ATP10D

Protein identityUniProt · HPA

UniProt accession

Q9P241

Gene

ATP10D

Ensembl

ENSG00000145246

Chromosome

4

Canonical length

1426 aa

Protein class

Enzymes, Predicted membrane proteins, Transporters

Subcellular location

Nucleoplasm,Plasma membrane

OverviewNCBI Gene

Enables glycosylceramide flippase activity. Predicted to be involved in phospholipid translocation. Located in endoplasmic reticulum; nucleoplasm; and plasma membrane. Part of phospholipid-translocating ATPase complex. [provided by Alliance of Genome Resources, Jul 2025]

Canonical amino-acid sequenceUniProt

1426 residues, UniProt reviewed canonical sequence.

>Q9P241|ATP10D
     1  MTEALQWARY HWRRLIRGAT RDDDSGPYNY SSLLACGRKS SQTPKLSGRH RIVVPHIQPF
    61  KDEYEKFSGA YVNNRIRTTK YTLLNFVPRN LFEQFHRAAN LYFLFLVVLN WVPLVEAFQK
   121  EITMLPLVVV LTIIAIKDGL EDYRKYKIDK QINNLITKVY SRKEKKYIDR CWKDVTVGDF
   181  IRLSCNEVIP ADMVLLFSTD PDGICHIETS GLDGESNLKQ RQVVRGYAEQ DSEVDPEKFS
   241  SRIECESPNN DLSRFRGFLE HSNKERVGLS KENLLLRGCT IRNTEAVVGI VVYAGHETKA
   301  MLNNSGPRYK RSKLERRANT DVLWCVMLLV IMCLTGAVGH GIWLSRYEKM HFFNVPEPDG
   361  HIISPLLAGF YMFWTMIILL QVLIPISLYV SIEIVKLGQI YFIQSDVDFY NEKMDSIVQC
   421  RALNIAEDLG QIQYLFSDKT GTLTENKMVF RRCSVAGFDY CHEENARRLE SYQEAVSEDE
   481  DFIDTVSGSL SNMAKPRAPS CRTVHNGPLG NKPSNHLAGS SFTLGSGEGA SEVPHSRQAA
   541  FSSPIETDVV PDTRLLDKFS QITPRLFMPL DETIQNPPME TLYIIDFFIA LAICNTVVVS
   601  APNQPRQKIR HPSLGGLPIK SLEEIKSLFQ RWSVRRSSSP SLNSGKEPSS GVPNAFVSRL
   661  PLFSRMKPAS PVEEEVSQVC ESPQCSSSSA CCTETEKQHG DAGLLNGKAE SLPGQPLACN
   721  LCYEAESPDE AALVYAARAY QCTLRSRTPE QVMVDFAALG PLTFQLLHIL PFDSVRKRMS
   781  VVVRHPLSNQ VVVYTKGADS VIMELLSVAS PDGASLEKQQ MIVREKTQKH LDDYAKQGLR
   841  TLCIAKKVMS DTEYAEWLRN HFLAETSIDN REELLLESAM RLENKLTLLG ATGIEDRLQE
   901  GVPESIEALH KAGIKIWMLT GDKQETAVNI AYACKLLEPD DKLFILNTQS KDACGMLMST
   961  ILKELQKKTQ ALPEQVSLSE DLLQPPVPRD SGLRAGLIIT GKTLEFALQE SLQKQFLELT
  1021  SWCQAVVCCR ATPLQKSEVV KLVRSHLQVM TLAIGDGAND VSMIQVADIG IGVSGQEGMQ
  1081  AVMASDFAVS QFKHLSKLLL VHGHWCYTRL SNMILYFFYK NVAYVNLLFW YQFFCGFSGT
  1141  SMTDYWVLIF FNLLFTSAPP VIYGVLEKDV SAETLMQLPE LYRSGQKSEA YLPHTFWITL
  1201  LDAFYQSLVC FFVPYFTYQG SDTDIFAFGN PLNTAALFIV LLHLVIESKS LTWIHLLVII
  1261  GSILSYFLFA IVFGAMCVTC NPPSNPYWIM QEHMLDPVFY LVCILTTSIA LLPRFVYRVL
  1321  QGSLFPSPIL RAKHFDRLTP EERTKALKKW RGAGKMNQVT SKYANQSAGK SGRRPMPGPS
  1381  AVFAMKSASS CAIEQGNLSL CETALDQGYS ETKAFEMAGP SKGKES

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against ATP10D 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)

0.34

Highest tissue expression

14 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about ATP10D.

Disease | ImmuneIEDB

Conditions an epitope on ATP10D was assayed in.

• melanoma T cell

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)

0.79

gnomAD pLI

0

gnomAD missense Z

0.66

DepMap mean gene effect

-0.02

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• monoatomic cation transport
• monoatomic ion transmembrane transport
• phospholipid translocation

Molecular functions

• ATP binding
• ATP hydrolysis activity
• ATPase-coupled intramembrane lipid transporter activity
• glycosylceramide flippase activity
• magnesium ion binding

Cellular components

• endoplasmic reticulum
• endoplasmic reticulum membrane
• membrane
• nucleoplasm
• phospholipid-translocating ATPase complex
• plasma membrane

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, cytoplasmic domain N
• Phospholipid-translocating ATPase N-terminal
• Phospholipid-translocating P-type ATPase C-terminal

KeywordsUniProt

• ATP-binding
• Cell membrane
• Endoplasmic reticulum
• Lipid transport
• Magnesium
• Membrane
• Metal-binding
• Nucleotide-binding
• Translocase
• Transmembrane
• Transmembrane helix
• Transport

InteractionsUniProt · HPA

Protein binding partners of ATP10D in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• TMEM30A