ID VA0D1_HUMAN Reviewed; 351 AA. AC P61421; P12953; Q02547; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 1. DT 28-JAN-2026, entry version 181. DE RecName: Full=V-type proton ATPase subunit d 1; DE Short=V-ATPase subunit d 1; DE AltName: Full=32 kDa accessory protein; DE AltName: Full=V-ATPase 40 kDa accessory protein; DE AltName: Full=V-ATPase AC39 subunit; DE Short=p39; DE AltName: Full=Vacuolar proton pump subunit d 1; GN Name=ATP6V0D1 {ECO:0000312|HGNC:HGNC:13724}; Synonyms=ATP6D, VPATPD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Osteoclastoma; RX PubMed=8250920; DOI=10.1006/bbrc.1993.2434; RA van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.; RT "Cloning and tissue distribution of subunits C, D, and E of the human RT vacuolar H(+)-ATPase."; RL Biochem. Biophys. Res. Commun. 197:15-21(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11118322; DOI=10.1006/bbrc.2000.4003; RA Agarwal A.K., White P.C.; RT "Structure of the VPATPD gene encoding subunit D of the human vacuolar RT proton ATPase."; RL Biochem. Biophys. Res. Commun. 279:543-547(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 264-351. RA Bhat K.S.; RT "Expressed sequence tags from a human cell line."; RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases. RN [5] RP TISSUE SPECIFICITY. RX PubMed=12384298; DOI=10.1016/s0378-1119(02)00884-3; RA Smith A.N., Borthwick K.J., Karet F.E.; RT "Molecular cloning and characterization of novel tissue-specific isoforms RT of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation RT in autosomal recessive distal renal tubular acidosis."; RL Gene 297:169-177(2002). RN [6] 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., Buerckstuemmer T., RA 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 [7] RP SUBCELLULAR LOCATION. RX PubMed=21844891; DOI=10.1038/cr.2011.134; RA Chen Y., Wu B., Xu L., Li H., Xia J., Yin W., Li Z., Shi D., Li S., Lin S., RA Shu X., Pei D.; RT "A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in vivo."; RL Cell Res. 22:333-345(2012). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [9] RP FUNCTION. RX PubMed=28296633; DOI=10.7554/elife.22693; RA Miles A.L., Burr S.P., Grice G.L., Nathan J.A.; RT "The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, RT control HIF1alpha prolyl hydroxylation by regulating cellular iron RT levels."; RL Elife 6:E22693-E22693(2017). RN [10] RP INTERACTION WITH PIP4P1. RX PubMed=29644770; DOI=10.1111/gtc.12583; RA Hashimoto Y., Shirane M., Nakayama K.I.; RT "TMEM55B contributes to lysosomal homeostasis and amino acid-induced mTORC1 RT activation."; RL Genes Cells 23:418-434(2018). RN [11] RP FUNCTION, INTERACTION WITH TMEM9 AND ATP6AP2, AND SUBCELLULAR LOCATION. RX PubMed=30374053; DOI=10.1038/s41556-018-0219-8; RA Jung Y.S., Jun S., Kim M.J., Lee S.H., Suh H.N., Lien E.M., Jung H.Y., RA Lee S., Zhang J., Yang J.I., Ji H., Wu J.Y., Wang W., Miller R.K., Chen J., RA McCrea P.D., Kopetz S., Park J.I.; RT "TMEM9 promotes intestinal tumorigenesis through vacuolar-ATPase-activated RT Wnt/beta-catenin signalling."; RL Nat. Cell Biol. 20:1421-1433(2018). RN [12] {ECO:0007744|PDB:6WLW, ECO:0007744|PDB:6WM2, ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS), FUNCTION, AND RP IDENTIFICATION IN THE V-ATPASE COMPLEX. RX PubMed=33065002; DOI=10.1016/j.molcel.2020.09.029; RA Wang L., Wu D., Robinson C.V., Wu H., Fu T.M.; RT "Structures of a Complete Human V-ATPase Reveal Mechanisms of Its RT Assembly."; RL Mol. Cell 80:501-511.e3(2020). CC -!- FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), CC a multisubunit enzyme composed of a peripheral complex (V1) that CC hydrolyzes ATP and a membrane integral complex (V0) that translocates CC protons (PubMed:28296633, PubMed:30374053, PubMed:33065002). V-ATPase CC is responsible for acidifying and maintaining the pH of intracellular CC compartments and in some cell types, is targeted to the plasma CC membrane, where it is responsible for acidifying the extracellular CC environment (PubMed:30374053). May play a role in coupling of proton CC transport and ATP hydrolysis (By similarity). In aerobic conditions, CC involved in intracellular iron homeostasis, thus triggering the CC activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to CC HIF1A hydroxylation and subsequent proteasomal degradation CC (PubMed:28296633). May play a role in cilium biogenesis through CC regulation of the transport and the localization of proteins to the CC cilium (By similarity). {ECO:0000250|UniProtKB:P51863, CC ECO:0000250|UniProtKB:Q6PGV1, ECO:0000269|PubMed:28296633, CC ECO:0000269|PubMed:30374053, ECO:0000269|PubMed:33065002}. CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two CC complexes: the ATP-hydrolytic V1 complex and the proton translocation CC V0 complex (PubMed:33065002). The V1 complex consists of three CC catalytic AB heterodimers that form a heterohexamer, three peripheral CC stalks each consisting of EG heterodimers, one central rotor including CC subunits D and F, and the regulatory subunits C and H CC (PubMed:33065002). The proton translocation complex V0 consists of the CC proton transport subunit a, a ring of proteolipid subunits c9c'', CC rotary subunit d, subunits e and f, and the accessory subunits CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002). Interacts with ATP6AP2; CC ATP6AP2 is a V-ATPase accessory protein and the interaction promotes v- CC ATPase complex assembly (PubMed:30374053). Interacts with TMEM9; TMEM9 CC is a v-ATPase assembly regulator and the interaction induces the CC interaction with ATP6AP2 (PubMed:30374053). Interacts with PIP4P1 CC (PubMed:29644770). {ECO:0000269|PubMed:29644770, CC ECO:0000269|PubMed:30374053, ECO:0000269|PubMed:33065002}. CC -!- INTERACTION: CC P61421; P54253: ATXN1; NbExp=7; IntAct=EBI-954063, EBI-930964; CC P61421; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-954063, EBI-9679045; CC P61421; P42858: HTT; NbExp=6; IntAct=EBI-954063, EBI-466029; CC P61421; O43711: TLX3; NbExp=3; IntAct=EBI-954063, EBI-3939165; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:21844891}; CC Peripheral membrane protein {ECO:0000305|PubMed:21844891}; Cytoplasmic CC side {ECO:0000305|PubMed:21844891}. Lysosome membrane CC {ECO:0000305|PubMed:30374053}; Peripheral membrane protein CC {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane CC {ECO:0000250|UniProtKB:P61420}; Peripheral membrane protein CC {ECO:0000305}. Note=Localizes to centrosome and the base of the cilium. CC {ECO:0000250|UniProtKB:Q6PGV1}. CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12384298, CC ECO:0000269|PubMed:8250920}. CC -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA50591.1; Type=Frameshift; 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; X71490; CAA50591.1; ALT_FRAME; mRNA. DR EMBL; BC008861; AAH08861.1; -; mRNA. DR EMBL; L05087; AAC15852.1; -; mRNA. DR CCDS; CCDS10838.1; -. DR RefSeq; NP_004682.2; NM_004691.4. DR PDB; 6WLW; EM; 3.00 A; Q=1-351. DR PDB; 6WM2; EM; 3.10 A; Q=1-351. DR PDB; 6WM3; EM; 3.40 A; Q=1-351. DR PDB; 6WM4; EM; 3.60 A; Q=1-351. DR PDB; 7U4T; EM; 3.60 A; Q=1-351. DR PDB; 7UNF; EM; 4.08 A; k=1-351. DR PDB; 9CF8; EM; 3.46 A; Q=1-351. DR PDB; 9CFC; EM; 3.47 A; Q=1-351. DR PDB; 9DET; EM; 3.00 A; d=1-351. DR PDBsum; 6WLW; -. DR PDBsum; 6WM2; -. DR PDBsum; 6WM3; -. DR PDBsum; 6WM4; -. DR PDBsum; 7U4T; -. DR PDBsum; 7UNF; -. DR PDBsum; 9CF8; -. DR PDBsum; 9CFC; -. DR PDBsum; 9DET; -. DR AlphaFoldDB; P61421; -. DR EMDB; EMD-21844; -. DR EMDB; EMD-21847; -. DR EMDB; EMD-21848; -. DR EMDB; EMD-21849; -. DR EMDB; EMD-26334; -. DR EMDB; EMD-26623; -. DR EMDB; EMD-45533; -. DR EMDB; EMD-45536; -. DR SMR; P61421; -. DR BioGRID; 114564; 255. DR ComplexPortal; CPX-2470; Vacuolar proton translocating ATPase