ID A0A485PT07_LYNPA Unreviewed; 1154 AA.
AC A0A485PT07;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=LYPA_23C015827 {ECO:0000313|EMBL:VFV45482.1};
OS Lynx pardinus (Iberian lynx) (Felis pardina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=191816 {ECO:0000313|EMBL:VFV45482.1, ECO:0000313|Proteomes:UP000386466};
RN [1] {ECO:0000313|EMBL:VFV45482.1, ECO:0000313|Proteomes:UP000386466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAAGRJ010037717; VFV45482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A485PT07; -.
DR Proteomes; UP000386466; Unassembled WGS sequence.
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: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:UP000386466};
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 280..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 334..353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 855..876
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 953..975
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 987..1011
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1023..1046
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1052..1078
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 24..81
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 839..1092
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1154 AA; 131787 MW; 9E35F7F3EF3AB65C CRC64;
MGFDPPHQSD TRTIYIANRF PQNGLYTPQK FIDNRIISSK YTVWNFVPKN LFEQFRRVAN
FYFLIIFLVQ LMIDTPTSPI TSGLPLFFVI TVTAIKQGYE DWLRHNSDNE VNGAPVYVVR
SGGLVKTRSK NIRVGDIVRI AKDEIFPADL VLLSSDRLDG SCHVTTASLD GETNLKTHVA
VPETAVLQTV ASLDTLIAVI ECQQPEADLY RFMGRMIITQ QMEEIVRPLG PESLLLRGAR
LKNTKEIFGV AIYTGMETKM ALNYKSKSQK RSAVEKSMNT FLIIYLIILI SEAIISTILK
YTWQAEEKWD EPWYNQKTEH QRNSSKILRF ISDFLAFLVL YNFIIPISLY VTVEMQKFLG
SFFIGWDLDL YHEESDQKAQ VNTSDLNEEL GQVEYVFTDK TGTLTENEMQ FRECSINGIK
YQEINGRLVS EGPTPDSSDG NLSYLNSLSH LNNLSHLTTS SSFRTSPENE TELIKEHDLF
FKAVSLCHTV QISNVQTDGI GDGPWQSNLA PSQLEYYASS PDEKALVEAA ARIGIVFIGN
SEETMEVKTL GKLERYKLLH ILEFDSDRRR MSVIVQAPSG EKFLFAKGAE SSILPNCVGG
EIEKTRIHVD EFALKGLRTL CMAYKQLTSK EYEEIDRRLF EARTALQQRE EKLADVFQFI
EKNLILLGAT AVEDRLQDRV RETIEGLRMA GIKVWVLTGD KHETAVSVSL SCGHFHRTMN
ILELINQKSD SQCAEQLRQL ARRIKEDHVI QHGLVVDGTS LSLALREHEK LFMEVCRNCS
AVLCCRMAPL QKAKVIRLIK ISPEKPITLA VGDGANDVSM IQEAHVGIGI MGKEGRQAAR
NSDYAIARFK FLSKLLFVHG HFYYIRIATL VQYFFYKNVC FITPQFLYQF YCLFSQQTLY
DSVYLTLYNI CFTSLPILIY SLLEQHIDPH VLQSKPTLYR DISKNRQLSI KTFLYWTILG
FSHAFIFFFG SYFLIGKDIS LLGNGQMFGN WTFGTLVFTV MVITVTVKMA LETHFWTWIN
HLVTWGSIIF YFVFSLFYGG ILWPFLGSQN MYFVFIQLLS SGSAWFAIIL MVVTCLLLDI
VKKVFERQLH PTNTEKAQMY SNTVALSDEF IALQPLSRAR NQLSKLRWKK IRVQSAQHMN
LLKASTEGRT VGTC
//
