ATP8A1

Protein identityUniProt · HPA

UniProt accession

Q9Y2Q0

Gene

ATP8A1

Ensembl

ENSG00000124406

Chromosome

4

Canonical length

1164 aa

Protein class

Enzymes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins, Predicted membrane proteins, Transporters

Subcellular location

Vesicles,Cytosol

OverviewNCBI Gene

The P-type adenosinetriphosphatases (P-type ATPases) are a family of proteins which use the free energy of ATP hydrolysis to drive uphill transport of ions across membranes. Several subfamilies of P-type ATPases have been identified. One subfamily catalyzes transport of heavy metal ions. Another subfamily transports non-heavy metal ions (NMHI). The protein encoded by this gene is a member of the third subfamily of P-type ATPases and acts to transport amphipaths, such as phosphatidylserine. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

1164 residues, UniProt reviewed canonical sequence.

>Q9Y2Q0|ATP8A1
     1  MPTMRRTVSE IRSRAEGYEK TDDVSEKTSL ADQEEVRTIF INQPQLTKFC NNHVSTAKYN
    61  IITFLPRFLY SQFRRAANSF FLFIALLQQI PDVSPTGRYT TLVPLLFILA VAAIKEIIED
   121  IKRHKADNAV NKKQTQVLRN GAWEIVHWEK VAVGEIVKVT NGEHLPADLI SLSSSEPQAM
   181  CYIETSNLDG ETNLKIRQGL PATSDIKDVD SLMRISGRIE CESPNRHLYD FVGNIRLDGH
   241  GTVPLGADQI LLRGAQLRNT QWVHGIVVYT GHDTKLMQNS TSPPLKLSNV ERITNVQILI
   301  LFCILIAMSL VCSVGSAIWN RRHSGKDWYL NLNYGGASNF GLNFLTFIIL FNNLIPISLL
   361  VTLEVVKFTQ AYFINWDLDM HYEPTDTAAM ARTSNLNEEL GQVKYIFSDK TGTLTCNVMQ
   421  FKKCTIAGVA YGHVPEPEDY GCSPDEWQNS QFGDEKTFSD SSLLENLQNN HPTAPIICEF
   481  LTMMAVCHTA VPEREGDKII YQAASPDEGA LVRAAKQLNF VFTGRTPDSV IIDSLGQEER
   541  YELLNVLEFT SARKRMSVIV RTPSGKLRLY CKGADTVIYD RLAETSKYKE ITLKHLEQFA
   601  TEGLRTLCFA VAEISESDFQ EWRAVYQRAS TSVQNRLLKL EESYELIEKN LQLLGATAIE
   661  DKLQDQVPET IETLMKADIK IWILTGDKQE TAINIGHSCK LLKKNMGMIV INEGSLDGTR
   721  ETLSRHCTTL GDALRKENDF ALIIDGKTLK YALTFGVRQY FLDLALSCKA VICCRVSPLQ
   781  KSEVVEMVKK QVKVVTLAIG DGANDVSMIQ TAHVGVGISG NEGLQAANSS DYSIAQFKYL
   841  KNLLMIHGAW NYNRVSKCIL YCFYKNIVLY IIEIWFAFVN GFSGQILFER WCIGLYNVMF
   901  TAMPPLTLGI FERSCRKENM LKYPELYKTS QNALDFNTKV FWVHCLNGLF HSVILFWFPL
   961  KALQYGTAFG NGKTSDYLLL GNFVYTFVVI TVCLKAGLET SYWTWFSHIA IWGSIALWVV
  1021  FFGIYSSLWP AIPMAPDMSG EAAMLFSSGV FWMGLLFIPV ASLLLDVVYK VIKRTAFKTL
  1081  VDEVQELEAK SQDPGAVVLG KSLTERAQLL KNVFKKNHVN LYRSESLQQN LLHGYAFSQD
  1141  ENGIVSQSEV IRAYDTTKQR PDEW

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against ATP8A1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Cell surface

Secreted

No

Transmembrane segments

10

Mean surface accessibility (rSASA)

0.25

Highest tissue expression

37 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about ATP8A1.

Disease | GeneticClinVar

1 pathogenic / likely-pathogenic of 131 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Hypercholesterolemia, familial, 1

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.35

gnomAD pLI

0.2

gnomAD missense Z

2.61

DepMap mean gene effect

0.02

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• aminophospholipid translocation
• learning
• monoatomic ion transmembrane transport
• phospholipid translocation
• positive regulation of cell migration
• positive regulation of phospholipid translocation
• synaptic vesicle endocytosis
• transport across blood-brain barrier

Molecular functions

• ATP binding
• ATP hydrolysis activity
• ATPase-coupled intramembrane lipid transporter activity
• ATPase-coupled monoatomic cation transmembrane transporter activity
• magnesium ion binding
• phosphatidylserine flippase activity
• phosphatidylserine floppase activity

Cellular components

• azurophil granule membrane
• chromaffin granule membrane
• cytoplasmic vesicle
• cytosol
• endoplasmic reticulum
• extracellular exosome
• glutamatergic synapse
• Golgi apparatus
• membrane
• organelle membrane
• phospholipid-translocating ATPase complex
• plasma membrane
• specific granule membrane
• synaptic vesicle membrane
• trans-Golgi network

Protein domainsUniProt · Pfam · InterPro

• P-type ATPase
• P-type ATPase, subfamily IV
• P-type ATPase, A domain superfamily
• P-type ATPase, phosphorylation site
• HAD superfamily
• P-type ATPase, transmembrane domain superfamily
• P-type ATPase, cytoplasmic domain N
• P-type ATPase, C-terminal
• P-type ATPase, N-terminal
• HAD-like superfamily
• P-type ATPase, haloacid dehalogenase domain
• P-type ATPase, A domain
• P-type ATPase actuator domain
• P-type ATPase, cytoplasmic domain N
• Phospholipid-translocating ATPase N-terminal
• Phospholipid-translocating P-type ATPase C-terminal

KeywordsUniProt

• ATP-binding
• Cell membrane
• Cytoplasmic vesicle
• Endoplasmic reticulum
• Golgi apparatus
• Lipid transport
• Magnesium
• Membrane
• Metal-binding
• Nucleotide-binding
• Phosphoprotein
• Translocase
• Transmembrane
• Transmembrane helix
• Transport

InteractionsUniProt · HPA

Protein binding partners of ATP8A1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• TMEM30A
• TMEM30B