AT10D_HUMAN
ID AT10D_HUMAN Reviewed; 1426 AA.
AC Q9P241; A2RRC8; D6REN2; Q8NC70; Q96SR3;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Phospholipid-transporting ATPase VD;
DE EC=7.6.2.1 {ECO:0000269|PubMed:30530492};
DE AltName: Full=ATPase class V type 10D;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP10D;
GN Name=ATP10D {ECO:0000303|PubMed:30530492}; Synonyms=ATPVD, KIAA1487;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Monocyte;
RX PubMed=12532265; DOI=10.1007/s00335-002-3032-3;
RA Flamant S., Pescher P., Lemercier B., Clement-Ziza M., Kepes F.,
RA Fellous M., Milon G., Marchal G., Besmond C.;
RT "Characterization of a putative type IV aminophospholipid transporter P-
RT type ATPase.";
RL Mamm. Genome 14:21-30(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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], AND VARIANTS ILE-43 AND ILE-1240.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 354-1426 (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 777-1426, AND VARIANT THR-1389.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21914794; DOI=10.1074/jbc.m111.281006;
RA Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M., Nakayama K.,
RA Shin H.W.;
RT "ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes
RT to the trans-Golgi network in a CDC50 protein-independent manner.";
RL J. Biol. Chem. 286:38159-38167(2011).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TMEM30A.
RX PubMed=25947375; DOI=10.1074/jbc.m115.655191;
RA Naito T., Takatsu H., Miyano R., Takada N., Nakayama K., Shin H.W.;
RT "Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and Is
RT Involved in Plasma Membrane Dynamics.";
RL J. Biol. Chem. 290:15004-15017(2015).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 110-ASN-TRP-111; GLU-215; GLN-381; VAL-382 AND 1148-LEU-ILE-1149.
RX PubMed=30530492; DOI=10.1074/jbc.ra118.005876;
RA Roland B.P., Naito T., Best J.T., Arnaiz-Yepez C., Takatsu H., Yu R.J.,
RA Shin H.W., Graham T.R.;
RT "Yeast and human P4-ATPases transport glycosphingolipids using conserved
RT structural motifs.";
RL J. Biol. Chem. 294:1794-1806(2019).
CC -!- FUNCTION: Catalytic component of a P4-ATPase flippase complex, which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC glucosylceramide (GlcCer) from the outer to the inner leaflet of the
CC plasma membrane. {ECO:0000269|PubMed:30530492}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:30530492};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP +
CC H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:66036, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:30530492};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037;
CC Evidence={ECO:0000305|PubMed:30530492};
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit ATP10A and an accessory beta subunit TMEM30A.
CC {ECO:0000269|PubMed:25947375}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21914794,
CC ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:30530492}; Multi-pass
CC membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25947375}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Exit from the endoplasmic
CC reticulum requires the presence of TMEM30A, but not that of TMEM30B.
CC {ECO:0000269|PubMed:25947375}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P241-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P241-2; Sequence=VSP_006954;
CC -!- TISSUE SPECIFICITY: Expressed in placenta and, to a lesser extent, in
CC kidney. {ECO:0000269|PubMed:12532265}.
CC -!- PTM: Autophosphorylated at the conserved aspartate of the P-type ATPase
CC signature sequence. {ECO:0000250|UniProtKB:O94823}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55221.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC11299.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ441078; CAD29577.1; -; mRNA.
DR EMBL; AC092597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471069; EAW93036.1; -; Genomic_DNA.
DR EMBL; BC131535; AAI31536.1; -; mRNA.
DR EMBL; AK027598; BAB55221.1; ALT_FRAME; mRNA.
DR EMBL; AK074930; BAC11299.1; ALT_INIT; mRNA.
DR EMBL; AB040920; BAA96011.1; -; mRNA.
DR CCDS; CCDS3476.1; -. [Q9P241-1]
DR RefSeq; NP_065186.3; NM_020453.3. [Q9P241-1]
DR AlphaFoldDB; Q9P241; -.
DR SMR; Q9P241; -.
DR BioGRID; 121446; 6.
DR ComplexPortal; CPX-6309; ATP10D-CDC50A P4-ATPase complex.
DR IntAct; Q9P241; 2.
DR STRING; 9606.ENSP00000273859; -.
DR TCDB; 3.A.3.8.25; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q9P241; -.
DR PhosphoSitePlus; Q9P241; -.
