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Protein

ATP-binding cassette sub-family G member 8

Gene

Abcg8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Transporter that appears to play an indispensable 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.

GO - Molecular functioni

  1. ATPase activity Source: InterPro
  2. ATP binding Source: InterPro
  3. cholesterol transporter activity Source: Ensembl
  4. protein heterodimerization activity Source: MGI

GO - Biological processi

  1. cholesterol efflux Source: BHF-UCL
  2. cholesterol homeostasis Source: MGI
  3. excretion Source: BHF-UCL
  4. intestinal cholesterol absorption Source: BHF-UCL
  5. metabolic process Source: GOC
  6. negative regulation of intestinal cholesterol absorption Source: MGI
  7. negative regulation of intestinal phytosterol absorption Source: MGI
  8. phospholipid transport Source: MGI
  9. response to drug Source: Ensembl
  10. response to nutrient Source: Ensembl
  11. sterol homeostasis Source: MGI
  12. sterol transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_343032. Trafficking of dietary sterols.
REACT_346149. ABCA transporters in lipid homeostasis.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-binding cassette sub-family G member 8
Alternative name(s):
Sterolin-2
Gene namesi
Name:Abcg8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1914720. Abcg8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 413413CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei414 – 43421Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini435 – 44713ExtracellularSequence AnalysisAdd
BLAST
Transmembranei448 – 46821Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini469 – 49628CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei497 – 51721Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini518 – 5269ExtracellularSequence Analysis
Transmembranei527 – 54721Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini548 – 56922CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei570 – 59021Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini591 – 63949ExtracellularSequence AnalysisAdd
BLAST
Transmembranei640 – 66021Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini661 – 67313CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: BHF-UCL
  2. ATP-binding cassette (ABC) transporter complex Source: MGI
  3. receptor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 673673ATP-binding cassette sub-family G member 8PRO_0000093397Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi619 – 6191N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ9DBM0.

PTM databases

PhosphoSiteiQ9DBM0.

Expressioni

Tissue specificityi

Expressed in the intestine and, at lower level, in the liver.1 Publication

Inductioni

Up-regulated by cholesterol feeding. Possibly mediated by the liver X receptor/retinoid X receptor (LXR/RXR) pathway. Endotoxin (LPS) significantly decreased mRNA levels in the liver but not in the small intestine.1 Publication

Gene expression databases

BgeeiQ9DBM0.
ExpressionAtlasiQ9DBM0. baseline and differential.
GenevestigatoriQ9DBM0.

Interactioni

Subunit structurei

May form heterodimers with ABCG5 or be tightly coupled to ABCG5 along a pathway regulating diatery-sterol absorption and excretion.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9DBM0.
SMRiQ9DBM0. Positions 31-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 314267ABC transporterPROSITE-ProRule annotationAdd
BLAST
Domaini411 – 665255ABC transmembrane type-2Add
BLAST

Sequence similaritiesi

Contains 1 ABC transporter domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1131.
GeneTreeiENSGT00740000114855.
HOGENOMiHOG000033764.
HOVERGENiHBG050444.
InParanoidiQ9DBM0.
KOiK05684.
OMAiELNTSTH.
PhylomeDBiQ9DBM0.
TreeFamiTF105212.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR013525. ABC_2_trans.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01061. ABC2_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9DBM0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEKTKEETQ LWNGTVLQDA SQGLQDSLFS SESDNSLYFT YSGQSNTLEV
60 70 80 90 100
RDLTYQVDIA SQVPWFEQLA QFKIPWRSHS SQDSCELGIR NLSFKVRSGQ
110 120 130 140 150
MLAIIGSSGC GRASLLDVIT GRGHGGKMKS GQIWINGQPS TPQLVRKCVA
160 170 180 190 200
HVRQHDQLLP NLTVRETLAF IAQMRLPRTF SQAQRDKRVE DVIAELRLRQ
210 220 230 240 250
CANTRVGNTY VRGVSGGERR RVSIGVQLLW NPGILILDEP TSGLDSFTAH
260 270 280 290 300
NLVTTLSRLA KGNRLVLISL HQPRSDIFRL FDLVLLMTSG TPIYLGAAQQ
310 320 330 340 350
MVQYFTSIGH PCPRYSNPAD FYVDLTSIDR RSKEREVATV EKAQSLAALF
360 370 380 390 400
LEKVQGFDDF LWKAEAKELN TSTHTVSLTL TQDTDCGTAV ELPGMIEQFS
410 420 430 440 450
TLIRRQISND FRDLPTLLIH GSEACLMSLI IGFLYYGHGA KQLSFMDTAA
460 470 480 490 500
LLFMIGALIP FNVILDVVSK CHSERSMLYY ELEDGLYTAG PYFFAKILGE
510 520 530 540 550
LPEHCAYVII YAMPIYWLTN LRPVPELFLL HFLLVWLVVF CCRTMALAAS
560 570 580 590 600
AMLPTFHMSS FFCNALYNSF YLTAGFMINL DNLWIVPAWI SKLSFLRWCF
610 620 630 640 650
SGLMQIQFNG HLYTTQIGNF TFSILGDTMI SAMDLNSHPL YAIYLIVIGI
660 670
SYGFLFLYYL SLKLIKQKSI QDW
Length:673
Mass (Da):75,996
Last modified:May 31, 2001 - v1
Checksum:i78012611A5DF2589
GO
Isoform 2 (identifier: Q9DBM0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     377-377: Missing.

Note: No experimental confirmation available.

Show »
Length:672
Mass (Da):75,909
Checksum:iFC57D60AB2D79D1F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei377 – 3771Missing in isoform 2. 1 PublicationVSP_000053

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF324495 mRNA. Translation: AAK84079.1.
AK004871 mRNA. Translation: BAB23630.1.
CCDSiCCDS29002.1. [Q9DBM0-1]
RefSeqiNP_001272934.1. NM_001286005.1.
NP_080456.1. NM_026180.3. [Q9DBM0-1]
UniGeneiMm.26581.

Genome annotation databases

EnsembliENSMUST00000045714; ENSMUSP00000035246; ENSMUSG00000024254. [Q9DBM0-1]
GeneIDi67470.
KEGGimmu:67470.
UCSCiuc008dta.1. mouse. [Q9DBM0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF324495 mRNA. Translation: AAK84079.1.
AK004871 mRNA. Translation: BAB23630.1.
CCDSiCCDS29002.1. [Q9DBM0-1]
RefSeqiNP_001272934.1. NM_001286005.1.
NP_080456.1. NM_026180.3. [Q9DBM0-1]
UniGeneiMm.26581.

3D structure databases

ProteinModelPortaliQ9DBM0.
SMRiQ9DBM0. Positions 31-323.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9DBM0.

Proteomic databases

PRIDEiQ9DBM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045714; ENSMUSP00000035246; ENSMUSG00000024254. [Q9DBM0-1]
GeneIDi67470.
KEGGimmu:67470.
UCSCiuc008dta.1. mouse. [Q9DBM0-1]

Organism-specific databases

CTDi64241.
MGIiMGI:1914720. Abcg8.

Phylogenomic databases

eggNOGiCOG1131.
GeneTreeiENSGT00740000114855.
HOGENOMiHOG000033764.
HOVERGENiHBG050444.
InParanoidiQ9DBM0.
KOiK05684.
OMAiELNTSTH.
PhylomeDBiQ9DBM0.
TreeFamiTF105212.

Enzyme and pathway databases

ReactomeiREACT_343032. Trafficking of dietary sterols.
REACT_346149. ABCA transporters in lipid homeostasis.

Miscellaneous databases

NextBioi324674.
PROiQ9DBM0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBM0.
ExpressionAtlasiQ9DBM0. baseline and differential.
GenevestigatoriQ9DBM0.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR013525. ABC_2_trans.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01061. ABC2_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two genes that map to the STSL locus cause sitosterolemia: genomic structure and spectrum of mutations involving sterolin-1 and sterolin-2, encoded by ABCG5 and ABCG8, respectively."
    Lu K., Lee M.-H., Hazard S., Brooks-Wilson A., Hidaka H., Kojima H., Ose L., Stalenhoef A.F.H., Mietinnen T., Bjorkhem I., Bruckert E., Pandya A., Brewer H.B. Jr., Salen G., Dean M., Srivastava A.K., Patel S.B.
    Am. J. Hum. Genet. 69:278-290(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Liver.
  3. "Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters."
    Berge K.E., Tian H., Graf G.A., Yu L., Grishin N.V., Schultz J., Kwiterovich P., Shan B., Barnes R., Hobbs H.H.
    Science 290:1771-1775(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  4. "Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and ABCG1 in J774 murine macrophages: differential role of LXR."
    Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C., Feingold K.R.
    J. Lipid Res. 44:1728-1736(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-REGULATION BY ENDOTOXIN.

Entry informationi

Entry nameiABCG8_MOUSE
AccessioniPrimary (citable) accession number: Q9DBM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2001
Last sequence update: May 31, 2001
Last modified: March 31, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Seems to have a defective ATP-binding region.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.