AT10D_MOUSE
ID AT10D_MOUSE Reviewed; 1416 AA.
AC Q8K2X1;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Phospholipid-transporting ATPase VD;
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:Q9P241};
DE AltName: Full=ATPase class V type 10D;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP10D;
GN Name=Atp10d;
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 {ECO:0000312|EMBL:AAH29551.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP ALA-700 AND LEU-716.
RC STRAIN=BALB/cJ, C57BL/6J, CAST/EiJ, MAI, MBT, and PWK; TISSUE=Monocyte;
RX PubMed=12532265; DOI=10.1007/s00335-002-3032-3;
RA Flamant S., Pescher P., Lemercier B., Clement-Ziza M., Kepes F.,
RA Fellous M., Milon G., Marchal G., Besmond C.;
RT "Characterization of a putative type IV aminophospholipid transporter P-
RT type ATPase.";
RL Mamm. Genome 14:21-30(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1079-1416 (ISOFORM 2).
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 INTERACTION WITH TMEM30A, AND TISSUE 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 glucosylceramide (GlcCer) from the outer to the inner leaflet of the
CC plasma membrane. {ECO:0000250|UniProtKB:Q9P241}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:Q9P241};
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:Q9P241};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037;
CC Evidence={ECO:0000250|UniProtKB:Q9P241};
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:0000269|PubMed:30018401}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9P241};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q9P241}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Exit from the endoplasmic reticulum requires the
CC presence of TMEM30A, but not that of TMEM30B.
CC {ECO:0000250|UniProtKB:Q9P241}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=Q8K2X1-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q8K2X1-2; Sequence=VSP_006959;
CC -!- TISSUE SPECIFICITY: Expressed at low amounts in liver, brain, testes,
CC and kidney (at protein level) (PubMed:30018401, PubMed:12532265).
CC Expressed in placenta (PubMed:12532265). {ECO:0000269|PubMed:12532265,
CC ECO:0000269|PubMed:30018401}.
CC -!- PTM: Autophosphorylated at the conserved aspartate of the P-type ATPase
CC signature sequence. {ECO:0000250|UniProtKB:O94823}.
CC -!- POLYMORPHISM: In strain C57BL/6, a polymorphism generates a premature
CC stop codon at position 764. {ECO:0000269|PubMed:12532265}.
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=AAH29551.1; Type=Frameshift; 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; AJ441079; CAD29578.1; -; mRNA.
DR EMBL; BC029551; AAH29551.1; ALT_FRAME; mRNA.
DR RefSeq; NP_700438.3; NM_153389.3.
DR AlphaFoldDB; Q8K2X1; -.
DR SMR; Q8K2X1; -.
DR iPTMnet; Q8K2X1; -.
DR PhosphoSitePlus; Q8K2X1; -.
DR jPOST; Q8K2X1; -.
DR MaxQB; Q8K2X1; -.
DR PRIDE; Q8K2X1; -.
DR ProteomicsDB; 281926; -. [Q8K2X1-1]
DR ProteomicsDB; 281927; -. [Q8K2X1-2]
DR DNASU; 231287; -.
DR GeneID; 231287; -.
DR KEGG; mmu:231287; -.
DR UCSC; uc008xrh.2; mouse. [Q8K2X1-1]
DR CTD; 57205; -.
DR MGI; MGI:2450125; Atp10d.
DR InParanoid; Q8K2X1; -.
DR PhylomeDB; Q8K2X1; -.
DR BRENDA; 7.6.2.1; 3474.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 231287; 0 hits in 17 CRISPR screens.
DR PRO; PR:Q8K2X1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K2X1; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
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; NAS:UniProtKB.
DR GO; GO:0006812; P:cation transport; NAS:UniProtKB.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 2.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR030360; ATP10D.
