ID K7GKR3_PIG Unreviewed; 995 AA.
AC K7GKR3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 60.
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:ENSSSCP00000028440.2};
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:ENSSSCP00000028440.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000028440.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000028440.2,
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:ENSSSCP00000028440.2}
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 AlphaFoldDB; K7GKR3; -.
DR PeptideAtlas; K7GKR3; -.
DR Ensembl; ENSSSCT00000032685.4; ENSSSCP00000028440.2; ENSSSCG00000007478.6.
DR GeneTree; ENSGT00940000159181; -.
DR HOGENOM; CLU_105546_0_0_1; -.
DR Proteomes; UP000008227; Chromosome 17.
DR Bgee; ENSSSCG00000007478; Expressed in prefrontal cortex and 44 other cell types or tissues.
DR ExpressionAtlas; K7GKR3; baseline and differential.
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; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:K7GKR3};
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 101..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 298..321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 819..842
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 898..919
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 926..946
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 952..978
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 46..106
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 807..987
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 995 AA; 112817 MW; FEA7FCB150948A1B CRC64;
MTDNIPLQPV RQKKRMDSRP RAGCCEWLRC CGAGEPRPRT VWLGHPEKRD QRYPRNVINN
QKYNFFTFLP GVLFNQFKYF FNLYFLLLAC SQFVPEMRLG ALYTYWVPLG FVLAVTIIRE
AVEEIRCYLR DKEVNSQVYS RLTARGTVKV KSCSIQVGDL IIVEKNQRVP ADMIFLRTSE
KNGSCFLRTD QLDGETDWKL RLPVACTQRL PTAADLLQIR SYVYAEEPNI DIHNFVGTFT
REDSDPPISE SLSIENTLWA GTVIASGTVV GVVLYTGREL RSVMNTSNPR SKIGLFDLEV
NCLTKILFGA LVVVSLVMVA LQHFAGRWYL QIIRFLLLFS NIIPISLRVN LDMGKIVYSW
VIRRDSKIPG TVVRSSTIPE QLGRISYLLT DKTGTLTQNE MVFKRLHLGT VAYGLDSMDE
VQSHIFSIYT QQPQDPPAQK GPALTTKVRR TMSSRVHEAV KAIALCHNVT PVYESNGVTD
QAEAEKQYED SCRVYQASSP DEVALVQWTE SVGLTLVGRD QSSMQLRTPG DQILNFTILQ
IFPFTYESKR MGIIVRDEST GEITFYMKGA DVVMAGIVQY NDWLEEECGN MAREGLRVLV
VAKKSLAEEQ YQDFEARYVQ AKLSVHDRSL KVATVIESLE MEMELLCLTG VEDQLQADVR
PTLETLRNAG IKVWMLTGDK LETATCTAKN AHLVTRNQDI HIFRLVTNRG EAHLELNAFR
RKHDCALVIS GDSLEVCLKY YEYEFMELAC QCPAVVCCRC APTQKAQIVR LLQERTGKLT
CAVGDGGNDV SMIQESDCGV GVEGKAVFSS VFYFASVPLY QGFLIIGYST IYTMFPVFSL
VLDKDVKSEV AMLYPELYKD LLKGRPLSYK TFLIWVLISI YQGSTIMYGA LLLFESEFVH
IVAISFTSLI LTELLMVALT IQTWHWLMTV AELLSLACYI ASLVFLHEFI DVYFIATLSF
LWKVSVITLV SCLPLYVLKY LRRRFSPPSY SKLTS
//
