ABCG1
entrez
9619
canonical
uniprot
P45844
canonical
ensembl
ENSG00000160179
resolver
ensp
ENSP00000291524
resolver
ensp
ENSP00000339744
resolver
ensp
ENSP00000354995
resolver
ensp
ENSP00000381464
resolver
ensp
ENSP00000381467
resolver
ensp
ENSP00000381475
resolver
ensp
ENSP00000662659
resolver
ensp
ENSP00000716796
resolver
genesymbol
ABCG1
resolver
genesymbol_syn
ABC8
resolver
genesymbol_syn
WHT1
resolver
hgnc
HGNC:73
resolver
uniprot
Q86SU8
resolver
uniprot
Q96L76
resolver
uniprot
Q9BXK6
resolver
uniprot
Q9BXK7
resolver
uniprot
Q9BXK8
resolver
uniprot
Q9BXK9
resolver
uniprot
Q9BXL0
resolver
uniprot
Q9BXL1
resolver
uniprot
Q9BXL2
resolver
uniprot
Q9BXL3
resolver
uniprot
Q9BXL4
resolver
uniprot_entry
ABCG1_HUMAN
resolver
uniprot_sec
Q86SU8
resolver
uniprot_sec
Q96L76
resolver
uniprot_sec
Q9BXK6
resolver
uniprot_sec
Q9BXK7
resolver
uniprot_sec
Q9BXK8
resolver
uniprot_sec
Q9BXK9
resolver
uniprot_sec
Q9BXL0
resolver
uniprot_sec
Q9BXL1
resolver
uniprot_sec
Q9BXL2
resolver
uniprot_sec
Q9BXL3
resolver
uniprot_sec
Q9BXL4
resolver
activity_regulation
ACTIVITY REGULATION: The cholesterol efflux is enhanced by APOA1. {ECO:0000269|PubMed:16702602}.
uniprot
proteins
amino_acid_sequence
MACLMAAFSVGTAMNASSYSAEMTEPKSVCVSVDEVVSSNMEATETDLLNGHLKKVDNNLTEAQRFSSLPRRAAVNIEFRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSRLVRAVREGMCDSDHKRDLGGDAEVNPFLWHRPSEEVKQTKRLKGLRKDSSSMEGCHSFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMGVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGLDREDLHCDIDETCHFQKSEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER
uniprot
proteins
ec_number
7.6.2.-
uniprot
proteins
function
FUNCTION: Catalyzes the efflux of phospholipids such as sphingomyelin, cholesterol and its oxygenated derivatives like 7beta-hydroxycholesterol and this transport is coupled to hydrolysis of ATP (PubMed:17408620, PubMed:24576892). The lipid efflux is ALB-dependent (PubMed:16702602). Is an active component of the macrophage lipid export complex. Could also be involved in intracellular lipid transport processes. The role in cellular lipid homeostasis may not be limited to macrophages. Prevents cell death by transporting cytotoxic 7beta-hydroxycholesterol (PubMed:17408620). {ECO:0000269|PubMed:16702602, ECO:0000269|PubMed:17408620, ECO:0000269|PubMed:24576892}.
