Q4WYP6 · SPFA_ASPFU
- ProteinEndoplasmic reticulum transmembrane helix translocase spfA
- GenespfA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1303 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Endoplasmic reticulum (ER) translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum (By similarity).
Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane (By similarity).
Works in concert with the ER Ca2+ pump srcA to support ER homeostasis (PubMed:34663092).
With srcA, supports also redox homeostasis and virulence (PubMed:34663092).
Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane (By similarity).
Works in concert with the ER Ca2+ pump srcA to support ER homeostasis (PubMed:34663092).
With srcA, supports also redox homeostasis and virulence (PubMed:34663092).
Catalytic activity
- [protein]-with a C-terminal TM segment(out) + ATP + H2O = [protein]-with a C-terminal TM segment(in) + ADP + phosphate + H+
Cofactor
Activity regulation
The ATPase activity is stimulated by phosphatidylinositol 4-phosphate (PI4P).
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 505 | 4-aspartylphosphate intermediate | ||||
Sequence: D | ||||||
Binding site | 505 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 505-507 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DKT | ||||||
Binding site | 507 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 616 | ATP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 678 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 746 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 862 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 862-866 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DGTND |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cis-Golgi network | |
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATPase-coupled monoatomic cation transmembrane transporter activity | |
Molecular Function | membrane protein dislocase activity | |
Molecular Function | metal ion binding | |
Molecular Function | P-type ion transporter activity | |
Molecular Function | phosphatidylinositol-4-phosphate binding | |
Biological Process | extraction of mislocalized protein from ER membrane | |
Biological Process | intracellular calcium ion homeostasis | |
Biological Process | intracellular manganese ion homeostasis | |
Biological Process | protein hexamerization | |
Biological Process | protein unfolding | |
Biological Process | response to unfolded protein | |
Biological Process | sterol homeostasis | |
Biological Process | transmembrane transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEndoplasmic reticulum transmembrane helix translocase spfA
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionQ4WYP6
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 25-45 | Helical | ||||
Sequence: LHAYVWPFLIIWPAFFAVYLS | ||||||
Transmembrane | 57-77 | Helical | ||||
Sequence: EWTFVWSGSIITAQSLLWLMT | ||||||
Transmembrane | 201-221 | Helical | ||||
Sequence: EHAVAPFFVFQVFCVGLWMLD | ||||||
Transmembrane | 223-243 | Helical | ||||
Sequence: YWYYSLFTLFMLVVFESTVVW | ||||||
Transmembrane | 415-435 | Helical | ||||
Sequence: VEALLFILFLLIFAIAAAWYV | ||||||
Transmembrane | 1060-1080 | Helical | ||||
Sequence: ILALNCLISAYSLSVIYLDGI | ||||||
Transmembrane | 1082-1102 | Helical | ||||
Sequence: FGDGQVTISGMLMSVCFLSIS | ||||||
Transmembrane | 1122-1142 | Helical | ||||
Sequence: VYIIGSVLGQFAIHIATLIYL | ||||||
Transmembrane | 1201-1221 | Helical | ||||
Sequence: AMYWGLVAASGVAFSCATEFI | ||||||
Transmembrane | 1239-1259 | Helical | ||||
Sequence: VTLTVLMIIDYAGCWIIENVL |
Keywords
- Cellular component
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000456886 | 1-1303 | Endoplasmic reticulum transmembrane helix translocase spfA | |||
