AT8B2_HUMAN
ID AT8B2_HUMAN Reviewed; 1209 AA.
AC P98198; B4E3P4; Q6NT69; Q7Z486; Q96I43; Q96NQ7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Phospholipid-transporting ATPase ID;
DE EC=7.6.2.1 {ECO:0000269|PubMed:25315773};
DE AltName: Full=ATPase class I type 8B member 2;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP8B2;
GN Name=ATP8B2 {ECO:0000303|PubMed:12880872}; Synonyms=ATPID, KIAA1137;
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 3), ALTERNATIVE SPLICING (ISOFORM 4),
RP AND TISSUE SPECIFICITY.
RC TISSUE=Colon;
RX PubMed=12880872; DOI=10.1016/s1388-1981(03)00107-0;
RA Harris M.J., Arias I.M.;
RT "FIC1, a P-type ATPase linked to cholestatic liver disease, has homologues
RT (ATP8B2 and ATP8B3) expressed throughout the body.";
RL Biochim. Biophys. Acta 1633:127-131(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 671-1209 (ISOFORMS 1/3).
RC TISSUE=Cerebellum, and Uterus;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 447-1209 (ISOFORMS 1/3).
RC TISSUE=Lung, Mammary gland, and Muscle;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 277-1209 (ISOFORMS 1/3).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1112-1209 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP INTERACTION WITH TMEM30A, AND SUBCELLULAR LOCATION.
RX PubMed=20947505; DOI=10.1074/jbc.m110.139006;
RA van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A.,
RA Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.;
RT "Heteromeric interactions required for abundance and subcellular
RT localization of human CDC50 proteins and class 1 P4-ATPases.";
RL J. Biol. Chem. 285:40088-40096(2010).
RN [9]
RP INTERACTION WITH TMEM30A AND TMEM30B, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF ASP-411.
RX PubMed=20961850; DOI=10.1074/jbc.m110.139543;
RA Bryde S., Hennrich H., Verhulst P.M., Devaux P.F., Lenoir G.,
RA Holthuis J.C.;
RT "CDC50 proteins are critical components of the human class-1 P4-ATPase
RT transport machinery.";
RL J. Biol. Chem. 285:40562-40572(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1175, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLU-204.
RX PubMed=25315773; DOI=10.1074/jbc.m114.593012;
RA Takatsu H., Tanaka G., Segawa K., Suzuki J., Nagata S., Nakayama K.,
RA Shin H.W.;
RT "Phospholipid flippase activities and substrate specificities of human type
RT IV P-type ATPases localized to the plasma membrane.";
RL J. Biol. Chem. 289:33543-33556(2014).
RN [12]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Catalytic component of P4-ATPase flippase complex, which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC phosphatidylcholine (PC) from the outer to the inner leaflet of the
CC plasma membrane. May contribute to the maintenance of membrane lipid
CC asymmetry. {ECO:0000269|PubMed:25315773}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:25315773};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a
CC 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:25315773};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584;
CC Evidence={ECO:0000305|PubMed:25315773};
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit ATP8B2 and an accessory beta subunit TMEM30A or
CC TMEM30B. {ECO:0000269|PubMed:20961850}.
CC -!- INTERACTION:
CC P98198; Q9NV96: TMEM30A; NbExp=4; IntAct=EBI-9539266, EBI-2836942;
CC P98198; Q3MIR4: TMEM30B; NbExp=3; IntAct=EBI-9539266, EBI-9527107;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20947505,
CC ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:25315773}; Multi-pass
CC membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20961850}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum
CC requires the presence of TMEM30A or TMEM30B.
CC {ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:25315773}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P98198-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P98198-2; Sequence=VSP_007302, VSP_007303;
CC Name=3;
CC IsoId=P98198-3; Sequence=VSP_037147;
CC Name=4;
CC IsoId=P98198-4; Sequence=VSP_037148, VSP_037149, VSP_037150;
CC -!- TISSUE SPECIFICITY: Isoform 3 is ubiquitous, with highest expression in
CC aorta, cerebellum and uterus. {ECO:0000269|PubMed:12880872}.
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=AAH30288.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB70822.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAG65556.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY302537; AAQ19027.1; -; mRNA.
DR EMBL; AK054886; BAB70822.1; ALT_FRAME; mRNA.
