ID F6X5R7_HORSE Unreviewed; 1120 AA.
AC F6X5R7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 75.
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|Ensembl:ENSECAP00000019302.2,
GN ECO:0000313|VGNC:VGNC:56195};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000019302.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000019302.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019302.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000019302.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019302.2};
RG Ensembl;
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 AlphaFoldDB; F6X5R7; -.
DR SMR; F6X5R7; -.
DR STRING; 9796.ENSECAP00000019302; -.
DR PaxDb; 9796-ENSECAP00000019302; -.
DR Ensembl; ENSECAT00000023315.3; ENSECAP00000019302.2; ENSECAG00000020949.4.
DR VGNC; VGNC:56195; ATP9A.
DR GeneTree; ENSGT00940000159181; -.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; F6X5R7; -.
DR OMA; XVYFIAT; -.
DR TreeFam; TF300590; -.
DR Proteomes; UP000002281; Chromosome 22.
DR Bgee; ENSECAG00000020949; Expressed in cerebellum and 23 other cell types or tissues.
DR ExpressionAtlas; F6X5R7; baseline.
DR GO; GO:0031901; C:early endosome membrane; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:1903542; P:negative regulation of exosomal secretion; IEA:Ensembl.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:2001135; P:regulation of endocytic recycling; IEA:Ensembl.
DR GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; IEA:Ensembl.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
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; 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:UP000002281};
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 43..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 125532 MW; B97FF633D0B7ED4C CRC64;
MVRPCPSVGP RGRLRAWPGA RELAPSLRAR PARCRRLLPR GGAATAGGGA EAGPGGGPGG
AGGAAAKAGG AGDMTDNIPL QPVRQKKRMD SRPRAGCCEW LRCCGRGEPR PRTVWLGHPE
KRDQRYPRNV INNQKYNFFT FLPGVLFNQF KYFFNLYFLL LACSQFVPEM RLGALYTYWV
PLGFVLAVTI IREAVEEIRC YLRDKEVNSQ VYSRLTARGT VKVKSSSIQV GDLIIVEKNQ
RVPADMIFLR TSEKNGSCFL RTDQLDGETD WKLRLPVACT QRLPTAADLL QIRSYVYAEE
PNIDIHNFVG TFTREDSDPP ISESLSIENA LWAGTVIASG TVVGVVLYTG RELRSVMNTS
NPRSKIGLFD LEVNCLTKIL FGALVVVSLV MVALQRFAGR WYLQIVRFLL LFSNIIPISL
RVNLDMGKIV YSWVIRRDAK VPGTVVRSST IPEQLGRISY LLTDKTGTLT QNEMVFKRLH
LGTVAYGLDS MDEVQSHIFS IYTQQSQDPP AQKGPTLTTK VRRTMSSRVH EAVKAIALCH
NVTPVYESNG VTDQAEAEKQ YEDSCRVYQA SSPDEVALVQ WTESVGLTLV GRDQSSMQLR
TPGDQILNFT ILQLFPFTYE 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 VITLVSCLPL YVLKYLRRRF SPPSYSKLTS
//