uniprot
proteins
mass_dalton
75592
uniprot
proteins
mutagenesis
MUTAGEN 30; /note="C->A: No significant effect."; /evidence="ECO:0000269|PubMed:23388354"; MUTAGEN 124; /note="K->M: Affects ATP binding. Does not affect efflux of 7beta-hydroxycholesterol. Does not affect localization at plasma membrane. Does not affect homodimerization. Decreases cholesterol and phospholipids efflux. Does not affect heretodimerization with ABCG4."; /evidence="ECO:0000269|PubMed:16702602, ECO:0000269|PubMed:17408620, ECO:0000269|PubMed:27228027"; MUTAGEN 154; /note="C->A: No significant effect."; /evidence="ECO:0000269|PubMed:23388354"; MUTAGEN 315; /note="C->A,S: Significantly decreases ABCG1-mediated cholesterol efflux."; /evidence="ECO:0000269|PubMed:23388354"; MUTAGEN 394; /note="C->A: No significant effect."; /evidence="ECO:0000269|PubMed:23388354"; MUTAGEN 406; /note="C->A: No significant effect."; /evidence="ECO:0000269|PubMed:23388354"; MUTAGEN 491; /note="Y->A: Significantly reduces interaction with CAV1; when associated with A-493. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-493."; /evidence="ECO:0000269|PubMed:24576892"; MUTAGEN 493; /note="Y->A: Significantly reduces interaction with CAV1; when associated with A-491. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-491."; /evidence="ECO:0000269|PubMed:24576892"; MUTAGEN 498; /note="Y->A: Significantly reduces interaction with CAV1; when associated with A-499. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-499. Affects subcellular location at plasma membrane; when associated with A-499. Affects ABCG1 traffincking to the plasma membrane; when associated with A-499."; /evidence="ECO:0000269|PubMed:24576892"; MUTAGEN 498; /note="Y->F: Does not affect ABCG1-mediated cholesterol efflux; when associated with I-499."; /evidence="ECO:0000269|PubMed:24576892"; MUTAGEN 498; /note="Y->I: Dramatically reduces the ability of ABCG1 to mediate cholesterol efflux; when associated with I-499."; /evidence="ECO:0000269|PubMed:24576892"; MUTAGEN 498; /note="Y->W: Does not affect ABCG1-mediated cholesterol efflux; when associated with I-499."; /evidence="ECO:0000269|PubMed:24576892"; MUTAGEN 499; /note="Y->A: Significantly reduces interaction with CAV1; when associated with A-498. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-498. Affects subcellular location at plasma membrane; when associated with A-498. Affects ABCG1 traffincking to the plasma membrane; when associated with A-498."; /evidence="ECO:0000269|PubMed:24576892"; MUTAGEN 499; /note="Y->F: Does not affect ABCG1-mediated cholesterol efflux; when associated with I-498."; /evidence="ECO:0000269|PubMed:24576892"; MUTAGEN 499; /note="Y->I: Dramatically reduces the ability of ABCG1 to mediate cholesterol efflux; when associated with I-498."; /evidence="ECO:0000269|PubMed:24576892"; MUTAGEN 499; /note="Y->W: Does not affect ABCG1-mediated cholesterol efflux; when associated with I-498."; /evidence="ECO:0000269|PubMed:24576892
uniprot
proteins
post_translational_modification
PTM: Palmitoylation at Cys-315 seems important for trafficking from the endoplasmic reticulum. {ECO:0000269|PubMed:23388354}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCG family
uniprot
proteins
protein_family
Eye pigment precursor importer (TC 3.A.1.204) subfamily
uniprot
proteins
pubmed
10639163
uniprot
proteins
pubmed
10799558
uniprot
proteins
pubmed
10830953
uniprot
proteins
pubmed
10950923
uniprot
proteins
pubmed
11162488
uniprot
proteins
pubmed
11279031
uniprot
proteins
pubmed
11350058
uniprot
proteins
pubmed
11500512
uniprot
proteins
pubmed
11590207
uniprot
proteins
pubmed
12032171
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16702602
uniprot
proteins
pubmed
17408620
uniprot
proteins
pubmed
22042635
uniprot
proteins
pubmed
23388354
uniprot
proteins
pubmed
24576892
uniprot
proteins
pubmed
27228027
uniprot
proteins
pubmed
8659545
uniprot
proteins
pubmed
9034316
uniprot
proteins
sequence_length
678
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22042635}; Multi-pass membrane protein {ECO:0000269|PubMed:22042635}. Golgi apparatus membrane {ECO:0000269|PubMed:22042635}; Multi-pass membrane protein {ECO:0000269|PubMed:22042635}. Cell membrane {ECO:0000269|PubMed:16702602, ECO:0000269|PubMed:24576892}. Note=Predominantly localized in the intracellular compartments mainly associated with the endoplasmic reticulum (ER) and Golgi membranes.
uniprot
proteins
transmembrane_region
TRANSMEM 427..445; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 457..477; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 507..525; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 534..555; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 568..586; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 650..669; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins