AT8B1_MOUSE
ID AT8B1_MOUSE Reviewed; 1251 AA.
AC Q148W0; Q3U010; Q6R964;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Phospholipid-transporting ATPase IC {ECO:0000305};
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:O43520};
DE AltName: Full=ATPase class I type 8B member 1;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP8B1;
GN Name=Atp8b1 {ECO:0000312|MGI:MGI:1859665};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=129;
RX PubMed=14976163; DOI=10.1093/hmg/ddh100;
RA Pawlikowska L., Groen A., Eppens E.F., Kunne C., Ottenhoff R., Looije N.,
RA Knisely A.S., Killeen N.P., Bull L.N., Elferink R.P.J.O., Freimer N.B.;
RT "A mouse genetic model for familial cholestasis caused by ATP8B1 mutations
RT reveals perturbed bile salt homeostasis but no impairment in bile
RT secretion.";
RL Hum. Mol. Genet. 13:881-892(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF GLY-308.
RX PubMed=19478059; DOI=10.1073/pnas.0807919106;
RA Stapelbroek J.M., Peters T.A., van Beurden D.H., Curfs J.H., Joosten A.,
RA Beynon A.J., van Leeuwen B.M., van der Velden L.M., Bull L.,
RA Oude Elferink R.P., van Zanten B.A., Klomp L.W., Houwen R.H.;
RT "ATP8B1 is essential for maintaining normal hearing.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9709-9714(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20852622; DOI=10.1038/nm.2213;
RA Ray N.B., Durairaj L., Chen B.B., McVerry B.J., Ryan A.J., Donahoe M.,
RA Waltenbaugh A.K., O'Donnell C.P., Henderson F.C., Etscheidt C.A.,
RA McCoy D.M., Agassandian M., Hayes-Rowan E.C., Coon T.A., Butler P.L.,
RA Gakhar L., Mathur S.N., Sieren J.C., Tyurina Y.Y., Kagan V.E., McLennan G.,
RA Mallampalli R.K.;
RT "Dynamic regulation of cardiolipin by the lipid pump Atp8b1 determines the
RT severity of lung injury in experimental pneumonia.";
RL Nat. Med. 16:1120-1127(2010).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20126555; DOI=10.1371/journal.pone.0008984;
RA Shah S., Sanford U.R., Vargas J.C., Xu H., Groen A., Paulusma C.C.,
RA Grenert J.P., Pawlikowska L., Sen S., Elferink R.P., Bull L.N.;
RT "Strain background modifies phenotypes in the ATP8B1-deficient mouse.";
RL PLoS ONE 5:e8984-e8984(2010).
RN [9]
RP FUNCTION.
RX PubMed=21820390; DOI=10.1053/j.gastro.2011.07.042;
RA Groen A., Romero M.R., Kunne C., Hoosdally S.J., Dixon P.H., Wooding C.,
RA Williamson C., Seppen J., Van den Oever K., Mok K.S., Paulusma C.C.,
RA Linton K.J., Oude Elferink R.P.;
RT "Complementary functions of the flippase ATP8B1 and the floppase ABCB4 in
RT maintaining canalicular membrane integrity.";
RL Gastroenterology 141:1927-1937(2011).
RN [10]
RP FUNCTION.
RX PubMed=21475228; DOI=10.1038/nm0411-413a;
RA Paulusma C.C., Houwen R.H., Williamson P.L.;
RT "The flip side of cardiolipin import.";
RL Nat. Med. 17:413-413(2011).
RN [11]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=26416959; DOI=10.1083/jcb.201505118;
RA Bruurs L.J., Donker L., Zwakenberg S., Zwartkruis F.J., Begthel H.,
RA Knisely A.S., Posthuma G., van de Graaf S.F., Paulusma C.C., Bos J.L.;
RT "ATP8B1-mediated spatial organization of Cdc42 signaling maintains
RT singularity during enterocyte polarization.";
RL J. Cell Biol. 210:1055-1063(2015).
RN [12]
RP INTERACTION WITH TMEM30A, IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE
RP SPECIFICITY.
