ID   B4E3T1_HUMAN            Unreviewed;       892 AA.
AC   B4E3T1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG65593.1};
RN   [1] {ECO:0000313|EMBL:BAG65593.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Uterus {ECO:0000313|EMBL:BAG65593.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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   EMBL; AK304855; BAG65593.1; -; mRNA.
DR   RefSeq; NP_055431.1; NM_014616.2.
DR   AlphaFoldDB; B4E3T1; -.
DR   PeptideAtlas; B4E3T1; -.
DR   DNASU; 23200; -.
DR   GeneID; 23200; -.
DR   KEGG; hsa:23200; -.
DR   CTD; 23200; -.
DR   OrthoDB; 275833at2759; -.
DR   BioGRID-ORCS; 23200; 15 hits in 1152 CRISPR screens.
DR   GenomeRNAi; 23200; -.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProt.
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   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; 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   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR24092:SF57; PHOSPHOLIPID-TRANSPORTING ATPASE IF; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 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   2: Evidence at transcript level;
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   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        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        53..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        676..698
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        710..734
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        746..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        775..801
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          562..815
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   892 AA;  101803 MW;  9429C934C85019D6 CRC64;
     MNTFLIIYLV ILISEAVIST ILKYTWQAEE KWDEPWYNQK TEHQRNSSKI LRFISDFLAF
     LVLYNFIIPI SLYVTVEMQK FLGSFFIGWD LDLYHEESDQ KAQVNTSDLN EELGQVEYVF
     TDKTGTLTEN EMQFRECSIN GMKYQEINGR LVPEGPTPDS SEGNLSYLSS LSHLNNLSHL
     TTSSSFRTSP ENETELIKEH DLFFKAVSLC HTVQISNVQT DCTGDGPWQS NLAPSQLEYY
     ASSPDEKALV EAAARIGIVF IGNSEETMEV KTLGKLERYK LLHILEFDSD RRRMSVIVQA
     PSGEKLLFAK GAESSILPKC IGGEIEKTRI HVDEFALKGL RTLCIAYRKF TSKEYEEIDK
     RIFEARTALQ QREEKLAAVF QFIEKDLILL GATAVEDRLQ DKVRETIEAL RMAGIKVWVL
     TGDKHETAVS VSLSCGHFHR TMNILELINQ KSDSECAEQL RQLARRITED HVIQHGLVVD
     GTSLSLALRE HEKLFMEVCR NCSAVLCCRM APLQKAKVIR LIKISPEKPI TLAVGDGAND
     VSMIQEAHVG IGIMGKEGRQ AARNSDYAIA RFKFLSKLLF VHGHFYYIRI ATLVQYFFYK
     NVCFITPQFL YQFYCLFSQQ TLYDSVYLTL YNICFTSLPI LIYSLLEQHV DPHVLQNKPT
     LYRDISKNRL LSIKTFLYWT ILGFSHAFIF FFGSYLLIGK DTSLLGNGQM FGNWTFGTLV
     FTVMVITVTV KMALETHFWT WINHLVTWGS IIFYFVFSLF YGGILWPFLG SQNMYFVFIQ
     LLSSGSAWFA IILMVVTCLF LDIIKKVFDR HLHPTSTEKA QLTETNAGIK CLDSMCCFPE
     GEAACASVGR MLERVIGRCS PTHISRSWSA SDPFYTNDRS ILTLSTMDSS TC
//