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ATP-binding cassette sub-family G member 5 (Sterolin-1)

 ABCG5_HUMAN             Reviewed;         651 AA.
Q9H222; Q2T9G2; Q96QZ2; Q96QZ3;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 158.
RecName: Full=ATP-binding cassette sub-family G member 5;
AltName: Full=Sterolin-1;
Name=ABCG5;
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), AND VARIANT GLU-604.
TISSUE=Liver;
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 [MRNA] (ISOFORM 1), VARIANTS STSL HIS-389; HIS-419
AND PRO-419, AND VARIANT GLU-604.
TISSUE=Liver;
PubMed=11138003; DOI=10.1038/83799;
Lee M.-H., Lu K., Hazard S., Yu H., Shulenin S., Hidaka H., Kojima H.,
Allikmets R., Sakuma N., Pegoraro R., Srivastava A.K., Salen G.,
Dean M., Patel S.B.;
"Identification of a gene, ABCG5, important in the regulation of
dietary cholesterol absorption.";
Nat. Genet. 27:79-83(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]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-88 (ISOFORM 1), VARIANTS STSL GLN-146;
HIS-389; PRO-419; HIS-419 AND SER-550, AND VARIANT GLU-604.
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).
[7]
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).
[8]
VARIANT STSL LYS-437, AND VARIANTS VAL-523; TYR-600; GLU-604 AND
VAL-622.
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).
-!- 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 ABCG8 or be tightly coupled to
ABCG8 along a pathway regulating diatery-sterol absorption and
excretion.
-!- INTERACTION:
Q9H221:ABCG8; NbExp=2; IntAct=EBI-1761423, EBI-3908684;
Q9H221-1:ABCG8; NbExp=5; IntAct=EBI-16205983, EBI-16205990;
P16333:NCK1; NbExp=2; IntAct=EBI-1761423, EBI-389883;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H222-1; Sequence=Displayed;
Name=2;
IsoId=Q9H222-2; Sequence=VSP_055770;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Strongly expressed in the liver, lower levels
in the small intestine and colon.
-!- 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:11138003, ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628}. 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}.
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q9H222";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF320293; AAG40003.1; -; mRNA.
EMBL; AF312715; AAG53099.1; -; mRNA.
EMBL; AC011242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471053; EAX00286.1; -; Genomic_DNA.
EMBL; BC111541; AAI11542.1; -; mRNA.
EMBL; AF404106; AAK85387.1; -; Genomic_DNA.
EMBL; AF404107; AAK85388.1; -; Genomic_DNA.
CCDS; CCDS1814.1; -. [Q9H222-1]
RefSeq; NP_071881.1; NM_022436.2. [Q9H222-1]
UniGene; Hs.132992; -.
PDB; 5DO7; X-ray; 3.93 A; A/C=1-651.
PDBsum; 5DO7; -.
ProteinModelPortal; Q9H222; -.
SMR; Q9H222; -.
BioGrid; 122124; 1.
DIP; DIP-42630N; -.
IntAct; Q9H222; 5.
MINT; MINT-2840498; -.
STRING; 9606.ENSP00000260645; -.
DrugBank; DB00973; Ezetimibe.
TCDB; 3.A.1.204.5; the atp-binding cassette (abc) superfamily.
iPTMnet; Q9H222; -.
PhosphoSitePlus; Q9H222; -.
BioMuta; ABCG5; -.
DMDM; 17432917; -.
EPD; Q9H222; -.
PaxDb; Q9H222; -.
PRIDE; Q9H222; -.
Ensembl; ENST00000260645; ENSP00000260645; ENSG00000138075. [Q9H222-1]
GeneID; 64240; -.
KEGG; hsa:64240; -.
UCSC; uc002rtn.3; human. [Q9H222-1]
CTD; 64240; -.
DisGeNET; 64240; -.
EuPathDB; HostDB:ENSG00000138075.11; -.
GeneCards; ABCG5; -.
GeneReviews; ABCG5; -.
HGNC; HGNC:13886; ABCG5.
HPA; HPA016514; -.
MalaCards; ABCG5; -.
MIM; 210250; phenotype.
MIM; 605459; gene.
neXtProt; NX_Q9H222; -.
OpenTargets; ENSG00000138075; -.
Orphanet; 2882; Sitosterolemia.
PharmGKB; PA24411; -.
eggNOG; KOG0061; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00870000136471; -.
HOGENOM; HOG000033763; -.
HOVERGEN; HBG050443; -.
InParanoid; Q9H222; -.
KO; K05683; -.
OMA; NAVNLFP; -.
OrthoDB; EOG091G0FOJ; -.
PhylomeDB; Q9H222; -.
TreeFam; TF105212; -.
Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
SIGNOR; Q9H222; -.
GeneWiki; ABCG5; -.
GenomeRNAi; 64240; -.
