Q9QZW0 · AT11C_MOUSE
- ProteinPhospholipid-transporting ATPase 11C
- GeneAtp11c
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1129 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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
- a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
- a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1440 μM | ATP |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
48.3 μmol/min/mg | toward ATP |
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 409 | 4-aspartylphosphate intermediate | ||||
Sequence: D | ||||||
Binding site | 409 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 409 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 410 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 411 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 411 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Site | 439-440 | Cleavage; by CASP3, CASP6 and CASP7 | ||||
Sequence: DG | ||||||
Site | 445-446 | Cleavage; by CASP3 | ||||
Sequence: DG | ||||||
Site | 481-482 | Cleavage; by CASP3 and CASP7 | ||||
Sequence: DG | ||||||
Binding site | 498 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 540 | ATP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 563 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 594 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 674 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 675 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 676 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 789 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 795 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 816 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 819 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 820 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 820 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | early endosome membrane | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | plasma membrane | |
Cellular Component | recycling endosome | |
Cellular Component | recycling endosome membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATPase-coupled intramembrane lipid transporter activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphatidylethanolamine flippase activity | |
Molecular Function | phosphatidylserine floppase activity | |
Biological Process | phospholipid translocation | |
Biological Process | positive regulation of B cell differentiation | |
Biological Process | pre-B cell differentiation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospholipid-transporting ATPase 11C
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9QZW0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-83 | Cytoplasmic | ||||
Sequence: MFRRTLNRLCAGEEKRVGTRTVFVGNHPISGTEPYIAQRFCDNRIVSSKYTLWNFLPKNLFEQFRRIANFYFLIIFLVQVTVD | ||||||
Transmembrane | 84-104 | Helical | ||||
Sequence: TPTSPVTSGLPLFFVITVTAI | ||||||
Topological domain | 105-287 | Extracellular | ||||
Sequence: KQGYEDWLRHRADNEVNKSAVYIIENAKRVRKESEKIKVGDVVEVQANETFPCDLILLSSCTTDGTCYVTTASLDGESNCKTHYAVRDTIALCTAESIDNLRATIECEQPQPDLYRFVGRISIYSNSIEAVARSLGPENLLLKGATLKNTKKIYGVAVYTGMETKMALNYQGKSQKCSAVEKS | ||||||
Transmembrane | 288-308 | Helical | ||||
Sequence: INAFLIVYLFILLTKAAVCTT | ||||||
Topological domain | 309-343 | Cytoplasmic | ||||
Sequence: LKYVWQSSPYNDEPWYNQKTQKERETFQVLKMFTD | ||||||
Transmembrane | 344-364 | Helical | ||||
Sequence: FLSFMVLFNFIIPVSMYVTVE | ||||||
Topological domain | 365-876 | Extracellular | ||||
Sequence: MQKFLGSFFISWDKDFFDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTENSMEFIECCIDGHKYKGTTQEVDGLSQTDGPLAYFDKADKNREALFLRALCLCHTVEMKTNDDVDGPVEGAGFTYISSSPDEIALVKGAKRFGFTFLGNQNGYIRVENQRKEIEEYELLHTLNFDSVRRRMSVIVRTQKGDILLFCKGADSSIFPRVHSHQIELTKDHVERNAMDGYRTLCVAFKEIPPDDFERINAQLVEAKMALQDREEKLEKVFDEIETNMNLIGATAVEDKLQDQAAETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHELLIEYRKKLLHEFPKSTRSLKKAWTEHQEYGLIIDGSTLSLILNSSQDCSSNNYKSIFLQICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKEGRQAARNSDYSVPKFKHLKKLLLVHGHLYYVRIAHLVQY | ||||||
