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Protein

ATP-binding cassette sub-family G member 5

Gene

Abcg5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

ABCG5 and ABCG8 form an obligate heterodimer that mediates Mg2+- and ATP-dependent sterol transport across the cell membrane. 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. Required for normal sterol homeostasis. The heterodimer with ABCG8 has ATPase activity.By similarity

Cofactori

Mg2+By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi87 – 94ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processLipid transport, Transport
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-1369062 ABC transporters in lipid homeostasis

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-binding cassette sub-family G member 5
Alternative name(s):
Sterolin-1
Gene namesi
Name:Abcg5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi620298 Abcg5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 384CytoplasmicBy similarityAdd BLAST384
Transmembranei385 – 405Helical; Name=1By similarityAdd BLAST21
Topological domaini406 – 422ExtracellularBy similarityAdd BLAST17
Transmembranei423 – 443Helical; Name=2By similarityAdd BLAST21
Topological domaini444 – 468CytoplasmicBy similarityAdd BLAST25
Transmembranei469 – 490Helical; Name=3By similarityAdd BLAST22
Topological domaini491 – 501ExtracellularBy similarityAdd BLAST11
Transmembranei502 – 522Helical; Name=4By similarityAdd BLAST21
Topological domaini523 – 529CytoplasmicBy similarity7
Transmembranei530 – 550Helical; Name=5By similarityAdd BLAST21
Topological domaini551 – 624ExtracellularBy similarityAdd BLAST74
Transmembranei625 – 645Helical; Name=6By similarityAdd BLAST21
Topological domaini646 – 652CytoplasmicBy similarity7

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000933951 – 652ATP-binding cassette sub-family G member 5Add BLAST652

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi585N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi592N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

N-glycosylated. N-glycosylation is important for efficient export out of the endoplasmic reticulum.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ99PE7
PRIDEiQ99PE7

Expressioni

Tissue specificityi

Detected in liver (at protein level). Expressed only in liver and intestine.1 Publication

Gene expression databases

BgeeiENSRNOG00000005250
GenevisibleiQ99PE7 RN

Interactioni

Subunit structurei

Heterodimer with ABCG8.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007174

Structurei

3D structure databases

ProteinModelPortaliQ99PE7
SMRiQ99PE7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 294ABC transporterPROSITE-ProRule annotationAdd BLAST256
Domaini389 – 646ABC transmembrane type-2Add BLAST258

Domaini

The Walker motif (consensus sequence G-X-X-G-X-G-K-[ST]-T) is expected to bind ATP. Within this motif, the conserved Lys is essential for transport activity mediated by the heterodimer with ABCG8.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0061 Eukaryota
COG1131 LUCA
GeneTreeiENSGT00910000144282
HOGENOMiHOG000033763
HOVERGENiHBG050443
InParanoidiQ99PE7
KOiK05683
OMAiNAVNLFP
OrthoDBiEOG091G0FOJ
PhylomeDBiQ99PE7
TreeFamiTF105212

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR013525 ABC_2_trans
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF01061 ABC2_membrane, 1 hit
PF00005 ABC_tran, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 1 hit
PS50893 ABC_TRANSPORTER_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q99PE7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELPFLSPE GARGPHNNRG SQSSLEEGSV TGSEARHSLG VLNVSFSVSN
60 70 80 90 100
RVGPWWNIKS CQQKWDRKIL KDVSLYIESG QTMCILGSSG SGKTTLLDAI
110 120 130 140 150
SGRLRRTGTL EGEVFVNGCE LRRDQFQDCV SYLLQSDVFL SSLTVRETLR
160 170 180 190 200
YTAMLALRSS SADFYDKKVE AVLTELSLSH VADQMIGNYN FGGISSGERR
210 220 230 240 250
RVSIAAQLLQ DPKVMMLDEP TTGLDCMTAN HIVLLLVELA RRNRIVIVTI
260 270 280 290 300
HQPRSELFHH FDKIAILTYG ELVFCGTPEE MLGFFNNCGY PCPEHSNPFD
310 320 330 340 350
FYMDLTSVDT QSREREIETY KRVQMLESAF RQSDICHKIL ENIERTRHLK
360 370 380 390 400
TLPMVPFKTK NPPGMFCKLG VLLRRVTRNL MRNKQVVIMR LVQNLIMGLF
410 420 430 440 450
LIFYLLRVQN NMLKGAVQDR VGLLYQLVGA TPYTGMLNAV NLFPMLRAVS
460 470 480 490 500
DQESQDGLYQ KWQMLLAYVL HALPFSIVAT VIFSSVCYWT LGLYPEVARF
510 520 530 540 550
GYFSAALLAP HLIGEFLTLV LLGMVQNPNI VNSIVALLSI SGLLIGSGFI
560 570 580 590 600
RNIEEMPIPL KILGYFTFQK YCCEILVVNE FYGLNFTCGG SNTSVPNNPM
610 620 630 640 650
CSMTQGIQFI EKTCPGATSR FTTNFLILYS FIPTLVILGM VVFKVRDYLI

SR
Length:652
Mass (Da):73,372
Last modified:August 15, 2003 - v3
Checksum:i49FEF7372269299D
GO

Polymorphismi

The polymorphism at position 583 is found in strains SHR, SHRSP and Wistar Kyoto which are both hypertensive and sitosterolemic. Strains which are hypertensive but not sitosterolemic do not contain a polymorphism at this position.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti583G → C in strain: SHR, SHRSP and Wistar Kyoto. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF312714 mRNA Translation: AAG53098.3
AY145899 Genomic DNA Translation: AAN64275.1
RefSeqiNP_446206.2, NM_053754.2
UniGeneiRn.74258

Genome annotation databases

EnsembliENSRNOT00000007174; ENSRNOP00000007174; ENSRNOG00000005250
GeneIDi114628
KEGGirno:114628
UCSCiRGD:620298 rat

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiABCG5_RAT
AccessioniPrimary (citable) accession number: Q99PE7
Secondary accession number(s): Q8CIQ4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: August 15, 2003
Last modified: May 23, 2018
This is version 129 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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