Q8K2X1 · AT10D_MOUSE
- ProteinPhospholipid-transporting ATPase VD
- GeneAtp10d
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1416 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic component of a P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide (GlcCer) from the outer to the inner leaflet of the plasma membrane.
Catalytic activity
- a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 438 | 4-aspartylphosphate intermediate | ||||
Sequence: D | ||||||
Binding site | 438 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 438 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 439 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 440 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 440 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 729 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 771 | ATP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 795 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 838 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 918 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 919 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 920 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 993-1000 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLVITGKT | ||||||
Binding site | 1027 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1033 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 1053 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1056 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1057 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1057 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1361-1368 | ATP (UniProtKB | ChEBI) | ||||
Sequence: ASQSAAMS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Cellular Component | mitochondrion | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATPase-coupled intramembrane lipid transporter activity | |
Molecular Function | magnesium ion binding | |
Biological Process | monoatomic cation transport | |
Biological Process | phospholipid translocation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospholipid-transporting ATPase VD
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8K2X1
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Note: Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not that of TMEM30B.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-97 | Cytoplasmic | ||||
Sequence: MTELLQWARHHWRRLSHGRAQGEDERPYNYASLLACGGKSSRTPRPAGKHRVVIPHLQCFKDEYERFSGTYVNNRIRTTKYTLLNFVPRNLFEQFHR | ||||||
Transmembrane | 98-118 | Helical | ||||
Sequence: AANLYFLFLVVLNWVPLVEAF | ||||||
Topological domain | 119-120 | Exoplasmic loop | ||||
Sequence: QK | ||||||
Transmembrane | 121-141 | Helical | ||||
Sequence: EITMLPLVVVLTIIAIKDGLE | ||||||
Topological domain | 142-321 | Cytoplasmic | ||||
Sequence: DYRKYKIDKQINNLITKVYSRKEKKYIDCCWKNVTVGDFIRLSCNEIIPADMVLLFSTDPDGICHIETSGLDGESNLKQRQVVRGYTEQDSEVDPEKFSSRIECESPNNDLSRFRGFLEHANKERVGLSKENLLLRGCTIRNTEAVVGIVVYAGHETKAMLNNSGPRYKRSKLERRANTD | ||||||
