ID A0A3P8TR13_AMPPE Unreviewed; 1106 AA.
AC A0A3P8TR13;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000025492.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000025492.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000025492.1}
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; A0A3P8TR13; -.
DR Ensembl; ENSAPET00000026164.1; ENSAPEP00000025492.1; ENSAPEG00000018052.1.
DR GeneTree; ENSGT00940000157071; -.
DR Proteomes; UP000265080; Chromosome 17.
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; cd07541; P-type_ATPase_APLT_Neo1-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:SF50; PHOSPHOLIPID-TRANSPORTING ATPASE IIB-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_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; 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:UP000265080};
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 158..177
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 378..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 905..925
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 931..953
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 983..1003
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1009..1030
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1037..1057
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1069..1089
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 104..161
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 871..1098
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 478..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1106 AA; 124594 MW; 7B2468B6FFF52B9D CRC64;
MCDSGFLTFS CFIEFFSRYS SEDDPSNLDE MPLMMSEEGF ENDESDYQTL PRARVNQRQS
GLGWFLLGGW KVLCGSCCDC LAHICRRKKE LKARTVWLGC PEKCEEKYPK NAIKNQKYNI
FTFVPGVLYQ QFKFFLNLYF LVVACSQFVP SLKIGYLYTY WAPLGFVLAV TMVREAVDEV
RRYQRDKEMN SQLYSKLTVR GKIQVKSSDI QVGDLIIVEK VNIYCFLSGA CFIRTDQLDG
ETDWKLKVAV GCTQRLPALG DLFSISAYVY AQRPQLDIHS FEGNFTREDT DPQIHESLSI
ENTLWASTVV ASGTVIGVVI YTGKETRSVL NTSFAKNKVG LLDLELNRLT KALFLAQVVL
SVVMVALQGF VGPWFRNLFR FVVLFSYIIP ISLRVNLDMG KSAYGWMIMK DENIPGTVVR
TSTIPEELGR LVYLLTDKTG TLTQNEMIFK RLHLGTVSYG TDTMDEIQSH IIQSYAQVTS
QPSNGSTSGA TPSRKTQTSG PKVRKSVSSR IHEAVKAIAL CHNVTPVYES HGGVNGETES
AEADQDFSDD NRTYQASSPD EVALVRWTES VGLTLVNRDL TSLQLKTPSG QILSFYILQI
FPFTSESKRM GIIVREESTG DITFYMKGAD VAMASIVQYN DWLEEECGNM AREGLRTLVV
AKKSLSEEQY QDFENRYNQA KLSIHDRGLK VAAVVESLER EMELLCLTGV EDQLQADVRP
TLELLRNAGI KIWMLTGDKL ETATCIAKSS HLVSRNQHIH VFKPVSNRGE AHLELNAFRR
KHDCALVISG DSLEVCLRYY EHEFVELACQ CPAVVCCRCS PTQKAQIVRL LQQHTANRTC
AIGDGGNDVS MIQAADCGIG IEGKEGKQAS LAADFSITQF KHIGRLLMVH GRNSYKRSAA
LGQFVMHRGM IISTMQAVFS SIFYFASVPL YQGFLMVGYA TIYTMFPVFS LVLDQDVKPE
MALLYPELYK DLTKGRSLSF KTFLIWVLIS VYQGGILMYG ALVLFESEFV HVVAISFTAL
ILTELLMVAL TIRTWHWLMV VAEFFSLGCY LASLAFLNEY FDLSFITTWP FLWKVSAITL
VSCLPLYIIK YLKRKFSPPS YSKLSS
//