complex, ATP6V0A1 variant. DR ComplexPortal; CPX-6904; Vacuolar proton translocating ATPase complex, ATP6V0A2 variant. DR ComplexPortal; CPX-6905; Vacuolar proton translocating ATPase complex, ATP6V0A3 variant. DR ComplexPortal; CPX-6912; Vacuolar proton translocating ATPase complex, ATP6V0A4 variant. DR CORUM; P61421; -. DR DIP; DIP-47435N; -. DR FunCoup; P61421; 2833. DR IntAct; P61421; 119. DR MINT; P61421; -. DR STRING; 9606.ENSP00000290949; -. DR DrugBank; DB01133; Tiludronic acid. DR TCDB; 3.A.2.2.4; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily. DR GlyGen; P61421; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61421; -. DR PhosphoSitePlus; P61421; -. DR SwissPalm; P61421; -. DR BioMuta; ATP6V0D1; -. DR DMDM; 47606646; -. DR jPOST; P61421; -. DR MassIVE; P61421; -. DR PaxDb; 9606-ENSP00000290949; -. DR PeptideAtlas; P61421; -. DR ProteomicsDB; 57300; -. DR Pumba; P61421; -. DR Antibodypedia; 2185; 205 antibodies from 27 providers. DR DNASU; 9114; -. DR Ensembl; ENST00000290949.8; ENSP00000290949.3; ENSG00000159720.14. DR GeneID; 9114; -. DR KEGG; hsa:9114; -. DR MANE-Select; ENST00000290949.8; ENSP00000290949.3; NM_004691.5; NP_004682.2. DR UCSC; uc002ete.2; human. DR AGR; HGNC:13724; -. DR ClinPGx; PA25150; -. DR CTD; 9114; -. DR DisGeNET; 9114; -. DR GeneCards; ATP6V0D1; -. DR HGNC; HGNC:13724; ATP6V0D1. DR HPA; ENSG00000159720; Low tissue specificity. DR MIM; 607028; gene. DR OpenTargets; ENSG00000159720; -. DR VEuPathDB; HostDB:ENSG00000159720; -. DR eggNOG; KOG2957; Eukaryota. DR GeneTree; ENSGT00390000002200; -. DR HOGENOM; CLU_051277_0_0_1; -. DR InParanoid; P61421; -. DR OMA; MTYGYMI; -. DR OrthoDB; 10250083at2759; -. DR PAN-GO; P61421; 5 GO annotations based on evolutionary models. DR PhylomeDB; P61421; -. DR BioCyc; MetaCyc:HS08417-MONOMER; -. DR PathwayCommons; P61421; -. DR Reactome; R-HSA-1222556; ROS and RNS production in phagocytes. DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes. DR Reactome; R-HSA-77387; Insulin receptor recycling. DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling. DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1. DR Reactome; R-HSA-983712; Ion channel transport. DR Reactome; R-HSA-9857377; Regulation of MITF-M-dependent genes involved in lysosome biogenesis and autophagy. DR SignaLink; P61421; -. DR SIGNOR; P61421; -. DR Agora; ENSG00000159720; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 9114; 616 hits in 1173 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; ATP6V0D1; human. DR GeneWiki; ATP6V0D1; -. DR GenomeRNAi; 9114; -. DR Pharos; P61421; Tbio. DR PRO; PR:P61421; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P61421; protein. DR Bgee; ENSG00000159720; Expressed in mucosa of transverse colon and 205 other cell types or tissues. DR ExpressionAtlas; P61421; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:0043679; C:axon terminus; IEA:Ensembl. DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005769; C:early endosome; IBA:GO_Central. DR GO; GO:0010008; C:endosome membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IBA:GO_Central. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl. DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IDA:UniProtKB. DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:Ensembl. DR GO; GO:0036295; P:cellular response to increased oxygen levels; IMP:UniProtKB. DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB. DR GO; GO:0006879; P:intracellular iron ion homeostasis; IMP:UniProtKB. DR GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB. DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL. DR GO; GO:0097401; P:synaptic vesicle lumen acidification; IEA:Ensembl. DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central. DR GO; GO:0007034; P:vacuolar transport; IBA:GO_Central. DR FunFam; 1.10.132.50:FF:000002; V-type proton ATPase subunit; 1. DR FunFam; 