AT11A_MOUSE
ID AT11A_MOUSE Reviewed; 1187 AA.
AC P98197; B2RS49;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Phospholipid-transporting ATPase IH;
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:P98196};
DE AltName: Full=ATPase IS;
DE AltName: Full=ATPase class VI type 11A;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP11A;
GN Name=Atp11a;
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].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=11015572; DOI=10.1152/physiolgenomics.1999.1.3.139;
RA Halleck M.S., Lawler J.F. Jr., Blackshaw S., Gao L., Nagarajan P.,
RA Hacker C., Pyle S., Newman J.T., Nakanishi Y., Ando H., Weinstock D.,
RA Williamson P.L., Schlegel R.A.;
RT "Differential expression of putative transbilayer amphipath transporters.";
RL Physiol. Genomics 1:139-150(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Testis;
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 [4]
RP FUNCTION, INTERACTION WITH TMEM30A, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29799007; DOI=10.1038/s41467-018-04436-w;
RA Tsuchiya M., Hara Y., Okuda M., Itoh K., Nishioka R., Shiomi A., Nagao K.,
RA Mori M., Mori Y., Ikenouchi J., Suzuki R., Tanaka M., Ohwada T., Aoki J.,
RA Kanagawa M., Toda T., Nagata Y., Matsuda R., Takayama Y., Tominaga M.,
RA Umeda M.;
RT "Cell surface flip-flop of phosphatidylserine is critical for PIEZO1-
RT mediated myotube formation.";
RL Nat. Commun. 9:2049-2049(2018).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TMEM30A, 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 aminophospholipids, phosphatidylserines (PS) and
CC phosphatidylethanolamines (PE), from the outer to the inner leaflet of
CC the plasma membrane (By similarity). Contributes to the maintenance of
CC membrane lipid asymmetry with a specific role in morphogenesis of
CC muscle cells. In myoblasts, mediates PS enrichment at the inner leaflet
CC of plasma membrane, triggering PIEZO1-dependent Ca2+ influx and Rho
CC GTPases signal transduction, subsequently leading to the assembly of
CC cortical actomyosin fibers and myotube formation (PubMed:29799007).
CC {ECO:0000250|UniProtKB:P98196, ECO:0000269|PubMed:29799007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:P98196};
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:P98196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000250|UniProtKB:P98196};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P98196};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000250|UniProtKB:P98196};
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit ATP11A and an accessory beta subunit TMEM30A.
CC {ECO:0000269|PubMed:29799007, ECO:0000269|PubMed:30018401}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29799007};
CC Multi-pass membrane protein {ECO:0000255}. Early endosome
CC {ECO:0000250|UniProtKB:P98196}. Recycling endosome
CC {ECO:0000250|UniProtKB:P98196}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P98196}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum
CC requires the presence of TMEM30A. {ECO:0000250|UniProtKB:P98196}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in myoblasts
CC (PubMed:29799007). Expressed in retina, brain, liver, testes and kidney
CC (at protein level) (PubMed:30018401). {ECO:0000269|PubMed:29799007,
CC ECO:0000269|PubMed:30018401}.
CC -!- PTM: Proteolytically cleaved by CASP3. {ECO:0000250|UniProtKB:P98196}.
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; AF156551; AAF09449.1; -; mRNA.
DR EMBL; BC138715; AAI38716.1; -; mRNA.
DR CCDS; CCDS40223.1; -.
DR RefSeq; NP_056619.1; NM_015804.3.
DR RefSeq; XP_011240370.1; XM_011242068.1.
DR AlphaFoldDB; P98197; -.
DR SMR; P98197; -.
DR STRING; 10090.ENSMUSP00000088779; -.
DR iPTMnet; P98197; -.
DR PhosphoSitePlus; P98197; -.
DR SwissPalm; P98197; -.
DR jPOST; P98197; -.
DR MaxQB; P98197; -.
DR PaxDb; P98197; -.
DR PRIDE; P98197; -.
DR ProteomicsDB; 281928; -.
DR Antibodypedia; 48747; 59 antibodies from 23 providers.
DR DNASU; 50770; -.
DR Ensembl; ENSMUST00000091237; ENSMUSP00000088779; ENSMUSG00000031441.
DR GeneID; 50770; -.
DR KEGG; mmu:50770; -.
DR UCSC; uc009kwg.1; mouse.
DR CTD; 23250; -.
DR MGI; MGI:1354735; Atp11a.
