AT8B1_XENTR
ID AT8B1_XENTR Reviewed; 1250 AA.
AC Q5BL50;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phospholipid-transporting ATPase IC;
DE EC=7.6.2.1;
DE AltName: Full=ATPase class I type 8B member 1;
DE AltName: Full=P4-ATPase flippase complex alpha subunit atp8b1;
GN Name=atp8b1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic component of a P4-ATPase flippase complex which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC aminophospholipids from the outer to the inner leaflet of various
CC membranes and ensures the maintenance of asymmetric distribution of
CC phospholipids (By similarity). Phospholipid translocation seems also to
CC be implicated in vesicle formation and in uptake of lipid signaling
CC molecules. May also participate in the establishment of the canalicular
CC membrane integrity by ensuring asymmetric distribution of phospholipids
CC in the canicular membrane (By similarity).
CC {ECO:0000250|UniProtKB:O43520, ECO:0000250|UniProtKB:Q148W0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:O43520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O43520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000250|UniProtKB:O43520};
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit and an accessory beta subunit. The flippase
CC ATP8B1:TMEM30A complex can form an intermediate phosphoenzyme in vitro.
CC Also interacts with beta subunit TMEM30B.
CC {ECO:0000250|UniProtKB:O43520}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43520};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O43520}. Apical cell
CC membrane {ECO:0000250|UniProtKB:O43520}. Cell projection, stereocilium
CC {ECO:0000250|UniProtKB:Q148W0}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O43520}. Golgi apparatus
CC {ECO:0000250|UniProtKB:O43520}. Note=Exit from the endoplasmic
CC reticulum requires the presence of TMEM30A or TMEM30B. Localizes to
CC apical membranes in epithelial cells. {ECO:0000250|UniProtKB:O43520}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
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DR EMBL; BC090602; AAH90602.1; -; mRNA.
DR RefSeq; NP_001025562.1; NM_001030391.1.
DR AlphaFoldDB; Q5BL50; -.
DR SMR; Q5BL50; -.
DR STRING; 8364.ENSXETP00000045089; -.
DR DNASU; 594952; -.
DR GeneID; 594952; -.
DR KEGG; xtr:594952; -.
DR CTD; 5205; -.
DR Xenbase; XB-GENE-490143; atp8b1.
DR eggNOG; KOG0206; Eukaryota.
DR InParanoid; Q5BL50; -.
DR OrthoDB; 587717at2759; -.
DR Reactome; R-XTR-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000020878; Expressed in 4-cell stage embryo and 10 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0140346; F:phosphatidylserine flippase activity; ISS:UniProtKB.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR GO; GO:0045176; P:apical protein localization; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:2001225; P:regulation of chloride transport; ISS:UniProtKB.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030346; ATP8B1.
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 PANTHER; PTHR24092:SF48; PTHR24092:SF48; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Cell projection; Endoplasmic reticulum;
KW Golgi apparatus; Lipid transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1250
FT /note="Phospholipid-transporting ATPase IC"
FT /id="PRO_0000370863"
FT TOPO_DOM 1..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..338
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..956
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 957..977
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 978..980
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 981..1001
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1002..1034
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1035..1055
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1056..1069
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1070..1090
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1091..1092
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1093..1113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1114..1117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1118..1138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1139..1140
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1141..1161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1162..1250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 454
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 891
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 895
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1250 AA; 142665 MW; D6957B3D9D6CCB7B CRC64;
MDTDYESTYE DDSQVPNDDV VPYSDDETDD ELDSPQTDEP EQNRRNVQAE QSREPVIKEC
TWQVKANDRN FYDQPEFKKK VFLCLKKSKY AGNAIKTYKY NPITFLPVNL YEQFKRAANA
YFLVLLILQT IPQISTVTWS TTLIPLLLVL GITAIKDLVD DIARHKMDNE INNRPSEVIT
DGRFKKTKWK HIHVGDIIRI NKNEFVPADV LLLSSSDPNS LCYVETAELD GETNLKFKMS
LEITDKLLQK EEQLAGFDGL VECEEPNNRL DKFVGTLFWR GNSFGLDADK ILLRGCTVRN
TEYCHGLVLF AGADTKIMRN SGKTRLKRTK IDYLMNYMVY TIFVLLILAA AGLAIGQTFW
EAKLGAANVS WYLYDGNNYS PSYRGFLAFW GYIIVLNTMV PISLYVSVEV IRLGQSYFIN
WDLQMYFSPK DTPAKARTTT LNEQLGQIQY IFSDKTGTLT QNIMTFKKCT INGTTYGDDD
DELKSGQTKQ VDFSWNPLAD PSFTFHDNYL IEQIRAGKDK DVYEFFKLLA LCHTVMAEKT
DGELIYQAAS PDEGALVTAA RNFGFVFLSR TQSTITISEL GQEKTYEVLA ILDFNSDRKR
MSIIVRQPDG RIRLYCKGAD TVIYERLHPD NPIKDQTQKA LDIFANASLR TLCLCYKDIN
KGDFENWSKK YKQASVATSN RDEALDRVYE AIETDLKLLG ATAIEDKLQD DVSGTIFNLA
RADIKIWVLT GDKKETAENI GYSCKLLDDD TEILYGEDIN VHLQTRMENQ RNQMSGNQGA
QSNQSGAFLP TDKKHALIIT GSWLNEILLE KKKRKKKRLK LKFPRTKEEK EQQLHEKLKA
YALKEQRQRS FVDLACECSA VICCRVTPKQ KAMVVDLVKR YKKAVTLAIG DGANDVNMIK
TAHIGVGISG QEGMQAVMSS DYSFAQFRYL QRLLLVHGRW SYIRMCKFLR YFFYKNFSFT
LVHFWYSFFN GFSAQTVYED WFITLYNVLY SSLPVLLVGL LDQDVSDKLS LAFPRLYVPG
QKDLLFNYKK FFLSLFHGIV TSLIIFFIPY GAFLLTMGQD GEAPSDYQSF AVTTATALVI
TVNFQIGLDT SYWTFVNAFS IFGSIAIYFG IMFDLHSAGI HVLFPSMFIF TGAAPNALRQ
PYLWLTIILT VAFCLLPIVA LRFLAKTIWP SESDKIQKKG KKFKAEVEQR AKPKPFARGV
STRRSAYAFS HQRGYADLIS SGRSIRKKRA SLDAVFDNYP AQITHFTPQT
