AT10D_MACFA
ID AT10D_MACFA Reviewed; 653 AA.
AC Q9GKS6;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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;
DE Flags: Fragment;
GN Name=ATP10D; ORFNames=QnpA-21212;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K., Kususda J.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9P241}.
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 -!- 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; AB052153; BAB19008.1; -; mRNA.
DR AlphaFoldDB; Q9GKS6; -.
DR SMR; Q9GKS6; -.
DR STRING; 9541.XP_005554880.1; -.
DR eggNOG; KOG0206; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0045332; P:phospholipid translocation; IEA:InterPro.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030360; ATP10D.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR PANTHER; PTHR24092:SF84; PTHR24092:SF84; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Endoplasmic reticulum; Lipid transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN <1..653
FT /note="Phospholipid-transporting ATPase VD"
FT /id="PRO_0000046383"
FT TOPO_DOM <1..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..407
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..487
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 538..555
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 259..266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT NON_TER 1
SQ SEQUENCE 653 AA; 73060 MW; FBE2C478DFB2B92D CRC64;
MACNLCYEAE SPDEAALVYA ARAYQCTLQS RTPEQVMVDF AASGPLTFQL LHILPFDSVR
KRMSVVVRHP LSNQVVVYTK GADSVIMELL SVASPDGAGP EKQQMIIREK TQRHLDDYAK
QGLRTLCIAK KVMSDTEYAE WLRNHFLAET SIDNREELLL ESAMRLENKL TLLGATGIED
RLQEGVPESI EALHKAGIKI WMLTGDKQET AVNIAYACML MSTILKELQK KTQALPEQVS
LSVDLHQPPV PQDSGLRAGL IITGKTLEFA LQESLQKQFL ELTSWCQTVV CCRATPLQKS
EVVKLVRSHL QVMTLAIGDG ANDVSMIQVA DIGIGVSGQE GMQAVMASDF AVSQFKHLSK
LLLVHGHWCY TRLSNMILYF FYKNVAYVNL LFWYQFFCGF SGTSMTDYWV LIFFNLLFTS
APPVIYGVLE KDVSAETLMQ LPELYKSGQK SEAYLPHTFW ITLLDAFYQS LVCFFVPYFT
YQGSDIDIFA FGNPLNTAAL FIILLHLIIE SKSLTWIHML VITGSILSYF LFAIVFGAMC
VTCNPPSNPY WIMQEHVLDP VFYLVCILTT CIALLPRFVY RGAGKMNQVT SNYANQSADK
SGRRPKPGPS TVFAMKSATS CAIEQGNLSL CETALDQGYS ETKAFEMARP CKD
