Abcg8
entrez
67470
canonical
uniprot
Q9DBM0
canonical
ensembl
ENSMUSG00000024254
resolver
ensp
ENSMUSP00000035246
resolver
ensp
ENSMUSP00000126675
resolver
ensp
ENSMUSP00000127785
resolver
enst
ENSMUST00000170725
resolver
enst
ENSMUST00000171915
resolver
genesymbol
Abcg8
resolver
uniprot
E9Q0P2
resolver
uniprot
F6ZTL4
resolver
uniprot
Q7TSR6
resolver
uniprot
Q8R543
resolver
uniprot_entry
ABCG8_MOUSE
resolver
uniprot_entry
E9Q0P2_MOUSE
resolver
uniprot_entry
F6ZTL4_MOUSE
resolver
uniprot_entry
Q7TSR6_MOUSE
resolver
uniprot_sec
Q8R543
resolver
activity_regulation
ACTIVITY REGULATION: Cholesterol transport is inhibited by vanadate and by beryllium fluoride. {ECO:0000269|PubMed:16867993}.
uniprot
proteins
amino_acid_sequence
MAEKTKEETQLWNGTVLQDASQGLQDSLFSSESDNSLYFTYSGQSNTLEVRDLTYQVDIASQVPWFEQLAQFKIPWRSHSSQDSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMKSGQIWINGQPSTPQLVRKCVAHVRQHDQLLPNLTVRETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQYFTSIGHPCPRYSNPADFYVDLTSIDRRSKEREVATVEKAQSLAALFLEKVQGFDDFLWKAEAKELNTSTHTVSLTLTQDTDCGTAVELPGMIEQFSTLIRRQISNDFRDLPTLLIHGSEACLMSLIIGFLYYGHGAKQLSFMDTAALLFMIGALIPFNVILDVVSKCHSERSMLYYELEDGLYTAGPYFFAKILGELPEHCAYVIIYAMPIYWLTNLRPVPELFLLHFLLVWLVVFCCRTMALAASAMLPTFHMSSFFCNALYNSFYLTAGFMINLDNLWIVPAWISKLSFLRWCFSGLMQIQFNGHLYTTQIGNFTFSILGDTMISAMDLNSHPLYAIYLIVIGISYGFLFLYYLSLKLIKQKSIQDW
uniprot
proteins
ec_number
7.6.2.-
uniprot
proteins
function
FUNCTION: ABCG5 and ABCG8 form an obligate heterodimer that mediates Mg(2+)- and ATP-dependent sterol transport across the cell membrane (PubMed:16352607, PubMed:16867993, PubMed:18402465). Plays an essential role in the selective transport of the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile (PubMed:12444248, PubMed:14504269, PubMed:14657202, PubMed:25378657). Plays an important role in preventing the accumulation of dietary plant sterols in the body (PubMed:12444248, PubMed:14657202). Required for normal sterol homeostasis (PubMed:12444248, PubMed:14657202). The heterodimer with ABCG5 has ATPase activity (PubMed:16352607, PubMed:16867993). {ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:14657202, ECO:0000269|PubMed:16352607, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465, ECO:0000269|PubMed:25378657}.
uniprot
proteins
mass_dalton
75996
uniprot
proteins
mutagenesis
MUTAGEN 112; /note="R->K,M: No effect on ATP-binding and on expression of both ABCG5 and ABCG8. No effect on sterol transport."; /evidence="ECO:0000269|PubMed:16352607"; MUTAGEN 214; /note="V->I: No effect on sterol transport; when associated with S-216."; /evidence="ECO:0000269|PubMed:16352607"; MUTAGEN 216; /note="G->S: No effect on sterol transport; when associated with I-214."; /evidence="ECO:0000269|PubMed:16352607"; MUTAGEN 217; /note="G->D: Abolishes cholesterol transport activity, and nearly abolishes plant sterol transport."; /evidence="ECO:0000269|PubMed:16352607, ECO:0000269|PubMed:16867993"; MUTAGEN 239; /note="E->D: No effect on sterol transport."; /evidence="ECO:0000269|PubMed:16352607"; MUTAGEN 239; /note="E->Q: Mildly decreases cholesterol transport. No effect on plant sterol transport."; /evidence="ECO:0000269|PubMed:16352607"; MUTAGEN 619; /note="N->A,Q: Abolishes N-glycosylation."; /evidence="ECO:0000269|PubMed:15054092"; MUTAGEN 664..673; /note="Missing: Abolishes expression at the apical cell membrane. Strongly decreases cholesterol secretion into bile."; /evidence="ECO:0000269|PubMed:18402465
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:12208867, PubMed:12444248, PubMed:15054092, PubMed:16867993, PubMed:18402465). N-glycosylation is important for efficient export out of the endoplasmic reticulum (PubMed:15054092). {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:15054092, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465}.
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
11099417
uniprot
proteins
pubmed
11452359
uniprot
proteins
pubmed
11907139
uniprot
proteins
pubmed
12208867
uniprot
proteins
pubmed
12444248
uniprot
proteins
pubmed
12777468
uniprot
proteins
pubmed
14504269
uniprot
proteins
pubmed
14657202
uniprot
proteins
pubmed
15040800
uniprot
proteins
pubmed
15054092
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16352607
uniprot
proteins
pubmed
16867993
uniprot
proteins
pubmed
18402465
uniprot
proteins
pubmed
25378657
uniprot
proteins
sequence_length
673
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:18402465, ECO:0000305|PubMed:16352607}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465}; Multi-pass membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 417..437; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:Q9H221"; TRANSMEM 448..468; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:Q9H221"; TRANSMEM 498..518; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:Q9H221"; TRANSMEM 528..548; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:Q9H221"; TRANSMEM 556..576; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:Q9H221"; TRANSMEM 640..660; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:Q9H221
uniprot
proteins