O75027 · ABCB7_HUMAN
- ProteinIron-sulfur clusters transporter ABCB7, mitochondrial
- GeneABCB7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids752 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Moreover, through a functional complex formed of ABCB7, FECH and ABCB10, also plays a role in the cellular iron homeostasis, mitochondrial function and heme biosynthesis (PubMed:30765471).
In cardiomyocytes, regulates cellular iron homeostasis and cellular reactive oxygen species (ROS) levels through its interaction with COX4I1 (By similarity).
May also play a role in hematopoiesis (By similarity).
Catalytic activity
- (glutathione)4[2Fe(III)-2S] cluster(in) + ATP + H2O = (glutathione)4[2Fe(III)-2S] cluster(out) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Activity regulation
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
5.3 mM | Mg-ATP | |||||
0.54 mM | Mg-ATP | in the presence of the [2Fe-2S](GS)4 cluster |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 315-319 | glutathione (UniProtKB | ChEBI) | ||||
Sequence: RTRFR | ||||||
Binding site | 378-381 | glutathione (UniProtKB | ChEBI) | ||||
Sequence: NFGQ | ||||||
Binding site | 428 | glutathione (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 481 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 505-516 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GGSGSGKSTIVR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrion | |
Molecular Function | ABC-type iron-sulfur cluster transporter activity | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATPase-coupled transmembrane transporter activity | |
Molecular Function | heme transmembrane transporter activity | |
Molecular Function | identical protein binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | intracellular iron ion homeostasis | |
Biological Process | iron ion transmembrane transport | |
Biological Process | iron-sulfur cluster assembly | |
Biological Process | iron-sulfur cluster export from the mitochondrion | |
Biological Process | negative regulation of reactive oxygen species biosynthetic process | |
Biological Process | positive regulation of heme biosynthetic process | |
Biological Process | positive regulation of iron-sulfur cluster assembly | |
Biological Process | transmembrane transport |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameIron-sulfur clusters transporter ABCB7, mitochondrial
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75027
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-140 | Mitochondrial matrix | ||||
Sequence: HSAILIRPLVSVSGSGPQWRPHQLGALGTARAYQIPESLKSITWQRLGKGNSGQFLDAAKALQVWPLIEKRTCWHGHAGGGLHTDPKEGLKDVDTRKIIKAMLSYVWPKDRPDLRARV | ||||||
Transmembrane | 141-161 | Helical | ||||
Sequence: AISLGFLGGAKAMNIVVPFMF | ||||||
Topological domain | 162-185 | Mitochondrial intermembrane | ||||
Sequence: KYAVDSLNQMSGNMLNLSDAPNTV | ||||||
Transmembrane | 186-206 | Helical | ||||
Sequence: ATMATAVLIGYGVSRAGAAFF | ||||||
Topological domain | 207-259 | Mitochondrial matrix | ||||
Sequence: NEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRG | ||||||
Transmembrane | 260-280 | Helical | ||||
Sequence: ISFVLSALVFNLLPIMFEVML | ||||||
Topological domain | 281-290 | Mitochondrial intermembrane | ||||
Sequence: VSGVLYYKCG | ||||||
Transmembrane | 291-311 | Helical | ||||
Sequence: AQFALVTLGTLGTYTAFTVAV | ||||||
Topological domain | 312-382 | Mitochondrial matrix | ||||
Sequence: TRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQS | ||||||
Transmembrane | 383-403 | Helical | ||||
Sequence: AIFSVGLTAIMVLASQGIVAG | ||||||
Topological domain | 404-409 | Mitochondrial intermembrane | ||||
Sequence: TLTVGD | ||||||
Transmembrane | 410-430 | Helical | ||||
Sequence: LVMVNGLLFQLSLPLNFLGTV | ||||||
Topological domain | 431-752 | Mitochondrial matrix | ||||
Sequence: YRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWHTQSSRVQNHDNPKWEAKKENISKEEERKKLQEEIVNSVKGCGNCSC |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Anemia, sideroblastic, spinocerebellar ataxia (ASAT)
- Note
- DescriptionAn X-linked recessive disorder characterized by an infantile to early childhood onset of non-progressive cerebellar ataxia and mild anemia, with hypochromia and microcytosis.
