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Database: UniProt
Entry: A0A671ENZ8_RHIFE
LinkDB: A0A671ENZ8_RHIFE
Original site: A0A671ENZ8_RHIFE 
ID   A0A671ENZ8_RHIFE        Unreviewed;      1139 AA.
AC   A0A671ENZ8;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-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=ATP11A {ECO:0000313|Ensembl:ENSRFEP00010014815.1};
OS   Rhinolophus ferrumequinum (Greater horseshoe bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC   Rhinolophinae; Rhinolophus.
OX   NCBI_TaxID=59479 {ECO:0000313|Ensembl:ENSRFEP00010014815.1, ECO:0000313|Proteomes:UP000472240};
RN   [1] {ECO:0000313|Ensembl:ENSRFEP00010014815.1, ECO:0000313|Proteomes:UP000472240}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25689317; DOI=10.1146/annurev-animal-090414-014900;
RA   Koepfli K.P., Paten B., O'Brien S.J., Koepfli K.P., Paten B., Antunes A.,
RA   Belov K., Bustamante C., Castoe T.A., Clawson H., Crawford A.J.,
RA   Diekhans M., Distel D., Durbin R., Earl D., Fujita M.K., Gamble T.,
RA   Georges A., Gemmell N., Gilbert M.T., Graves J.M., Green R.E., Hickey G.,
RA   Jarvis E.D., Johnson W., Komissarov A., Korf I., Kuhn R., Larkin D.M.,
RA   Lewin H., Lopez J.V., Ma J., Marques-Bonet T., Miller W., Murphy R.,
RA   Pevzner P., Shapiro B., Steiner C., Tamazian G., Venkatesh B., Wang J.,
RA   Wayne R., Wiley E., Yang H., Zhang G., Haussler D., Ryder O., O'Brien S.J.;
RT   "The Genome 10K Project: a way forward.";
RL   Annu Rev Anim Biosci 3:57-111(2015).
RN   [2] {ECO:0000313|Ensembl:ENSRFEP00010014815.1, ECO:0000313|Proteomes:UP000472240}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29166127; DOI=10.1146/annurev-animal-022516-022811;
RA   Teeling E.C., Vernes S.C., Davalos L.M., Ray D.A., Gilbert M.T.P.,
RA   Myers E.;
RT   "Bat Biology, Genomes, and the Bat1K Project: To Generate Chromosome-Level
RT   Genomes for All Living Bat Species.";
RL   Annu Rev Anim Biosci 6:23-46(2018).
RN   [3] {ECO:0000313|Ensembl:ENSRFEP00010014815.1, ECO:0000313|Proteomes:UP000472240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Teeling E., Myers G., Vernes S., Pippel M., Winkler S., Fedrigo O.,
RA   Rhie A., Koren S., Phillippy A., Lewin H., Damas J., Howe K.,
RA   Mountcastle J., Jarvis E.D.;
RT   "G10K-VGP greater horseshoe bat female genome, primary haplotype.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Ensembl:ENSRFEP00010014815.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A671ENZ8; -.
DR   Ensembl; ENSRFET00010016188.1; ENSRFEP00010014815.1; ENSRFEG00010010044.1.
DR   GeneTree; ENSGT00940000157849; -.
DR   Proteomes; UP000472240; Chromosome 4.
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; 3.
DR   PANTHER; PTHR24092:SF33; PHOSPHOLIPID-TRANSPORTING ATPASE IH; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00122; E1-E2_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:UP000472240};
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        69..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        295..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        349..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        965..987
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        999..1021
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1033..1057
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1063..1088
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          42..96
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          851..1103
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          1115..1139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1139 AA;  130366 MW;  2C7FBFBCF486D4FF CRC64;
     MDCSLVRTLV QRYCAGEENW VDSRTIYVGH KEPPPGAEAY IPQRYPDNRI VSSKYTFWNF
     IPKNLFEQFR RIANFYFLII FLVQLIIDTP TSPVTSGLPL FFVITVTAIK QGYEDWLRHK
     ADNAMNQCPV HFIQHGKLVR KQSRKLRVGD IVMVKEDETF PCDLIFLSSS RGDGTCHVTT
     ASLDGESSQK THYAVQDTKG FHTEEDIDGL HATIECEQPQ PDLYKFVGRI NVYNDQNDPA
     VRPLGSENLL LRGATLKNTE KIFGVAIYTG METKMALNYQ SKSQKRSAVE KSMNVFLIVY
     LCILISKALI NTVLKYVWQS EPFRDEPWYN QKTESERQRN LFLRAFTDFL AFMVLFNYII
     PVSMYVTVEM QKFLGSYFIT WDEDMFDEEM GEGPLVNTSD LNEELGQVEY IFTDKTGTLT
     ENNMEFKECC IEGHVYVPHV ICNGQVLPGA SGIDMIDSSP GVSGREREEL FFRALCLCHT
     IQVKDDDDVD GPRKSPDSGK SCVYISSSPD EVALVEGVQR LGFTYLRLKD NYMEILNRDN
     DIERFELLEI LSFDSVRRRM SVIVRSATGE IYLFCKGADS SIFPRVIEGK VDQIRSRVER
     NAVEGLRTLC VAYKRLIQEE YEGICRLLQA AKVALQDREK KLAEAYEQIE KDLILLGATA
     VEDRLQEKAA DTIEALQKAG IKVWVLTGDK METAAATCYA CKLFRRNTQL LELTTKKIEE
     QSLHDVLFEL SKTVLRYSGS LTRDNLSGLS TDMQDYGLII DGAALSLIMK PREDGSSSNY
     RELFLEICRN CSAVLCCRMA PLQKAQIVKL IKLSKEHPIT LAIGDGANDV SMILEAHVGI
     GVIGKEGRQA ARNSDYAIPK FKHLKKMLLV HGHFYYIRIS ELVQYFFYKN VCFIFPQFLY
     QFFCGFSQQT LYDTAYLTLY NISFTSLPIL LYSLMEQHVS IDTLKRDPSL YRDIAKNALL
     RWRVFIYWTF LGVFDALVFF FGAYFLFENT TVTSNGQIFG NWTFGTLVFT VMVFTVTLKL
     ALDTHYWTWI NHFVIWGSLL FYIVFSLLWG GIIWPFLSYQ RMYYVFIQML SSGPAWLAIV
     LLITVSLLPD VLKKVLCKQL WPSATERVQK SSKLKTAVDA APSTDRPLLK DVLPGPRRD
//
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