Q9QZW0 · AT11C_MOUSE

  • Protein
    Phospholipid-transporting ATPase 11C
  • Gene
    Atp11c
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane (PubMed:24898253, PubMed:24904167, PubMed:26799398, PubMed:30018401).
Major PS-flippase in immune cell subsets (PubMed:30018401).
In erythrocyte plasma membrane, it is required to maintain PS in the inner leaflet preventing its exposure on the surface. This asymmetric distribution is critical for the survival of erythrocytes in circulation since externalized PS is a phagocytic signal for erythrocyte clearance by splenic macrophages (PubMed:24898253).
Required for B cell differentiation past the pro-B cell stage (PubMed:21423173).
Seems to mediate PS flipping in pro-B cells (PubMed:21423172, PubMed:26799398).
May be involved in the transport of cholestatic bile acids (PubMed:21518881).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
1440 μMATP
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
48.3 μmol/min/mgtoward ATP

Features

Showing features for active site, binding site, site.

TypeIDPosition(s)Description
Active site4094-aspartylphosphate intermediate
Binding site409ATP (UniProtKB | ChEBI)
Binding site409Mg2+ (UniProtKB | ChEBI)
Binding site410ATP (UniProtKB | ChEBI)
Binding site411ATP (UniProtKB | ChEBI)
Binding site411Mg2+ (UniProtKB | ChEBI)
Site439-440Cleavage; by CASP3, CASP6 and CASP7
Site445-446Cleavage; by CASP3
Site481-482Cleavage; by CASP3 and CASP7
Binding site498ATP (UniProtKB | ChEBI)
Binding site540ATP (UniProtKB | ChEBI)
Binding site563ATP (UniProtKB | ChEBI)
Binding site594ATP (UniProtKB | ChEBI)
Binding site674ATP (UniProtKB | ChEBI)
Binding site675ATP (UniProtKB | ChEBI)
Binding site676ATP (UniProtKB | ChEBI)
Binding site789ATP (UniProtKB | ChEBI)
Binding site795ATP (UniProtKB | ChEBI)
Binding site816Mg2+ (UniProtKB | ChEBI)
Binding site819ATP (UniProtKB | ChEBI)
Binding site820ATP (UniProtKB | ChEBI)
Binding site820Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentearly endosome membrane
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Cellular Componentplasma membrane
Cellular Componentrecycling endosome
Cellular Componentrecycling endosome membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATPase-coupled intramembrane lipid transporter activity
Molecular Functionmagnesium ion binding
Molecular Functionphosphatidylethanolamine flippase activity
Molecular Functionphosphatidylserine floppase activity
Biological Processphospholipid translocation
Biological Processpositive regulation of B cell differentiation
Biological Processpre-B cell differentiation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phospholipid-transporting ATPase 11C
  • EC number
  • Alternative names
    • ATPase class VI type 11C
    • P4-ATPase flippase complex alpha subunit ATP11C

Gene names

    • Name
      Atp11c

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9QZW0
  • Secondary accessions
    • Q3KQR4

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Endoplasmic reticulum membrane
; Multi-pass membrane protein
Early endosome membrane
; Multi-pass membrane protein
Recycling endosome membrane
; Multi-pass membrane protein
Note: Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A. Internalized via clathrin-dependent endocytosis in response to ca2+ signaling induced by G-protein coupled serotonin and histamine receptors, HTR2A and HRH1 respectively.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-83Cytoplasmic
Transmembrane84-104Helical
Topological domain105-287Extracellular
Transmembrane288-308Helical
Topological domain309-343Cytoplasmic
Transmembrane344-364Helical
Topological domain365-876Extracellular
Transmembrane877-897Helical
Topological domain898-905Cytoplasmic
Transmembrane906-926Helical
Topological domain927-952Extracellular
Transmembrane953-973Helical
Topological domain974-988Cytoplasmic
Transmembrane989-1009Helical
Topological domain1010-1023Extracellular
Transmembrane1024-1044Helical
Topological domain1045-1066Cytoplasmic
Transmembrane1067-1087Helical
Topological domain1088-1129Extracellular

Keywords

Phenotypes & Variants

Involvement in disease

  • Mice defective in Atp11c show defective B lymphopoiesis, specifically in mature bone marrow, pronounced stomatocytosis associated with anemia, hyperbilirubinemia linked to mild cholestasis and hepatocellular carcinoma