DR VEuPathDB; HostDB:ENSMUSG00000031441; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000157849; -.
DR HOGENOM; CLU_000846_3_2_1; -.
DR InParanoid; P98197; -.
DR OMA; DAQITEY; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; P98197; -.
DR TreeFam; TF326897; -.
DR BRENDA; 7.6.2.1; 3474.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 50770; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Atp11a; mouse.
DR PRO; PR:P98197; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P98197; protein.
DR Bgee; ENSMUSG00000031441; Expressed in lacrimal gland and 269 other tissues.
DR ExpressionAtlas; P98197; baseline and differential.
DR Genevisible; P98197; MM.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
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:0090555; F:phosphatidylethanolamine flippase activity; ISO:MGI.
DR GO; GO:0140346; F:phosphatidylserine flippase activity; ISO:MGI.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IMP:UniProtKB.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030361; ATP11A.
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:SF33; PTHR24092:SF33; 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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Endoplasmic reticulum; Endosome;
KW Lipid transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1187
FT /note="Phospholipid-transporting ATPase IH"
FT /id="PRO_0000046370"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..88
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..884
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 885..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..917
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 918..937
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 938..967
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 968..989
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 990..1003
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1004..1026
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1027..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="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1072..1096
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1097..1138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 414
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 828
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT SITE 457..458
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000250|UniProtKB:P98196"
FT SITE 493..494
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000250|UniProtKB:P98196"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98196"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 1158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
SQ SEQUENCE 1187 AA; 135502 MW; 999A8BE19E9296C1 CRC64;
MDCSLLRTLV RRYCAGEENW VDSRTIYVGH KEPPPGAEAY IPQRYPDNRI VSSKYTFWNF
IPKNLFEQFR RIANFYFLII FLVQLIIDTP TSPVTSGLPL FFVITVTAIK QGYEDWLRHK
ADNAMNQCPV HFIQHGKLVR KQSRKLRVGD IVMVKEDETF PCDLIFLSSN RADGTCHVTT
ASLDGESSHK THYAVQDTKG FHTEADVDSL HATIECEQPQ PDLYKFVGRI NVYNDLNDPV
VRPLGSENLL LRGATLKNTE KIFGVAIYTG METKMALNYQ SKSQKRSAVE KSMNTFLIVY
LCILVSKALI NTVLKYVWQS EPFRDEPWYN EKTESERQRN LFLRAFTDFL AFMVLFNYII
PVSMYVTVEM QKFLGSYFIT WDEDMFDEEM GEGPLVNTSD LNEELGQVEY IFTDKTGTLT
ENNMAFKECC IEGHVYVPHV ICNGQVLPDS SGIDMIDSSP GVCGREREEL FFRAICLCHT
VQVKDDHCGD DVDGPQKSPD AKSCVYISSS PDEVALVEGV QRLGFTYLRL KDNYMEILNR
ENDIERFELL EVLTFDSVRR RMSVIVKSTT GEIYLFCKGA DSSIFPRVIE GKVDQVRSRV
ERNAVEGLRT LCVAYKRLEP EQYEDACRLL QSAKVALQDR EKKLAEAYEQ IEKDLVLLGA
TAVEDRLQEK AADTIEALQK AGIKVWVLTG DKMETASATC YACKLFRRST QLLELTTKKL
EEQSLHDVLF DLSKTVLRCS GSMTRDSFSG LSTDMHDYGL IIDGAALSLI MKPREDGSSS
GNYRELFLEI CRNCSAVLCC RMAPLQKAQI VKLIKFSKEH PITLAIGDGA NDVSMILEAH
VGIGVIGKEG RQAARNSDYA IPKFKHLKKM LLVHGHFYYI RISELVQYFF YKNVCFIFPQ
FLYQFFCGFS QQTLYDTAYL TLYNISFTSL PILLYSLMEQ HVGIDVLKRD PTLYRDIAKN
ALLRWRVFIY WTFLGVFDAL VFFFGAYFIF ENTTVTINGQ MFGNWTFGTL VFTVMVLTVT
LKLALDTHYW TWINHFVIWG SLLFYIAFSL LWGGVIWPFL SYQRMYYVFI SMLSSGPAWL
GIILLVTVGL LPDVLKKVLC RQLWPTATER TQNIQHQDSI SEFTPLASLP SWGAQGSRLL
AAQCSSPSGR VVCSRWESEE CPVLPLHPGL PHKARYGCCR SSLEMPT
