ID A0A1S3FAV7_DIPOR Unreviewed; 1491 AA.
AC A0A1S3FAV7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC105987070 {ECO:0000313|RefSeq:XP_012873681.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012873681.1};
RN [1] {ECO:0000313|RefSeq:XP_012873681.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012873681.1};
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_012873681.1; XM_013018227.1.
DR GeneID; 105987070; -.
DR KEGG; dord:105987070; -.
DR InParanoid; A0A1S3FAV7; -.
DR OrthoDB; 4811563at2759; -.
DR Proteomes; UP000081671; Unplaced.
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; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 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; 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; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF78; PHOSPHOLIPID-TRANSPORTING ATPASE IK; 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 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:UP000081671};
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 80..97
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 351..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 928..948
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 960..980
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1005..1028
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1040..1061
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1068..1094
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1114..1137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 44..108
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 897..1138
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1199..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1491 AA; 170713 MW; 3F5F5132C7A21FB6 CRC64;
MDTTAFYEKE DDKDTGAFLD RDTQWVAFTW EVRANNHAFH ATSTEKRFLC WRKKKYNTNK
ICTAKYNVFT FLPLNLYEQF HRASNIYFLI IIILQSIPEI STLPWFTLFA PLVCLLFIRA
IRDLVDDIGR HRSDRAINNR PCQILRRKRF KWKKWEDICV GDVVCLKKDS IVPADLLLLV
STEPSSLCYV ETADIDGETN LKFKQALTVT HQELTSSKNI ESFQGTVLCE EPNSRMHHFV
GSLELNKKTY SLDISNMLLR GYKIRNVEAC YGLVIYAGVD TKIMKNCGKI HLKRTKVDLF
MNKLVAMIFL SLVIISLLLT LGFSFNIKDF KWKHYYVSAK HLRSEIAESF LIFWSFLILL
STTVPMALFI MAEFVYLGNS LFIDWDMQMY YEPRDATAKA RNTSLADQLG QVQYIFSDKT
GTLTQNIMTF KKCCINGQVY GPDDEETPRQ ENPYLWNEFA DGKFLFYDKK LLHVVRHEKD
RVVQEFWRLL AICHTVMVQE ENDQPLYQAA SPDEEALVTA ARNFGYVFRS RTQDSITVME
MGEERVYQVL AMMDFNSVRK RMSVLVRNPE GSICLYTKGA DTVILERLHK KGEMEMTTEE
VLAAFAEQTL RTLCLAYKEI DEDDYEEWES QHHEATLLLQ NRAQALHQVY DKMEQNLQLL
GVTAIEDKLQ DHVSEAISNL KRANIKVWVL TGDKRETALN IGFACQLLEE NMLILEDKEI
KRILEIYWEN ISKLQTSKGN LKVLPQINMA MVISGDFLDQ LMFSLHQKPQ ALTDVEEVNE
VWQEPRQMRK NFPRARRISH LFQNLGTSQD PLSTKVLNTN ESFEMWRERA FVELASRCQA
VICCRMTPKQ KALVVGLVKK YQQVVTLAIG DGANDVNMIK TADIGVGLMG QEGMQAVQNS
DYMLAQFCFL QRLLLVHGRW SYMRVSKFLT FFFYKTVACM MAQIWFSFYN GFTAQPLYEG
WFLSFTNMFY TTLPVLYMGL FEQDVSAEQS LNMPQLYMMG QKDALFNYGV FFQAISHGLV
TSMINFIITL LASQDSPSDY QSFAVLVALS GLLSITIEAI LIIKYWTIIC VACILLSLGS
YAVLTSLTQS FWLYKIAPKT FPFLYADYNA LTQLHGLLVI LLNVTLNTLF VLAFRVIQLL
RQLRPKEEEV PKEEVQGVEP MPYLPRESRA RRSSYAFSHH EGYADLITHG TILRRPHEAP
SEPLYASPIP SEGEEEEEPS TGRKRSLWLP RKTSSWLRSR RHHTAKDLAE DRAAFSAQSS
FETAGTPSVL YSESQASRPS RSPTTISMPS RSSQKMSSLP GSQPSLAEDS RLVSPSEPPF
QTWESQPDSL EGRSQSWTPF WKNWQKETHP LGEDAESLPR LTHTVPPKTL PPSVDEEPLG
EKKEEEAAET GKGEGRRFHR APSPTHGQEP GSSPCTEGNK EKDRPKSALE LERKPRLSKG
GGRSADEETE VERQACAGSL GRTALTRDYP DSCDLRVQSI AQERRGEGGP A
//
