ID A0A2U4C267_TURTR Unreviewed; 1120 AA.
AC A0A2U4C267;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP9A {ECO:0000313|RefSeq:XP_019799562.2};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019799562.2};
RN [1] {ECO:0000313|RefSeq:XP_019799562.2}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019799562.2};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_019799562.2; XM_019944003.2.
DR AlphaFoldDB; A0A2U4C267; -.
DR STRING; 9739.ENSTTRP00000007325; -.
DR InParanoid; A0A2U4C267; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000245320; Chromosome 15.
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:SF49; PHOSPHOLIPID-TRANSPORTING ATPASE IIA-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:UP000245320};
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 371..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 401..420
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 945..967
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 997..1017
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1023..1044
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1051..1071
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1077..1103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 119..179
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 885..1112
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 38..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 125386 MW; 50D652A358A9B9DE CRC64;
MVRPCPSVGP RGRLRAWPGA RELAPSLRAR PARCRRLLPR GGAAPAGGGA EAGPGGGPGG
AGGTAAKAGG AGDMTDNIPL QPVRQKKRMD SRPRGGCCEW LRCCGAGEPR PRTVWLGHPE
KRDQRYPRNV INNQKYNFFT FLPGVLFNQF KYFFNLYFLL LACSQFVPEM RLGALYTYWV
PLGFVLAVTI IREAVEEIRC YVRDKEVNSQ VYSRLTARGT VKVKSSSIQV GDLIIVEKNQ
RVPADMIFLR TSEKNGSCFL RTDQLDGETD WKLRLPVACT QRLPTAADLL QIRSYVYAEE
PNIDIHNFVG TFTREDSDAP ISESLSIENA LWAGTVTASG TIVGVVLYTG RELRSVMNTS
NPRSKIGLFD LEVNCLTKIL FGALVVVSLV MVALQHFAGR WYLQIIRFLL LFSNIIPISL
RVNLDMGKIV YSWVIRRDSK IPGTVVRSST IPEQLGRISY LLTDKTGTLT QNEMVFKRLH
LGTVAYGLDS MDEVQSHIFS IYTQQSQDPP AQKGPALTTK VRRTMGTRVH EAVKAIALCH
NVTPVYESSG VTDQAEAEKQ YEDSCRVYQA SSPDEVALVQ WTESVGLTLV GRDQSSMQLR
TPGDQILNFT ILQIFPFTYE SKRMGIIVRD ESTGEITFYM KGADVVMAGI VQYNDWLEEE
CGNMAREGLR VLVVAKKSLA EEQYQDFEAR YVQAKLSVHD RSLKVATVIE SLEMEMELLC
LTGVEDQLQA DVRPTLETLR NAGIKVWMLT GDKLETATCT AKNAHLVTRN QDIHVFRLVT
NRGEAHLELN AFRRKHDCAL VISGDSLEVC LKYYEYEFME LACQCPAVVC CRCAPTQKAQ
IVRLLQERTG KLTCAVGDGG NDVSMIQESD CGVGVEGKEG KQASLAADFS ITQFKHLGRL
LMVHGRNSYK RSAALSQFVI HRSLCISTMQ AVFSSVFYFA SVPLYQGFLI IGYSTIYTMF
PVFSLVLDKD VKSEVAMLYP ELYKDLLKGR PLSYKTFLIW VLISIYQGST IMYGALLLFE
SEFVHIVAIS FTSLILTELL MVALTIQTWH WLMTVAELLS LACYIASLVF LHEFIDVYFI
ATLSFLWKVS VITLISCLPL YVLKYLRRRF SPPSYSKLTS
//
