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ATP-binding cassette sub-family G member 8 (Sterolin-2)

 ABCG8_HUMAN             Reviewed;         673 AA.
Q9H221; Q53QN8;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 162.
RecName: Full=ATP-binding cassette sub-family G member 8;
AltName: Full=Sterolin-2;
Name=ABCG8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS STSL THR-231;
GLN-263; ARG-574 AND ARG-596, AND VARIANT CYS-54.
PubMed=11099417; DOI=10.1126/science.290.5497.1771;
Berge K.E., Tian H., Graf G.A., Yu L., Grishin N.V., Schultz J.,
Kwiterovich P., Shan B., Barnes R., Hobbs H.H.;
"Accumulation of dietary cholesterol in sitosterolemia caused by
mutations in adjacent ABC transporters.";
Science 290:1771-1775(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANTS
STSL HIS-184; THR-231; GLN-263; HIS-405; PRO-501; SER-543; PHE-570
DEL; PRO-572; ARG-574; GLU-574 AND ARG-596, AND VARIANTS HIS-19;
CYS-54; LYS-238; VAL-259; LYS-400; ARG-575 AND ALA-632.
TISSUE=Liver;
PubMed=11452359; DOI=10.1086/321294;
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.;
"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.";
Am. J. Hum. Genet. 69:278-290(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
REVIEW.
PubMed=11590207;
Schmitz G., Langmann T., Heimerl S.;
"Role of ABCG1 and other ABCG family members in lipid metabolism.";
J. Lipid Res. 42:1513-1520(2001).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[6]
VARIANTS HIS-19; CYS-54; LYS-400; ALA-632 AND PHE-641.
PubMed=11668628; DOI=10.1002/humu.1206;
Hubacek J.A., Berge K.E., Cohen J.C., Hobbs H.H.;
"Mutations in ATP-cassette binding proteins G5 (ABCG5) and G8 (ABCG8)
causing sitosterolemia.";
Hum. Mutat. 18:359-360(2001).
[7]
VARIANTS CYS-54 AND LYS-400.
PubMed=12111378; DOI=10.1007/s100380200041;
Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K.,
Harigae S., Osawa S., Nakamura Y.;
"Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes
encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8,
ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and
ABCG8.";
J. Hum. Genet. 47:285-310(2002).
[8]
VARIANT HIS-19, AND INVOLVEMENT IN GBD4.
PubMed=17632509; DOI=10.1038/ng2101;
Buch S., Schafmayer C., Voelzke H., Becker C., Franke A.,
von Eller-Eberstein H., Kluck C., Baessmann I., Brosch M., Lammert F.,
Miquel J.F., Nervi F., Wittig M., Rosskopf D., Timm B., Hoell C.,
Seeger M., ElSharawy A., Lu T., Egberts J., Faendrich F.,
Foelsch U.R., Krawczak M., Schreiber S., Nuernberg P., Tepel J.,
Hampe J.;
"A genome-wide association scan identifies the hepatic cholesterol
transporter ABCG8 as a susceptibility factor for human gallstone
disease.";
Nat. Genet. 39:995-999(2007).
-!- 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: May form heterodimers with ABCG5 or be tightly coupled to
ABCG5 along a pathway regulating diatery-sterol absorption and
excretion.
-!- INTERACTION:
Q9H222:ABCG5; NbExp=2; IntAct=EBI-3908684, EBI-1761423;
Q9H222-1:ABCG5; NbExp=5; IntAct=EBI-16205990, EBI-16205983;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H221-1; Sequence=Displayed;
Name=2;
IsoId=Q9H221-2; Sequence=VSP_000052;
Note=Minor form detected in approximately 10% of the cDNA
clones.;
-!- TISSUE SPECIFICITY: Strongly expressed in the liver, lower levels
in the small intestine and colon. Detectable in a wide variety of
human tissues.
-!- DISEASE: Gallbladder disease 4 (GBD4) [MIM:611465]: One of the
major digestive diseases. Gallstones composed of cholesterol
(cholelithiasis) are the common manifestations in western
countries. Most people with gallstones, however, remain
asymptomatic through their lifetimes.
{ECO:0000269|PubMed:17632509}. Note=Disease susceptibility may be
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Sitosterolemia (STSL) [MIM:210250]: Rare autosomal
recessive disorder characterized by increased intestinal
absorption of all sterols including cholesterol, plant and
shellfish sterols, and decreased biliary excretion of dietary
sterols into bile. Sitosterolemia patients have
hypercholesterolemia, very high levels of plant sterols in the
plasma, and frequently develop tendon and tuberous xanthomas,
accelerated atherosclerosis and premature coronary artery disease.
{ECO:0000269|PubMed:11099417, ECO:0000269|PubMed:11452359}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG
family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.
{ECO:0000305}.
-!- CAUTION: Seems to have a defective ATP-binding region.
{ECO:0000305}.
