Q9DBM0 (ABCG8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-binding cassette sub-family G member 8

Alternative name(s):
Sterolin-2

Gene names

Name:

Abcg8

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	673 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Subunit structure	May form heterodimers with ABCG5 or be tightly coupled to ABCG5 along a pathway regulating diatery-sterol absorption and excretion By similarity.
Subcellular location	Membrane; Multi-pass membrane protein Probable.
Tissue specificity	Expressed in the intestine and, at lower level, in the liver. Ref.3
Induction	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. Ref.3 Ref.4
Sequence similarities	Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. [View classification] Contains 1 ABC transmembrane type-2 domain. Contains 1 ABC transporter domain.
Caution	Seems to have a defective ATP-binding region.

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol efflux Inferred from mutant phenotype PubMed 14504269. Source: BHF-UCL cholesterol homeostasis Inferred from mutant phenotype PubMed 15040800. Source: MGI excretion Inferred from mutant phenotype PubMed 14504269. Source: BHF-UCL intestinal cholesterol absorption Inferred by curator PubMed 12208868. Source: BHF-UCL negative regulation of intestinal cholesterol absorption Inferred from electronic annotation. Source: Compara negative regulation of intestinal phytosterol absorption Inferred from electronic annotation. Source: Compara phospholipid transport Inferred from mutant phenotype PubMed 15040800. Source: MGI response to drug Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara
Cellular_component	apical plasma membrane Inferred from mutant phenotype PubMed 14504269. Source: BHF-UCL integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: Compara ATPase activity Inferred from electronic annotation. Source: Compara cholesterol transporter activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9DBM0-1)

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.

Isoform 2 (identifier: Q9DBM0-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 673	673	ATP-binding cassette sub-family G member 8		PRO_0000093397
Regions
	Topological domain	1 – 413	413	Cytoplasmic Potential
	Transmembrane	414 – 434	21	Helical; Name=1; Potential
	Topological domain	435 – 447	13	Extracellular Potential
	Transmembrane	448 – 468	21	Helical; Name=2; Potential
	Topological domain	469 – 496	28	Cytoplasmic Potential
	Transmembrane	497 – 517	21	Helical; Name=3; Potential
	Topological domain	518 – 526	9	Extracellular Potential
	Transmembrane	527 – 547	21	Helical; Name=4; Potential
	Topological domain	548 – 569	22	Cytoplasmic Potential
	Transmembrane	570 – 590	21	Helical; Name=5; Potential
	Topological domain	591 – 639	49	Extracellular Potential
	Transmembrane	640 – 660	21	Helical; Name=6; Potential
	Topological domain	661 – 673	13	Cytoplasmic Potential
	Domain	48 – 314	267	ABC transporter
	Domain	411 – 665	255	ABC transmembrane type-2
Amino acid modifications
	Glycosylation	619	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	377	1	Missing in isoform 2.		VSP_000053

