transforming growth factor beta1 production ...proton-transporting two-sector ATPase complex / Ion channel transport / Regulation of MITF-M-dependent genes involved in lysosome biogenesis and autophagy / intracellular pH reduction / plasma membrane proton-transporting V-type ATPase complex / eye pigmentation / central nervous system maturation / ATPase-coupled ion transmembrane transporter activity / rostrocaudal neural tube patterning / positive regulation of transforming growth factor beta1 production / Golgi lumen acidification / synaptic vesicle lumen acidification / proton-transporting V-type ATPase, V0 domain / extrinsic component of synaptic vesicle membrane / Transferrin endocytosis and recycling / cellular response to increased oxygen levels / vacuolar transport / lysosomal lumen acidification / vacuolar proton-transporting V-type ATPase, V1 domain / clathrin-coated vesicle membrane / endosome to plasma membrane protein transport / vacuolar proton-transporting V-type ATPase, V0 domain / endosomal lumen acidification / XBP1(S) activates chaperone genes / Amino acids regulate mTORC1 / proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase complex / head morphogenesis / protein localization to cilium / osteoclast development / ROS and RNS production in phagocytes / vacuolar acidification / regulation of cellular pH / dendritic spine membrane / azurophil granule membrane / microvillus / proton transmembrane transporter activity / ATPase activator activity / regulation of MAPK cascade / tertiary granule membrane / autophagosome membrane / ficolin-1-rich granule membrane / cilium assembly / proton-transporting ATPase activity, rotational mechanism / RHOA GTPase cycle / positive regulation of Wnt signaling pathway / regulation of macroautophagy / transporter activator activity / specific granule membrane / ATP metabolic process / H+-transporting two-sector ATPase / Metabolism of Angiotensinogen to Angiotensins / angiotensin maturation / Insulin receptor recycling / receptor-mediated endocytosis of virus by host cell / axon terminus / ruffle / proton-transporting ATP synthase activity, rotational mechanism / endoplasmic reticulum-Golgi intermediate compartment membrane / RNA endonuclease activity / proton transmembrane transport / receptor-mediated endocytosis / secretory granule / secretory granule membrane / small GTPase binding / transmembrane transport / phagocytic vesicle membrane / synaptic vesicle membrane / positive regulation of canonical Wnt signaling pathway / melanosome / signaling receptor activity / ATPase binding / postsynaptic membrane / Hydrolases; Acting on ester bonds / intracellular iron ion homeostasis / early endosome / lysosome / endosome membrane / endosome / nuclear speck / cilium / apical plasma membrane / Golgi membrane / axon / lysosomal membrane / external side of plasma membrane / focal adhesion / intracellular membrane-bounded organelle / ubiquitin protein ligase binding / centrosome / endoplasmic reticulum membrane / Neutrophil degranulation / protein-containing complex binding / perinuclear region of cytoplasm / Golgi apparatus / ATP hydrolysis activity / extracellular exosome / nucleoplasm / ATP binding / membrane
Similarity search - Function
ATPase, V0 complex, subunit e1/e2, metazoa / V0 complex accessory subunit Ac45 / V-type proton ATPase subunit S1, luminal domain / V-type proton ATPase subunit S1, luminal domain / Renin receptor-like / : / Renin receptor-like transmembrane spanning segment / Renin receptor N-terminal domain / ATPase, V1 complex, subunit A / : ...ATPase, V0 complex, subunit e1/e2, metazoa / V0 complex accessory subunit Ac45 / V-type proton ATPase subunit S1, luminal domain / V-type proton ATPase subunit S1, luminal domain / Renin receptor-like / : / Renin receptor-like transmembrane spanning segment / Renin receptor N-terminal domain / ATPase, V1 complex, subunit A / : / V-type proton ATPase subunit f-like / Ribonuclease kappa / V-type proton ATPase subunit S1/VOA1, transmembrane domain / V0 complex accessory subunit Ac45/VOA1 transmembrane domain / Vacuolar (H+)-ATPase G subunit / Vacuolar (H+)-ATPase G subunit / ATPase, V1 complex, subunit B / ATPase, V1 complex, subunit F, eukaryotic / ATPase, V0 