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:SF84; PTHR24092:SF84; 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 Alternative splicing; ATP-binding; Cell membrane; Endoplasmic reticulum;
KW Lipid transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1416
FT /note="Phospholipid-transporting ATPase VD"
FT /id="PRO_0000046384"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..120
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..365
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..1110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1111..1131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1132..1142
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1143..1163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1164..1192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1193..1213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1214..1221
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1222..1242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1243..1252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1253..1273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1274..1289
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1290..1310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1311..1416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 498..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 438
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 993..1000
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 1053
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 1057
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 1361..1368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1120..1135
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006959"
FT VARIANT 700
FT /note="V -> A (in strain: CAST, MAI, MBT and PWK)"
FT /evidence="ECO:0000269|PubMed:12532265"
FT VARIANT 716
FT /note="S -> L (in strain: CAST, MAI, MBT and PWK)"
FT /evidence="ECO:0000269|PubMed:12532265"
FT CONFLICT 1239
FT /note="L -> F (in Ref. 2; AAH29551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1416 AA; 158330 MW; 1799CCF062E22BB0 CRC64;
MTELLQWARH HWRRLSHGRA QGEDERPYNY ASLLACGGKS SRTPRPAGKH RVVIPHLQCF
KDEYERFSGT YVNNRIRTTK YTLLNFVPRN LFEQFHRAAN LYFLFLVVLN WVPLVEAFQK
EITMLPLVVV LTIIAIKDGL EDYRKYKIDK QINNLITKVY SRKEKKYIDC CWKNVTVGDF
IRLSCNEIIP ADMVLLFSTD PDGICHIETS GLDGESNLKQ RQVVRGYTEQ DSEVDPEKFS
SRIECESPNN DLSRFRGFLE HANKERVGLS KENLLLRGCT IRNTEAVVGI VVYAGHETKA
MLNNSGPRYK RSKLERRANT DVLWCVLLLI VMCLTGALGH GIWLSRYENM LFFNIPEPDG
RVISPVLTGF YVFWTMIILL QVLIPISLYV SIEIVKLGQI YFIQSDVDFY NEKMDSTIQC
RALNITEDLG QIQYLFSDKT GTLTENKMVF RRCSVAGFDY CHEENAKRLE SYQEAVSEEE
ECTDTLGGSL SNMARPRAQG CRTVPSGPLG KPSAQLSGST SAVGNGEGSG EVPHSRQAAF
SSPMETDVVP DTRLLDKFSQ LTPQLLTGLD GTAQSSPLET LYIMDFFIAL AICNTVVVSA
PNQPRQKIGL SSLGGMPIKS LEEIKNIFQK LSVRRSSSPS LASGKDSSSG TPCAFVSRIS
FFSRPKLSPP MEDESSQMDE IPQASNSACC TETEAQNRAV GLSVSSAEAL SGPPPSASNL
CYEAESPDEA ALVYAARAYR CTLQSRTPEQ VMVDFAALGS LTFQLLHILP FDSVRKRMSV
VVRHPLSKQV VVYTKGADSV IMELLSVAAS DGTNPEQQMI IRERTQRHLD EYAKRGLRTL
CVAKKVMSDT EYAEWLRNHF LAETSIDNRE ELLVESAMRL ENKLTLLGAT GIEDRLQEGV
PESIEALHQA GIKIWMLTGD KQETAVNIAY ACKLLEPDDK LFILNTQSQD ACGMLMSAIL
EELQKRAQVS PELASSRKNF PQPSDAQGQG RAGLVITGKT LEFALQESLQ RQFLELTAWC
QAVICCRATP LQKSEVVKLV RNHHHVLTLP IGDGANDVSM IQVADIGIGV SGQEGMQAVM
ASDFAISQFR HLSKLLLVHG HWCYTRLSNM ILYFFYKNVA YVNLLFWYQF FCGFSGTSMT
DYWVLIFFNL LFTSVPPIIY GVLEKDVSAE TLLQLPELYR SGQRSEEYLP LTFWITLLDA
FYQSLVCFFV PYFTYQGSDI DIFTFGNPLN TAALFIILLH LVIESKSLTW IHMLVTVGSI
LSYFFFALAF GALCVTCNPP SNPYGIMRKH MLDPVFYLVC VLTTFVALLP RFLYRVLQGS
VFPSPVLRAK YFDRLPPEER AEALKRWRGT AKVNHVASKH ASQSAAMSGR PTPGSSAVLA
MKSATVSTVE QSTRETALDR GCSEPGASKM TGSSAS
