ID AT131_HUMAN Reviewed; 1204 AA. AC Q9HD20; B3KPJ2; B3KTA7; Q6NT90; Q6ZMG7; Q9H6C6; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 18-OCT-2001, sequence version 2. DT 27-MAR-2024, entry version 197. DE RecName: Full=Endoplasmic reticulum transmembrane helix translocase {ECO:0000305}; DE EC=7.4.2.- {ECO:0000269|PubMed:24392018}; DE AltName: Full=Endoplasmic reticulum P5A-ATPase {ECO:0000303|PubMed:32973005}; GN Name=ATP13A1 {ECO:0000303|PubMed:32973005, GN ECO:0000312|HGNC:HGNC:24215}; GN Synonyms=ATP13A {ECO:0000312|HGNC:HGNC:24215}, KIAA1825 GN {ECO:0000303|PubMed:11347906}; ORFNames=CGI-152 {ECO:0000303|Ref.1}; 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 [LARGE SCALE MRNA] (ISOFORM B). RA Chou M.C.-H., Lin W.-C.; RT "Identification of novel human genes by comparative proteomics."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C). RC TISSUE=Hepatoma, and Kidney epithelium; 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]. RA Mural R.J., Istrail S., Sutton G.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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1204 (ISOFORM A). RC TISSUE=Brain; RX PubMed=11347906; DOI=10.1093/dnares/8.2.85; RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 8:85-95(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 844-1204. RC TISSUE=Brain, and Kidney; 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 [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-420. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-899, AND IDENTIFICATION BY RP 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 [8] 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). RN [9] 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-899 AND SER-905, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP SUBCELLULAR LOCATION. RX PubMed=24392018; DOI=10.1371/journal.pone.0085519; RA Cohen Y., Megyeri M., Chen O.C., Condomitti G., Riezman I., RA Loizides-Mangold U., Abdul-Sada A., Rimon N., Riezman H., Platt F.M., RA Futerman A.H., Schuldiner M.; RT "The yeast p5 type ATPase, spf1, regulates manganese transport into the RT endoplasmic reticulum."; RL PLoS ONE 8:E85519-E85519(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-899, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] 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 [16] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASP-533. RX PubMed=32973005; DOI=10.1126/science.abc5809; RA McKenna M.J., Sim S.I., Ordureau A., Wei L., Harper J.W., Shao S., Park E.; RT "The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase."; RL Science 369:0-0(2020). RN [17] RP FUNCTION. RX PubMed=36264797; DOI=10.1126/science.add1856; RA Guna A., Stevens T.A., Inglis A.J., Replogle J.M., Esantsi T.K., RA Muthukumar G., Shaffer K.C.L., Wang M.L., Pogson A.N., Jones J.J., RA Lomenick B., Chou T.F., Weissman J.S., Voorhees R.M.; RT "MTCH2 is a mitochondrial outer membrane protein insertase."; RL Science 378:317-322(2022). RN [18] RP VARIANT LYS-349. RX PubMed=28940097; DOI=10.1007/s00439-017-1843-2; RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A., RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M., RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A., RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S., RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T., RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C., RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M., RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.; RT "Expanding the genetic heterogeneity of intellectual disability."; RL Hum. Genet. 136:1419-1429(2017). RN [19] RP ERRATUM OF PUBMED:28940097. RX PubMed=29288388; DOI=10.1007/s00439-017-1859-7; RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A., RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M., RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A., RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S., RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T., RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C., RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M., RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.; RT "Correction to: Expanding the genetic heterogeneity of intellectual RT disability."; RL Hum. Genet. 137:105-109(2018). CC -!- FUNCTION: Endoplasmic reticulum translocase required to remove CC mitochondrial transmembrane proteins mistargeted to the endoplasmic CC reticulum (PubMed:32973005, PubMed:36264797). Acts as a dislocase that CC mediates the ATP-dependent extraction of mislocalized mitochondrial CC transmembrane proteins from the endoplasmic reticulum membrane CC (PubMed:32973005). Specifically binds mitochondrial tail-anchored CC transmembrane proteins: has an atypically large substrate-binding CC pocket that recognizes and binds moderately hydrophobic transmembranes CC with short hydrophilic lumenal domains (PubMed:32973005). CC {ECO:0000269|PubMed:32973005, ECO:0000269|PubMed:36264797}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-with a C-terminal TM segment(out) + ATP + H2O = CC [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate; CC Xref=Rhea:RHEA:66168, Rhea:RHEA-COMP:16963, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:90782, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:32973005}; CC -!- INTERACTION: CC Q9HD20-3; Q92624: APPBP2; NbExp=3; IntAct=EBI-12069500, EBI-743771; CC Q9HD20-3; Q13520: AQP6; NbExp=3; IntAct=EBI-12069500, EBI-13059134; CC Q9HD20-3; Q8N350-4: CBARP; NbExp=3; IntAct=EBI-12069500, EBI-19051169; CC Q9HD20-3; P25025: CXCR2; NbExp=3; IntAct=EBI-12069500, EBI-2835281; CC Q9HD20-3; Q15125: EBP; NbExp=3; IntAct=EBI-12069500, EBI-3915253; CC Q9HD20-3; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-12069500, EBI-18535450; CC Q9HD20-3; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12069500, EBI-18304435; CC Q9HD20-3; O15552: FFAR2; NbExp=3; IntAct=EBI-12069500, EBI-2833872; CC Q9HD20-3; O15529: GPR42; NbExp=3; IntAct=EBI-12069500, EBI-18076404; CC Q9HD20-3; Q8IZD2-3: KMT2E; NbExp=3; IntAct=EBI-12069500, EBI-12900093; CC Q9HD20-3; Q9NQG1: MANBAL; NbExp=3; IntAct=EBI-12069500, EBI-3867271; CC Q9HD20-3; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-12069500, EBI-373355; CC Q9HD20-3; Q15546: MMD; NbExp=3; IntAct=EBI-12069500, EBI-17873222; CC Q9HD20-3; Q6P5S7: RNASEK; NbExp=3; IntAct=EBI-12069500, EBI-18397230; CC Q9HD20-3; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-12069500, EBI-17247926; CC Q9HD20-3; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12069500, EBI-18159983; CC Q9HD20-3; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-12069500, EBI-12243266; CC Q9HD20-3; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-12069500, EBI-8644112; CC Q9HD20-3; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-12069500, EBI-10262251; CC Q9HD20-3; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-12069500, EBI-17295964; CC Q9HD20-3; Q5VXT5-2: SYPL2; NbExp=3; IntAct=EBI-12069500, EBI-18196631; CC Q9HD20-3; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-12069500, EBI-12947623; CC Q9HD20-3; P55061: TMBIM6; NbExp=3; IntAct=EBI-12069500, EBI-1045825; CC Q9HD20-3; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-12069500, EBI-8638294; CC Q9HD20-3; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-12069500, EBI-10982110; CC Q9HD20-3; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-12069500, EBI-13356252; CC Q9HD20-3; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-12069500, EBI-1055364; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:24392018}; Multi-pass membrane protein CC {ECO:0000269|PubMed:24392018}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=A; CC IsoId=Q9HD20-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9HD20-2; Sequence=VSP_000434, VSP_000435; CC Name=C; CC IsoId=Q9HD20-3; Sequence=VSP_000433; CC -!