DR BioMuta; ATP10D; -.
DR DMDM; 300669610; -.
DR EPD; Q9P241; -.
DR jPOST; Q9P241; -.
DR MassIVE; Q9P241; -.
DR PaxDb; Q9P241; -.
DR PeptideAtlas; Q9P241; -.
DR PRIDE; Q9P241; -.
DR ProteomicsDB; 83721; -. [Q9P241-1]
DR ProteomicsDB; 83722; -. [Q9P241-2]
DR Antibodypedia; 23760; 41 antibodies from 13 providers.
DR DNASU; 57205; -.
DR Ensembl; ENST00000273859.8; ENSP00000273859.3; ENSG00000145246.14. [Q9P241-1]
DR GeneID; 57205; -.
DR KEGG; hsa:57205; -.
DR MANE-Select; ENST00000273859.8; ENSP00000273859.3; NM_020453.4; NP_065186.3.
DR UCSC; uc003gxk.2; human. [Q9P241-1]
DR CTD; 57205; -.
DR DisGeNET; 57205; -.
DR GeneCards; ATP10D; -.
DR HGNC; HGNC:13549; ATP10D.
DR HPA; ENSG00000145246; Low tissue specificity.
DR MIM; 619815; gene.
DR neXtProt; NX_Q9P241; -.
DR OpenTargets; ENSG00000145246; -.
DR PharmGKB; PA25100; -.
DR VEuPathDB; HostDB:ENSG00000145246; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000156728; -.
DR HOGENOM; CLU_000846_3_4_1; -.
DR InParanoid; Q9P241; -.
DR OMA; CETALDQ; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q9P241; -.
DR TreeFam; TF354252; -.
DR BRENDA; 7.6.2.1; 2681.
DR PathwayCommons; Q9P241; -.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; Q9P241; -.
DR BioGRID-ORCS; 57205; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; ATP10D; human.
DR GenomeRNAi; 57205; -.
DR Pharos; Q9P241; Tdark.
DR PRO; PR:Q9P241; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9P241; protein.
DR Bgee; ENSG00000145246; Expressed in corpus epididymis and 181 other tissues.
DR ExpressionAtlas; Q9P241; baseline and differential.
DR Genevisible; Q9P241; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0140351; F:glycosylceramide flippase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
DR GO; GO:0006812; P:cation transport; NAS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 2.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR030360; ATP10D.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PANTHER; PTHR24092:SF84; PTHR24092:SF84; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
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; TIGR01652; ATPase-Plipid; 2.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Endoplasmic reticulum;
KW Lipid transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1426
FT /note="Phospholipid-transporting ATPase VD"
FT /id="PRO_0000046382"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..121
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..365
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..1113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1114..1134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1135..1145
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1146..1166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1167..1195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1196..1216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1217..1224
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1225..1245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1246..1252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1253..1273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1274..1292
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1293..1313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1314..1426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 506..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 438
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 996..1003
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1056
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 1060