Sequence: MLRAKLVDDPQIKYASLHNPLPTQLHAYVWPFLIIWPAFFAVYLSPERYDTYIQGQEWTFVWSGSIITAQSLLWLMTKWNINIQTLFTATKARSLDSAQLIKVIPVANAGSAEICPLHCDTMGGKKTFSFLFQKRRFLYYPERQCFAPLSYVLDAEPKPPVKVFQQAQGLTSKEEIDRIQHHYGDNTFDIPVPTFMELFKEHAVAPFFVFQVFCVGLWMLDEYWYYSLFTLFMLVVFESTVVWQRQRTLNEFRGMNIKPYDVWVYRQKKWQELTSDKLLPGDLMSVNRTKEDSGVACDILLIEGSAIVNEAMLSGESTPLLKESIQLRPGDDLIDPDGLDKNAFVHGGTKVLQITHHNSNGEDGSEKARKLSSGVPLPPDNGAVGVVVKTGFETSQGSLVRTMIYSTERVSANNVEALLFILFLLIFAIAAAWYVWQEGVAKDRKRSKLLLDCVLIVTSVVPPELPMELSLAVNTSLAALSKFAIFCTEPFRIPFAGRVDVACFDKTGTLTGEDLVVDGIAGLTLGHEGADVGKDGAHTELAKSANVPLDTTLVLASAHALVKLDEGEVVGDPMEKATLQWLGWTLGRNDTLMSKAAALAGPRTVESVQIKRRFQFSSALKRQSTIATVVTADRKTSKKTKATFVGVKGAPETIRTMLVNTPPHYEETFKYFTRNGARVLALAYKYLSEESELSQGRINGYIREEIEADLIFAGFLVLQCPLKEDAIKAVRMLNESSHRVVMITGDNPLTAVHVARKVEIVDRDVLILDAPEDDMSGTRLVWRSIDDKFNRDVDPTQDLDPEIIETKDICITGYALAKFKGQKAFSTLLRHTWVYARVSPKQKEDILVGLKDAGYTTLMCGDGTNDVGALKQAHVGVALLNGSPEDLAKIAEHYRTTKMKEIYEKQVSMMQRFNQPPPPVPVQIAHLYPPGPRNPHYQKAMEREAQRKGAATLATAGNQTEHIPTITSPGAQALQQSNANLTPQQQRQQQASIAAAGFADKLTSSMLEQELDDSEPPTIKLGDASVAAPFTSKLANVIAIPNILRQGRCTLVATIQMYKILALNCLISAYSLSVIYLDGIKFGDGQVTISGMLMSVCFLSISRAKSVEGLSKERPQPNIFNVYIIGSVLGQFAIHIATLIYLSNYVYSIEPRKSDIDLEGEFEPSLLNSAIYLLQLIQQISTFSINYQGRPFRESIRENKAMYWGLVAASGVAFSCATEFIPELNEKMRLVPFSTEFKVTLTVLMIIDYAGCWIIENVLKNLFSDFRPKDIAVRRPDQLQREMERKKQEELETQAEKERQRKV | ||||||
Glycosylation | 287 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 474 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 589 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 734 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 958 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Expression
Interaction
Protein-protein interaction databases
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 158-191 | A-domain; part 1 | ||||
Sequence: KPPVKVFQQAQGLTSKEEIDRIQHHYGDNTFDIP | ||||||
Region | 256-408 | A-domain; part 2 | ||||
Sequence: NIKPYDVWVYRQKKWQELTSDKLLPGDLMSVNRTKEDSGVACDILLIEGSAIVNEAMLSGESTPLLKESIQLRPGDDLIDPDGLDKNAFVHGGTKVLQITHHNSNGEDGSEKARKLSSGVPLPPDNGAVGVVVKTGFETSQGSLVRTMIYSTE | ||||||
Region | 484-513 | P-domain; part 1 | ||||
Sequence: AIFCTEPFRIPFAGRVDVACFDKTGTLTGE | ||||||
Region | 515-721 | N-domain | ||||
Sequence: LVVDGIAGLTLGHEGADVGKDGAHTELAKSANVPLDTTLVLASAHALVKLDEGEVVGDPMEKATLQWLGWTLGRNDTLMSKAAALAGPRTVESVQIKRRFQFSSALKRQSTIATVVTADRKTSKKTKATFVGVKGAPETIRTMLVNTPPHYEETFKYFTRNGARVLALAYKYLSEESELSQGRINGYIREEIEADLIFAGFLVLQCP | ||||||
Region | 724-883 | P-domain; part 2 | ||||
Sequence: EDAIKAVRMLNESSHRVVMITGDNPLTAVHVARKVEIVDRDVLILDAPEDDMSGTRLVWRSIDDKFNRDVDPTQDLDPEIIETKDICITGYALAKFKGQKAFSTLLRHTWVYARVSPKQKEDILVGLKDAGYTTLMCGDGTNDVGALKQAHVGVALLNGS | ||||||
Region | 884-1019 | Arm-like | ||||
Sequence: PEDLAKIAEHYRTTKMKEIYEKQVSMMQRFNQPPPPVPVQIAHLYPPGPRNPHYQKAMEREAQRKGAATLATAGNQTEHIPTITSPGAQALQQSNANLTPQQQRQQQASIAAAGFADKLTSSMLEQELDDSEPPTI | ||||||
Region | 1020-1035 | P-domain; part 3 | ||||
Sequence: KLGDASVAAPFTSKLA | ||||||
Region | 1277-1303 | Disordered | ||||
Sequence: DQLQREMERKKQEELETQAEKERQRKV |
Domain
Contains a large substrate-binding pocket that recognizes alpha-helical transmembranes, which alternately faces the endoplasmic reticulum lumen and cytosol, while remaining accessible to the lipid bilayer through a lateral opening (By similarity).
The translocase alternates between two conformations: inward-open (E1) and outward-open (E2) states (By similarity).
Undergoes a series of conformational changes with ATP-binding, phosphorylation of the Asp active site and subsequent dephosphorylation in a Post-Albers cycle (i.e., E1 -> E1-ATP -> E1P-ADP -> E1P -> E2P -> E2-Pi -> E1) (By similarity).
A substrate transmembrane helix with a short, preferentially positively charged lumenal segment binds to the outward-open pocket and the E2P-to-E1 transition flips the transmembrane by a switch from the outward-open to inward-open conformation (By similarity).
The translocase alternates between two conformations: inward-open (E1) and outward-open (E2) states (By similarity).
Undergoes a series of conformational changes with ATP-binding, phosphorylation of the Asp active site and subsequent dephosphorylation in a Post-Albers cycle (i.e., E1 -> E1-ATP -> E1P-ADP -> E1P -> E2P -> E2-Pi -> E1) (By similarity).
A substrate transmembrane helix with a short, preferentially positively charged lumenal segment binds to the outward-open pocket and the E2P-to-E1 transition flips the transmembrane by a switch from the outward-open to inward-open conformation (By similarity).
Sequence similarities
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,303
- Mass (Da)145,555
- Last updated2005-07-05 v1
- Checksum6B8B5E48DFDE9268
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAHF01000002 EMBL· GenBank· DDBJ | EAL92207.1 EMBL· GenBank· DDBJ | Genomic DNA |