Transmembrane | 322-342 | Helical | ||||
Sequence: VLWCVLLLIVMCLTGALGHGI | ||||||
Topological domain | 343-365 | Exoplasmic loop | ||||
Sequence: WLSRYENMLFFNIPEPDGRVISP | ||||||
Transmembrane | 366-386 | Helical | ||||
Sequence: VLTGFYVFWTMIILLQVLIPI | ||||||
Topological domain | 387-1110 | Cytoplasmic | ||||
Sequence: SLYVSIEIVKLGQIYFIQSDVDFYNEKMDSTIQCRALNITEDLGQIQYLFSDKTGTLTENKMVFRRCSVAGFDYCHEENAKRLESYQEAVSEEEECTDTLGGSLSNMARPRAQGCRTVPSGPLGKPSAQLSGSTSAVGNGEGSGEVPHSRQAAFSSPMETDVVPDTRLLDKFSQLTPQLLTGLDGTAQSSPLETLYIMDFFIALAICNTVVVSAPNQPRQKIGLSSLGGMPIKSLEEIKNIFQKLSVRRSSSPSLASGKDSSSGTPCAFVSRISFFSRPKLSPPMEDESSQMDEIPQASNSACCTETEAQNRAVGLSVSSAEALSGPPPSASNLCYEAESPDEAALVYAARAYRCTLQSRTPEQVMVDFAALGSLTFQLLHILPFDSVRKRMSVVVRHPLSKQVVVYTKGADSVIMELLSVAASDGTNPEQQMIIRERTQRHLDEYAKRGLRTLCVAKKVMSDTEYAEWLRNHFLAETSIDNREELLVESAMRLENKLTLLGATGIEDRLQEGVPESIEALHQAGIKIWMLTGDKQETAVNIAYACKLLEPDDKLFILNTQSQDACGMLMSAILEELQKRAQVSPELASSRKNFPQPSDAQGQGRAGLVITGKTLEFALQESLQRQFLELTAWCQAVICCRATPLQKSEVVKLVRNHHHVLTLPIGDGANDVSMIQVADIGIGVSGQEGMQAVMASDFAISQFRHLSKLLLVHGHWCYTRLSNM | ||||||
Transmembrane | 1111-1131 | Helical | ||||
Sequence: ILYFFYKNVAYVNLLFWYQFF | ||||||
Topological domain | 1132-1142 | Exoplasmic loop | ||||
Sequence: CGFSGTSMTDY | ||||||
Transmembrane | 1143-1163 | Helical | ||||
Sequence: WVLIFFNLLFTSVPPIIYGVL | ||||||
Topological domain | 1164-1192 | Cytoplasmic | ||||
Sequence: EKDVSAETLLQLPELYRSGQRSEEYLPLT | ||||||
Transmembrane | 1193-1213 | Helical | ||||
Sequence: FWITLLDAFYQSLVCFFVPYF | ||||||
Topological domain | 1214-1221 | Exoplasmic loop | ||||
Sequence: TYQGSDID | ||||||
Transmembrane | 1222-1242 | Helical | ||||
Sequence: IFTFGNPLNTAALFIILLHLV | ||||||
Topological domain | 1243-1252 | Cytoplasmic | ||||
Sequence: IESKSLTWIH | ||||||
Transmembrane | 1253-1273 | Helical | ||||
Sequence: MLVTVGSILSYFFFALAFGAL | ||||||
Topological domain | 1274-1289 | Exoplasmic loop | ||||
Sequence: CVTCNPPSNPYGIMRK | ||||||
Transmembrane | 1290-1310 | Helical | ||||
Sequence: HMLDPVFYLVCVLTTFVALLP | ||||||
Topological domain | 1311-1416 | Cytoplasmic | ||||
Sequence: RFLYRVLQGSVFPSPVLRAKYFDRLPPEERAEALKRWRGTAKVNHVASKHASQSAAMSGRPTPGSSAVLAMKSATVSTVEQSTRETALDRGCSEPGASKMTGSSAS |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 700 | in strain: CAST, MAI, MBT and PWK | ||||
Sequence: V → A | ||||||
Natural variant | 716 | in strain: CAST, MAI, MBT and PWK | ||||
Sequence: S → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000046384 | 1-1416 | Phospholipid-transporting ATPase VD | |||