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis181Impairs ATPase activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 60 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000463741-1129Phospholipid-transporting ATPase 11C
Modified residue442Phosphoserine
Modified residue1105Phosphoserine
Modified residue1113Phosphoserine
Modified residue1123Phosphoserine

Post-translational modification

Proteolytically cleaved by CASP3, CASP6 and CASP7.
Phosphorylated at Ser-1113 likely by PRKCA; this creates a functional di-leucine motif that is sufficient for endocytosis.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed. Expressed in retina, brain, liver and testes (at protein level) (PubMed:30018401).
Expressed in lung, bone marrow, lymph nodes, prostate, ovary and uterus (PubMed:24904167).
Expressed in fetus (PubMed:24904167).

Gene expression databases

Interaction

Subunit

Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit ATP11C and an accessory beta subunit TMEM30A.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for coiled coil, motif.

TypeIDPosition(s)Description
Coiled coil607-643
Coiled coil695-726
Motif1113-1118Di-leucine motif

Domain

The di-leucine motif is required for sorting to clathrin-coated endosomes upon ca2+-dependent PRKCA activation.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9QZW0-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    1,129
  • Mass (Da)
    129,240
  • Last updated
    2007-01-09 v2
  • Checksum
    EE82DFD1F0669294
MFRRTLNRLCAGEEKRVGTRTVFVGNHPISGTEPYIAQRFCDNRIVSSKYTLWNFLPKNLFEQFRRIANFYFLIIFLVQVTVDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHRADNEVNKSAVYIIENAKRVRKESEKIKVGDVVEVQANETFPCDLILLSSCTTDGTCYVTTASLDGESNCKTHYAVRDTIALCTAESIDNLRATIECEQPQPDLYRFVGRISIYSNSIEAVARSLGPENLLLKGATLKNTKKIYGVAVYTGMETKMALNYQGKSQKCSAVEKSINAFLIVYLFILLTKAAVCTTLKYVWQSSPYNDEPWYNQKTQKERETFQVLKMFTDFLSFMVLFNFIIPVSMYVTVEMQKFLGSFFISWDKDFFDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTENSMEFIECCIDGHKYKGTTQEVDGLSQTDGPLAYFDKADKNREALFLRALCLCHTVEMKTNDDVDGPVEGAGFTYISSSPDEIALVKGAKRFGFTFLGNQNGYIRVENQRKEIEEYELLHTLNFDSVRRRMSVIVRTQKGDILLFCKGADSSIFPRVHSHQIELTKDHVERNAMDGYRTLCVAFKEIPPDDFERINAQLVEAKMALQDREEKLEKVFDEIETNMNLIGATAVEDKLQDQAAETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHELLIEYRKKLLHEFPKSTRSLKKAWTEHQEYGLIIDGSTLSLILNSSQDCSSNNYKSIFLQICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKEGRQAARNSDYSVPKFKHLKKLLLVHGHLYYVRIAHLVQYFFYKNLCFILPQFLYQFFCGFSQQPLYDAAYLTMYNICFTSLPILAYSLLEQHINIDTLTADPRLYMKITGNAMLQLGPFLHWTFLAAFEGTVFFFGTYFLFQTSSLEDNGKIYGNWTFGTIVFTVLVFTVTLKLALDTRFWTWINHFVIWGSLAFYVFFSFFWGGIIWPFLKQQRMYFVFAQMLCSVSTWLAIILLIFISLFPEILLIVVKNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNIL

Q9QZW0-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 833-835: Missing
    • 1097-1129: RNLSCRRASDSLSARPSVRPLLLRTFSDESNIL → NPNLELPMLLSYKHIDRGCS

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F6Q8D3F6Q8D3_MOUSEAtp11c1129
E9QKK8E9QKK8_MOUSEAtp11c1116

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict786-791in Ref. 2; AAF09445
Alternative sequenceVSP_022222833-835in isoform 2
Alternative sequenceVSP_0222231097-1129in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC106087
EMBL· GenBank· DDBJ
AAI06088.1
EMBL· GenBank· DDBJ
mRNA
AF156547
EMBL· GenBank· DDBJ
AAF09445.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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