ATP9A_MOUSE
ID ATP9A_MOUSE Reviewed; 1047 AA.
AC O70228; Q8VDI5; Q922L9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Probable phospholipid-transporting ATPase IIA;
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:O75110};
DE AltName: Full=ATPase class II type 9A;
GN Name=Atp9a;
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 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].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 28-1047.
RX PubMed=9548971; DOI=10.1101/gr.8.4.354;
RA Halleck M.S., Pradhan D., Blackman C.F., Berkes C., Williamson P.L.,
RA Schlegel R.A.;
RT "Multiple members of a third subfamily of P-type ATPases identified by
RT genomic sequences and ESTs.";
RL Genome Res. 8:354-361(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, and Lung;
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).
CC -!- FUNCTION: Plays a role in regulating membrane trafficking of cargo
CC proteins, namely endosome to plasma membrane recycling and endosome to
CC trans-Golgi network retrograde transport. In complex with MON2 and
CC DOP1B, regulates SNX3 retromer-mediated endosomal sorting of WLS, a
CC transporter of Wnt morphogens in developing tissues. Participates in
CC the formation of endosomal carriers that direct WLS trafficking back to
CC Golgi, away from lysosomal degradation. Appears to be implicated in
CC intercellular communication by negatively regulating the release of
CC exosomes. The flippase activity towards membrane lipids and its role in
CC membrane asymmetry remains to be proved.
CC {ECO:0000250|UniProtKB:O75110}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:O75110};
CC -!- SUBUNIT: Heterotrimer with MON2 and DOP1B; this complex regulates SNX3-
CC retromer mediated endosomal sorting of WLS.
CC {ECO:0000250|UniProtKB:O75110}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:O75110}; Multi-pass membrane protein
CC {ECO:0000255}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:O75110}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:O75110}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O75110}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:O75110}. Note=Efficient exit
CC from the endoplasmic reticulum does not require TMEM30A, nor TMEM30B.
CC Transiently expressed in the plasma membrane.
CC {ECO:0000250|UniProtKB:O75110}.
CC -!- TISSUE SPECIFICITY: Found in most tissues except spleen. Most abundant
CC in brain. Also detected in fetal tissues.
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; AF152243; AAF08396.1; -; mRNA.
DR EMBL; BC021814; AAH21814.1; -; mRNA.
DR EMBL; BC006949; AAH06949.1; -; mRNA.
DR EMBL; AF011336; AAC05245.1; -; mRNA.
DR CCDS; CCDS38345.1; -.
DR PIR; T42229; T42229.
DR RefSeq; NP_056546.2; NM_015731.3.
DR AlphaFoldDB; O70228; -.
DR SMR; O70228; -.
DR BioGRID; 198271; 13.
DR IntAct; O70228; 1.
DR STRING; 10090.ENSMUSP00000104805; -.
DR iPTMnet; O70228; -.
DR PhosphoSitePlus; O70228; -.
DR SwissPalm; O70228; -.
DR MaxQB; O70228; -.
DR PaxDb; O70228; -.
DR PRIDE; O70228; -.
DR ProteomicsDB; 281820; -.
DR Antibodypedia; 28658; 68 antibodies from 16 providers.
DR DNASU; 11981; -.
DR Ensembl; ENSMUST00000029060; ENSMUSP00000029060; ENSMUSG00000027546.
DR Ensembl; ENSMUST00000178504; ENSMUSP00000136793; ENSMUSG00000027546.
DR GeneID; 11981; -.
DR KEGG; mmu:11981; -.
DR UCSC; uc008obc.1; mouse.
DR CTD; 10079; -.
DR MGI; MGI:1330826; Atp9a.
DR VEuPathDB; HostDB:ENSMUSG00000027546; -.
DR eggNOG; KOG0210; Eukaryota.
DR GeneTree; ENSGT00940000159181; -.
DR InParanoid; O70228; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; O70228; -.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 11981; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Atp9a; mouse.
DR PRO; PR:O70228; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O70228; protein.
DR Bgee; ENSMUSG00000027546; Expressed in perirhinal cortex and 260 other tissues.
DR ExpressionAtlas; O70228; baseline and differential.
DR Genevisible; O70228; MM.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
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:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:1903542; P:negative regulation of exosomal secretion; ISS:UniProtKB.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:2001135; P:regulation of endocytic recycling; ISS:UniProtKB.
