AT131_HUMAN
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 03-AUG-2022, entry version 188.
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, ECO:0000312|HGNC:HGNC:24215};
GN Synonyms=ATP13A {ECO:0000312|HGNC:HGNC:24215},
GN KIAA1825 {ECO:0000303|PubMed:11347906};
GN 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 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 [18]
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). Acts as a dislocase that mediates the ATP-
CC dependent extraction of mislocalized mitochondrial transmembrane
CC proteins from the endoplasmic reticulum membrane (PubMed:32973005).
CC Specifically binds mitochondrial tail-anchored transmembrane proteins:
CC has an atypically large substrate-binding pocket that recognizes and
CC binds moderately hydrophobic transmembranes with short hydrophilic
CC lumenal domains (PubMed:32973005). {ECO:0000269|PubMed:32973005}.
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/";
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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; 204.
DR IntAct; Q9HD20; 51.
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 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; Q9HD20; -.
DR PeptideAtlas; Q9HD20; -.
DR PRIDE; Q9HD20; -.
DR ProteomicsDB; 81811; -. [Q9HD20-1]
DR ProteomicsDB; 81812; -. [Q9HD20-2]
DR ProteomicsDB; 81813; -. [Q9HD20-3]
DR Antibodypedia; 28529; 84 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 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; RFAPKQK; -.
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; 110 hits in 1079 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 175 other tissues.
DR ExpressionAtlas; Q9HD20; baseline and differential.
DR Genevisible; Q9HD20; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0140567; F:transmembrane protein dislocase activity; IDA:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0140569; P:extraction of mislocalized protein from ER membrane; IDA:UniProtKB.
DR GO; GO:0034220; P: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 Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
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; unknown pathological 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