- DOMAIN: Contains a large substrate-binding pocket that recognizes CC alpha-helical transmembranes, which alternately faces the endoplasmic CC reticulum lumen and cytosol, while remaining accessible to the lipid CC bilayer through a lateral opening. The translocase alternates between CC two conformations: inward-open (E1) and outward-open (E2) states. CC Undergoes a series of conformational changes with ATP-binding, CC phosphorylation of the Asp active site and subsequent dephosphorylation CC in a Post-Albers cycle (i.e., E1 -> E1-ATP -> E1P-ADP -> E1P -> E2P -> CC E2-Pi -> E1). A substrate transmembrane helix with a short, CC preferentially positively charged lumenal segment binds to the outward- CC open pocket and the E2P-to-E1 transition flips the transmembrane by a CC switch from the outward-open to inward-open conformation. CC {ECO:0000250|UniProtKB:P39986}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) CC family. Type V subfamily. {ECO:0000305}. CC -!- CAUTION: Was initially thought to mediate manganese transport CC (PubMed:24392018). However, it was later shown to specifically bind CC moderately hydrophobic transmembrane with short hydrophilic lumenal CC domains that misinsert into the endoplasmic reticulum CC (PubMed:32973005). {ECO:0000269|PubMed:24392018, CC ECO:0000269|PubMed:32973005}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH69211.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Wrong place - Issue 234 of CC March 2021; CC URL="https://web.expasy.org/spotlight/back_issues/234/"; 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; AF288687; AAG01173.1; -; mRNA. DR EMBL; AK026044; BAB15334.1; -; mRNA. DR EMBL; AK056420; BAG51704.1; -; mRNA. DR EMBL; AK095287; BAG53019.1; -; mRNA. DR EMBL; AK172778; BAD18759.1; -; mRNA. DR EMBL; AB058728; BAB47454.1; -; mRNA. DR EMBL; CH471106; EAW84849.1; -; Genomic_DNA. DR EMBL; CH471106; EAW84850.1; -; Genomic_DNA. DR EMBL; BC009302; AAH09302.2; -; mRNA. DR EMBL; BC069211; AAH69211.1; ALT_FRAME; mRNA. DR CCDS; CCDS32970.2; -. [Q9HD20-1] DR RefSeq; NP_065143.2; NM_020410.2. [Q9HD20-1] DR AlphaFoldDB; Q9HD20; -. DR SMR; Q9HD20; -. DR BioGRID; 121393; 223. DR IntAct; Q9HD20; 52. DR MINT; Q9HD20; -. DR STRING; 9606.ENSP00000349877; -. DR TCDB; 3.A.3.10.19; the p-type atpase (p-atpase) superfamily. DR CarbonylDB; Q9HD20; -. DR GlyCosmos; Q9HD20; 3 sites, 1 glycan. DR GlyGen; Q9HD20; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q9HD20; -. DR PhosphoSitePlus; Q9HD20; -. DR SwissPalm; Q9HD20; -. DR BioMuta; ATP13A1; -. DR DMDM; 18202961; -. DR EPD; Q9HD20; -. DR jPOST; Q9HD20; -. DR MassIVE; Q9HD20; -. DR MaxQB; Q9HD20; -. DR PaxDb; 9606-ENSP00000349877; -. DR PeptideAtlas; Q9HD20; -. DR ProteomicsDB; 81811; -. [Q9HD20-1] DR ProteomicsDB; 81812; -. [Q9HD20-2] DR ProteomicsDB; 81813; -. [Q9HD20-3] DR Pumba; Q9HD20; -. DR Antibodypedia; 28529; 91 antibodies from 27 providers. DR DNASU; 57130; -. DR Ensembl; ENST00000291503.9; ENSP00000291503.5; ENSG00000105726.17. [Q9HD20-2] DR Ensembl; ENST00000357324.11; ENSP00000349877.6; ENSG00000105726.17. [Q9HD20-1] DR GeneID; 57130; -. DR KEGG; hsa:57130; -. DR MANE-Select; ENST00000357324.11; ENSP00000349877.6; NM_020410.3; NP_065143.2. DR UCSC; uc002nng.4; human. [Q9HD20-1] DR AGR; HGNC:24215; -. DR CTD; 57130; -. DR DisGeNET; 57130; -. DR GeneCards; ATP13A1; -. DR HGNC; HGNC:24215; ATP13A1. DR HPA; ENSG00000105726; Low tissue specificity. DR MIM; 619118; gene. DR neXtProt; NX_Q9HD20; -. DR OpenTargets; ENSG00000105726; -. DR PharmGKB; PA134988892; -. DR VEuPathDB; HostDB:ENSG00000105726; -. DR eggNOG; KOG0209; Eukaryota. DR GeneTree; ENSGT00550000075064; -. DR