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Database: UniProt
Entry: A0A5F7ZS82_MACMU
LinkDB: A0A5F7ZS82_MACMU
Original site: A0A5F7ZS82_MACMU 
ID   A0A5F7ZS82_MACMU        Unreviewed;      1441 AA.
AC   A0A5F7ZS82;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
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:ENSMMUP00000068010.1,
GN   ECO:0000313|VGNC:VGNC:100201};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000068010.1, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000068010.1}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000068010.1};
RG   Ensembl;
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   SMR; A0A5F7ZS82; -.
DR   STRING; 9544.ENSMMUP00000068010; -.
DR   PaxDb; 9544-ENSMMUP00000028678; -.
DR   Ensembl; ENSMMUT00000100083.1; ENSMMUP00000068010.1; ENSMMUG00000021778.4.
DR   VEuPathDB; HostDB:ENSMMUG00000021778; -.
DR   VGNC; VGNC:100201; ATP10D.
DR   GeneTree; ENSGT00940000156728; -.
DR   InParanoid; A0A5F7ZS82; -.
DR   OMA; FKVAREC; -.
DR   Proteomes; UP000006718; Chromosome 5.
DR   Bgee; ENSMMUG00000021778; Expressed in spleen and 21 other cell types or tissues.
DR   ExpressionAtlas; A0A5F7ZS82; baseline.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:1990531; C:phospholipid-translocating ATPase complex; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0140351; F:glycosylceramide flippase activity; IEA:Ensembl.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
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; 2.
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; SFLDS00003; Haloacid_Dehalogenase; 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   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
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:UP000006718};
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}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT   TRANSMEM        117..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        142..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        340..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        381..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1132..1151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1163..1184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1214..1235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1241..1264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1271..1296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1316..1335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          85..141
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          1100..1345
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1441 AA;  162291 MW;  440877F7E0B9F333 CRC64;
     MCAEGGIATQ PGSHHSLDMA EALQWARYHW RQLIGGATRD DDSRPYNYSS LLACGRKSLQ
     TPKLAGRHRI VVPHLQPFKD EYEKFSGAYV NNRIRTTKYT LLNFVPRNLF EQFHRAANLY
     FLFLVVLNWV PLVEAFQKEI TMLPLVVVLT IIAIKDGLED YRKYKIDKQI NNLITKVYSR
     KEKKYIDRCW KDVTVGDFIR LSCNEVIPAD MVLLFSTDPD GICHIETSGL DGESNLKQRQ
     VVRGYAEQDS EVDPEKFSTR IECENPNNDL SRFRGFLEHS NKERVGLSKE NLLLRGCTIR
     NTEAVVGIVV YAGHETKAML NNSGPRYKRS KLERRANTDV LWCVMLLVIM CLTGSVGHGI
     WLSRYEKMHF FNNPEPDRHI ISPLLAGFYM FWTMIILLQV LIPISLYVSI EIVKLGQIYF
     IQSDMDFYNE KTDSTVQCRA LNIAEDLGQI QYLFSDKTGT LTENKMVFRR CSVAGFDYCH
     EENAKRLESY QEAVSEDEDF TDTLSGSLSN MAKPRAPSCR TVHNGLLGNK PSNHLTGSSF
     TLGSRERASE VLHSRQAAFS SPIETDVVPD TRLLDKFSQI TPRLFMPLDE TVQNPLLETL
     YIIDFFIALA ICNTVVVSAP NQCRQKIRHP SLGGLPIKSL EEIKSLFQRL SVRRSSSPSL
     NSGKEPSSGV PNAFVSRLPL FSRIKLASPV EEEVSQVCES PQCSSSSACC TETEKQHSNA
     GLLNGKAESL PGQPMACNLC YEAESPDEAA LVYAARAYQC TLQSRTPEQV MVDFAALGPL
     TFQLLHILPF DSVRKRMSVV VRHPLSNQVV VYTKGADSVI MELLSVASPD GASPEKQQMI
     IREKTQKHLD DYAKQGLRTL CIAKKVMSDT EYAEWLRNHF LAETSIDNRE ELLLESAMRL
     ENKLTLLGAT GIEDRLQEGV PESIEALHKA GIKIWMLTGD KQETAVNIAY ACKLLEPDDK
     LFILNTQSKD ACGMLMSTIL KELQKKTQAL PEQVSLSVDL HQPPVPQDSG LRAGLIITGK
     TLEFALQESL QKQFLELTSW CQTVVCCRAT PLQKSEVVKL VRSHLQVMTL AIGDGANDVS
     MIQVADIGIG VSGQEGMQAV MASDFAVSQF KHLSKLLLVH GHWCYTRLSN MILYFFYKNV
     AYVNLLFWYQ FFCGFSGTSM TDYWVLIFFN LLFTSAPPVI YGVLEKDVSA ETLMQLPELY
     KSGQKSEAYL PHTFWITLLD AFYQSLVCFF VPYFTYQGSD IDIFAFGNPL NTAALFIILL
     HLIIESKSLT WIHMLVITGS ILSYFLFAIV FGAMCVTCNP PSNPYWIMQE HMLDPVFYLV
     CILTTCIALL PRFVYRVLQG SLFPSPILRA KHFDRLTPEE RTEALKKWRG AGKMNQVTSN
     YANQSADKSG RRPKPGPSTV FAMKSATSCA IEQGNLSLCE TALDQGYSET KAFEMARPCK
     D
//
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