O94911 · ABCA8_HUMAN
- ProteinABC-type organic anion transporter ABCA8
- GeneABCA8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1621 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Isoform 1
Catalyzes ATP-dependent import of organic anions such as taurocholate and estrone sulfate (PubMed:12379217).
In vitro, also imports ochratoxin A (PubMed:12379217).
Also mediates cholesterol efflux independent of apolipoprotein, and plays a role in sphingomyelin production in oligodendrocytes (PubMed:23560799).
In vitro, also imports ochratoxin A (PubMed:12379217).
Also mediates cholesterol efflux independent of apolipoprotein, and plays a role in sphingomyelin production in oligodendrocytes (PubMed:23560799).
Isoform 3
Catalyzes ATP-dependent efflux of cholesterol and taurocholate (PubMed:29300488).
Interaction with ABCA1 potentiates cholesterol efflux to lipid-free APOA1, which regulates high-density lipoprotein cholesterol levels (PubMed:28882873).
Interaction with ABCA1 potentiates cholesterol efflux to lipid-free APOA1, which regulates high-density lipoprotein cholesterol levels (PubMed:28882873).
Catalytic activity
Isoform 3
ATP + H2O + taurocholate(in) = ADP + H+ + phosphate + taurocholate(out)This reaction proceeds in the forward direction.CHEBI:30616 + CHEBI:15377 + taurocholate (in)CHEBI:36257= CHEBI:456216 + CHEBI:15378 + CHEBI:43474 + taurocholate (out)CHEBI:36257- ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H+ + phosphateThis reaction proceeds in the forward direction.
Isoform 1
ATP + estrone 3-sulfate(out) + H2O = ADP + estrone 3-sulfate(in) + H+ + phosphateThis reaction proceeds in the forward direction.Isoform 1
ATP + H2O + leukotriene C4(out) = ADP + H+ + leukotriene C4(in) + phosphateThis reaction proceeds in the forward direction.Isoform 1
ATP + H2O + taurocholate(out) = ADP + H+ + phosphate + taurocholate(in)This reaction proceeds in the forward direction.Isoform 1
17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Activity regulation
Isoform 1
Dofequidar (MS-209) and ochratoxin A inhibited the 17beta-estradiol 17-O-(beta-D-glucuronate) influx.
Isoform 3
Cholesterol efflux is increased by extracellularly applied taurocholate.
Kinetics
Isoform 1
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
30.4 μM | estradiol-beta-glucuronide | |||||
0.1 μM | LTC4 | |||||
10.3 μM | taurochlorate | |||||
5 μM | PAH | |||||
0.5 μM | estrone sulfate | |||||
0.4 μM | ochratoxin A |
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | basolateral plasma membrane | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | plasma membrane | |
Molecular Function | ABC-type transporter activity | |
Molecular Function | ABC-type xenobiotic transporter activity | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATPase-coupled transmembrane transporter activity | |
Molecular Function | lipid transporter activity | |
Biological Process | cholesterol efflux | |
Biological Process | cholesterol transport | |
Biological Process | lipid transport | |
Biological Process | positive regulation of cholesterol efflux | |
Biological Process | regulation of cholesterol efflux | |
Biological Process | sphingomyelin biosynthetic process | |
Biological Process | transmembrane transport | |
Biological Process | xenobiotic transmembrane transport | |
Biological Process | xenobiotic transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameABC-type organic anion transporter ABCA8
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO94911