Sequence: MTELLQWARHHWRRLSHGRAQGEDERPYNYASLLACGGKSSRTPRPAGKHRVVIPHLQCFKDEYERFSGTYVNNRIRTTKYTLLNFVPRNLFEQFHRAANLYFLFLVVLNWVPLVEAFQKEITMLPLVVVLTIIAIKDGLEDYRKYKIDKQINNLITKVYSRKEKKYIDCCWKNVTVGDFIRLSCNEIIPADMVLLFSTDPDGICHIETSGLDGESNLKQRQVVRGYTEQDSEVDPEKFSSRIECESPNNDLSRFRGFLEHANKERVGLSKENLLLRGCTIRNTEAVVGIVVYAGHETKAMLNNSGPRYKRSKLERRANTDVLWCVLLLIVMCLTGALGHGIWLSRYENMLFFNIPEPDGRVISPVLTGFYVFWTMIILLQVLIPISLYVSIEIVKLGQIYFIQSDVDFYNEKMDSTIQCRALNITEDLGQIQYLFSDKTGTLTENKMVFRRCSVAGFDYCHEENAKRLESYQEAVSEEEECTDTLGGSLSNMARPRAQGCRTVPSGPLGKPSAQLSGSTSAVGNGEGSGEVPHSRQAAFSSPMETDVVPDTRLLDKFSQLTPQLLTGLDGTAQSSPLETLYIMDFFIALAICNTVVVSAPNQPRQKIGLSSLGGMPIKSLEEIKNIFQKLSVRRSSSPSLASGKDSSSGTPCAFVSRISFFSRPKLSPPMEDESSQMDEIPQASNSACCTETEAQNRAVGLSVSSAEALSGPPPSASNLCYEAESPDEAALVYAARAYRCTLQSRTPEQVMVDFAALGSLTFQLLHILPFDSVRKRMSVVVRHPLSKQVVVYTKGADSVIMELLSVAASDGTNPEQQMIIRERTQRHLDEYAKRGLRTLCVAKKVMSDTEYAEWLRNHFLAETSIDNREELLVESAMRLENKLTLLGATGIEDRLQEGVPESIEALHQAGIKIWMLTGDKQETAVNIAYACKLLEPDDKLFILNTQSQDACGMLMSAILEELQKRAQVSPELASSRKNFPQPSDAQGQGRAGLVITGKTLEFALQESLQRQFLELTAWCQAVICCRATPLQKSEVVKLVRNHHHVLTLPIGDGANDVSMIQVADIGIGVSGQEGMQAVMASDFAISQFRHLSKLLLVHGHWCYTRLSNMILYFFYKNVAYVNLLFWYQFFCGFSGTSMTDYWVLIFFNLLFTSVPPIIYGVLEKDVSAETLLQLPELYRSGQRSEEYLPLTFWITLLDAFYQSLVCFFVPYFTYQGSDIDIFTFGNPLNTAALFIILLHLVIESKSLTWIHMLVTVGSILSYFFFALAFGALCVTCNPPSNPYGIMRKHMLDPVFYLVCVLTTFVALLPRFLYRVLQGSVFPSPVLRAKYFDRLPPEERAEALKRWRGTAKVNHVASKHASQSAAMSGRPTPGSSAVLAMKSATVSTVEQSTRETALDRGCSEPGASKMTGSSAS |
Post-translational modification
Autophosphorylated at the conserved aspartate of the P-type ATPase signature sequence.
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 498-544 | Disordered | ||||
Sequence: AQGCRTVPSGPLGKPSAQLSGSTSAVGNGEGSGEVPHSRQAAFSSPM | ||||||
Compositional bias | 510-526 | Polar residues | ||||
Sequence: GKPSAQLSGSTSAVGNG | ||||||
Compositional bias | 971-986 | Polar residues | ||||
Sequence: PELASSRKNFPQPSDA | ||||||
Region | 971-990 | Disordered | ||||
Sequence: PELASSRKNFPQPSDAQGQG | ||||||
Region | 1358-1416 | Disordered | ||||
Sequence: SKHASQSAAMSGRPTPGSSAVLAMKSATVSTVEQSTRETALDRGCSEPGASKMTGSSAS | ||||||
Compositional bias | 1378-1398 | Polar residues | ||||
Sequence: VLAMKSATVSTVEQSTRETAL |
Sequence similarities
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8K2X1-1
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
- Length1,416
- Mass (Da)158,330
- Last updated2003-03-25 v2
- Checksum1799CCF062E22BB0
Q8K2X1-2
- Name2
- Differences from canonical
- 1120-1135: Missing
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 510-526 | Polar residues | ||||
Sequence: GKPSAQLSGSTSAVGNG | ||||||
Compositional bias | 971-986 | Polar residues | ||||
Sequence: PELASSRKNFPQPSDA | ||||||
Alternative sequence | VSP_006959 | 1120-1135 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 1239 | in Ref. 2; AAH29551 | ||||
Sequence: L → F | ||||||
Compositional bias | 1378-1398 | Polar residues | ||||
Sequence: VLAMKSATVSTVEQSTRETAL |
Polymorphism
In strain C57BL/6, a polymorphism generates a premature stop codon at position 764.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ441079 EMBL· GenBank· DDBJ | CAD29578.1 EMBL· GenBank· DDBJ | mRNA | ||
BC029551 EMBL· GenBank· DDBJ | AAH29551.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |