ID VPP4_HUMAN Reviewed; 840 AA. AC Q9HBG4; A4D1R4; A8KA80; Q32M47; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 2. DT 28-JAN-2026, entry version 191. DE RecName: Full=V-type proton ATPase 116 kDa subunit a 4; DE Short=V-ATPase 116 kDa isoform a 4; DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4; DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform; GN Name=ATP6V0A4; Synonyms=ATP6N1B, ATP6N2; 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], FUNCTION, SUBCELLULAR LOCATION, VARIANTS DRTA3 RP LEU-524; THR-580 AND ARG-820, AND VARIANT ALA-2. RC TISSUE=Kidney; RX PubMed=10973252; DOI=10.1038/79208; RA Smith A.N., Skaug J., Choate K.A., Nayir A., Bakkaloglu A., Ozen S., RA Hulton S.A., Sanjad S.A., Al-Sabban E.A., Lifton R.P., Scherer S.W., RA Karet F.E.; RT "Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD RT subunit, cause recessive distal renal tubular acidosis with preserved RT hearing."; RL Nat. Genet. 26:71-75(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-2. RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [7] RP FUNCTION, AND VARIANTS DRTA3 ASP-175; LYS-237 DEL; HIS-449 AND GLN-807. RX PubMed=12414817; DOI=10.1136/jmg.39.11.796; RA Stover E.H., Borthwick K.J., Bavalia C., Eady N., Fritz D.M., Rungroj N., RA Giersch A.B.S., Morton C.C., Axon P.R., Akil I., Al-Sabban E.A., RA Baguley D.M., Bianca S., Bakkaloglu A., Bircan Z., Chauveau D., RA Clermont M.-J., Guala A., Hulton S.A., Kroes H., Li Volti G., Mir S., RA Mocan H., Nayir A., Ozen S., Rodriguez Soriano J., Sanjad S.A., Tasic V., RA Taylor C.M., Topaloglu R., Smith A.N., Karet F.E.; RT "Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal RT tubular acidosis with new evidence for hearing loss."; RL J. Med. Genet. 39:796-803(2002). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). 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 (By similarity). V-ATPase is responsible for acidifying and CC maintaining the pH of intracellular compartments and in some cell CC types, is targeted to the plasma membrane, where it is responsible for CC acidifying the extracellular environment (By similarity). Involved in CC normal vectorial acid transport into the urine by the kidney CC (PubMed:10973252, PubMed:12414817). {ECO:0000250|UniProtKB:Q29466, CC ECO:0000250|UniProtKB:Q93050, ECO:0000269|PubMed:10973252, CC ECO:0000269|PubMed:12414817}. 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 (By similarity). The V1 complex consists of three catalytic CC AB heterodimers that form a heterohexamer, three peripheral stalks each CC consisting of EG heterodimers, one central rotor including subunits D CC and F, and the regulatory subunits C and H (By similarity). The proton CC translocation complex V0 consists of the proton transport subunit a, a CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, CC and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By CC similarity). Interacts with the V1 complex V-ATPase subunit A ATP6V1A CC (By similarity). Interacts with the V0 complex V-ATPase subunit c CC ATP6V0C (By similarity). {ECO:0000250|UniProtKB:Q920R6, CC ECO:0000250|UniProtKB:Q93050}. CC -!- INTERACTION: CC Q9HBG4; P02649: APOE; NbExp=3; IntAct=EBI-25832286, EBI-1222467; CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000269|PubMed:10973252}; Multi-pass membrane protein CC {ECO:0000255}. Basolateral cell membrane CC {ECO:0000250|UniProtKB:Q920R6}; Multi-pass membrane protein CC {ECO:0000255}. Note=Localizes to the apical surface of alpha- CC intercalated cells in the cortical collecting ducts of the distal CC nephron (PubMed:10973252). Localizes to the basolateral surface of CC beta-intercalated cells in the cortical collecting ducts of the distal CC nephron (By similarity). {ECO:0000250|UniProtKB:Q920R6, CC ECO:0000269|PubMed:10973252}. CC -!- TISSUE SPECIFICITY: Expressed in adult and fetal kidney. Found in the CC inner ear. {ECO:0000269|PubMed:12414817}. CC -!