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 1364..1371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 553..747
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_006954"
FT VARIANT 43
FT /note="T -> I (in dbSNP:rs33995001)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048385"
FT VARIANT 171
FT /note="C -> R (in dbSNP:rs7683838)"
FT /id="VAR_048386"
FT VARIANT 320
FT /note="T -> I (in dbSNP:rs35596623)"
FT /id="VAR_048387"
FT VARIANT 337
FT /note="A -> T (in dbSNP:rs35012290)"
FT /id="VAR_048388"
FT VARIANT 511
FT /note="N -> S (in dbSNP:rs10003238)"
FT /id="VAR_048389"
FT VARIANT 522
FT /note="F -> L (in dbSNP:rs6843325)"
FT /id="VAR_048390"
FT VARIANT 716
FT /note="P -> T (in dbSNP:rs34208443)"
FT /id="VAR_048391"
FT VARIANT 720
FT /note="N -> S (in dbSNP:rs34169638)"
FT /id="VAR_048392"
FT VARIANT 959
FT /note="S -> N (in dbSNP:rs17462252)"
FT /id="VAR_048393"
FT VARIANT 1183
FT /note="R -> K (in dbSNP:rs16851681)"
FT /id="VAR_048394"
FT VARIANT 1240
FT /note="V -> I (in dbSNP:rs1058793)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_020187"
FT VARIANT 1389
FT /note="S -> T (in dbSNP:rs4145944)"
FT /evidence="ECO:0000269|PubMed:10819331"
FT /id="VAR_024371"
FT VARIANT 1392
FT /note="A -> G (in dbSNP:rs35375547)"
FT /id="VAR_048395"
FT MUTAGEN 110..111
FT /note="NW->QA: Impairs ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:30530492"
FT MUTAGEN 215
FT /note="E->Q: Impairs ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:30530492"
FT MUTAGEN 381
FT /note="Q->N: Impairs ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:30530492"
FT MUTAGEN 382
FT /note="V->T: Increases ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:30530492"
FT MUTAGEN 1148..1149
FT /note="LI->IT: Impairs ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:30530492"
FT CONFLICT 142
FT /note="D -> G (in Ref. 1; CAD29577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1002
FT /note="K -> R (in Ref. 1; CAD29577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1090
FT /note="S -> Y (in Ref. 1; CAD29577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1426 AA; 160274 MW; 97EE929F81AC59AE CRC64;
MTEALQWARY HWRRLIRGAT RDDDSGPYNY SSLLACGRKS SQTPKLSGRH RIVVPHIQPF
KDEYEKFSGA YVNNRIRTTK YTLLNFVPRN LFEQFHRAAN LYFLFLVVLN WVPLVEAFQK
EITMLPLVVV LTIIAIKDGL EDYRKYKIDK QINNLITKVY SRKEKKYIDR CWKDVTVGDF
IRLSCNEVIP ADMVLLFSTD PDGICHIETS GLDGESNLKQ RQVVRGYAEQ DSEVDPEKFS
SRIECESPNN DLSRFRGFLE HSNKERVGLS KENLLLRGCT IRNTEAVVGI VVYAGHETKA
MLNNSGPRYK RSKLERRANT DVLWCVMLLV IMCLTGAVGH GIWLSRYEKM HFFNVPEPDG
HIISPLLAGF YMFWTMIILL QVLIPISLYV SIEIVKLGQI YFIQSDVDFY NEKMDSIVQC
RALNIAEDLG QIQYLFSDKT GTLTENKMVF RRCSVAGFDY CHEENARRLE SYQEAVSEDE
DFIDTVSGSL SNMAKPRAPS CRTVHNGPLG NKPSNHLAGS SFTLGSGEGA SEVPHSRQAA
FSSPIETDVV PDTRLLDKFS QITPRLFMPL DETIQNPPME TLYIIDFFIA LAICNTVVVS
APNQPRQKIR HPSLGGLPIK SLEEIKSLFQ RWSVRRSSSP SLNSGKEPSS GVPNAFVSRL
PLFSRMKPAS PVEEEVSQVC ESPQCSSSSA CCTETEKQHG DAGLLNGKAE SLPGQPLACN
LCYEAESPDE AALVYAARAY QCTLRSRTPE QVMVDFAALG PLTFQLLHIL PFDSVRKRMS
VVVRHPLSNQ VVVYTKGADS VIMELLSVAS PDGASLEKQQ MIVREKTQKH LDDYAKQGLR
TLCIAKKVMS DTEYAEWLRN HFLAETSIDN REELLLESAM RLENKLTLLG ATGIEDRLQE
GVPESIEALH KAGIKIWMLT GDKQETAVNI AYACKLLEPD DKLFILNTQS KDACGMLMST
ILKELQKKTQ ALPEQVSLSE DLLQPPVPRD SGLRAGLIIT GKTLEFALQE SLQKQFLELT
SWCQAVVCCR ATPLQKSEVV KLVRSHLQVM TLAIGDGAND VSMIQVADIG IGVSGQEGMQ
AVMASDFAVS QFKHLSKLLL VHGHWCYTRL SNMILYFFYK NVAYVNLLFW YQFFCGFSGT
SMTDYWVLIF FNLLFTSAPP VIYGVLEKDV SAETLMQLPE LYRSGQKSEA YLPHTFWITL
LDAFYQSLVC FFVPYFTYQG SDTDIFAFGN PLNTAALFIV LLHLVIESKS LTWIHLLVII
GSILSYFLFA IVFGAMCVTC NPPSNPYWIM QEHMLDPVFY LVCILTTSIA LLPRFVYRVL
QGSLFPSPIL RAKHFDRLTP EERTKALKKW RGAGKMNQVT SKYANQSAGK SGRRPMPGPS
AVFAMKSASS CAIEQGNLSL CETALDQGYS ETKAFEMAGP SKGKES