RX PubMed=30018401; DOI=10.1038/s41598-018-29108-z;
RA Wang J., Molday L.L., Hii T., Coleman J.A., Wen T., Andersen J.P.,
RA Molday R.S.;
RT "Proteomic Analysis and Functional Characterization of P4-ATPase
RT Phospholipid Flippases from Murine Tissues.";
RL Sci. Rep. 8:10795-10795(2018).
CC -!- FUNCTION: Catalytic component of a P4-ATPase flippase complex which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC phospholipids, in particular phosphatidylcholines (PC), from the outer
CC to the inner leaflet of the plasma membrane (By similarity). May
CC participate in the establishment of the canalicular membrane integrity
CC by ensuring asymmetric distribution of phospholipids in the canicular
CC membrane (PubMed:21820390). Thus may have a role in the regulation of
CC bile acids transport into the canaliculus, uptake of bile acids from
CC intestinal contents into intestinal mucosa or both and protect
CC hepatocytes from bile salts (PubMed:14976163, PubMed:21820390,
CC PubMed:20126555). Involved in the microvillus formation in polarized
CC epithelial cells; the function seems to be independent from its
CC flippase activity (By similarity). Participates in correct apical
CC membrane localization of CDC42, CFTR and SLC10A2 (PubMed:26416959).
CC Enables CDC42 clustering at the apical membrane during enterocyte
CC polarization through the interaction between CDC42 polybasic region and
CC negatively charged membrane lipids provided by ATP8B1
CC (PubMed:26416959). Together with TMEM30A is involved in uptake of the
CC synthetic drug alkylphospholipid perifosine (By similarity). Required
CC for the preservation of cochlear hair cells in the inner ear
CC (PubMed:19478059). According PubMed:20852622 is proposed to act as
CC cardiolipin transporter during inflammatory injury; the function is
CC questioned by PubMed:21475228 (PubMed:20852622, PubMed:21475228).
CC {ECO:0000250|UniProtKB:O43520, ECO:0000269|PubMed:14976163,
CC ECO:0000269|PubMed:19478059, ECO:0000269|PubMed:20126555,
CC ECO:0000269|PubMed:20852622, ECO:0000269|PubMed:21475228,
CC ECO:0000269|PubMed:21820390, ECO:0000269|PubMed:26416959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:O43520};
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:0000250|UniProtKB:O43520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584;
CC Evidence={ECO:0000250|UniProtKB:O43520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O43520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000250|UniProtKB:O43520};
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit ATP8B1 and an accessory beta subunit TMEM30A
CC (PubMed:30018401). The flippase ATP8B1:TMEM30A complex can form an
CC intermediate phosphoenzyme in vitro. Also interacts with beta subunit
CC TMEM30B. {ECO:0000250|UniProtKB:O43520, ECO:0000269|PubMed:30018401}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20852622};
CC Multi-pass membrane protein {ECO:0000269|PubMed:20852622}. Apical cell
CC membrane {ECO:0000269|PubMed:26416959}. Cell projection, stereocilium
CC {ECO:0000269|PubMed:20852622}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O43520}. Golgi apparatus
CC {ECO:0000250|UniProtKB:O43520}. Note=Exit from the endoplasmic
CC reticulum requires the presence of TMEM30A or TMEM30B. Localizes to
CC apical membranes in epithelial cells. {ECO:0000250|UniProtKB:O43520}.
CC -!- TISSUE SPECIFICITY: Hepatocytes, bile duct, intestinal epithelial cells
CC (cholangiocytes and ileocytes), and pancreatic acinar cells.
CC {ECO:0000269|PubMed:14976163, ECO:0000269|PubMed:30018401}.
CC -!- DISRUPTION PHENOTYPE: Mice have unimpaired bile secretion, and no liver
CC damage, but show mild abnormalities including depressed weight at
CC weaning and elevated serum bile salt levels. Do not suffer from
CC jaundice or diarrhea and have normal serum bilirubin levels and normal
CC liver enzyme activities, except for mildly elevated serum AST
CC (aspartate aminotransferase) activity. Display unimpaired transhepatic
CC bile salt transport and are resistant to bile salt-induced cholestasis.