complex, subunit e1/e2 / ATP synthase subunit H / ATPase, V0 complex, subunit d / V-ATPase proteolipid subunit C, eukaryotic / ATPase, V0 complex, subunit 116kDa, eukaryotic / ATPase, V0 complex, c/d subunit / V-type ATPase subunit C/d / V-type ATP synthase subunit c/d subunit superfamily / V-type ATP synthase c/d subunit, domain 3 superfamily / ATP synthase (C/AC39) subunit / V-ATPase proteolipid subunit / V-type ATPase, V0 complex, 116kDa subunit family / V-type ATPase 116kDa subunit family / ATPase, V1 complex, subunit D / V-type ATPase subunit E / ATPase, V1 complex, subunit F / ATPase, V1 complex, subunit F superfamily / V-type ATPase subunit E, C-terminal domain superfamily / ATP synthase subunit D / ATP synthase (F/14-kDa) subunit / ATP synthase (E/31 kDa) subunit / V-type ATP synthase regulatory subunit B/beta / V-type ATP synthase catalytic alpha chain / ATPsynthase alpha/beta subunit, N-terminal extension / ATPsynthase alpha/beta subunit barrel-sandwich domain / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / : / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / C-terminal domain of V and A type ATP synthase / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / V-type proton ATPase subunit e 1 / V-type proton ATPase subunit G 1 / Renin receptor / V-type proton ATPase subunit B, brain isoform / V-type proton ATPase 16 kDa proteolipid subunit c / V-type proton ATPase subunit E 1 / V-type proton ATPase catalytic subunit A / V-type proton ATPase subunit d 1 / V-type proton ATPase subunit S1 ...ADENOSINE-5'-DIPHOSPHATE / V-type proton ATPase subunit e 1 / V-type proton ATPase subunit G 1 / Renin receptor / V-type proton ATPase subunit B, brain isoform / V-type proton ATPase 16 kDa proteolipid subunit c / V-type proton ATPase subunit E 1 / V-type proton ATPase catalytic subunit A / V-type proton ATPase subunit d 1 / V-type proton ATPase subunit S1 / V-type proton ATPase subunit F / Ribonuclease kappa / V-type proton ATPase 116 kDa subunit a 1 / V-type proton ATPase 21 kDa proteolipid subunit c'' / V-type proton ATPase subunit D
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.47 Å
AuthorsZhang, Z. / Lyu, M.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) United States
CitationJournal: To Be Published
Title: Cryo-EM structure of human kidney V-ATPase state 2
Authors: Zhang, Z. / Lyu, M.
History
DepositionJun 27, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 6, 2025Provider: repository / Type: Initial release
Revision 1.0Aug 6, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Aug 6, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Aug 6, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
0: V-type proton ATPase 21 kDa proteolipid subunit
1: V-type proton ATPase 16 kDa proteolipid subunit
2: V-type proton ATPase 16 kDa proteolipid subunit
3: V-type proton ATPase 16 kDa proteolipid subunit
4: V-type proton ATPase 16 kDa proteolipid subunit
5: V-type proton ATPase 16 kDa proteolipid subunit
6: V-type proton ATPase 16 kDa proteolipid subunit
7: V-type proton ATPase 16 kDa proteolipid subunit
8: V-type proton ATPase 16 kDa proteolipid subunit
9: V-type proton ATPase 16 kDa proteolipid subunit
A: V-type proton ATPase catalytic subunit A
B: V-type proton ATPase catalytic subunit A
C: V-type proton ATPase catalytic subunit A
D: V-type proton ATPase subunit B, brain isoform
E: V-type proton ATPase subunit B, brain isoform
F: V-type proton ATPase subunit B, brain isoform
G: V-type proton ATPase subunit D
H: V-type proton ATPase subunit E 1
I: V-type proton ATPase subunit E 1
J: V-type proton ATPase subunit E 1
K: V-type proton ATPase subunit G 1
L: V-type proton ATPase subunit G 1
M: V-type proton ATPase subunit G 1
N: V-type proton ATPase subunit F
Q: V-type proton ATPase subunit d 1
R: V-type proton ATPase 116 kDa subunit a isoform 1
S: V-type proton ATPase subunit e 1
T: Ribonuclease kappa
U: V-type proton ATPase subunit S1
V: Renin receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)952,76831
Polymers952,34130
Non-polymers4271
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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V-type proton ATPase ... , 12 types, 28 molecules 0123456789ABCDEFGHIJKLMNQRSU