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Predominantly expressed on the sinusoidal plasma membrane.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 30-50 | Helical | ||||
Sequence: SLMEWLNSLLLLLCLYIYPHS | ||||||
Transmembrane | 220-240 | Helical | ||||
Sequence: VITDLYLFSCIISFSSFIYYA | ||||||
Transmembrane | 268-288 | Helical | ||||
Sequence: SWGLLYAGFIFIMALFLALVI | ||||||
Transmembrane | 299-319 | Helical | ||||
Sequence: FMVVFSLFLLYGLSLVALAFL | ||||||
Transmembrane | 327-347 | Helical | ||||
Sequence: SFLTGLVVFLLTVFWGCLGFT | ||||||
Transmembrane | 359-379 | Helical | ||||
Sequence: WILSLLSPFAFMLGMAQLLHL | ||||||
Transmembrane | 397-417 | Helical | ||||
Sequence: LIVATNFMLAFDTCLYLALAI | ||||||
Transmembrane | 864-884 | Helical | ||||
Sequence: LALLLILMAGFCPLLVEYTMV | ||||||
Transmembrane | 1019-1039 | Helical | ||||
Sequence: IGFLAYIMFWLVLTSSCPPYI | ||||||
Transmembrane | 1070-1090 | Helical | ||||
Sequence: ALVDVSLYFLVFVFIYLMSYI | ||||||
Transmembrane | 1106-1126 | Helical | ||||
Sequence: IPCAVGYSFSLIFMTYVISFI | ||||||
Transmembrane | 1136-1156 | Helical | ||||
Sequence: IWSFCFYVVTVFSVAGFAFSI | ||||||
Transmembrane | 1161-1181 | Helical | ||||
Sequence: IPFIFTFLIPPATMIGCLFLS | ||||||
Transmembrane | 1197-1217 | Helical | ||||
Sequence: VQPFLVFLIPFLHFIIFLFTL |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_027590 | 256 | in dbSNP:rs16973446 | |||
Sequence: T → A | ||||||
Natural variant | VAR_027591 | 331 | in dbSNP:rs4147979 | |||
Sequence: G → S | ||||||
Natural variant | VAR_048130 | 416 | in dbSNP:rs35621847 | |||
Sequence: A → V | ||||||
Natural variant | VAR_027592 | 489 | in dbSNP:rs12150510 | |||
Sequence: Y → F | ||||||
Natural variant | VAR_084139 | 649 | affects localization at the plasma membrane; loss of cholesterol efflux to APOA1; dbSNP:rs144777539 | |||
Sequence: P → R | ||||||
Natural variant | VAR_048131 | 659 | in dbSNP:rs35844316 | |||
Sequence: L → R | ||||||
Natural variant | VAR_027593 | 720 | in dbSNP:rs16973424 | |||
Sequence: C → G | ||||||
Natural variant | VAR_084140 | 781-1621 | loss of expression; loss of cholesterol efflux to APOA1 | |||
Sequence: Missing | ||||||
Natural variant | VAR_048132 | 1470 | in dbSNP:rs35403175 | |||
Sequence: G → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,726 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000250677 | 1-1621 | UniProt | ABC-type organic anion transporter ABCA8 | |||
Sequence: MRKRKISVCQQTWALLCKNFLKKWRMKRESLMEWLNSLLLLLCLYIYPHSHQVNDFSSLLTMDLGRVDTFNESRFSVVYTPVTNTTQQIMNKVASTPFLAGKEVLGLPDEESIKEFTANYPEEIVRVTFTNTYSYHLKFLLGHGMPAKKEHKDHTAHCYETNEDVYCEVSVFWKEGFVALQAAINAAIIEITTNHSVMEELMSVTGKNMKMHSFIGQSGVITDLYLFSCIISFSSFIYYASVNVTRERKRMKALMTMMGLRDSAFWLSWGLLYAGFIFIMALFLALVIRSTQFIILSGFMVVFSLFLLYGLSLVALAFLMSILVKKSFLTGLVVFLLTVFWGCLGFTSLYRHLPASLEWILSLLSPFAFMLGMAQLLHLDYDLNSNAFPHPSDGSNLIVATNFMLAFDTCLYLALAIYFEKILPNEYGHRRPPLFFLKSSFWSQTQKTDHVALEDEMDADPSFHDSFEQAPPEFQGKEAIRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWGIGYHLSLQLNEICVEENITSLVKQHIPDAKLSAKSEGKLIYTLPLERTNKFPELYKDLDSYPDLGIENYGVSMTTLNEVFLKLEGKSTINESDIAILGEVQAEKADDTERLVEMEQVLSSLNKMRKTIGGVALWRQQICAIARVRLLKLKHERKALLALLLILMAGFCPLLVEYTMVKIYQNSYTWELSPHLYFLAPGQQPHDPLTQLLIINKTGASIDDFIQSVEHQNIALEVDAFGTRNGTDDPSYNGAITVCCNEKNYSFSLACNAKRLNCFPVLMDIVSNGLLGMVKPSVHIRTERSTFLENGQDNPIGFLAYIMFWLVLTSSCPPYIAMSSIDDYKNRARSQLRISGLSPSAYWFGQALVDVSLYFLVFVFIYLMSYISNFEDMLLTIIHIIQIPCAVGYSFSLIFMTYVISFIFRKGRKNSGIWSFCFYVVTVFSVAGFAFSIFESDIPFIFTFLIPPATMIGCLFLSSHLLFSSLFSEERMDVQPFLVFLIPFLHFIIFLFTLRCLEWKFGKKSMRKDPFFRISPRSSDVCQNPEEPEGEDEDVQMERVRTANALNSTNFDEKPVIIASCLRKEYAGKRKGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMKVKNLAQVEPLHAEILRLFPQAARQERYSSLMVYKLPVEDVQPLAQAFFKLEKVKQSFDLEEYSLSQSTLEQVFLELSKEQELGDFEEDFDPSVKWKLLPQEEP | |||||||