CC Upon bile salt feeding, demonstrate serum bile salt accumulation,
CC hepatic injury and expansion of the systemic bile salt pool and this
CC failure of bile salt homeostasis occurs in the absence of any defect in
CC hepatic bile secretion (PubMed:14976163). Mutant mice with B6
CC background show greater abnormalities than 129 and/or F1 background
CC ones. Pups of B6 background gain less weight. In adult B6 background
CC has lower serum cholesterol levels, higher serum alkaline phosphatase
CC levels, and larger livers. After challenge with cholate-supplemented
CC diet, these mice exhibit higher serum alkaline phosphatase and
CC bilirubin levels, greater weight loss and larger livers
CC (PubMed:20126555). {ECO:0000269|PubMed:14976163,
CC ECO:0000269|PubMed:20126555}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
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DR EMBL; AY506548; AAR90342.1; -; mRNA.
DR EMBL; AK157316; BAE34046.1; -; mRNA.
DR EMBL; BC117946; AAI17947.1; -; mRNA.
DR CCDS; CCDS29304.1; -.
DR RefSeq; NP_001001488.2; NM_001001488.3.
DR AlphaFoldDB; Q148W0; -.
DR SMR; Q148W0; -.
DR BioGRID; 207714; 1.
DR STRING; 10090.ENSMUSP00000025482; -.
DR iPTMnet; Q148W0; -.
DR PhosphoSitePlus; Q148W0; -.
DR MaxQB; Q148W0; -.
DR PaxDb; Q148W0; -.
DR PeptideAtlas; Q148W0; -.
DR PRIDE; Q148W0; -.
DR ProteomicsDB; 265134; -.
DR Antibodypedia; 9722; 48 antibodies from 12 providers.
DR DNASU; 54670; -.
DR Ensembl; ENSMUST00000025482; ENSMUSP00000025482; ENSMUSG00000039529.
DR GeneID; 54670; -.
DR KEGG; mmu:54670; -.
DR UCSC; uc008fem.1; mouse.
DR CTD; 5205; -.
DR MGI; MGI:1859665; Atp8b1.
DR VEuPathDB; HostDB:ENSMUSG00000039529; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000158002; -.
DR HOGENOM; CLU_000846_3_2_1; -.
DR InParanoid; Q148W0; -.
DR OMA; VQEPFFP; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q148W0; -.
DR TreeFam; TF300654; -.
DR BRENDA; 7.6.2.1; 3474.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 54670; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q148W0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q148W0; protein.
DR Bgee; ENSMUSG00000039529; Expressed in epithelium of small intestine and 145 other tissues.
DR ExpressionAtlas; Q148W0; baseline and differential.
DR Genevisible; Q148W0; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0032420; C:stereocilium; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0015247; F:aminophospholipid flippase activity; IDA:BHF-UCL.
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:1901612; F:cardiolipin binding; IDA:UniProtKB.
DR GO; GO:0005319; F:lipid transporter activity; IMP:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; ISO:MGI.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; IEA:RHEA.
DR GO; GO:0140346; F:phosphatidylserine flippase activity; ISS:UniProtKB.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR GO; GO:0015917; P:aminophospholipid transport; IDA:BHF-UCL.
DR GO; GO:0045176; P:apical protein localization; ISS:UniProtKB.
DR GO; GO:0015721; P:bile acid and bile salt transport; IMP:UniProtKB.
DR GO; GO:0008206; P:bile acid metabolic process; IMP:MGI.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0060119; P:inner ear receptor cell development; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0015711; P:organic anion transport; IMP:UniProtKB.
DR GO; GO:0045332; P:phospholipid translocation; ISO:MGI.
DR GO; GO:2001225; P:regulation of chloride transport; ISS:UniProtKB.
DR GO; GO:0032534; P:regulation of microvillus assembly; ISO:MGI.
DR GO; GO:1903729; P:regulation of plasma membrane organization; IMP:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0021650; P:vestibulocochlear nerve formation; IMP:UniProtKB.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; ISO:MGI.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030346; ATP8B1.
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:SF48; PTHR24092:SF48; 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 ATP-binding; Cell membrane; Cell projection; Endoplasmic reticulum;
KW Golgi apparatus; Hearing; Lipid transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1251
FT /note="Phospholipid-transporting ATPase IC"
FT /id="PRO_0000370862"
FT TOPO_DOM 1..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..144
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..385
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..952
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 953..973
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 974..982
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 983..1003
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1004..1032
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1033..1053
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1054..1071
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1072..1092
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1093..1094
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1095..1115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1116..1142
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1143..1163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1164..1251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..38
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 454
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 893
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 897
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 1223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MUTAGEN 308
FT /note="G->V: Markly decreased expression, hearing loss
FT associated with degeneration of cochlear hair cells and
FT spiral ganglion cells."