HOGENOM; CLU_001828_4_1_1; -. DR InParanoid; Q9HD20; -. DR OMA; QKTKYVW; -. DR OrthoDB; 6047at2759; -. DR PhylomeDB; Q9HD20; -. DR TreeFam; TF300725; -. DR PathwayCommons; Q9HD20; -. DR Reactome; R-HSA-936837; Ion transport by P-type ATPases. DR SignaLink; Q9HD20; -. DR SIGNOR; Q9HD20; -. DR BioGRID-ORCS; 57130; 118 hits in 1168 CRISPR screens. DR ChiTaRS; ATP13A1; human. DR GenomeRNAi; 57130; -. DR Pharos; Q9HD20; Tbio. DR PRO; PR:Q9HD20; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9HD20; Protein. DR Bgee; ENSG00000105726; Expressed in granulocyte and 177 other cell types or tissues. DR ExpressionAtlas; Q9HD20; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0015410; F:ABC-type manganese transporter activity; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0140567; F:membrane protein dislocase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central. DR GO; GO:0140569; P:extraction of mislocalized protein from ER membrane; IDA:UniProtKB. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central. DR GO; GO:0034220; P:monoatomic ion transmembrane transport; TAS:Reactome. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR CDD; cd07543; P-type_ATPase_cation; 1. DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1. DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR006544; P-type_TPase_V. DR InterPro; IPR047820; P5A-type_ATPase. DR InterPro; IPR001757; P_typ_ATPase. DR InterPro; IPR044492; P_typ_ATPase_HD_dom. DR NCBIfam; TIGR01494; ATPase_P-type; 2. DR NCBIfam; TIGR01657; P-ATPase-V; 1. DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1. DR PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR PRINTS; PR00119; CATATPASE. DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1. DR SFLD; SFLDF00027; p-type_atpase; 1. DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1. DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. DR Genevisible; Q9HD20; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ATP-binding; Endoplasmic reticulum; KW Glycoprotein; Magnesium; Membrane; Metal-binding; Nucleotide-binding; KW Phosphoprotein; Protein transport; Reference proteome; Translocase; KW Transmembrane; Transmembrane helix; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..1204 FT /note="Endoplasmic reticulum transmembrane helix FT translocase" FT /id="PRO_0000046421" FT TOPO_DOM 2..66 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 67..87 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 88..95 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 96..116 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 117..243 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 244..264 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 265..443 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 444..464 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 465..989 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 990..1010 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1011 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1012..1032 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1033..1051 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1052..1072 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1073..1096 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1097..1117 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1118..1132 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 1133..1153 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1154..1166 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1167..1187 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1188..1204 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 199..230 FT /note="A-domain; part 1" FT /evidence="ECO:0000250|UniProtKB:P39986" FT REGION 295..435 FT /note="A-domain; part 2" FT /evidence="ECO:0000250|UniProtKB:P39986" FT REGION 512..541 FT /note="P-domain; part 1" FT /evidence="ECO:0000250|UniProtKB:P39986" FT REGION 543..724 FT /note="N-domain" FT /evidence="ECO:0000250|UniProtKB:P39986" FT REGION 727..885 FT /note="P-domain; part 2" FT /evidence="ECO:0000250|UniProtKB:P39986" FT REGION 886..949 FT /note="Arm-like" FT /evidence="ECO:0000250|UniProtKB:P39986" FT REGION 889..933 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 950..965 FT /note="P-domain; part 3" FT /evidence="ECO:0000250|UniProtKB:P39986" FT COMPBIAS 900..933 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 533 FT /note="4-aspartylphosphate intermediate" FT /evidence="ECO:0000305|PubMed:24392018" FT BINDING 533..535 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P39986" FT BINDING 533 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P39986" FT BINDING 535 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P39986" FT BINDING 626 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0" FT BINDING 684 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P39986" FT BINDING 749 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P39986" FT BINDING 864..868 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P39986" FT BINDING 864 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P39986" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 899 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 905 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CARBOHYD 287 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 420 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT VAR_SEQ 1..860 FT /note="Missing (in isoform C)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_000433" FT VAR_SEQ 1..118 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_000434" FT VAR_SEQ 119..132 FT /note="HWSVHAHCALTCTP -> MEKWEELNSHQPGE (in isoform B)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_000435" FT VARIANT 349 FT /note="E -> K (found in a patient with intellectual FT disability; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28940097" FT /id="VAR_084651" FT MUTAGEN 533 FT /note="D->A: Loss of ATPase activity." FT /evidence="ECO:0000269|PubMed:32973005" FT CONFLICT 364 FT /note="I -> T (in Ref. 2; BAD18759)" FT /evidence="ECO:0000305" FT CONFLICT 501 FT /note="V -> D (in Ref. 2; BAD18759)" FT /evidence="ECO:0000305" FT CONFLICT 1150 FT /note="L -> P (in Ref. 2; BAD18759)" FT /evidence="ECO:0000305" SQ SEQUENCE 1204 AA; 132955 MW; 9DE335C025FBBA89 CRC64; MAAAAAVGNA VPCGARPCGV RPDGQPKPGP QPRALLAAGP ALIANGDELV AAVWPYRRLA LLRRLTVLPF AGLLYPAWLG AAAAGCWGWG SSWVQIPEAA LLVLATICLA HALTVLSGHW SVHAHCALTC TPEYDPSKAT FVKVVPTPNN GSTELVALHR NEGEDGLEVL SFEFQKIKYS YDALEKKQFL PVAFPVGNAF SYYQSNRGFQ EDSEIRAAEK KFGSNKAEMV VPDFSELFKE RATAPFFVFQ VFCVGLWCLD EYWYYSVFTL SMLVAFEASL VQQQMRNMSE IRKMGNKPHM IQVYRSRKWR PIASDEIVPG DIVSIGRSPQ ENLVPCDVLL LRGRCIVDEA MLTGESVPQM KEPIEDLSPD RVLDLQADSR LHVIFGGTKV VQHIPPQKAT TGLKPVDSGC VAYVLRTGFN TSQGKLLRTI LFGVKRVTAN NLETFIFILF LLVFAIAAAA YVWIEGTKDP SRNRYKLFLE CTLILTSVVP PELPIELSLA VNTSLIALAK LYMYCTEPFR IPFAGKVEVC CFDKTGTLTS DSLVVRGVAG LRDGKEVTPV SSIPVETHRA LASCHSLMQL DDGTLVGDPL EKAMLTAVDW TLTKDEKVFP RSIKTQGLKI HQRFHFASAL KRMSVLASYE KLGSTDLCYI AAVKGAPETL HSMFSQCPPD YHHIHTEISR EGARVLALGY KELGHLTHQQ AREVKREALE CSLKFVGFIV VSCPLKADSK AVIREIQNAS HRVVMITGDN PLTACHVAQE LHFIEKAHTL ILQPPSEKGR QCEWRSIDGS IVLPLARGSP KALALEYALC LTGDGLAHLQ ATDPQQLLRL IPHVQVFARV APKQKEFVIT SLKELGYVTL MCGDGTNDVG ALKHADVGVA LLANAPERVV ERRRRPRDSP TLSNSGIRAT SRTAKQRSGL PPSEEQPTSQ RDRLSQVLRD LEDESTPIVK LGDASIAAPF TSKLSSIQCI CHVIKQGRCT LVTTLQMFKI LALNALILAY SQSVLYLEGV KFSDFQATLQ GLLLAGCFLF ISRSKPLKTL SRERPLPNIF NLYTILTVML QFFVHFLSLV YLYREAQARS PEKQEQFVDL YKEFEPSLVN STVYIMAMAM QMATFAINYK GPPFMESLPE NKPLVWSLAV SLLAIIGLLL GSSPDFNSQF GLVDIPVEFK LVIAQVLLLD FCLALLADRV LQFFLGTPKL KVPS //