DR EMBL; AK304806; BAG65556.1; ALT_INIT; mRNA.
DR EMBL; AL162591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53205.1; -; Genomic_DNA.
DR EMBL; BC007837; AAH07837.2; -; mRNA.
DR EMBL; BC030288; AAH30288.1; ALT_INIT; mRNA.
DR EMBL; BC069264; AAH69264.1; -; mRNA.
DR EMBL; AB032963; BAA86451.1; -; mRNA.
DR EMBL; AL137537; CAB70799.1; -; mRNA.
DR CCDS; CCDS41405.1; -. [P98198-4]
DR PIR; T46381; T46381.
DR RefSeq; NP_001005855.1; NM_001005855.1. [P98198-4]
DR RefSeq; NP_065185.1; NM_020452.3.
DR RefSeq; XP_005245412.1; XM_005245355.2.
DR AlphaFoldDB; P98198; -.
DR SMR; P98198; -.
DR BioGRID; 121445; 41.
DR ComplexPortal; CPX-6302; ATP8B2-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6303; ATP8B2-CDC50B P4-ATPase complex.
DR IntAct; P98198; 15.
DR STRING; 9606.ENSP00000357475; -.
DR iPTMnet; P98198; -.
DR PhosphoSitePlus; P98198; -.
DR BioMuta; ATP8B2; -.
DR DMDM; 30316371; -.
DR EPD; P98198; -.
DR jPOST; P98198; -.
DR MassIVE; P98198; -.
DR MaxQB; P98198; -.
DR PaxDb; P98198; -.
DR PeptideAtlas; P98198; -.
DR PRIDE; P98198; -.
DR ProteomicsDB; 57827; -. [P98198-1]
DR ProteomicsDB; 57828; -. [P98198-2]
DR ProteomicsDB; 57829; -. [P98198-3]
DR ProteomicsDB; 57830; -. [P98198-4]
DR Antibodypedia; 34152; 92 antibodies from 16 providers.
DR DNASU; 57198; -.
DR Ensembl; ENST00000368487.7; ENSP00000357472.3; ENSG00000143515.19. [P98198-4]
DR Ensembl; ENST00000672630.1; ENSP00000500034.1; ENSG00000143515.19. [P98198-3]
DR GeneID; 57198; -.
DR KEGG; hsa:57198; -.
DR UCSC; uc001few.4; human. [P98198-1]
DR CTD; 57198; -.
DR DisGeNET; 57198; -.
DR GeneCards; ATP8B2; -.
DR HGNC; HGNC:13534; ATP8B2.
DR HPA; ENSG00000143515; Low tissue specificity.
DR MIM; 605867; gene.
DR neXtProt; NX_P98198; -.
DR OpenTargets; ENSG00000143515; -.
DR PharmGKB; PA25167; -.
DR VEuPathDB; HostDB:ENSG00000143515; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000160804; -.
DR HOGENOM; CLU_000846_8_4_1; -.
DR InParanoid; P98198; -.
DR PhylomeDB; P98198; -.
DR TreeFam; TF300654; -.
DR BRENDA; 7.6.2.1; 2681.
DR PathwayCommons; P98198; -.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; P98198; -.
DR BioGRID-ORCS; 57198; 15 hits in 1075 CRISPR screens.
DR ChiTaRS; ATP8B2; human.
DR GenomeRNAi; 57198; -.
DR Pharos; P98198; Tbio.
DR PRO; PR:P98198; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P98198; protein.
DR Bgee; ENSG00000143515; Expressed in mucosa of stomach and 168 other tissues.
DR ExpressionAtlas; P98198; baseline and differential.
DR Genevisible; P98198; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; IDA:UniProtKB.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; IEA:RHEA.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
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; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030347; ATP8B2.