Glycosylation | 71 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 84 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 194 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 243 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 484 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 555 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 616 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 724 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 748 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 749 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 755 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 762 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Glycosylation | 797 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 919 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 948 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 967 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1270 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1308 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1373 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1435 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed with higher expression in heart, skeletal muscle and liver (PubMed:12379217, PubMed:28882873, PubMed:29300488).
Highly expressed in the superior frontal white matter and inferior temporal white matter (PubMed:12379217).
Highly expressed in the superior frontal white matter and inferior temporal white matter (PubMed:12379217).
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 480-715 | ABC transporter 1 | ||||
Sequence: IRIRNVTKEYKGKPDKIEALKDLVFDIYEGQITAILGHSGAGKSTLLNILSGLSVPTKGSVTIYNNKLSEMADLENLSKLTGVCPQSNVQFDFLTVRENLRLFAKIKGILPQEVDKEIQRVLLELEMKNIQDVLAQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHQVWNLLKERKTDRVILFSTQFMDEADILADRKVFLSQGKLKCAGSSLFLKKKWGIGYHLSLQ | ||||||
Domain | 1285-1518 | ABC transporter 2 | ||||
Sequence: LRKEYAGKRKGCFSKRKNKIATRNVSFCVRKGEVLGLLGHNGAGKSTSIKVITGDTKPTAGQVLLKGSGGGDALEFLGYCPQENALWPNLTVRQHLEVYAAVKGLRKGDAEVAITRLVDALKLQDQLKSPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIRATFRNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMK |
Sequence similarities
Belongs to the ABC transporter superfamily. ABCA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O94911-3
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.
- Name3
- Length1,621
- Mass (Da)183,677
- Last updated2021-02-10 v4
- ChecksumC50C8E2624BA4734
O94911-1
- Name1
- Differences from canonical
- 598-637: Missing
O94911-2
- Name2
- Differences from canonical
- 267-1621: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A075B774 | A0A075B774_HUMAN | ABCA8 | 702 | ||
A0A0A0MSU4 | A0A0A0MSU4_HUMAN | ABCA8 | 1616 | ||
K7ELK9 | K7ELK9_HUMAN | ABCA8 | 115 |
Sequence caution
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB020629 EMBL· GenBank· DDBJ | BAA74845.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC005922 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC015844 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC024003 EMBL· GenBank· DDBJ | AAH24003.1 EMBL· GenBank· DDBJ | mRNA | ||
BC047765 EMBL· GenBank· DDBJ | AAH47765.1 EMBL· GenBank· DDBJ | mRNA | ||
BC094689 EMBL· GenBank· DDBJ | AAH94689.1 EMBL· GenBank· DDBJ | mRNA | ||
BC130280 EMBL· GenBank· DDBJ | AAI30281.1 EMBL· GenBank· DDBJ | mRNA |