ABCG5_RAT
ID ABCG5_RAT Reviewed; 652 AA.
AC Q99PE7; Q8CIQ4;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ATP-binding cassette sub-family G member 5 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:Q99PE8};
DE AltName: Full=Sterolin-1 {ECO:0000250|UniProtKB:Q99PE8};
GN Name=Abcg5 {ECO:0000312|RGD:620298};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Small intestine;
RX PubMed=11138003; DOI=10.1038/83799;
RA Lee M.-H., Lu K., Hazard S., Yu H., Shulenin S., Hidaka H., Kojima H.,
RA Allikmets R., Sakuma N., Pegoraro R., Srivastava A.K., Salen G., Dean M.,
RA Patel S.B.;
RT "Identification of a gene, ABCG5, important in the regulation of dietary
RT cholesterol absorption.";
RL Nat. Genet. 27:79-83(2001).
RN [2]
RP SEQUENCE REVISION TO 2.
RA Lu K., Lee M.-H., Patel S.B.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE, TISSUE SPECIFICITY, POLYMORPHISM, AND VARIANT CYS-583.
RC STRAIN=GH, SHR, SHRSP, Sprague-Dawley, Wistar, Wistar Kyoto, and WKA;
RX PubMed=12783625; DOI=10.1186/1471-2261-3-4;
RA Yu H., Pandit B., Klett E., Lee M.-H., Lu K., Helou K., Ikeda I.,
RA Egashira N., Sato M., Klein R., Batta A., Salen G., Patel S.B.;
RT "The rat STSL locus: characterization, chromosomal assignment, and genetic
RT variations in sitosterolemic hypertensive rats.";
RL BMC Cardiovasc. Disord. 3:4-4(2003).
CC -!- FUNCTION: ABCG5 and ABCG8 form an obligate heterodimer that mediates
CC Mg(2+)- and ATP-dependent sterol transport across the cell membrane.
CC Plays an essential role in the selective transport of dietary plant
CC sterols and cholesterol in and out of the enterocytes and in the
CC selective sterol excretion by the liver into bile. Required for normal
CC sterol homeostasis. The heterodimer with ABCG8 has ATPase activity.
CC {ECO:0000250|UniProtKB:Q9H222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q99PE8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000250|UniProtKB:Q99PE8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + sitosterol(in) = ADP + H(+) + phosphate +
CC sitosterol(out); Xref=Rhea:RHEA:39103, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27693, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q99PE8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39104;
CC Evidence={ECO:0000250|UniProtKB:Q99PE8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q99PE8};
CC -!- SUBUNIT: Heterodimer with ABCG8. {ECO:0000250|UniProtKB:Q9H222}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H222};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H222}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q9H222}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9H222}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level). Expressed
CC only in liver and intestine. {ECO:0000269|PubMed:12783625}.
CC -!- DOMAIN: The Walker motif (consensus sequence G-X-X-G-X-G-K-[ST]-T) is
CC expected to bind ATP. Within this motif, the conserved Lys is essential
CC for transport activity mediated by the heterodimer with ABCG8.
CC {ECO:0000250|UniProtKB:Q99PE8}.
CC -!- PTM: N-glycosylated. N-glycosylation is important for efficient export
CC out of the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q99PE8}.
CC -!- POLYMORPHISM: The polymorphism at position 583 is found in strains SHR,
CC SHRSP and Wistar Kyoto which are both hypertensive and sitosterolemic.
CC Strains which are hypertensive but not sitosterolemic do not contain a
CC polymorphism at this position. {ECO:0000269|PubMed:12783625}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR EMBL; AF312714; AAG53098.3; -; mRNA.
DR EMBL; AY145899; AAN64275.1; -; Genomic_DNA.
DR RefSeq; NP_446206.2; NM_053754.2.
DR AlphaFoldDB; Q99PE7; -.
DR SMR; Q99PE7; -.
DR STRING; 10116.ENSRNOP00000007174; -.
DR GlyGen; Q99PE7; 2 sites.
DR PaxDb; Q99PE7; -.
DR Ensembl; ENSRNOT00000007174; ENSRNOP00000007174; ENSRNOG00000005250.
DR GeneID; 114628; -.
DR KEGG; rno:114628; -.
DR UCSC; RGD:620298; rat.
DR CTD; 64240; -.
DR RGD; 620298; Abcg5.
DR eggNOG; KOG0061; Eukaryota.
DR GeneTree; ENSGT00940000157985; -.
DR HOGENOM; CLU_000604_57_9_1; -.
DR InParanoid; Q99PE7; -.
DR OMA; RVRPWWD; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; Q99PE7; -.
DR TreeFam; TF105212; -.
DR Reactome; R-RNO-1369062; ABC transporters in lipid homeostasis.
DR PRO; PR:Q99PE7; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000005250; Expressed in jejunum and 7 other tissues.
DR Genevisible; Q99PE7; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0038183; P:bile acid signaling pathway; IEP:RGD.
DR GO; GO:0033344; P:cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IEP:RGD.
DR GO; GO:0045796; P:negative regulation of intestinal cholesterol absorption; ISO:RGD.
DR GO; GO:0010949; P:negative regulation of intestinal phytosterol absorption; ISO:RGD.
DR GO; GO:0010212; P:response to ionizing radiation; IEP:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0015918; P:sterol transport; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0070328; P:triglyceride homeostasis; IEP:RGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Lipid transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..652
FT /note="ATP-binding cassette sub-family G member 5"
FT /id="PRO_0000093395"
FT TOPO_DOM 1..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 385..405
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 406..422
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 423..443
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 444..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 469..490
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 491..501
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 502..522
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 523..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 530..550
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 551..624
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 625..645
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 646..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT DOMAIN 39..294
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 389..646
FT /note="ABC transmembrane type-2"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 583
FT /note="G -> C (in strain: SHR, SHRSP and Wistar Kyoto)"
FT /evidence="ECO:0000269|PubMed:12783625"
SQ SEQUENCE 652 AA; 73372 MW; 49FEF7372269299D CRC64;
MSELPFLSPE GARGPHNNRG SQSSLEEGSV TGSEARHSLG VLNVSFSVSN RVGPWWNIKS
CQQKWDRKIL KDVSLYIESG QTMCILGSSG SGKTTLLDAI SGRLRRTGTL EGEVFVNGCE
LRRDQFQDCV SYLLQSDVFL SSLTVRETLR YTAMLALRSS SADFYDKKVE AVLTELSLSH
VADQMIGNYN FGGISSGERR RVSIAAQLLQ DPKVMMLDEP TTGLDCMTAN HIVLLLVELA
RRNRIVIVTI HQPRSELFHH FDKIAILTYG ELVFCGTPEE MLGFFNNCGY PCPEHSNPFD
FYMDLTSVDT QSREREIETY KRVQMLESAF RQSDICHKIL ENIERTRHLK TLPMVPFKTK
NPPGMFCKLG VLLRRVTRNL MRNKQVVIMR LVQNLIMGLF LIFYLLRVQN NMLKGAVQDR
VGLLYQLVGA TPYTGMLNAV NLFPMLRAVS DQESQDGLYQ KWQMLLAYVL HALPFSIVAT
VIFSSVCYWT LGLYPEVARF GYFSAALLAP HLIGEFLTLV LLGMVQNPNI VNSIVALLSI
SGLLIGSGFI RNIEEMPIPL KILGYFTFQK YCCEILVVNE FYGLNFTCGG SNTSVPNNPM
CSMTQGIQFI EKTCPGATSR FTTNFLILYS FIPTLVILGM VVFKVRDYLI SR