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q9H221";
-----------------------------------------------------------------------
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EMBL; AF320294; AAG40004.1; -; mRNA.
EMBL; AF324494; AAK84078.1; -; mRNA.
EMBL; AF351824; AAK84663.1; -; Genomic_DNA.
EMBL; AF351812; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351813; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351814; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351815; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351816; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351817; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351818; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351819; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351820; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351821; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351822; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AF351823; AAK84663.1; JOINED; Genomic_DNA.
EMBL; AC108476; AAY24011.1; -; Genomic_DNA.
CCDS; CCDS1815.1; -. [Q9H221-1]
RefSeq; NP_071882.1; NM_022437.2. [Q9H221-1]
RefSeq; XP_005264540.1; XM_005264483.3. [Q9H221-2]
UniGene; Hs.413931; -.
PDB; 5DO7; X-ray; 3.93 A; B/D=2-673.
PDBsum; 5DO7; -.
ProteinModelPortal; Q9H221; -.
SMR; Q9H221; -.
BioGrid; 122125; 13.
DIP; DIP-42631N; -.
IntAct; Q9H221; 8.
MINT; MINT-2840535; -.
STRING; 9606.ENSP00000272286; -.
DrugBank; DB00973; Ezetimibe.
TCDB; 3.A.1.204.5; the atp-binding cassette (abc) superfamily.
iPTMnet; Q9H221; -.
PhosphoSitePlus; Q9H221; -.
BioMuta; ABCG8; -.
DMDM; 17432916; -.
PaxDb; Q9H221; -.
PeptideAtlas; Q9H221; -.
PRIDE; Q9H221; -.
DNASU; 64241; -.
Ensembl; ENST00000272286; ENSP00000272286; ENSG00000143921. [Q9H221-1]
GeneID; 64241; -.
KEGG; hsa:64241; -.
UCSC; uc002rtq.3; human. [Q9H221-1]
CTD; 64241; -.
DisGeNET; 64241; -.
EuPathDB; HostDB:ENSG00000143921.6; -.
GeneCards; ABCG8; -.
GeneReviews; ABCG8; -.
HGNC; HGNC:13887; ABCG8.
HPA; HPA019556; -.
MalaCards; ABCG8; -.
MIM; 210250; phenotype.
MIM; 605460; gene.
MIM; 611465; phenotype.
neXtProt; NX_Q9H221; -.
OpenTargets; ENSG00000143921; -.
Orphanet; 2882; Sitosterolemia.
PharmGKB; PA24412; -.
eggNOG; KOG0061; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00870000136471; -.
HOGENOM; HOG000033764; -.
HOVERGEN; HBG050444; -.
InParanoid; Q9H221; -.
KO; K05684; -.
OMA; RRQISND; -.
OrthoDB; EOG091G0E38; -.
PhylomeDB; Q9H221; -.
TreeFam; TF105212; -.
Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
Reactome; R-HSA-5679090; Defective ABCG8 causes gallbladder disease 4 and sitosterolemia.
Reactome; R-HSA-5679096; Defective ABCG5 causes sitosterolemia.
SIGNOR; Q9H221; -.
GeneWiki; ABCG8; -.
GenomeRNAi; 64241; -.
PRO; PR:Q9H221; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000143921; -.
CleanEx; HS_ABCG8; -.
Genevisible; Q9H221; HS.
GO; GO:0016324; C:apical plasma membrane; IMP:BHF-UCL.
GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0017127; F:cholesterol transporter activity; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0033344; P:cholesterol efflux; IGI:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0007588; P:excretion; IGI:BHF-UCL.
GO; GO:0030299; P:intestinal cholesterol absorption; IC:BHF-UCL.
GO; GO:0045796; P:negative regulation of intestinal cholesterol absorption; IMP:BHF-UCL.
GO; GO:0010949; P:negative regulation of intestinal phytosterol absorption; IMP:BHF-UCL.
GO; GO:0015914; P:phospholipid transport; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
InterPro; IPR013525; ABC_2_trans.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF01061; ABC2_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Glycoprotein; Membrane; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 673 ATP-binding cassette sub-family G member
8.
/FTId=PRO_0000093396.
TOPO_DOM 1 416 Cytoplasmic. {ECO:0000255}.
TRANSMEM 417 437 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 438 447 Extracellular. {ECO:0000255}.
TRANSMEM 448 468 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 469 492 Cytoplasmic. {ECO:0000255}.
TRANSMEM 493 513 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 514 531 Extracellular. {ECO:0000255}.
TRANSMEM 532 552 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 553 569 Cytoplasmic. {ECO:0000255}.
TRANSMEM 570 590 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 591 639 Extracellular. {ECO:0000255}.
TRANSMEM 640 660 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 661 673 Cytoplasmic. {ECO:0000255}.
DOMAIN 47 313 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 411 665 ABC transmembrane type-2.
