ID A0A6I8RU97_XENTR Unreviewed; 1373 AA.
AC A0A6I8RU97;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=atp10d {ECO:0000313|Ensembl:ENSXETP00000088455,
GN ECO:0000313|RefSeq:XP_012818017.1,
GN ECO:0000313|Xenbase:XB-GENE-1000388};
GN Synonyms=atpvd {ECO:0000313|RefSeq:XP_012818017.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000088455};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000088455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000088455};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000088455}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2020) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_012818017.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_012818017.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_012818017.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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DR RefSeq; XP_012818017.1; XM_012962563.3.
DR Ensembl; ENSXETT00000076780; ENSXETP00000088455; ENSXETG00000009839.
DR GeneID; 549378; -.
DR CTD; 57205; -.
DR Xenbase; XB-GENE-1000388; atp10d.
DR OMA; FKVAREC; -.
DR OrthoDB; 275833at2759; -.
DR Reactome; R-XTR-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000008143; Chromosome 1.
DR Bgee; ENSXETG00000009839; Expressed in 4-cell stage embryo and 12 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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 NCBIfam; TIGR01652; ATPase-Plipid; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR24092:SF84; PHOSPHOLIPID-TRANSPORTING ATPASE VD; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 124..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 321..345
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 365..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1091..1110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1122..1143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1173..1194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1200..1223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1230..1255
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1275..1294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 64..123
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1059..1304
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 508..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1373 AA; 154634 MW; E23E1895FD07FAD7 CRC64;
MADPFQWVRY RWQRFMSGDS RNRDLEDSST SRKLLGFNKS NGTSSNSTKH RVVIPCLGQF
KEEYEKLTKA YKNNRIQTTK YTLLNFIPRN LFEQFHRAAN LYFLFLVFLN WVPLVEAFQK
EITMLPLVAV LTIIAIKDGL EDYRKYKLDK VINNIVTQVY CRKEKKYKES CWKDVNVGHF
IRLQCDEIIP ADMVLLHSSD PDGICHIETS SLDGETNLKQ RQVVKGYSMD DEFDPEKFSG
RIQCENPTSD ISSFKGFLDH PNKEKIGLSK QNLLLRGCIV RNTEAVVGIV VYAGHETKAM
LNNSGPRYKR SRLERRLNTD ILWSVLLLIA MCLFGAIGHG LWLAGFPESP IFSIPEPGGQ
HTSPALAGFY MFWTMIILLQ VLIPISLYVS IEIVKLGQIY FIQNDSEFYC EKSDSMIECR
ALNIAEDLGQ VQYIFSDKTG TLTENKMVFR RCSIAGMEYS HEANARRLES YQESDMHGSN
LCHVTCISQS SVCKSKEQRK AASNKSLNNF AQGEDNDGAS HPPNPRHVAF SSPMEKDVVP
DPRLLSKFDQ INPKSLYMSE EAEDTALETS YIVDFFLALA ICNTVVVSLP NQPRQKVRMP
SMVRTPMKSL EEIKQMFQRF SVRKLSASSF TSGKDCPSEN GSNFGSKLSF FTRGKLASPT
AELADKSIND LQAAGSLNST AELEPEVLEQ SNFVTACDEL DKAAACELCY EAESPDEAAL
VHAARAYNCT LQSRTPDQVT VELGFIGPLT FQVLHILPFD SVRKRMSVII RHPLTNKVVV
YTKGADSAIM DLIAMTSEDN KAAMVKKNIQ MLTQKHLDDY AKGGLRTLCI AKKVMTDSEY
AEWLQSHFLA ETSIDNREEM LYESAVRLET KLTLLGATGI EDRLQEGVPD TIESLRKAGI
NIWMLTGDKE ETAVNIAYAC RLLEHSDKLF NLSKHEKESC ETLMNIMIDE IDSLGKPNAF
SSGQQDKSGL HFGLVIDGGT LEIAMHESLQ SKFLQLTERC RAVICCRATP LQKSKVVKLV
RNNLQVMALA IGDGANDVSM IQVADIGVGI SGQEGMQAVM SSDFAVSHFK HLRKLLLVHG
HWCYTRLANM ILYFFYKNLM FVNLLFWYQF FCGFSGTAMT DFWMLILFNL LFTSVPPIIY
GILDKDVSAE TLTALPELYK SGQTSQAYRS STFWVTILDA FYQSLACFFI PYFAYIGSDL
GIYSFGNFLI TSALFVVLLH LLIESKSLTW IHWIVMGASI AAYFAFSLAF GAVCINCNPP
ANPYWIVQNH VRDPAFYLVC LLSIFIALLP RYVCRIFQGT VFPTPQLLAK KLDVMSPEER
SRALKRWRGG QSLKGRKASQ HLEPAGGSVT TKEEATCMLP GKQASFSPEY VEV
//