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 78012611A5DF2589	FASTA	673	75,996
	10 20 30 40 50 60 MAEKTKEETQ LWNGTVLQDA SQGLQDSLFS SESDNSLYFT YSGQSNTLEV RDLTYQVDIA 70 80 90 100 110 120 SQVPWFEQLA QFKIPWRSHS SQDSCELGIR NLSFKVRSGQ MLAIIGSSGC GRASLLDVIT 130 140 150 160 170 180 GRGHGGKMKS GQIWINGQPS TPQLVRKCVA HVRQHDQLLP NLTVRETLAF IAQMRLPRTF 190 200 210 220 230 240 SQAQRDKRVE DVIAELRLRQ CANTRVGNTY VRGVSGGERR RVSIGVQLLW NPGILILDEP 250 260 270 280 290 300 TSGLDSFTAH NLVTTLSRLA KGNRLVLISL HQPRSDIFRL FDLVLLMTSG TPIYLGAAQQ 310 320 330 340 350 360 MVQYFTSIGH PCPRYSNPAD FYVDLTSIDR RSKEREVATV EKAQSLAALF LEKVQGFDDF 370 380 390 400 410 420 LWKAEAKELN TSTHTVSLTL TQDTDCGTAV ELPGMIEQFS TLIRRQISND FRDLPTLLIH 430 440 450 460 470 480 GSEACLMSLI IGFLYYGHGA KQLSFMDTAA LLFMIGALIP FNVILDVVSK CHSERSMLYY 490 500 510 520 530 540 ELEDGLYTAG PYFFAKILGE LPEHCAYVII YAMPIYWLTN LRPVPELFLL HFLLVWLVVF 550 560 570 580 590 600 CCRTMALAAS AMLPTFHMSS FFCNALYNSF YLTAGFMINL DNLWIVPAWI SKLSFLRWCF 610 620 630 640 650 660 SGLMQIQFNG HLYTTQIGNF TFSILGDTMI SAMDLNSHPL YAIYLIVIGI SYGFLFLYYL 670 SLKLIKQKSI QDW
	Isoform 2 [UniParc]. Checksum: FC57D60AB2D79D1F	FASTA	672	75,909
	10 20 30 40 50 60 MAEKTKEETQ LWNGTVLQDA SQGLQDSLFS SESDNSLYFT YSGQSNTLEV RDLTYQVDIA 70 80 90 100 110 120 SQVPWFEQLA QFKIPWRSHS SQDSCELGIR NLSFKVRSGQ MLAIIGSSGC GRASLLDVIT 130 140 150 160 170 180 GRGHGGKMKS GQIWINGQPS TPQLVRKCVA HVRQHDQLLP NLTVRETLAF IAQMRLPRTF 190 200 210 220 230 240 SQAQRDKRVE DVIAELRLRQ CANTRVGNTY VRGVSGGERR RVSIGVQLLW NPGILILDEP 250 260 270 280 290 300 TSGLDSFTAH NLVTTLSRLA KGNRLVLISL HQPRSDIFRL FDLVLLMTSG TPIYLGAAQQ 310 320 330 340 350 360 MVQYFTSIGH PCPRYSNPAD FYVDLTSIDR RSKEREVATV EKAQSLAALF LEKVQGFDDF 370 380 390 400 410 420 LWKAEAKELN TSTHTVLTLT QDTDCGTAVE LPGMIEQFST LIRRQISNDF RDLPTLLIHG 430 440 450 460 470 480 SEACLMSLII GFLYYGHGAK QLSFMDTAAL LFMIGALIPF NVILDVVSKC HSERSMLYYE 490 500 510 520 530 540 LEDGLYTAGP YFFAKILGEL PEHCAYVIIY AMPIYWLTNL RPVPELFLLH FLLVWLVVFC 550 560 570 580 590 600 CRTMALAASA MLPTFHMSSF FCNALYNSFY LTAGFMINLD NLWIVPAWIS KLSFLRWCFS 610 620 630 640 650 660 GLMQIQFNGH LYTTQIGNFT FSILGDTMIS AMDLNSHPLY AIYLIVIGIS YGFLFLYYLS 670 LKLIKQKSIQ DW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(2001) [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(2005) [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(2000) [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(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DOWN-REGULATION BY ENDOTOXIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF324495 mRNA. Translation: AAK84079.1. AK004871 mRNA. Translation: BAB23630.1.
IPI	IPI00119879. IPI00221906.
RefSeq	NP_080456.1. NM_026180.2.
UniGene	Mm.26581.
3D structure databases
ProteinModelPortal	Q9DBM0.
SMR	Q9DBM0. Positions 31-323.
ModBase	Search...
PTM databases
PhosphoSite	Q9DBM0.
Proteomic databases
PRIDE	Q9DBM0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000045714; ENSMUSP00000035246; ENSMUSG00000024254.
GeneID	67470.
KEGG	mmu:67470.
UCSC	uc008dta.1. mouse.
Organism-specific databases
CTD	64241.
MGI	MGI:1914720. Abcg8.
Phylogenomic databases
eggNOG	COG1131.
GeneTree	ENSGT00700000104032.
HOGENOM	HOG000033764.
HOVERGEN	HBG050444.
InParanoid	Q9DBM0.
KO	K05684.
OMA	IDRRSHE.
OrthoDB	EOG4J3WGN.
Gene expression databases
ArrayExpress	Q9DBM0.
Bgee	Q9DBM0.
Genevestigator	Q9DBM0.
GermOnline	ENSMUSG00000024254. Mus musculus.
Family and domain databases
InterPro	IPR013525. ABC_2_trans. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR027417. P-loop_NTPase. [Graphical view]
Pfam	PF01061. ABC2_membrane. 1 hit. PF00005. ABC_tran. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
PROSITE	PS51012. ABC_TM2. False negative. PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	324674.
SOURCE	Search...

Entry information

Entry name

ABCG8_MOUSE

Accession

Primary (citable) accession number: Q9DBM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program