CARBOHYD 619 619 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 376 376 Missing (in isoform 2).
{ECO:0000303|PubMed:11452359}.
/FTId=VSP_000052.
VARIANT 19 19 D -> H (associated significantly with
GBD4; dbSNP:rs11887534).
{ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628,
ECO:0000269|PubMed:17632509}.
/FTId=VAR_012250.
VARIANT 54 54 Y -> C (in dbSNP:rs4148211).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628,
ECO:0000269|PubMed:12111378}.
/FTId=VAR_012251.
VARIANT 184 184 R -> H (in STSL; dbSNP:rs766212636).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012252.
VARIANT 210 210 V -> M (in dbSNP:rs9282574).
/FTId=VAR_022074.
VARIANT 231 231 P -> T (in STSL; dbSNP:rs137852993).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359}.
/FTId=VAR_012253.
VARIANT 238 238 E -> K (in dbSNP:rs34754243).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012254.
VARIANT 259 259 A -> V (in dbSNP:rs35518570).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012255.
VARIANT 263 263 R -> Q (in STSL; dbSNP:rs137852990).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359}.
/FTId=VAR_012256.
VARIANT 400 400 T -> K (in dbSNP:rs4148217).
{ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628,
ECO:0000269|PubMed:12111378}.
/FTId=VAR_012257.
VARIANT 405 405 R -> H (in STSL).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012258.
VARIANT 501 501 L -> P (in STSL).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012259.
VARIANT 543 543 R -> S (in STSL; dbSNP:rs201690654).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012260.
VARIANT 570 570 Missing (in STSL).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012261.
VARIANT 572 572 L -> P (in STSL; dbSNP:rs769576789).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012262.
VARIANT 574 574 G -> E (in STSL).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012263.
VARIANT 574 574 G -> R (in STSL; dbSNP:rs137852988).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359}.
/FTId=VAR_012264.
VARIANT 575 575 G -> R (in dbSNP:rs36209700).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012265.
VARIANT 596 596 L -> R (in STSL; dbSNP:rs137852992).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11452359}.
/FTId=VAR_012266.
VARIANT 632 632 V -> A (in dbSNP:rs6544718).
{ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628}.
/FTId=VAR_012267.
VARIANT 641 641 Y -> F (in dbSNP:rs145125968).
{ECO:0000269|PubMed:11668628}.
/FTId=VAR_020785.
VARIANT 655 655 M -> V (in dbSNP:rs9282573).
/FTId=VAR_022075.
SEQUENCE 673 AA; 75679 MW; 594AFD1D6C1BB50F CRC64;
MAGKAAEERG LPKGATPQDT SGLQDRLFSS ESDNSLYFTY SGQPNTLEVR DLNYQVDLAS
QVPWFEQLAQ FKMPWTSPSC QNSCELGIQN LSFKVRSGQM LAIIGSSGCG RASLLDVITG
RGHGGKIKSG QIWINGQPSS PQLVRKCVAH VRQHNQLLPN LTVRETLAFI AQMRLPRTFS
QAQRDKRVED VIAELRLRQC ADTRVGNMYV RGLSGGERRR VSIGVQLLWN PGILILDEPT
SGLDSFTAHN LVKTLSRLAK GNRLVLISLH QPRSDIFRLF DLVLLMTSGT PIYLGAAQHM
VQYFTAIGYP CPRYSNPADF YVDLTSIDRR SREQELATRE KAQSLAALFL EKVRDLDDFL
WKAETKDLDE DTCVESSVTP LDTNCLPSPT KMPGAVQQFT TLIRRQISND FRDLPTLLIH
GAEACLMSMT IGFLYFGHGS IQLSFMDTAA LLFMIGALIP FNVILDVISK CYSERAMLYY
ELEDGLYTTG PYFFAKILGE LPEHCAYIII YGMPTYWLAN LRPGLQPFLL HFLLVWLVVF
CCRIMALAAA ALLPTFHMAS FFSNALYNSF YLAGGFMINL SSLWTVPAWI SKVSFLRWCF
EGLMKIQFSR RTYKMPLGNL TIAVSGDKIL SVMELDSYPL YAIYLIVIGL SGGFMVLYYV
SLRFIKQKPS QDW


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EH1420 ATP-binding cassette sub-family A member 1 Elisa Kit 96T
ABCC8_RAT Rat ELISA Kit FOR ATP-binding cassette sub-family C member 8 96T
EM796 ATP-binding cassette sub-family G member 3 Elisa Kit 96T
ABCD2_RAT Rat ELISA Kit FOR ATP-binding cassette sub-family D member 2 96T
CG47 ATP-binding cassette sub-family B member 5 ABCB5 lmg
EH1095 ATP-binding cassette sub-family G member 2 Elisa Kit 96T
EH1708 ATP-binding cassette sub-family A member 7 Elisa Kit 96T


 

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