- See alsoMIM:301310
Natural variants in ASAT
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_067354 | 208 | E>D | in ASAT; dbSNP:rs515726147 | |
VAR_009156 | 400 | I>M | in ASAT; dbSNP:rs72554634 | |
VAR_022874 | 411 | V>L | in ASAT; dbSNP:rs80356713 | |
VAR_012640 | 433 | E>K | in ASAT; impaired maturation of cytosolic Fe/S proteins, loss of the ability to couple MgATP binding with stimulation of ATPase activity at the nucleotide binding domain;; loss of [2Fe-2S]-(GS)4 cluster transport; dbSNP:rs80356714 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_067354 | 208 | in ASAT; dbSNP:rs515726147 | |||
Sequence: E → D | ||||||
Natural variant | VAR_022872 | 315 | ||||
Sequence: R → G | ||||||
Natural variant | VAR_022873 | 346 | ||||
Sequence: F → I | ||||||
Natural variant | VAR_009156 | 400 | in ASAT; dbSNP:rs72554634 | |||
Sequence: I → M | ||||||
Natural variant | VAR_022874 | 411 | in ASAT; dbSNP:rs80356713 | |||
Sequence: V → L | ||||||
Natural variant | VAR_012640 | 433 | in ASAT; impaired maturation of cytosolic Fe/S proteins, loss of the ability to couple MgATP binding with stimulation of ATPase activity at the nucleotide binding domain;; loss of [2Fe-2S]-(GS)4 cluster transport; dbSNP:rs80356714 | |||
Sequence: E → K | ||||||
Mutagenesis | 433 | Significantly increases ATPase activity by [2Fe-2S]-(GS)4 cluster stimulation. Increases affinity for Mg-ATP. Does not affect affinity for Mg-ATP in the presence of the in the presence of [2Fe-2S]-(GS)4 cluster. Does not affect [2Fe-2S]-(GS)4 cluster transport. | ||||
Sequence: E → D | ||||||
Mutagenesis | 433 | Loss of ATPase activity stimulation by [2Fe-2S]-(GS)4 cluster stimulation. Loss of the ability to couple MgATP binding with stimulation of ATPase activity at the nucleotide binding domain. Loss of [2Fe-2S]-(GS)4 cluster transport. | ||||
Sequence: E → K | ||||||
Mutagenesis | 433 | Loss of ATPase activity stimulation by [2Fe-2S]-(GS)4 cluster stimulation. Loss of the ability to couple MgATP binding with stimulation of ATPase activity at the nucleotide binding domain. Loss of [2Fe-2S]-(GS)4 cluster transport. | ||||
Sequence: E → Q | ||||||
Natural variant | VAR_055471 | 580 | in dbSNP:rs1340989 | |||
Sequence: A → V | ||||||
Natural variant | VAR_037972 | 581 | in dbSNP:rs1340989 | |||
Sequence: V → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 606 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-22 | UniProt | Mitochondrion | ||||
Sequence: MALLAMHSWRWAAAAAAFEKRR | |||||||
Chain | PRO_0000000249 | 23-752 | UniProt | Iron-sulfur clusters transporter ABCB7, mitochondrial | |||
Sequence: HSAILIRPLVSVSGSGPQWRPHQLGALGTARAYQIPESLKSITWQRLGKGNSGQFLDAAKALQVWPLIEKRTCWHGHAGGGLHTDPKEGLKDVDTRKIIKAMLSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWHTQSSRVQNHDNPKWEAKKENISKEEERKKLQEEIVNSVKGCGNCSC | |||||||
Modified residue | 216 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 251 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 336 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 340 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 342 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 743 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with C10orf88/PAAT (PubMed:25063848).
Forms a complex with ABCB10 and FECH, where a dimeric FECH bridges ABCB7 and ABCB10 homodimers; this complex may be required for cellular iron homeostasis, mitochondrial function and heme biosynthesis (PubMed:30765471).
