ID A0A2R9AAA6_PANPA Unreviewed; 1162 AA.
AC A0A2R9AAA6;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
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=ATP8A2 {ECO:0000313|Ensembl:ENSPPAP00000012377.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000012377.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000012377.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000012377.1}
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 EMBL; AJFE02062797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02062798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02062799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02062800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02062801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02062802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02062803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02062804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02062805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02062806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9AAA6; -.
DR STRING; 9597.ENSPPAP00000012377; -.
DR Ensembl; ENSPPAT00000035042.1; ENSPPAP00000012377.1; ENSPPAG00000029372.1.
DR GeneTree; ENSGT00940000157332; -.
DR OMA; DMMIYQR; -.
DR Proteomes; UP000240080; Chromosome 13.
DR Bgee; ENSPPAG00000029372; Expressed in cerebellum and 2 other cell types or tissues.
DR GO; GO:0005794; C:Golgi apparatus; 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; 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; 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; 2.
DR PANTHER; PTHR24092:SF98; PHOSPHOLIPID-TRANSPORTING ATPASE IB; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_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 Lipid transport {ECO:0000256|ARBA:ARBA00023055};
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:UP000240080};
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}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TRANSMEM 289..313
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 333..356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 861..881
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 887..905
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 934..952
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 972..991
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1003..1023
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1043..1063
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 32..95
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 822..1072
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1162 AA; 130802 MW; E89985A4BE520059 CRC64;
PVRSSLGYKK AEDEMSRATS VGDQLEAPAR TIYLNQPHLN KFRDNQISTA KYSVLTFLPR
FLYEQIRRAA NAFFLFIALL QQIPDVSPTG RYTTLVPLII ILTIAGIKEI VEDFKRHKAD
NAVNKKKTIV LRNGMWHTIM WKEVAVGDIV KVVNGQYLPA DVVLLSSSEP QAMCYVETAN
LDGETNLKIR QGLSHTADMQ TREVLMKLSG TIECEGPNRH LYDFTGNLNL DGKSLVALGP
DQILLRGTQL RNTQWVFGIV VYTGHDTKLM QNSTKAPLKR SNVEKVTNVQ ILVLFGILLV
MALVSSAGAL YWNRSHGEKN WYIKKMDTTS DNFGYNLLTF IILYNNLIPI SLLVTLEVVK
YTQALFINWD TDMYYIGNDT PAMARTSNLN EELGQVKYLF SDKTGTLTCN IMNFKKCSIA
GVTYGHFPEL AREPSSDDFC RMPPPCSDSC DFDDPRLLKN IEDRHPTAPC IQEFLTLLAV
CHTVVPEKDG DNIIYQASSP DEAALVKGAK KLGFVFTART PFSVIIEAMG QEQTFGILNV
LEFSSDRKRM SVIVRTPSGR LRLYCKGADN VIFERLSKDS KYMEETLCHL EYFATEGLRT
LCVAYADLSE NEYEEWLKVY QEASTILKDR AQRLEECYEI IEKNLLLLGA TAIEDRLQAG
VPETIATLLK AEIKIWVLTG DKQETAINIG YSCRLVSQNM ALILLKEDSL DATRAAITQH
CTDLGNLLGK ENDVALIIDG HTLKYALSFE VRRSFLDLAL SCKAVICCRV SPLQKSEIVD
VVKKRVKAIT LAIGDGANDV GMIQTAHVGV GISGNEGMQA TNNSDYAIAQ FSYLEKLLLV
HGAWSYNRVT KCILYCFYKN VVLYIIELWF AFVNGFSGQI LFERWCIGLY NVIFTALPPF
TLGIFERSCT QESMLRFPQL YKITQNGEGF NTKVFWGHCI NALVHSLILF WFPMKALEHD
TVLTSGHATD YLFVGNIVYT YVVVTVCLKA GLETTAWTKF SHLAVWGSML TWLVFFGIYS
TIWPTIPIAP DMRGQATMVL SSAHFWLGLF LVPTACLIED VAWRAAKHTC KKTLLEEVQE
LETKSRVLGK AVLRDSNGKR LNERDRLIKR LGRKTPPTLF RGSSLQQGVP HGYAFSQEEH
GAVSQEEVIR AYDTTKKKSR KK
//