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:SF46; PTHR24092:SF46; 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; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
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 Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1209
FT /note="Phospholipid-transporting ATPase ID"
FT /id="PRO_0000046365"
FT TOPO_DOM 1..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..92
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..346
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..889
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 890..910
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 911..922
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..972
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..994
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 995..1008
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1009..1031
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1032..1037
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1059..1078
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1079..1103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1104..1209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 833
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 837
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..29
FT /note="MTVPKEMPEKWARAQAPPSWSRKKPSWGT -> MDTLRAVPLFSISGLFSFP
FT YRVSHGIAGILLGEMAVCAKKRPP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12880872"
FT /id="VSP_037147"
FT VAR_SEQ 1..29
FT /note="MTVPKEMPEKWARAQAPPSWSRKKPSWGT -> MAVCAKKRPP (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037148"
FT VAR_SEQ 364..406
FT /note="SVEVIRLGHSYFINWDKKMFCMKKRTPAEARTTTLNEELGQVE -> RYVPS
FT LTWGLSRESGGPIELFFSMKMKSLRSNEKSSSSCTVNI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037149"
FT VAR_SEQ 407..1209
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037150"
FT VAR_SEQ 434..461
FT /note="GDVFDVLGHKAELGERPEPVDFSFNPLA -> VGSEGPRRKGPSWPGTVAHA
FT YSHSTLGG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007302"
FT VAR_SEQ 462..1209
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007303"
FT MUTAGEN 204
FT /note="E->Q: Impairs ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:25315773"
FT MUTAGEN 411
FT /note="D->N: Impairs ATPase activity."
FT /evidence="ECO:0000269|PubMed:20961850"
FT CONFLICT 834
FT /note="G -> E (in Ref. 5; BAA86451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1209 AA; 137440 MW; D905A97E9D9724BD CRC64;
MTVPKEMPEK WARAQAPPSW SRKKPSWGTE EERRARANDR EYNEKFQYAS NCIKTSKYNI
LTFLPVNLFE QFQEVANTYF LFLLILQLIP QISSLSWFTT IVPLVLVLTI TAVKDATDDY
FRHKSDNQVN NRQSQVLING ILQQEQWMNV CVGDIIKLEN NQFVAADLLL LSSSEPHGLC
YIETAELDGE TNMKVRQAIP VTSELGDISK LAKFDGEVIC EPPNNKLDKF SGTLYWKENK
FPLSNQNMLL RGCVLRNTEW CFGLVIFAGP DTKLMQNSGR TKFKRTSIDR LMNTLVLWIF
GFLVCMGVIL AIGNAIWEHE VGMRFQVYLP WDEAVDSAFF SGFLSFWSYI IILNTVVPIS
LYVSVEVIRL GHSYFINWDK KMFCMKKRTP AEARTTTLNE ELGQVEYIFS DKTGTLTQNI
MVFNKCSING HSYGDVFDVL GHKAELGERP EPVDFSFNPL ADKKFLFWDP SLLEAVKIGD
PHTHEFFRLL SLCHTVMSEE KNEGELYYKA QSPDEGALVT AARNFGFVFR SRTPKTITVH
EMGTAITYQL LAILDFNNIR KRMSVIVRNP EGKIRLYCKG ADTILLDRLH HSTQELLNTT
MDHLNEYAGE GLRTLVLAYK DLDEEYYEEW AERRLQASLA QDSREDRLAS IYEEVENNMM
LLGATAIEDK LQQGVPETIA LLTLANIKIW VLTGDKQETA VNIGYSCKML TDDMTEVFIV
TGHTVLEVRE ELRKAREKMM DSSRSVGNGF TYQDKLSSSK LTSVLEAVAG EYALVINGHS
LAHALEADME LEFLETACAC KAVICCRVTP LQKAQVVELV KKYKKAVTLA IGDGANDVSM
IKTAHIGVGI SGQEGIQAVL ASDYSFSQFK FLQRLLLVHG RWSYLRMCKF LCYFFYKNFA
FTMVHFWFGF FCGFSAQTVY DQYFITLYNI VYTSLPVLAM GVFDQDVPEQ RSMEYPKLYE
PGQLNLLFNK REFFICIAQG IYTSVLMFFI PYGVFADATR DDGTQLADYQ SFAVTVATSL
VIVVSVQIGL DTGYWTAINH FFIWGSLAVY FAILFAMHSN GLFDMFPNQF RFVGNAQNTL
AQPTVWLTIV LTTVVCIMPV VAFRFLRLNL KPDLSDTVRY TQLVRKKQKA QHRCMRRVGR
TGSRRSGYAF SHQEGFGELI MSGKNMRLSS LALSSFTTRS SSSWIESLRR KKSDSASSPS
GGADKPLKG