DR GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030356; ATP9A.
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:SF49; PTHR24092:SF49; 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 Acetylation; ATP-binding; Cell membrane; Endosome; Golgi apparatus;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75110"
FT CHAIN 2..1047
FT /note="Probable phospholipid-transporting ATPase IIA"
FT /id="PRO_0000046376"
FT TOPO_DOM 2..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..332
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..841
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..862
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 863..874
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 875..893
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 894..923
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 924..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..949
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 950..972
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 973..978
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 979..999
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1000..1006
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1007..1030
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1031..1047
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 391
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 785
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 789
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:O75110"
FT CONFLICT 29
FT /note="R -> K (in Ref. 3; AAC05245)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="V -> I (in Ref. 3; AAC05245)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="V -> I (in Ref. 3; AAC05245)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="E -> K (in Ref. 1; AAF08396 and 3; AAC05245)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="D -> N (in Ref. 1; AAF08396 and 3; AAC05245)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="R -> K (in Ref. 3; AAC05245)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="E -> K (in Ref. 1; AAF08396 and 3; AAC05245)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="Q -> P (in Ref. 3; AAC05245)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="S -> C (in Ref. 3; AAC05245)"
FT /evidence="ECO:0000305"
FT CONFLICT 504..510
FT /note="ALVQWTE -> TLAGKEG (in Ref. 2; AAH21814)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="V -> I (in Ref. 3; AAC05245)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="D -> H (in Ref. 1; AAF08396)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="E -> D (in Ref. 3; AAC05245)"
FT /evidence="ECO:0000305"
FT CONFLICT 784
FT /note="G -> W (in Ref. 1; AAF08396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1047 AA; 118609 MW; 5CCFAB1A83A7B966 CRC64;
MTDSIPLQPV RHKKRVDSRP RAGCCEWLRC CGGGEPRPRT VWLGHPEKRD QRYPRNVINN
QKYNFFTFLP GVLFSQFRYF FNFYFLLLAC SQFVPEMRLG ALYTYWVPLG FVLAVTIIRE
AVEEIRCYVR DKEMNSQVYS RLTSRGTVKV KSSNIQVGDL ILVEKNQRVP ADMIFLRTSE
KNGSCFLRTD QLDGETDWKL RLPVACTQRL PTAADLLQIR SYVYAEEPNI DIHNFLGTFT
REDSDPPISE SLSIENTLWA GTVIASGTVV GVVLYTGREL RSVMNTSDPR SKIGLFDLEV
NCLTKILFGA LVVVSLVMVA LQHFAGRWYL QIIRFLLLFS NIIPISLRVN LDMGKIVYSW
VIRRDSKIPG TVVRSSTIPE QLGRISYLLT DKTGTLTQNE MVFKRLHLGT VAYGLDSMDE
VQSHIFSIYT QQSQDPPAQK GPTVTTKVRR TMSSRVHEAV KAIALCHNVT PVYESNGVTD
QAEAEKQFED SCRVYQASSP DEVALVQWTE SVGLTLVGRD QSSMQLRTPG DQVLNLTILQ
VFPFTYESKR MGIIVRDEST GEITFYMKGA DVVMAGIVQY NDWLEEECGN MAREGLRVLV
VAKKSLTEEQ YQDFEARYVQ AKLSVHDRSL KVATVIESLE MEMELLCLTG VEDQLQADVR
PTLETLRNAG IKVWMLTGDK LETATCTAKN AHLVTRNQDI HVFRLVTNRG EAHLELNAFR
RKHDCALVIS GDSLEVCLKY YEYEFMELAC QCPAVVCCRC APTQKAQIVR LLQERTGKLT
CAVGDGGNDV SMIQESDCGV GVEGKEGKQA SLAADFSITQ FKHLGRLLMV HGRNSYKRSA
ALSQFVIHRS LCISTMQAVF SSVFYFASVP LYQGFLIIGY STIYTMFPVF SLVLDKDVKS
EVAMLYPELY KDLLKGRPLS YKTFLIWVLI SIYQGSTIMY GALLLFESEF VHIVAISFTS
LILTELLMVA LTIQTWHWLM TVAELLSLAC YIASLVFLHE FIDVYFIATL SFLWKVSVIT
LVSCLPLYVL KYLRRRFSPP SYSKLTS