#1: Protein V-type proton ATPase 21 kDa proteolipid subunit / V-ATPase 21 kDa proteolipid subunit / Vacuolar proton pump 21 kDa proteolipid subunit / hATPL


Mass: 21418.213 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q99437
#2: Protein
V-type proton ATPase 16 kDa proteolipid subunit / V-ATPase 16 kDa proteolipid subunit / Vacuolar proton pump 16 kDa proteolipid subunit


Mass: 15743.655 Da / Num. of mol.: 9 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P27449
#3: Protein V-type proton ATPase catalytic subunit A / V-ATPase subunit A / V-ATPase 69 kDa subunit / Vacuolar ATPase isoform VA68 / Vacuolar proton pump ...V-ATPase subunit A / V-ATPase 69 kDa subunit / Vacuolar ATPase isoform VA68 / Vacuolar proton pump subunit alpha


Mass: 68379.875 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
References: UniProt: P38606, H+-transporting two-sector ATPase
#4: Protein V-type proton ATPase subunit B, brain isoform / V-ATPase subunit B 2 / Endomembrane proton pump 58 kDa subunit / HO57 / Vacuolar proton pump subunit B 2


Mass: 56561.500 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P21281
#5: Protein V-type proton ATPase subunit D / V-ATPase subunit D / V-ATPase 28 kDa accessory protein / Vacuolar proton pump subunit D


Mass: 28311.918 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y5K8
#6: Protein V-type proton ATPase subunit E 1 / V-ATPase subunit E 1 / V-ATPase 31 kDa subunit / p31 / Vacuolar proton pump subunit E 1


Mass: 26183.346 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P36543
#7: Protein V-type proton ATPase subunit G 1 / V-ATPase subunit G 1 / V-ATPase 13 kDa subunit 1 / Vacuolar proton pump subunit G 1 / Vacuolar ...V-ATPase subunit G 1 / V-ATPase 13 kDa subunit 1 / Vacuolar proton pump subunit G 1 / Vacuolar proton pump subunit M16


Mass: 13781.547 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75348
#8: Protein V-type proton ATPase subunit F / V-ATPase subunit F / V-ATPase 14 kDa subunit / Vacuolar proton pump subunit F


Mass: 13388.210 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q16864
#9: Protein V-type proton ATPase subunit d 1 / V-ATPase subunit d 1 / 32 kDa accessory protein / V-ATPase 40 kDa accessory protein / V-ATPase AC39 ...V-ATPase subunit d 1 / 32 kDa accessory protein / V-ATPase 40 kDa accessory protein / V-ATPase AC39 subunit / p39 / Vacuolar proton pump subunit d 1


Mass: 40369.949 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P61421
#10: Protein V-type proton ATPase 116 kDa subunit a isoform 1 / V-ATPase 116 kDa isoform a1 / Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit ...V-ATPase 116 kDa isoform a1 / Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit / Vacuolar adenosine triphosphatase subunit Ac116 / Vacuolar proton pump subunit 1 / Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1


Mass: 96512.414 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q93050
#11: Protein V-type proton ATPase subunit e 1 / V-ATPase subunit e 1 / V-ATPase 9.2 kDa membrane accessory protein / V-ATPase M9.2 subunit / ...V-ATPase subunit e 1 / V-ATPase 9.2 kDa membrane accessory protein / V-ATPase M9.2 subunit / Vacuolar proton pump subunit e 1


Mass: 9380.329 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O15342
#13: Protein V-type proton ATPase subunit S1 / V-ATPase subunit S1 / Protein XAP-3 / V-ATPase Ac45 subunit / V-ATPase S1 accessory protein / ...V-ATPase subunit S1 / Protein XAP-3 / V-ATPase Ac45 subunit / V-ATPase S1 accessory protein / Vacuolar proton pump subunit S1


Mass: 52067.480 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15904

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Protein , 2 types, 2 molecules TV

#12: Protein Ribonuclease kappa / RNase kappa


Mass: 15435.220 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
References: UniProt: Q6P5S7, Hydrolases; Acting on ester bonds
#14: Protein Renin receptor / ATPase H(+)-transporting lysosomal accessory protein 2 / ATPase H(+)-transporting lysosomal- ...ATPase H(+)-transporting lysosomal accessory protein 2 / ATPase H(+)-transporting lysosomal-interacting protein 2 / ER-localized type I transmembrane adapter / Embryonic liver differentiation factor 10 / N14F / Renin/prorenin receptor / Vacuolar ATP synthase membrane sector-associated protein M8-9 / V-ATPase M8.9 subunit


Mass: 39045.855 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75787

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Non-polymers , 1 types, 1 molecules

#15: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM

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Details

Has ligand of interestN
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: V-ATPase / Type: COMPLEX / Entity ID: #1-#14 / Source: NATURAL
Source (natural)Organism: Homo sapiens (human)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1500 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 38 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM softwareName: PHENIX / Version: 1.20.1_4487: / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.47 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 24168 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00657237
ELECTRON MICROSCOPYf_angle_d0.55277467
ELECTRON MICROSCOPYf_dihedral_angle_d12.52921029
ELECTRON MICROSCOPYf_chiral_restr0.0398872
ELECTRON MICROSCOPYf_plane_restr0.0049895

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