Interacts with FECH (PubMed:30765471).
Interacts with ATP5F1A (By similarity).
Interacts with COX4I1; this interaction allows the regulation of cellular iron homeostasis and cellular reactive oxygen species (ROS) levels in cardiomyocytes (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O75027 | ABCB7 O75027 | 3 | EBI-1236950, EBI-1236950 | |
BINARY | O75027 | FECH P22830 | 9 | EBI-1236950, EBI-1390356 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 140-436 | ABC transmembrane type-1 | ||||
Sequence: VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQ | ||||||
Domain | 472-706 | ABC transporter | ||||
Sequence: VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWH |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 3 isoforms produced by Alternative splicing.
O75027-1
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
- Length752
- Mass (Da)82,641
- Last updated2000-12-01 v2
- ChecksumB1FFA57ABD24FB90
O75027-2
- Name2
- Differences from canonical
- 56-56: Q → QQ
O75027-3
- Name3
- Differences from canonical
- 112-151: Missing
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y473 | A0A2R8Y473_HUMAN | ABCB7 | 651 | ||
A0A2R8Y3N2 | A0A2R8Y3N2_HUMAN | ABCB7 | 159 | ||
A0A2R8YF35 | A0A2R8YF35_HUMAN | ABCB7 | 47 | ||
B4DGL8 | B4DGL8_HUMAN | ABCB7 | 702 | ||
A0A590UJS8 | A0A590UJS8_HUMAN | ABCB7 | 693 | ||
A0A5F9ZA98 | A0A5F9ZA98_HUMAN | ABCB7 | 757 | ||
E9PNQ5 | E9PNQ5_HUMAN | ABCB7 | 159 | ||
E9PJR8 | E9PJR8_HUMAN | ABCB7 | 188 | ||
A0A087WW65 | A0A087WW65_HUMAN | ABCB7 | 713 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_014635 | 56 | in isoform 2 | |||
Sequence: Q → QQ | ||||||
Alternative sequence | VSP_054700 | 112-151 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 141 | in Ref. 4; AAC39865 | ||||
Sequence: A → P | ||||||
Sequence conflict | 258 | in Ref. 1; BAA28861 | ||||
Sequence: R → K | ||||||
Sequence conflict | 271-276 | in Ref. 4; AAC39865 | ||||
Sequence: LLPIMF → PLPNHV | ||||||
Sequence conflict | 280 | in Ref. 4; AAC39865 | ||||
Sequence: L → LL | ||||||
Sequence conflict | 290 | in Ref. 4; AAC39865 | ||||
Sequence: G → C | ||||||
Sequence conflict | 293-297 | in Ref. 4; AAC39865 | ||||
Sequence: FALVT → LLGN | ||||||
Sequence conflict | 320-324 | in Ref. 4; AAC39865 | ||||
Sequence: IEMNK → LEIDQ | ||||||
Sequence conflict | 542 | in Ref. 9; AAD47141 | ||||
Sequence: E → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB005289 EMBL· GenBank· DDBJ | BAA28861.1 EMBL· GenBank· DDBJ | mRNA | ||
AF133659 EMBL· GenBank· DDBJ | AAD33045.1 EMBL· GenBank· DDBJ | mRNA | ||
AF241887 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241872 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241873 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241874 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241875 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241876 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241877 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241878 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241879 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241880 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241881 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241882 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241883 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241884 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241885 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF241886 EMBL· GenBank· DDBJ | AAK20173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF038950 EMBL· GenBank· DDBJ | AAC39865.1 EMBL· GenBank· DDBJ | mRNA | ||
BT009918 EMBL· GenBank· DDBJ | AAP88920.1 EMBL· GenBank· DDBJ | mRNA | ||
AL360179 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL359545 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471104 EMBL· GenBank· DDBJ | EAW98635.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC006323 EMBL· GenBank· DDBJ | AAH06323.1 EMBL· GenBank· DDBJ | mRNA | ||
AF078777 EMBL· GenBank· DDBJ | AAD47141.1 EMBL· GenBank· DDBJ | mRNA |