Transmembrane | 877-897 | Helical | ||||
Sequence: FFYKNLCFILPQFLYQFFCGF | ||||||
Topological domain | 898-905 | Cytoplasmic | ||||
Sequence: SQQPLYDA | ||||||
Transmembrane | 906-926 | Helical | ||||
Sequence: AYLTMYNICFTSLPILAYSLL | ||||||
Topological domain | 927-952 | Extracellular | ||||
Sequence: EQHINIDTLTADPRLYMKITGNAMLQ | ||||||
Transmembrane | 953-973 | Helical | ||||
Sequence: LGPFLHWTFLAAFEGTVFFFG | ||||||
Topological domain | 974-988 | Cytoplasmic | ||||
Sequence: TYFLFQTSSLEDNGK | ||||||
Transmembrane | 989-1009 | Helical | ||||
Sequence: IYGNWTFGTIVFTVLVFTVTL | ||||||
Topological domain | 1010-1023 | Extracellular | ||||
Sequence: KLALDTRFWTWINH | ||||||
Transmembrane | 1024-1044 | Helical | ||||
Sequence: FVIWGSLAFYVFFSFFWGGII | ||||||
Topological domain | 1045-1066 | Cytoplasmic | ||||
Sequence: WPFLKQQRMYFVFAQMLCSVST | ||||||
Transmembrane | 1067-1087 | Helical | ||||
Sequence: WLAIILLIFISLFPEILLIVV | ||||||
Topological domain | 1088-1129 | Extracellular | ||||
Sequence: KNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNIL |
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 181 | Impairs ATPase activity. | ||||
Sequence: E → Q |
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.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000046374 | 1-1129 | Phospholipid-transporting ATPase 11C | |||
Sequence: MFRRTLNRLCAGEEKRVGTRTVFVGNHPISGTEPYIAQRFCDNRIVSSKYTLWNFLPKNLFEQFRRIANFYFLIIFLVQVTVDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHRADNEVNKSAVYIIENAKRVRKESEKIKVGDVVEVQANETFPCDLILLSSCTTDGTCYVTTASLDGESNCKTHYAVRDTIALCTAESIDNLRATIECEQPQPDLYRFVGRISIYSNSIEAVARSLGPENLLLKGATLKNTKKIYGVAVYTGMETKMALNYQGKSQKCSAVEKSINAFLIVYLFILLTKAAVCTTLKYVWQSSPYNDEPWYNQKTQKERETFQVLKMFTDFLSFMVLFNFIIPVSMYVTVEMQKFLGSFFISWDKDFFDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTENSMEFIECCIDGHKYKGTTQEVDGLSQTDGPLAYFDKADKNREALFLRALCLCHTVEMKTNDDVDGPVEGAGFTYISSSPDEIALVKGAKRFGFTFLGNQNGYIRVENQRKEIEEYELLHTLNFDSVRRRMSVIVRTQKGDILLFCKGADSSIFPRVHSHQIELTKDHVERNAMDGYRTLCVAFKEIPPDDFERINAQLVEAKMALQDREEKLEKVFDEIETNMNLIGATAVEDKLQDQAAETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHELLIEYRKKLLHEFPKSTRSLKKAWTEHQEYGLIIDGSTLSLILNSSQDCSSNNYKSIFLQICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKEGRQAARNSDYSVPKFKHLKKLLLVHGHLYYVRIAHLVQYFFYKNLCFILPQFLYQFFCGFSQQPLYDAAYLTMYNICFTSLPILAYSLLEQHINIDTLTADPRLYMKITGNAMLQLGPFLHWTFLAAFEGTVFFFGTYFLFQTSSLEDNGKIYGNWTFGTIVFTVLVFTVTLKLALDTRFWTWINHFVIWGSLAFYVFFSFFWGGIIWPFLKQQRMYFVFAQMLCSVSTWLAIILLIFISLFPEILLIVVKNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNIL | ||||||
Modified residue | 442 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1105 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1113 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1123 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for coiled coil, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 607-643 | |||||
Sequence: DFERINAQLVEAKMALQDREEKLEKVFDEIETNMNLI | ||||||
Coiled coil | 695-726 | |||||
Sequence: TELLELTTKTIEESERKEDRLHELLIEYRKKL | ||||||
Motif | 1113-1118 | Di-leucine motif | ||||
Sequence: SVRPLL |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length1,129
- Mass (Da)129,240
- Last updated2007-01-09 v2
- ChecksumEE82DFD1F0669294
Q9QZW0-2
- Name2
- Differences from canonical
- 833-835: Missing
- 1097-1129: RNLSCRRASDSLSARPSVRPLLLRTFSDESNIL → NPNLELPMLLSYKHIDRGCS
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC106087 EMBL· GenBank· DDBJ | AAI06088.1 EMBL· GenBank· DDBJ | mRNA | ||
AF156547 EMBL· GenBank· DDBJ | AAF09445.1 EMBL· GenBank· DDBJ | mRNA |