ID M3XFQ5_FELCA Unreviewed; 1120 AA.
AC M3XFQ5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 3.
DT 24-JAN-2024, entry version 72.
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:ENSFCAP00000025466.3,
GN ECO:0000313|VGNC:VGNC:79997};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000025466.3, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000025466.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025466.3,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000025466.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025466.3,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000025466.3}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025466.3};
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 EMBL; AANG04000928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3XFQ5; -.
DR STRING; 9685.ENSFCAP00000025466; -.
DR PaxDb; 9685-ENSFCAP00000025466; -.
DR Ensembl; ENSFCAT00000029234.4; ENSFCAP00000025466.3; ENSFCAG00000022069.4.
DR VGNC; VGNC:79997; ATP9A.
DR eggNOG; KOG0210; Eukaryota.
DR GeneTree; ENSGT00940000159181; -.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; M3XFQ5; -.
DR OMA; XVYFIAT; -.
DR Proteomes; UP000011712; Chromosome A3.
DR Bgee; ENSFCAG00000022069; Expressed in prefrontal cortex and 9 other cell types or tissues.
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; 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:UP000011712};
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..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 125434 MW; 062952CFE0DB7953 CRC64;
MVRPCPSVGP RGRLRAWPGA RELAPSLRAR PARCRRLLPR GGAAPAGGGA EAGPGGGPGG
AGGAAAKAGG AGDMTDNIPL QPVRQKKRMD SRPRAGCCEW LRCCGGGEPR PRTVWLGHPE
KRDQRYPRNV INNQKYNVFT FLPGVLFNQF KYFFNLYFLL LACSQFVPEM RLGALYTYWV
PLGFVLAVTV IREAVEEIRC YVRDREVNCQ VFSRLTARGT VKVKSSNIQV GDLIIVEKNQ
RVPADMIFLR TSEKNGSCFL RTDQLDGETD WKLRLPVACA QRLPTAADLL QIRSYVYAEE
PNIDIHNFVG TFTREDSDPP ISESLSIENT LWAGTVIASG TVVGVVLYTG RELRSVMNTS
NPRSKIGLFD LEVNCLTKIL FGALVVVSLV MVALQHFAGR WYLQIIRFLL LFSNIIPISL
RVNLDMGKIV YSWVIRRDSK IPGTVVRSST IPEQLGRISY LLTDKTGTLT QNEMVFKRLH
LGTVAYGLDS MDEVQSHIFS IYTQQSQDPP AQKGPTLTTK VRRTMSSRVH EAVKAIALCH
NVTPVYESNG ATDQAEAEKR YEDSCRVYQA SSPDEVALVQ WTESVGLTLV GRDQSSMQLR
TPGDQILNFT ILQIFPFTYE SKRMGIIVRD ESTGEITFYM KGADVVMAGI VQYNDWLEEE
CGNMAREGLR VLVVAKKSLA EEQYQDFEAR YVQAKLSVHD RSLKVATVIE SLEMEMGLLC
LTGVEDQLQA DVRPTLETLR NAGIKVWMLT GDKLETATCT AKNAHLVTRN QDIHVFRLVT
NRSEAHLELN AFRRKHDCAL VISGDSLEIC LKYYEYEFME LACQCPAVVC CRCTPTQKAQ
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
//
