ID A0A671XQ40_SPAAU Unreviewed; 1127 AA.
AC A0A671XQ40;
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:ENSSAUP00010053313.1, ECO:0000313|Proteomes:UP000472265};
RN [1] {ECO:0000313|Ensembl:ENSSAUP00010053313.1}
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; A0A671XQ40; -.
DR Ensembl; ENSSAUT00010056030.1; ENSSAUP00010053313.1; 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; 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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
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; 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 Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1127
FT /note="Phospholipid-transporting ATPase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025440131"
FT TRANSMEM 310..333
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 353..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 830..850
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 856..874
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 903..921
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 941..960
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 972..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1012..1032
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 42..105
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 790..1041
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1127 AA; 127011 MW; 49C9CDB0831BC9A4 CRC64;
FLCMSQILCL IHCLVSHAAG YEKTEDASEK TSLADQEDAR LIHINQPQFT KFCSNRVSTA
KYNVLTFLPR FLYSQFRRAA NAFFLFIALL QQIPDVSPTG RWTTLVPLLF ILVVAAVKET
LSHCLFISSF SSFPPPPPPP SLLTTVLRNG AWEIVHWEKV CTKNVSLKLM IEQEFITTSS
VHILFLHNSE PQGMCYIETS NLDGETNLKI RQGLQVTADI KDIDSLMRLS GRMECESPNR
HLYEFVGNIR LDRRSTIPLG PDQILLRGAQ LRNTQWVHGV VVYTGHDTKL MQNSTRPPLK
LSNVERITNF QILVLFGCLL AISLVCSIGQ TIWKYQYGND AWYMDLNYGG AANFGLNFLT
FIILFNNLIP ISLLVTLEVI KFIQAFFINW DTDMLYEPTN TPAMARTSNL NEELGQVKYI
FSDKTGTLTC NVMQFKKFSS YSPAFILPPT AAVIQEFMTM MAICHTAVPE RTDGNITYQA
ASPDEGALVR AARNLGFVFS GRTPDTVIME MVRGTRRRMS VIMRTPSGKI RLYCKGADTV
IYDRLADSSR YKEITLKHLE QFATEGLRTL CFAVADVSES SYQHWLEIQN RASTALQNRA
LKLEESYELI EKNLQLLGAT AIEDKLQDKV PETIETLMKA DIKIWILTGD KQETAINIGH
SCKLLTKNMG MLVINEDTLD RTRETLSHHC GMLGDALYKE NDFALIIDGK TLKYALTFGV
RQYFLDLALS CKAVICCRVS PLQKSEVVEM VKKQVKVITL AIGDGANDVG MIQTAHVGVG
ISGNEGLQAA NSSDYSIAQF KYLKNLLLVH GAWNYNRVAK CILYCFYKNI VLYIIEIWFA
FVNGFSGQIL FERWCIGLYN VIFTALPPLT LGIFERSCRK ENMLKYPELY KTSQNAMGFN
TKVFWAHCLN GLFHSVILFW FPLKAFQHDT VFGNGRTPDY LLLGNMVYTV SAPIFLTVSV
SAGLNGSGFS HIAIWGSIGL WVVFFIIYSS LWPLIPLAPD MSGEAAMMFS SGVFWTGLVF
IPITSLVFDV AYKVVKRVCF KTLVDEVQEL EALSKDPGAV VHGKSLTERA QLLKNVFKKS
TVSLYRSDSM QQNLLHGYAF SQDENGVVSQ SEVIRAYDTT KQRTNEW
//