PRO; PR:Q9H222; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138075; -.
CleanEx; HS_ABCG5; -.
ExpressionAtlas; Q9H222; baseline and differential.
Genevisible; Q9H222; 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:UniProtKB-KW.
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:0006855; P:drug transmembrane transport; IBA:GO_Central.
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:0010212; P:response to ionizing radiation; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR013525; ABC_2_trans.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF01061; ABC2_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Disease mutation; Glycoprotein; Membrane; Nucleotide-binding;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 651 ATP-binding cassette sub-family G member
5.
/FTId=PRO_0000093393.
TOPO_DOM 1 383 Cytoplasmic. {ECO:0000255}.
TRANSMEM 384 404 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 405 421 Extracellular. {ECO:0000255}.
TRANSMEM 422 442 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 443 462 Cytoplasmic. {ECO:0000255}.
TRANSMEM 463 483 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 484 503 Extracellular. {ECO:0000255}.
TRANSMEM 504 524 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 525 528 Cytoplasmic. {ECO:0000255}.
TRANSMEM 529 549 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 550 623 Extracellular. {ECO:0000255}.
TRANSMEM 624 644 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 645 651 Cytoplasmic. {ECO:0000255}.
DOMAIN 52 293 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 388 645 ABC transmembrane type-2.
NP_BIND 86 93 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
CARBOHYD 584 584 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 591 591 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 395 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055770.
VARIANT 50 50 R -> C (in dbSNP:rs6756629).
/FTId=VAR_048142.
VARIANT 146 146 E -> Q (in STSL; dbSNP:rs758551848).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012244.
VARIANT 389 389 R -> H (in STSL; dbSNP:rs119480069).
{ECO:0000269|PubMed:11138003,
ECO:0000269|PubMed:11452359}.
/FTId=VAR_012245.
VARIANT 419 419 R -> H (in STSL; dbSNP:rs119479067).
{ECO:0000269|PubMed:11138003,
ECO:0000269|PubMed:11452359}.
/FTId=VAR_012246.
VARIANT 419 419 R -> P (in STSL; dbSNP:rs119479067).
{ECO:0000269|PubMed:11138003,
ECO:0000269|PubMed:11452359}.
/FTId=VAR_012247.
VARIANT 437 437 N -> K (in STSL; dbSNP:rs575266356).
{ECO:0000269|PubMed:11668628}.
/FTId=VAR_020781.
VARIANT 517 517 T -> S (in dbSNP:rs17031672).
/FTId=VAR_033457.
VARIANT 523 523 I -> V (in dbSNP:rs140899003).
{ECO:0000269|PubMed:11668628}.
/FTId=VAR_020782.
VARIANT 550 550 R -> S (in STSL).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012248.
VARIANT 600 600 C -> Y (in dbSNP:rs779109455).
{ECO:0000269|PubMed:11668628}.
/FTId=VAR_020783.
VARIANT 604 604 Q -> E (in dbSNP:rs6720173).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11138003,
ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628}.
/FTId=VAR_012249.
VARIANT 622 622 M -> V (in dbSNP:rs140374206).
{ECO:0000269|PubMed:11668628}.
/FTId=VAR_020784.
SEQUENCE 651 AA; 72504 MW; 950BABFCBB6A1536 CRC64;
MGDLSSLTPG GSMGLQVNRG SQSSLEGAPA TAPEPHSLGI LHASYSVSHR VRPWWDITSC
RQQWTRQILK DVSLYVESGQ IMCILGSSGS GKTTLLDAMS GRLGRAGTFL GEVYVNGRAL
RREQFQDCFS YVLQSDTLLS SLTVRETLHY TALLAIRRGN PGSFQKKVEA VMAELSLSHV
ADRLIGNYSL GGISTGERRR VSIAAQLLQD PKVMLFDEPT TGLDCMTANQ IVVLLVELAR
RNRIVVLTIH QPRSELFQLF DKIAILSFGE LIFCGTPAEM LDFFNDCGYP CPEHSNPFDF
YMDLTSVDTQ SKEREIETSK RVQMIESAYK KSAICHKTLK NIERMKHLKT LPMVPFKTKD
SPGVFSKLGV LLRRVTRNLV RNKLAVITRL LQNLIMGLFL LFFVLRVRSN VLKGAIQDRV
GLLYQFVGAT PYTGMLNAVN LFPVLRAVSD QESQDGLYQK WQMMLAYALH VLPFSVVATM
IFSSVCYWTL GLHPEVARFG YFSAALLAPH LIGEFLTLVL LGIVQNPNIV NSVVALLSIA
GVLVGSGFLR NIQEMPIPFK IISYFTFQKY CSEILVVNEF YGLNFTCGSS NVSVTTNPMC
AFTQGIQFIE KTCPGATSRF TMNFLILYSF IPALVILGIV VFKIRDHLIS R


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