AT10A_MOUSE
ID AT10A_MOUSE Reviewed; 1508 AA.
AC O54827; Q8R3B8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 4.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Phospholipid-transporting ATPase VA;
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:O60312};
DE AltName: Full=ATPase class V type 10A;
DE AltName: Full=P-locus fat-associated ATPase;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP10A;
GN Name=Atp10a; Synonyms=Atpc5, Pfatp;
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=Teratocarcinoma;
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 [MRNA] OF 16-435.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 155-1508.
RX PubMed=12105293; DOI=10.1038/oby.2002.94;
RA Dhar M., Hauser L., Johnson D.;
RT "An aminophospholipid translocase associated with body fat and type 2
RT diabetes phenotypes.";
RL Obes. Res. 10:695-702(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 840-1508.
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 TISSUE SPECIFICITY.
RX PubMed=11074018; DOI=10.1152/physiolgenomics.2000.4.1.93;
RA Dhar M., Webb L.S., Smith L., Hauser L., Johnson D., West D.B.;
RT "A novel ATPase on mouse chromosome 7 is a candidate gene for increased
RT body fat.";
RL Physiol. Genomics 4:93-100(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: 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. Initiates inward plasma membrane bending and
CC recruitment of Bin/amphiphysin/Rvs (BAR) domain-containing proteins
CC involved in membrane tubulation and cell trafficking. Facilitates
CC ITGB1/beta1 integrin endocytosis, delaying cell adhesion and cell
CC spreading on extracellular matrix. Has low flippase activity toward
CC glucosylceramide (GlcCer). {ECO:0000250|UniProtKB:O60312}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:O60312};
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:O60312};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584;
CC Evidence={ECO:0000250|UniProtKB:O60312};
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:0000250|UniProtKB:O60312};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037;
CC Evidence={ECO:0000250|UniProtKB:O60312};
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:0000250|UniProtKB:O60312}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60312};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O60312}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:O60312}. Note=Exit from the
CC endoplasmic reticulum requires the presence of TMEM30A, but not that of
CC TMEM30B. {ECO:0000250|UniProtKB:O60312}.
CC -!- TISSUE SPECIFICITY: Found in testis and in white adipose tissue. Also
CC detected in fetal tissues. {ECO:0000269|PubMed:11074018}.
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}.
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DR EMBL; AF156549; AAF09447.1; -; mRNA.
DR EMBL; AF011337; AAC02902.1; -; mRNA.
DR EMBL; AF372979; AAM20894.1; -; Genomic_DNA.
DR EMBL; BC025643; AAH25643.1; -; mRNA.
DR CCDS; CCDS39972.1; -.
DR RefSeq; NP_033858.2; NM_009728.2.
DR RefSeq; XP_006540643.1; XM_006540580.3.
DR RefSeq; XP_006540644.1; XM_006540581.3.
DR AlphaFoldDB; O54827; -.
DR SMR; O54827; -.
DR STRING; 10090.ENSMUSP00000129811; -.
DR iPTMnet; O54827; -.
DR PhosphoSitePlus; O54827; -.
DR EPD; O54827; -.
DR jPOST; O54827; -.
DR PaxDb; O54827; -.
DR PeptideAtlas; O54827; -.
DR PRIDE; O54827; -.
DR ProteomicsDB; 281865; -.
DR Antibodypedia; 58541; 22 antibodies from 12 providers.
DR DNASU; 11982; -.
DR Ensembl; ENSMUST00000168747; ENSMUSP00000129811; ENSMUSG00000025324.
DR GeneID; 11982; -.
DR KEGG; mmu:11982; -.
DR UCSC; uc009hef.2; mouse.
DR CTD; 57194; -.
DR MGI; MGI:1330809; Atp10a.
DR VEuPathDB; HostDB:ENSMUSG00000025324; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000157895; -.
DR HOGENOM; CLU_000846_3_4_1; -.
DR InParanoid; O54827; -.
DR OMA; QALRCGR; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; O54827; -.
DR TreeFam; TF354252; -.
DR BRENDA; 7.6.2.1; 3474.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 11982; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Atp10a; mouse.
DR PRO; PR:O54827; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O54827; protein.
DR Bgee; ENSMUSG00000025324; Expressed in cumulus cell and 218 other tissues.
DR ExpressionAtlas; O54827; baseline and differential.
DR Genevisible; O54827; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; 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: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:0140351; F:glycosylceramide flippase activity; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; ISS:UniProtKB.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; IEA:RHEA.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:1903527; P:positive regulation of membrane tubulation; ISS:UniProtKB.
DR Gene3D; 3.40.1110.10; -; 2.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR030357; ATP10A.
