ID F1S3S6_PIG Unreviewed; 1423 AA.
AC F1S3S6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 3.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP10D {ECO:0000313|Ensembl:ENSSSCP00000009393.3,
GN ECO:0000313|VGNC:VGNC:98913};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000009393.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000009393.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000009393.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000009393.3}
RP IDENTIFICATION.
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 STRING; 9823.ENSSSCP00000009393; -.
DR PaxDb; 9823-ENSSSCP00000009393; -.
DR Ensembl; ENSSSCT00000009642.4; ENSSSCP00000009393.3; ENSSSCG00000008812.5.
DR VGNC; VGNC:98913; ATP10D.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000156728; -.
DR HOGENOM; CLU_000846_3_4_1; -.
DR InParanoid; F1S3S6; -.
DR TreeFam; TF354252; -.
DR Reactome; R-SSC-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000008227; Chromosome 8.
DR Bgee; ENSSSCG00000008812; Expressed in oocyte and 46 other cell types or tissues.
DR ExpressionAtlas; F1S3S6; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0140351; F:glycosylceramide flippase activity; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF84; PHOSPHOLIPID-TRANSPORTING ATPASE VD; 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; 2.
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:UP000008227};
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 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 124..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 322..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 371..392
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1114..1133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1145..1166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1196..1217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1223..1246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1253..1278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1298..1317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 66..123
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1082..1327
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 671..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1423 AA; 159216 MW; 5A518459E4915A6A CRC64;
MTEALQWARY HWQRLIGSTN TDDDERPYNY SSLLGCGGKS SQTPKVAGRH RVVVPHLRPF
KDEYEKFSGT YVNNRIRTTK YTLLNFVPRN LFEQFHRAAN LYFLFLVVLN WVPLVEAFQK
EITMLPLVVV LTIIAVKDGL EDYRKYKIDK RINNLVTKVY SSKEKKYVDR CWKDVTVGDF
IRLSCNEVIP ADMVLLFSTD PDGICHIETS GLDGESNLKQ RQVVRGYSEQ DSEVDPEKFS
SRIECESPNN DLNRFRGFLE HSNKERVGLS KENLLLRGCT IRNTEAVMGI VVYAGHETKA
MLNNSGPRYK RSKLERRANT DVLWCVLLLV IMCLTGALGH GIWLSRYKNI PFFNIPEPDG
HVTSPVLAGF YMFWTMIILL QVLIPISLYV SIEIVKLGQI YFIQSDVDFY NEKMDSTVQC
RALNITEDLG QIQYLFSDKT GTLTENKMVF RRCSVAGFDY CHEENAKRLE SYQEAVSEDE
DFADTLSGSL GNMAKPRTPS CRTVHNGPLG SKSSNHLSGS CFALGSGEGA GEVPHSRQAA
FSSPIETDVV PDTRLWDKCS QITPQLFTPL DDAVPDPPLE TLYIIDFFIA LAICNTVVVS
APNQPRQKIR LSSLSGMPIK SLEEIKNLFQ KLSVRRSSSP SLASGKEPFS GVPNAFVSRL
SLFSRMKPAS PLEEEISQTS ESPQGRGSLA CPTETEQQSS DEGITDGKVG SPPGQPSASS
LCYEAESPDE AALVYAARAY QCTLQSRTPE QVVVDFAALG PLTFQLLHIL PFDSVRKRMS
VVVRHPLSNQ VVVYTKGADS VIMELLSGAS PDGPSLEKQQ MMIREKTQKH LDDYAKQGLR
TLCIAKKVMS DTEYAEWLRS HFLAETSIDN KEELLLESAM RLENKLTLLG ATGIEDRLQE
GVPESIEALH KAGIKIWMLT GDKQETAVNI AYACKLLEPD DKLFILNTET KDACEVLMDT
ILKELQGKNP AAPERGPLSE DSQQPPGPQD PGLRAGLIIT GRTLEFALQE SLQRQFLELT
ACCRAVVCCR ATPLQKSEVV KLVRGHLRVM TLAIGDGAND VSMIQVADIG IGISGQEGMQ
AVMASDFAIS QFKHLSKLLL VHGHWCYTRL SNMILYFFYK NVAYVNLLFW YQFFCGFSGT
SMTDYWVLIF FNLLFTSAPP VIYGVLEKDV SAEMLLQLPE LYRSGQRSEA YLPHTFWITL
LDAFYQSLVC FFVPYYTYQG SDIDIFAFGN PLNTAALFII LLHLVIESKS LTWIHMLVIV
GSILCYFLFA LAFGAMCVTC NPPSNPYWIM QAHMLDPVFY LVCVLTTCIA LLPRFIYRVL
QGSLFPSPIL RAKHFDRLTA EERKEALKKW RGAGKMDPVT SKCADYSAAK SERIPISDPP
AVFTVMSSTS CVFEHGNLVV CETAIDSDSS KTKVSGMAGP SND
//
