Abcg5
entrez
27409
canonical
uniprot
Q99PE8
canonical
ensembl
ENSMUSG00000040505
resolver
ensp
ENSMUSP00000069495
resolver
enst
ENSMUST00000066175
resolver
genesymbol
Abcg5
resolver
uniprot
Q540E8
resolver
uniprot_entry
ABCG5_MOUSE
resolver
uniprot_sec
Q540E8
resolver
activity_regulation
ACTIVITY REGULATION: Cholesterol transport is inhibited by vanadate and by beryllium fluoride. {ECO:0000269|PubMed:16867993}.
uniprot
proteins
amino_acid_sequence
MGELPFLSPEGARGPHINRGSLSSLEQGSVTGTEARHSLGVLHVSYSVSNRVGPWWNIKSCQQKWDRQILKDVSLYIESGQIMCILGSSGSGKTTLLDAISGRLRRTGTLEGEVFVNGCELRRDQFQDCFSYVLQSDVFLSSLTVRETLRYTAMLALCRSSADFYNKKVEAVMTELSLSHVADQMIGSYNFGGISSGERRRVSIAAQLLQDPKVMMLDEPTTGLDCMTANQIVLLLAELARRDRIVIVTIHQPRSELFQHFDKIAILTYGELVFCGTPEEMLGFFNNCGYPCPEHSNPFDFYMDLTSVDTQSREREIETYKRVQMLECAFKESDIYHKILENIERARYLKTLPTVPFKTKDPPGMFGKLGVLLRRVTRNLMRNKQAVIMRLVQNLIMGLFLIFYLLRVQNNTLKGAVQDRVGLLYQLVGATPYTGMLNAVNLFPMLRAVSDQESQDGLYHKWQMLLAYVLHVLPFSVIATVIFSSVCYWTLGLYPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNSIVALLSISGLLIGSGFIRNIQEMPIPLKILGYFTFQKYCCEILVVNEFYGLNFTCGGSNTSMLNHPMCAITQGVQFIEKTCPGATSRFTANFLILYGFIPALVILGIVIFKVRDYLISR
uniprot
proteins
disease_involvement
DISEASE: Note=A spontaneous mutation gives raise to thrombocytopenia and cardiomyopathy (trac), with recessive inheritance and fully penetrant phenotype. Mice are small, infertile, and have shortened lifespan. {ECO:0000269|PubMed:19846887}.
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 dietary plant sterols and 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:19846887, PubMed:25378657). Required for normal sterol homeostasis (PubMed:12444248, PubMed:14657202). The heterodimer with ABCG8 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:19846887, ECO:0000269|PubMed:25378657}.
uniprot
proteins
mass_dalton
73244
uniprot
proteins
mutagenesis
MUTAGEN 61; /note="C->A: Abolishes palmitoylation. No effect on function and subcellular location."; /evidence="ECO:0000269|PubMed:18402465"; MUTAGEN 93; /note="K->M: Disrupts sterol transport activity. Decreases expression of both ABCG5 and ABCG8."; /evidence="ECO:0000269|PubMed:16352607, ECO:0000269|PubMed:16867993"; MUTAGEN 93; /note="K->R: Strongly reduces cholesterol transport activity, but has little effect on biliary secretion of campesterol and sitosterol. No effect on ATP-binding and on expression of ABCG5 and ABCG8."; /evidence="ECO:0000269|PubMed:16352607"; MUTAGEN 194; /note="I->V: No effect on cholesterol and sitosterol transport activity; when associated with G-196."; /evidence="ECO:0000269|PubMed:16352607"; MUTAGEN 196; /note="S->G: No effect on cholesterol and sitosterol transport activity; when associated with V-194."; /evidence="ECO:0000269|PubMed:16352607"; MUTAGEN 197; /note="G->D: No effect on cholesterol and sitosterol transport activity. Mildly reduced expression of ABCG5 and ABCG8."; /evidence="ECO:0000269|PubMed:16352607"; MUTAGEN 219; /note="E->D: Decreases expression of both ABCG5 and ABCG8. Disrupts sterol transport activity."; /evidence="ECO:0000269|PubMed:16352607"; MUTAGEN 219; /note="E->Q: Strongly decreases expression of both ABCG5 and ABCG8. Disrupts sterol transport activity."; /evidence="ECO:0000269|PubMed:16352607"; MUTAGEN 585; /note="N->Q: Loss of one N-glycosylation site. Abolishes N-glycosylation; when associated with Q-592."; /evidence="ECO:0000269|PubMed:15054092"; MUTAGEN 592; /note="N->Q: Loss of one N-glycosylation site. Abolishes N-glycosylation; when associated with Q-585."; /evidence="ECO:0000269|PubMed:15054092
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:12208867, PubMed:12444248, PubMed:15040800, PubMed:15054092, PubMed:16867993, PubMed:18402465, PubMed:25378657). 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:15040800, ECO:0000269|PubMed:15054092, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465, ECO:0000269|PubMed:25378657}.
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
11138003
uniprot
proteins
pubmed
11907139
uniprot
proteins
pubmed
12208867
uniprot
proteins
pubmed
12444248
uniprot
proteins
pubmed
12777468
uniprot
proteins
pubmed
12949731
uniprot
proteins
pubmed
14504269
uniprot
proteins
pubmed
14657202
uniprot
proteins
pubmed
15040800
uniprot
proteins
pubmed
15054092
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16352607
uniprot
proteins
pubmed
16867993
uniprot
proteins
pubmed
18402465
uniprot
proteins
pubmed
19846887
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25378657
uniprot
proteins
sequence_length
652
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:15040800, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465}; Multi-pass membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 385..405; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:Q9H222"; TRANSMEM 423..443; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:Q9H222"; TRANSMEM 469..490; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:Q9H222"; TRANSMEM 502..522; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:Q9H222"; TRANSMEM 530..550; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:Q9H222"; TRANSMEM 625..645; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:Q9H222
uniprot
proteins