- DISEASE: Renal tubular acidosis, distal, 3, with or without CC sensorineural hearing loss (DRTA3) [MIM:602722]: An autosomal recessive CC disease characterized by reduced ability to acidify urine, variable CC hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and CC nephrolithiasis. It is due to functional failure of alpha-intercalated CC cells of the cortical collecting duct of the distal nephron, where CC vectorial proton transport is required for urinary acidification. CC {ECO:0000269|PubMed:10973252, ECO:0000269|PubMed:12414817}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family. CC {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; AF245517; AAG11415.1; -; mRNA. DR EMBL; AK292945; BAF85634.1; -; mRNA. DR EMBL; AC018663; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC020983; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236950; EAL24043.1; -; Genomic_DNA. DR EMBL; CH471070; EAW83892.1; -; Genomic_DNA. DR EMBL; BC109304; AAI09305.1; -; mRNA. DR EMBL; BC109305; AAI09306.1; -; mRNA. DR CCDS; CCDS5849.1; -. DR RefSeq; NP_065683.2; NM_020632.3. DR RefSeq; NP_570855.2; NM_130840.3. DR RefSeq; NP_570856.2; NM_130841.3. DR PDB; 7UNF; EM; 4.08 A; a=1-840. DR PDB; 9DET; EM; 3.00 A; a=1-840. DR PDBsum; 7UNF; -. DR PDBsum; 9DET; -. DR AlphaFoldDB; Q9HBG4; -. DR EMDB; EMD-26623; -. DR SMR; Q9HBG4; -. DR BioGRID; 119097; 39. DR ComplexPortal; CPX-6912; Vacuolar proton translocating ATPase complex, ATP6V0A4 variant. DR FunCoup; Q9HBG4; 524. DR IntAct; Q9HBG4; 28. DR STRING; 9606.ENSP00000308122; -. 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; Q9HBG4; 1 site. DR iPTMnet; Q9HBG4; -. DR PhosphoSitePlus; Q9HBG4; -. DR BioMuta; ATP6V0A4; -. DR DMDM; 308153516; -. DR jPOST; Q9HBG4; -. DR MassIVE; Q9HBG4; -. DR PaxDb; 9606-ENSP00000308122; -. DR PeptideAtlas; Q9HBG4; -. DR ProteomicsDB; 81539; -. DR Antibodypedia; 3120; 125 antibodies from 23 providers. DR DNASU; 50617; -. DR Ensembl; ENST00000310018.7; ENSP00000308122.2; ENSG00000105929.17. DR Ensembl; ENST00000353492.4; ENSP00000253856.6; ENSG00000105929.17. DR Ensembl; ENST00000393054.5; ENSP00000376774.1; ENSG00000105929.17. DR Ensembl; ENST00000645515.1; ENSP00000496421.1; ENSG00000105929.17. DR GeneID; 50617; -. DR KEGG; hsa:50617; -. DR MANE-Select; ENST00000310018.7; ENSP00000308122.2; NM_020632.3; NP_065683.2. DR UCSC; uc003vuf.4; human. DR AGR; HGNC:866; -. DR ClinPGx; PA25147; -. DR CTD; 50617; -. DR DisGeNET; 50617; -. DR GeneCards; ATP6V0A4; -. DR GeneReviews; ATP6V0A4; -. DR HGNC; HGNC:866; ATP6V0A4. DR HPA; ENSG00000105929; Group enriched (kidney, salivary gland). DR MalaCards; ATP6V0A4; -. DR MIM; 602722; phenotype. DR MIM; 605239; gene. DR OpenTargets; ENSG00000105929; -. DR Orphanet; 402041; Autosomal recessive distal renal tubular acidosis. DR VEuPathDB; HostDB:ENSG00000105929; -. DR eggNOG; KOG2189; Eukaryota. DR GeneTree; ENSGT00950000182881; -. DR HOGENOM; CLU_005230_0_2_1; -. DR InParanoid; Q9HBG4; -. DR OMA; HYVIHTI; -. DR OrthoDB; 10264220at2759; -. DR PAN-GO; Q9HBG4; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q9HBG4; -. DR BioCyc; MetaCyc:ENSG00000105929-MONOMER; -. DR PathwayCommons; Q9HBG4; -. DR Reactome; R-HSA-1222556; ROS and RNS production in phagocytes. DR Reactome; R-HSA-77387; Insulin receptor recycling. DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling. DR Reactome; R-HSA-983712; Ion channel transport. DR SignaLink; Q9HBG4; -. DR Agora; ENSG00000105929; -. DR BioGRID-ORCS; 50617; 18 hits in 1152 CRISPR screens. DR ChiTaRS; ATP6V0A4; human. DR GeneWiki; ATP6V0A4; -. DR GenomeRNAi; 50617; -. DR Pharos; Q9HBG4; Tbio. DR PRO; PR:Q9HBG4; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9HBG4; protein. DR Bgee; ENSG00000105929; Expressed in metanephros cortex and 109 other cell types or tissues. DR ExpressionAtlas; Q9HBG4; baseline and differential. DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031526; C:brush border membrane; IDA:HGNC-UCL. DR GO; GO:0005768; C:endosome; ISS:UniProtKB. 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:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; NAS:ComplexPortal. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl. DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IDA:HGNC-UCL. DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro. DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0051452; P:intracellular pH reduction; NAS:ComplexPortal. DR GO; GO:0001503; P:ossification; IMP:HGNC-UCL. DR GO; GO:1902600; P:proton transmembrane transport; IMP:HGNC-UCL. DR GO; GO:0006885; P:regulation of pH; IMP:HGNC-UCL. DR GO; GO:0097254; P:renal tubular secretion; IMP:HGNC-UCL. DR GO; GO:0007605; P:sensory perception of sound; IMP:HGNC-UCL. DR GO; GO:0097401; P:synaptic vesicle lumen acidification; IEA:Ensembl. DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central. DR InterPro; IPR002490; V-ATPase_116kDa_su. DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka. DR PANTHER; PTHR11629:SF26; V-TYPE PROTON ATPASE 116 KDA SUBUNIT A 4; 1. DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1. DR Pfam; PF01496; V_ATPase_I; 1. DR PIRSF; PIRSF001293; ATP6V0A1; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Disease variant; Hydrogen ion transport; KW Ion transport; Membrane; Proteomics identification; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..840 FT /note="V-type proton ATPase 116 kDa subunit a 4" FT /id="PRO_0000119219" FT TOPO_DOM 1..390 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 391..409 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 410..411 FT /note="Vacuolar" FT /evidence="ECO:0000255" FT TRANSMEM 412..428 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 429..443 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 444..473 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 474..538 FT /note="Vacuolar" FT /evidence="ECO:0000255" FT TRANSMEM 539..558 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 559..576 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 577..597 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 598..642 FT /note="Vacuolar" FT /evidence="ECO:0000255" FT TRANSMEM 643..662 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 663..727 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 728..752 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 753..773 FT /note="Vacuolar" FT /evidence="ECO:0000255" FT TRANSMEM 774..812 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 813..840 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 675..704 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 2 FT /note="V -> A (in dbSNP:rs10258719)" FT /evidence="ECO:0000269|PubMed:10973252, FT ECO:0000269|PubMed:14702039" FT /id="VAR_020992" FT VARIANT 175 FT /note="G -> D (in DRTA3)" FT /evidence="ECO:0000269|PubMed:12414817" FT /id="VAR_020993" FT VARIANT 237 FT /note="Missing (in DRTA3)" FT /evidence="ECO:0000269|PubMed:12414817" FT /id="VAR_020994" FT VARIANT 449 FT /note="R -> H (in DRTA3; dbSNP:rs1443883930)" FT /evidence="ECO:0000269|PubMed:12414817" FT /id="VAR_020995" FT VARIANT 524 FT /note="P -> L (in DRTA3; uncertain significance; FT dbSNP:rs121908368)" FT /evidence="ECO:0000269|PubMed:10973252" FT /id="VAR_017255" FT VARIANT 554 FT /note="F -> L (in dbSNP:rs1026435)" FT /id="VAR_066612" FT VARIANT 580 FT /note="M -> T (in DRTA3; benign; dbSNP:rs3807153)" FT /evidence="ECO:0000269|PubMed:10973252" FT /id="VAR_017256" FT VARIANT 604 FT /note="H -> Q (in dbSNP:rs3807154)" FT /id="VAR_066613" FT VARIANT 807 FT /note="R -> Q (in DRTA3; dbSNP:rs28939081)" FT /evidence="ECO:0000269|PubMed:12414817" FT /id="VAR_020996" FT VARIANT 820 FT /note="G -> R (in DRTA3; dbSNP:rs267606671)" FT /evidence="ECO:0000269|PubMed:10973252" FT /id="VAR_017257" FT CONFLICT 252 FT /note="P -> R (in Ref. 6; AAI09305/AAI09306)" FT /evidence="ECO:0000305" SQ SEQUENCE 840 AA; 96386 MW; 449964EBC01D4649 CRC64; MVSVFRSEEM CLSQLFLQVE AAYCCVAELG ELGLVQFKDL NMNVNSFQRK FVNEVRRCES LERILRFLED EMQNEIVVQL LEKSPLTPLP REMITLETVL EKLEGELQEA NQNQQALKQS FLELTELKYL LKKTQDFFET ETNLADDFFT EDTSGLLELK AVPAYMTGKL GFIAGVINRE RMASFERLLW RICRGNVYLK FSEMDAPLED PVTKEEIQKN IFIIFYQGEQ LRQKIKKICD GFRATVYPCP EPAVERREML ESVNVRLEDL ITVITQTESH RQRLLQEAAA NWHSWLIKVQ KMKAVYHILN MCNIDVTQQC VIAEIWFPVA DATRIKRALE QGMELSGSSM APIMTTVQSK TAPPTFNRTN KFTAGFQNIV DAYGVGSYRE INPAPYTIIT FPFLFAVMFG DCGHGTVMLL AALWMILNER RLLSQKTDNE IWNTFFHGRY LILLMGIFSI YTGLIYNDCF SKSLNIFGSS WSVQPMFRNG TWNTHVMEES LYLQLDPAIP GVYFGNPYPF GIDPIWNLAS NKLTFLNSYK MKMSVILGIV QMVFGVILSL FNHIYFRRTL NIILQFIPEM IFILCLFGYL VFMIIFKWCC FDVHVSQHAP SILIHFINMF LFNYSDSSNA PLYKHQQEVQ SFFVVMALIS VPWMLLIKPF ILRASHRKSQ LQASRIQEDA TENIEGDSSS PSSRSGQRTS ADTHGALDDH GEEFNFGDVF VHQAIHTIEY CLGCISNTAS YLRLWALSLA HAQLSEVLWT MVMNSGLQTR GWGGIVGVFI IFAVFAVLTV AILLIMEGLS AFLHALRLHW VEFQNKFYVG DGYKFSPFSF KHILDGTAEE //