ID A0A670IXU5_PODMU Unreviewed; 1106 AA.
AC A0A670IXU5;
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};
OS Podarcis muralis (Wall lizard) (Lacerta muralis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=64176 {ECO:0000313|Ensembl:ENSPMRP00000016631.1, ECO:0000313|Proteomes:UP000472272};
RN [1] {ECO:0000313|Ensembl:ENSPMRP00000016631.1, ECO:0000313|Proteomes:UP000472272}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30819892; DOI=10.1073/pnas.1820320116;
RA Andrade P., Pinho C., Perez I de Lanuza G., Afonso S., Brejcha J.,
RA Rubin C.J., Wallerman O., Pereira P., Sabatino S.J., Bellati A.,
RA Pellitteri-Rosa D., Bosakova Z., Bunikis I., Carretero M.A., Feiner N.,
RA Marsik P., Pauperio F., Salvi D., Soler L., While G.M., Uller T., Font E.,
RA Andersson L., Carneiro M.;
RT "Regulatory changes in pterin and carotenoid genes underlie balanced color
RT polymorphisms in the wall lizard.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:5633-5642(2019).
RN [2] {ECO:0000313|Ensembl:ENSPMRP00000016631.1}
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; A0A670IXU5; -.
DR Ensembl; ENSPMRT00000017732.1; ENSPMRP00000016631.1; ENSPMRG00000010537.1.
DR GeneTree; ENSGT00940000161917; -.
DR Proteomes; UP000472272; Chromosome 11.
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; 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; 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:SF52; PHOSPHOLIPID-TRANSPORTING ATPASE FETA; 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 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; 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:UP000472272};
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 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 280..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 323..349
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 825..846
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 858..878
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 908..927
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 947..965
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 977..1001
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 69..120
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 794..1048
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1106 AA; 123847 MW; 10A4075F43676162 CRC64;
MGSGPLCSPL VDQALVKEVG GSAWDQVAAF GGGAGCWRAA LLVCCQGEGS GPDAPFSPGL
NHRLFFPQRN SIQTSKYNVF TFLPLNLFEQ FQRVANAYFL FLLILQLIPE ISSLSWFTTV
VPLILVLAVS AAKDAIDDVV RILSLQTPPI KSFSTKPGLL SLLPLGVLSL QADVLLLSSS
EPHSLTYIET TELDGACSLP AGEIKCEAPN NKLDKFMGTL LFKGEKYALD NEKMLLRGCT
IRNTDWCFGL VIFAGPDTKL MQNSGRTTFK RTSIDRLMNF LVLVIFVLLA AMCSVLAIGN
SIWEYKRGSA FQVYLPWPHD VHSAFYSAFL MFWSYVIILN TVVPISLYVS VEIIRLGNSF
YIEWDRKMYY PLNDTPAQAR TTTLNEELGQ IKYIFSDKTG TLTQNIMVFN KCCINGKIYG
RDEEPLRGLS TPKVDFSYNP LADPKFSFYD QSLVEEVKAG DVITHKFFRL LSLCHTVMPE
EKKPGELVYQ AQSPDEGALV TAARNFGFVF RARTPETITV VEMGKTIVYK LLAILDFNNV
RKRMSVIVRR PDGRVTLYCK GADTILYELL HPSCVPLKEE TTEYLEEFAG EGLRTLVVAY
KDLERKSFAN WQKRHHEAST ALQDREEKLS ELYEEIEKDL ILLGATAIED KLQDGVPQTI
ETLGKAQIKI WVLTGDKQGT ARGGDDTLLS APPKNSWRLI LPPSEVHPRI LCDVTGREEQ
RRELELELVR TACLCKVVIC CRVTPLQKAQ VVELVKKYKN AVTLAIGDGA NDVSMIKAAH
IGVGISGQEG MQAVLSSDFS FAQFRYLQRL LLVHGRWSYI RMCKFLAYFF YKNFAFTLVH
FWYGFFSGFS AQTVYDEWFI TLYNMVYTSL PVLGMSLFDQ DVDDRWSLQF PQLYMPGQQN
LYFNKKEFVK CVLYSVYSSL VLFFIPYGTL FDSLRSDGKA IADYQSFALM AQTCLLIVVS
VQMGLDTAYW TAVNQLFIWG SLAMYFAITF TMYSDGTYLI FTGSFPFVGS ARNTLNQPNV
WLSIFLCVTL CVLPVVGFRF LKVQLKPTIS DQVRPPPPGK VLLGGGCLPL SGGTRGGTRR
CPHSASACFC DASCHPRGQV TPAICG
//
