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Database: UniProt
Entry: A0A5F5XKV0_FELCA
LinkDB: A0A5F5XKV0_FELCA
Original site: A0A5F5XKV0_FELCA 
ID   A0A5F5XKV0_FELCA        Unreviewed;      1372 AA.
AC   A0A5F5XKV0;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=ATP8B3 {ECO:0000313|Ensembl:ENSFCAP00000054662.1,
GN   ECO:0000313|VGNC:VGNC:82323};
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:ENSFCAP00000054662.1, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000054662.1, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000054662.1,
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:ENSFCAP00000054662.1, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000054662.1,
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:ENSFCAP00000054662.1}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000054662.1};
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; AANG04002859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSFCAT00000082513.1; ENSFCAP00000054662.1; ENSFCAG00000002436.6.
DR   VGNC; VGNC:82323; ATP8B3.
DR   GeneTree; ENSGT00940000160463; -.
DR   Proteomes; UP000011712; Chromosome A2.
DR   Bgee; ENSFCAG00000002436; Expressed in testis and 4 other cell types or tissues.
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; 1.
DR   PANTHER; PTHR24092:SF78; PHOSPHOLIPID-TRANSPORTING ATPASE IK; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_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:UP000011712};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1372
FT                   /note="Phospholipid-transporting ATPase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5023934845"
FT   TRANSMEM        170..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        318..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        367..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        954..974
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        986..1006
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1034..1057
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1077..1097
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1104..1127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1147..1169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          102..175
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          923..1172
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          32..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1263..1304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1318..1372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1372 AA;  154132 MW;  45A758AD2898B882 CRC64;
     MGRNGGRRGD LGLLAWELLG VRLSQVWGAA GAPPGLRTAR EGHVRRLERQ SPGAGQRSGH
     RPGCWCDLGP SPRSPTSMGS LAYREDLEEE KNSAFTWELE ANSRDYNSQF KEKSFLCWQR
     RKYKSNVIHT AKYSVFSFLP LNLYEQFHRV SNLYFLFIII LQGLPEISTL PWFTLFVPLI
     CLLVIRATRD LVDDIGRHRS DRVINNRPCQ ILVGKSFLWR KWEDLYVGDV VCLHKDNIVP
     ADLLLLASTE PSSLCYVETA DIDGETNLKF RQAPPVTHHE LTSIRKMASF QGFDTKIMRN
     CGKIHPKRSR IDRLLNRLVA LIFLFLVLIS VALSLGFWFK VKEFKAKHHY VSPRHVQSVA
     AETFLTFWGF FILLSVMVPM AMFIMVEFIY LGNSMFINWD VQMYYAPQDV PAKARSTSLN
     DQLGQVGYVF SDKTGTLTQN VMTFKKCCIG GIVYGPDDEE AAPCKGSPYL WNKFADGKFP
     YRNAELLRAV RGRTDEAVRE FWRLLAICHT VMVQEKDHQP VYQAASPDEE ALVTAARNFG
     YVFVARTRDS ITVMELGDKR VYQVLAMMDF NSMRKRMSVL VRNPEGAIYL YTKGADVVIF
     ERLSKKGMTE WTTEEALASF AEETLRTLCL AYKRVDEDTY EEWRQRHREA SLRLQNRAHA
     LHQVYEEMEK GLQLLGATAI EDRLQDGVCD TIQCLKQGNI KVWVLTGDKQ ETAVNIGFAC
     QLLSENMLVL EEKEITRILE AHWGSDDGLL AGQGPLQSRF LQQTKVAMVI NGEFLDQLLL
     SLRKEPRALV RDEDVDVDVE EAWQEPGERT TNFLRAQRVS LMWRTLGTQL RGTGLGPRVV
     KDSGARDGPE VRRERAFVEL AARCQAVICC RVTPKQKALI VALVKKYQRA VTLAIGDGAN
     DVNMIKTADI GVGLAGPEGM QAVQNSDYAL AQFCFLKRLL LVHGRWSYVR VCKFLRYFVY
     KTLATMMAQV WFAFYSGFTA QPLYEGWFLA LFNLLFSTLP VLYIGLFEQD VSAERSLQLP
     QLYIAGQEDE LFNYWVFLQA LAHGTATSLV NFFVTLWVSH DSAGPTSFSD YQSFSEVVAL
     SSLLSITVEA ILIIKYWTAL SVLAILLSFC FYMVVTWGCQ SFWLFQISPE TFPFLYADRN
     VLSHPSILLV ILLNVSLNTL PTLALRVIYQ ALEKPRPKEV EEAPSEDITA VEAAPYLRRE
     SRRRRSSYAF SHREGYAELI TQGTILRRAP GVDSDMLMGQ IIPCHEELSP SIQESPRCSR
     KMSFLGKTGR QHRGKVSSRD GGRAARRPQI PGSPRGLAVR GVPGDVAGGA GGLTVVQGER
     AGAVGGSPAP PAARGRGGQG VPRGVTAGAR GGRSGARGGG AAPPRPPTPE EQ
//
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