ID H9GFQ2_ANOCA Unreviewed; 1187 AA.
AC H9GFQ2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP8B1 {ECO:0000313|Ensembl:ENSACAP00000009666.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000009666.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000009666.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000009666.4};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000009666.4}
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; H9GFQ2; -.
DR STRING; 28377.ENSACAP00000009666; -.
DR Ensembl; ENSACAT00000009863.4; ENSACAP00000009666.4; ENSACAG00000009654.4.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000158002; -.
DR HOGENOM; CLU_000846_5_2_1; -.
DR OrthoDB; 275833at2759; -.
DR TreeFam; TF300654; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000009654; Expressed in dewlap and 9 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
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; 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:SF48; PHOSPHOLIPID-TRANSPORTING ATPASE IC; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001646};
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 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 339..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 389..408
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 939..960
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 972..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1022..1043
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1058..1075
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1082..1102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1133..1160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 69..145
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 908..1162
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 818..848
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..38
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1187 AA; 136130 MW; D2D4F1EC493EA79F CRC64;
MNSERDSETT FDEDSSQPND EEVPYSDDET EDELDIQPAV EPEQNRINRE VEATRETLRK
DCNWQVKAND RAFHEQPQFM KTEYLCLKKS KYAGNAIKTY KYNPITFLPL NLFEQFKRAA
NFYFLVLLIL QTIPQITTLS WYTTLIPLLL VLGITAIKDL VDDVARHRMD NEINNRNCDV
IREERFINAK WKDIKVGDVI RLGKNAFVPA DILLLSSSEP HSLCYVETAE LDGETNLKFK
MSLDVTDRYL QEERALAAFD GLVECEEPNN RLDKFTGTLI WKGRRYGLDA DKILLRGCKI
RNTDVCHGLV IFAGADTKIM RNSGKTRFKR TKIDSLMNYM VYTIFILLIL VSAGLAIGHT
YWEQQIGNSS WYLYDGKDYT PSYRGFLNFW GYIIVLNTMV PISLYVSVEV IRLGQSYFIN
WDLQMYYPPK DTPAKARTTT LNEQLGQIHY IFSDKTGTLT QNIMAFKKCC ISGETYVQQV
NSDFSWNMYA DGKLTFHDQY LIEKIKQGKE PEIRQFFFLL ALCHTVMVDN SDGELNYQAA
SPDEGALVTA ARNFGFVFLS RTQNTITISE MGTVKTYDVL AILDFNSDRK RMSVITREPN
GAIRLYCKGA DTVIYERLHR NDPQKQTTER ALDIFASETL RTLCLCYKDI SNEEYEAWNK
KFMAASVALR NRDEALDKVY EEIEQNLILL GATAIEDKLQ DGVPETISKL SKADIKIWVL
TGDKKETAEN IGFSCELLTD ETTIYYGENI SALLQTRLEN QKNRTGSNAN SSHGDNENFF
PPGGNRALII TGSWLNEILL EKKKKKKKLL KLKFPRTMEE KQKQMESKRR AELNKEQQQR
NFVDLACECN SVICCRVTPK QKAMVVDLVK RYKKAITLAI GDGANDVNMI KTAHIGVGIS
GQEGMQAVMS SDYSFGQFRY LQRLLLVHGR WSYIRMCKFL RYFFYKNFAF TLVHFWYSFF
NGYSAQTAYE DWFITLYNVL YSSLPVLLVG LLDQDVSDKL SIRFPSLYIL GQRDLLFNYR
KFFISLFHGV VTSLIIFFIP YGAYLQTMGE DGEAPSDYQS FAVTAASSLI IAVNFQMGLD
TSYWTFVNAF SIFGSIALYF GITFDLHSSG IHVLFPSAFQ FTGTAPNALR QPYIWLTIIL
SVAICLLPVV ALRFLTMTIW PTESDKVRRQ KGSSAPHSRT SFSMNRG
//
