ID A0A671UKW1_SPAAU Unreviewed; 1146 AA.
AC A0A671UKW1;
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=ATP11B {ECO:0000313|Ensembl:ENSSAUP00010015077.1};
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:ENSSAUP00010015077.1, ECO:0000313|Proteomes:UP000472265};
RN [1] {ECO:0000313|Ensembl:ENSSAUP00010015077.1}
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; A0A671UKW1; -.
DR Ensembl; ENSSAUT00010015991.1; ENSSAUP00010015077.1; ENSSAUG00010006965.1.
DR GeneTree; ENSGT00940000156162; -.
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; 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; 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; 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; 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: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 66..81
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 288..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 342..361
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 886..906
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 936..958
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 978..1001
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1013..1037
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1043..1068
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 36..90
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 822..1083
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1146 AA; 130597 MW; A5AEFBA2364940C7 CRC64;
MLRWIRQQLG FDPPHQSDTR TVYVANRFPQ HGHYIPQRFA DNRIISSKYT IWNFVPKNLF
EQFRRIANFY FLIIFLVQLM IDTPTSPVTS GLPLFFVITV TAIKQGYEDW LRHKADNEVN
GAPVFVVRSG SLVQTRSKNI RVGDIVRVAK DETFPVDLVL LSSDRADGTC HITTASLDGE
TNLKTHYSVA ETAECQSVTR LESLQAVVEC QQPDADLYRF VGRMTVTQHG EEIVRPLGPE
NLLLRGARLK NTKEIFGVAI YTGMESKMAL NYKCKSQKRS AVEKSMNTFL IIYLGILLFE
AILSTILKYA WQAEEEWDEP FYNRKTEQER NSSPILKFIS DFLAFLVLYN FIIPISLYVT
VEMQKFLGSF FIGWDLDLYH EESDQKAQVN TSDLNEELGQ VEYVFTDKTG TLTENEMHFR
ECSINGTKYR EVNGKLVPEG MTDDAPDGST PQLIGDELLF LKAVSLCHTV QISYDQPDLV
GGGDPFSHAN GFSSSHMEYY ASSPDEKALV EAAKRIGVAF LGTSGDTMEI KTFGKSERYK
LLHVLEFDAN RRRMSVILQT PSGGYVLFTK GAESAILPFA TGGEIEKTRL HVDEFALKGL
RTLVIACRHF SPEEYIEVDR HLNAARTALQ QREERLQEAF GYIERDLQLL GATGVEDKLQ
DKVQETIEAL RLAGIKVWVL TGDKHETAVS VSLSCGHFHR TMNILELLQQ RSDNECAEQL
RILARRIKED HVIQHGLVVD GASLSLALRE HEKLFMEVCK NCSAVLCCRM APLQKAKVVR
LLKTSPEKPI TLAIGDGAND VSMIQEAHVG IGIMGKEGRQ AVRNSDYAIA RFKFLAKLLL
VHGHFYYIRI ATLVQYFFYK NVCFITPQFL YQFFCLFSQQ TLYDSVYLTL YNICFTSLPI
LVYSLFEQLV HPHVLQNKPG LYRDISKNSL LSFRTFLYWT LLGFCHAFIF FFGSYILMGE
DTTLMGNGQI LRANRQLMFG NWTFGTLVFT VMVITVTLKL ALETHFWTWM NHFVTWGSIA
FYFIFSLFYG GIIWPFLHTQ DMYFVFVQLL SSGSAWFAII IIVITCLFPD VVKKVFYRHL
LPTSTQKSQM YSNRVAIGDD FIALQPLSRA KSQLGKIRWK RVRVQSAQNM TLLKPSGAQG
RTIGTC
//