1.20.1690.10:FF:000001; V-type proton ATPase subunit; 1. DR FunFam; 1.20.1690.10:FF:000002; V-type proton ATPase subunit; 1. DR Gene3D; 1.10.132.50; ATP synthase (C/AC39) subunit, domain 3; 1. DR Gene3D; 1.20.1690.10; V-type ATP synthase subunit C domain; 2. DR InterPro; IPR036079; ATPase_csu/dsu_sf. DR InterPro; IPR002843; ATPase_V0-cplx_csu/dsu. DR InterPro; IPR016727; ATPase_V0-cplx_dsu. DR InterPro; IPR035067; V-type_ATPase_csu/dsu. DR InterPro; IPR044911; V-type_ATPase_csu/dsu_dom_3. DR PANTHER; PTHR11028; VACUOLAR ATP SYNTHASE SUBUNIT AC39; 1. DR Pfam; PF01992; vATP-synt_AC39; 1. DR PIRSF; PIRSF018497; V-ATP_synth_D; 1. DR SUPFAM; SSF103486; V-type ATP synthase subunit C; 1. PE 1: Evidence at protein level; KW 3D-structure; Cilium biogenesis/degradation; Cytoplasmic vesicle; KW Hydrogen ion transport; Ion transport; Lysosome; Membrane; Phosphoprotein; KW Proteomics identification; Reference proteome; Transport. FT CHAIN 1..351 FT /note="V-type proton ATPase subunit d 1" FT /id="PRO_0000119350" FT MOD_RES 270 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P51863" FT MOD_RES 283 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51863" FT CONFLICT 27 FT /note="V -> E (in Ref. 1; CAA50591)" FT /evidence="ECO:0000305" FT CONFLICT 266..267 FT /note="NV -> KL (in Ref. 1; CAA50591)" FT /evidence="ECO:0000305" FT TURN 5..8 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 9..11 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 16..24 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 30..33 FT /evidence="ECO:0007829|PDB:6WLW" FT TURN 34..38 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 42..48 FT /evidence="ECO:0007829|PDB:6WLW" FT TURN 50..54 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 67..85 FT /evidence="ECO:0007829|PDB:6WLW" FT TURN 86..88 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 91..99 FT /evidence="ECO:0007829|PDB:6WLW" FT TURN 100..105 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 106..116 FT /evidence="ECO:0007829|PDB:6WLW" FT TURN 117..119 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 126..128 FT /evidence="ECO:0007829|PDB:6WM2" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:6WM3" FT TURN 136..143 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 147..156 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 161..164 FT /evidence="ECO:0007829|PDB:6WLW" FT TURN 165..167 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 178..197 FT /evidence="ECO:0007829|PDB:6WLW" FT TURN 202..208 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 209..225 FT /evidence="ECO:0007829|PDB:6WLW" FT STRAND 228..231 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 234..237 FT /evidence="ECO:0007829|PDB:6WLW" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 248..251 FT /evidence="ECO:0007829|PDB:6WLW" FT TURN 252..256 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 264..267 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 272..277 FT /evidence="ECO:0007829|PDB:6WLW" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 294..303 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:6WLW" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 313..325 FT /evidence="ECO:0007829|PDB:6WLW" FT TURN 326..328 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 329..336 FT /evidence="ECO:0007829|PDB:6WLW" FT TURN 337..339 FT /evidence="ECO:0007829|PDB:6WLW" FT HELIX 343..346 FT /evidence="ECO:0007829|PDB:6WM3" SQ SEQUENCE 351 AA; 40329 MW; A720F8A87511203C CRC64; MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN EASPLTVSVI DDRLKEKMVV EFRHMRNHAY EPLASFLDFI TYSYMIDNVI LLITGTLHQR SIAELVPKCH PLGSFEQMEA VNIAQTPAEL YNAILVDTPL AAFFQDCISE QDLDEMNIEI IRNTLYKAYL ESFYKFCTLL GGTTADAMCP ILEFEADRRA FIITINSFGT ELSKEDRAKL FPHCGRLYPE GLAQLARADD YEQVKNVADY YPEYKLLFEG AGSNPGDKTL EDRFFEHEVK LNKLAFLNQF HFGVFYAFVK LKEQECRNIV WIAECIAQRH RAKIDNYIPI F //