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Database: UniProt
Entry: A0A671XQI8_SPAAU
LinkDB: A0A671XQI8_SPAAU
Original site: A0A671XQI8_SPAAU 
ID   A0A671XQI8_SPAAU        Unreviewed;      1074 AA.
AC   A0A671XQI8;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Sparus.
OX   NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010053354.1, ECO:0000313|Proteomes:UP000472265};
RN   [1] {ECO:0000313|Ensembl:ENSSAUP00010053354.1}
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; A0A671XQI8; -.
DR   Ensembl; ENSSAUT00010056072.1; ENSSAUP00010053354.1; ENSSAUG00010017273.1.
DR   GeneTree; ENSGT00940000157110; -.
DR   Proteomes; UP000472265; 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; 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:SF225; PHOSPHOLIPID-TRANSPORTING ATPASE IA; 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; 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:UP000472265};
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        239..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        282..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        793..813
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        819..837
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        866..884
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        904..923
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        935..955
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        975..995
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          24..87
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          753..1000
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1074 AA;  121071 MW;  8FB4EF691F93A887 CRC64;
     YRYEKTEDAS EKTSLADQED ARLIHINQPQ FTKFCSNRVS TAKYNVLTFL PRFLYSQFRR
     AANAFFLFIA LLQQIPDVSP TGRWTTLVPL LFILVVAAVK EFIEDLKRHN ADSVVNKKEC
     QGIGNHFIHQ IILCFLMIEQ EFITTSSVHI LFLHNSEPQG MCYIETSNLD GETNLKIRQV
     NYLYSLLILL YTILLRGAQL RNTQWVHGVV VYTGHDTKLM QNSTRPPLKL SNVERITNFQ
     ILVLFGCLLA ISLVCSIGQT IWKYQYGNDA WYMDLNYGGA ANFGLNFLTF IILFNNLIPI
     SLLVTLEVIK FIQAFFINWD TDMLYEPTNT PAMARTSNLN EELGQVKYIF SDKTGTLTCN
     VMQFKKCTIA GVAYGSVVLT SPSLLSRHST QSSEEAGFND PSLLENLQSN HPTAAVIQEF
     MTMMAICHTA VPERTDGNIT YQAASPDEGA LVRAARNLGF VFSGRTPDTV IMEMVRGTRR
     RMSVIMRTPS GKIRLYCKGA DTVIYDRLAD SSRYKEITLK HLEQFATEGL RTLCFAVADV
     SESSYQHWLE IQNRASTALQ NRALKLEESY ELIEKNLQLL GATAIEDKLQ DKVPETIETL
     MKADIKIWIL TGDKQETAIN IGHSCKLLTK NMGMLVINED TLDRTRETLS HHCGMLGDAL
     YKENDFALII DGKTLKYALT FGVRQYFLDL ALSCKAVICC RVSPLQKSEV VEMVKKQVKV
     ITLAIGDGAN DVGMIQTAHV GVGISGNEGL QAANSSDYSI AQFKYLKNLL LVHGAWNYNR
     VAKCILYCFY KNIVLYIIEI WFAFVNGFSG QILFERWCIG LYNVIFTALP PLTLGIFERS
     CRKENMLKYP ELYKTSQNAM GFNTKVFWAH CLNGLFHSVI LFWFPLKAFQ HDTVFGNGRT
     PDYLLLGNMV YTVSAPIFLT VSVSAGLNGS GFSHIAIWGS IGLWVVFFII YSSLWPLIPL
     APDMSGEAAM MFSSGVFWTG LVFIPITSLV FDVAYKHAAN TLPVSVPVCV CSLTERAQLL
     KNVFKKSTVS LYRSDSMQQN LLHGYAFSQD ENGVVSQSEV IRAYDTTKQR TNEW
//
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