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:SF81; PTHR24092:SF81; 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 ATP-binding; Cell membrane; Endoplasmic reticulum; Lipid transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1508
FT /note="Phospholipid-transporting ATPase VA"
FT /id="PRO_0000046380"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..107
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..366
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..1101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1102..1122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1123..1134
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1135..1154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1155..1184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1185..1206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1207..1213
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1214..1236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1237..1242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1243..1263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1264..1281
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1282..1306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1307..1508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1481..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 431
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 1045
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 1049
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 16..22
FT /note="WRRPRRR -> KLAAAKK (in Ref. 2; AAC02902)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="T -> L (in Ref. 2; AAC02902)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="I -> V (in Ref. 3; AAM20894)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="E -> D (in Ref. 1; AAF09447)"
FT /evidence="ECO:0000305"
FT CONFLICT 840..842
FT /note="CWL -> TRP (in Ref. 4; AAH25643)"
FT /evidence="ECO:0000305"
FT CONFLICT 978
FT /note="T -> A (in Ref. 3; AAM20894)"
FT /evidence="ECO:0000305"
FT CONFLICT 1113
FT /note="F -> S (in Ref. 1; AAF09447)"
FT /evidence="ECO:0000305"
FT CONFLICT 1434
FT /note="T -> S (in Ref. 1; AAF09447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1508 AA; 168788 MW; B542F86C9CD80E5B CRC64;
MERELPAAEE SASSGWRRPR RRRWEGRTRT VRSNLLPPLG TEDSTIGAPK GERLLMRGCI
QHLADNRLKT TKYTLLSFLP KNLFEQFHRL ANVYFVFIAL LNFVPAVNAF QPGLALAPVL
FILAVTAIKD LWEDYSRHRS DHEINHLGCL VFSREEKKYV NRYWKEIRVG DFVRLCCNEI
IPADILLLSS SDPDGLCHIE TANLDGETNL KRRQVVRGFS ELVSEFNPLT FTSVIECEKP
NNDLSRFRGY IMHSNGEKAG LHKENLLLRG CTIRNTEAVA GIVIYAGHET KALLNNSGPR
YKRSQLERQM NCDVLWCVLL LVCISLFSAV GHGLWVRRYQ EKKALFDVPE SDGSSLSPAT
AAVYSFFTMI IVLQVLIPIS LYVSIEIVKV CQVYFINQDI ELYDEETDSQ LQCRALNITE
DLGQIKYIFS DKTGTLTENK MVFRRCTVSG IEYSHDANAQ RLARYQEADS EEEEVVSKVG
TISHRGSTGS HQSIWMTHKT QSIKSHRRTG SRAEAKRASM LSKHTAFSSP MEKDITPDPK
LLEKVSECDR FLAIARHQEH PLAHLSPELS DVFDFFIALT ICNTVVVTSP DQPRQKVRVR
FELKSPVKTI EDFLRRFTPS RLASGCSSIG NLSTSKSSHK SGSAFLPSLS QDSMLLGLEE
KLGQTAPSIA SNGYASQAGQ EESWASECTT DQKCPGEQRE QQEGELRYEA ESPDEAALVY
AARAYNCALV DRLHDQVSVE LPHLGRLTFE LLHTLGFDSI RKRMSVVIRH PLTDEINVYT
KGADSVVMDL LLPCSSDDAR GRHQKKIRSK TQNYLNLYAV EGLRTLCIAK RVLSKEEYAC
WLQSHIEAEA SVESREELLF QSAVRLETNL HLLGATGIED RLQEGVPETI AKLRQAGLQI
WVLTGDKQET AINIAYACKL LDHGEEVITL NADSQEACAA LLDQCLSYVQ SRNPRSTLQN
SESNLSVGFS FNPVSTSTDA SPSPSLVIDG RSLAYALEKS LEDKFLFLAK QCRSVLCCRS
TPLQKSMVVK LVRSKLKAMT LAIGDGANDV SMIQVADVGV GISGQEGMQA VMASDFAVPR
FRYLERLLIV HGHWCYSRLA NMVLYFFYKN TMFVGLLFWF QFYCGFSASA MIDQWYLIFF
NLLFSSLPQL VTGVLDKDVP ADMLLREPQL YKSGQNMEEY RPRAFWLNMV DAAFQSLVCF
FIPYLAYYDS DVDVFTWGTP VTAIALFTFL LHLGIETKTW TWLNWLACGF STFLFFSVAL
IYNTSCATCY PPSNPYWTMQ TLLGDPLFYL TCLIAPIAAL LPRLFFKALQ GSLFPTQLQL
GRQLAKKPLN KFSDPKETFA QGQPPGHSET ELSERKTMGP FETLPRDCAS QASQFTQQLT
CSPEASGEPS AVDTNMPLRE NTLLEGLGSQ ASGSSMPRGA ISEVCPGDSK RQSTSASQTA
RLSSLFHLPS FGSLNWISSL SLASGLGSVL QLSGSSLQMD KQDGEFLSNP PQPEQDLHSF
QGQVTGYL