FT /evidence="ECO:0000269|PubMed:19478059"
FT CONFLICT 104
FT /note="G -> A (in Ref. 1; AAR90342)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="L -> I (in Ref. 1; AAR90342)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="T -> M (in Ref. 2; BAE34046)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="N -> S (in Ref. 1; AAR90342)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="R -> M (in Ref. 1; AAR90342)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="L -> P (in Ref. 2; BAE34046)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="N -> Y (in Ref. 2; BAE34046)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="T -> A (in Ref. 3; AAI17947)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="N -> K (in Ref. 3; AAI17947)"
FT /evidence="ECO:0000305"
FT CONFLICT 893
FT /note="D -> E (in Ref. 2; BAE34046)"
FT /evidence="ECO:0000305"
FT CONFLICT 1226
FT /note="S -> C (in Ref. 2; BAE34046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1251 AA; 143798 MW; 394920189075875D CRC64;
MSTERDSETT FDEESQPNDE VVPYSDDETE DELEDQGSTV EPEQNRVNRE AEKKRETFRK
DCTWQVKAND RKFHEQPHFM NTKFFCIKES KYASNAIKTY KYNGFTFLPM NLFEQFKRAA
NFYFLILLIL QAIPQISTLA WYTTLVPLLL VLGITAIKDL VDDVARHKMD KEINNRTCEV
IKDGRFKIIK WKDIQVGDVI RLKKNDFIPA DILLLSSSEP NSLCYVETAE LDGETNLKFK
MALEITDQYL QIEDNLATFD GFIECEEPNN RLDKFTGTLF WKNQSFPLDA DKILLRGCVI
RNTDVCHGLV IFAGADTKIM KNSGKTRFKR TKIDYLMNYM VYTIFIVLIL VSAGLAIGHA
YWEAQVGNYS WYLYDGENAT PSYRGFLNFW GYIIVLNTMV PISLYVSVEV IRLGQSHFIN
WDLQMYYAEK DTPAKARTTT LNEQLGQIHY IFSDKTGTLT QNIMTFKKCC INGTIYGDHR
DASQHSHSKI ELVDFSWNTF ADGKLAFYDH YLIEQIQSGK EPEVRQFFFL LSICHTVMVD
RIDGQINYQA ASPDEGALVN AARNFGFAFL ARTQNTITVS ELGSERTYNV LAILDFNSDR
KRMSIIVRTP EGSIRLYCKG ADTVIYERLH RMNPTKQETQ DALDIFASET LRTLCLCYKE
IEEKEFTEWN NKFMAASVAS SNRDEALDKV YEEIEKDLIL LGATAIEDKL QDGVPETISK
LAKADIKIWV LTGDKKETAE NIGFACELLT EDTTICYGED INSLLHTRME NQRNRGGVSA
KFAPPVYEPF FPPGENRALI ITGSWLNEIL LEKKTKRSKI LKLKFPRTEE ERRMRSQSRR
RLEEKKEQRQ KNFVDLACEC SAVICCRVTP KQKAMVVDLV KRYKKAITLA IGDGANDVNM
IKTAHIGVGI SGQEGMQAVM SSDYSFAQFR YLQRLLLVHG RWSYIRMCKF LRYFFYKNFA
FTLVHFWYSF FNGYSAQTAY EDWFITLYNV LYSSLPVLLM GLLDQDVSDK LSLRFPGLYV
VGQRDLLFNY KRFFVSLLHG VLTSMVLFFI PLGAYLQTVG QDGEAPSDYQ SFAVTVASAL
VITVNFQIGL DTSYWTFVNA FSIFGSIALY FGIMFDFHSA GIHVLFPSAF QFTGTASNAL
RQPYIWLTII LTVAVCLLPV VAIRFLSMTI WPSESDKIQK HRKRLKAEEQ WKRRQSVFRR
GVSSRRSAYA FSHQRGYADL ISSGRSIRKK RSPLDAIIAD GTAEYRRTVE S
