ABCG4_RAT
ID ABCG4_RAT Reviewed; 650 AA.
AC D3ZCM3;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=ATP-binding cassette subfamily G member 4;
DE EC=7.6.2.- {ECO:0000250|UniProtKB:Q91WA9};
DE AltName: Full=ATP-binding cassette, sub-family G (WHITE), member 4 {ECO:0000303|Ref.2};
GN Name=Abcg4 {ECO:0000312|RGD:1305840};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RC TISSUE=Spinal ganglion;
RX PubMed=12183068; DOI=10.1016/s0167-4889(02)00269-0;
RA Oldfield S., Lowry C., Ruddick J., Lightman S.;
RT "ABCG4: a novel human white family ABC-transporter expressed in the brain
RT and eye.";
RL Biochim. Biophys. Acta 1591:175-179(2002).
RN [4]
RP TISSUE SPECIFICITY, AND MISCELLANEOUS.
RX PubMed=21972082; DOI=10.1002/jnr.22743;
RA Nelissen K., Mulder M., Smets I., Timmermans S., Smeets K., Ameloot M.,
RA Hendriks J.J.;
RT "Liver X receptors regulate cholesterol homeostasis in oligodendrocytes.";
RL J. Neurosci. Res. 90:60-71(2012).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that may be involved in the cellular efflux of sterols, in
CC particular cholesterol and desmosterol (a cholesterol precursor), to
CC high-density lipoprotein (HDL) (By similarity). May play an important
CC role in the removal of amyloid-beta peptides from brain,in a process
CC that can be antagonized by desmosterol. However it is unclear whether
CC ABCG4 can directly transport amyloid-beta peptides or whether peptide
CC export may be facilitated due to changes in the membrane lipid
CC environment (By similarity). Induces apoptosis in various cells (By
CC similarity). {ECO:0000250|UniProtKB:Q91WA9,
CC ECO:0000250|UniProtKB:Q9H172}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q91WA9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000250|UniProtKB:Q91WA9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + desmosterol(in) + H2O = ADP + desmosterol(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:67932, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17737, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q91WA9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67933;
CC Evidence={ECO:0000250|UniProtKB:Q91WA9};
CC -!- SUBUNIT: Half-transporter that form a functional transporter via
CC homo- or heterodimerization. Homodimer. Heterodimers with ABCG1.
CC {ECO:0000250|UniProtKB:Q9H172}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H172};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q91WA9}; Multi-pass membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q91WA9}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the brain and the eye
CC (PubMed:12183068). Expressed in both neonatal and adult
CC oligodendrocytes (PubMed:21972082). {ECO:0000269|PubMed:12183068,
CC ECO:0000269|PubMed:21972082}.
CC -!- MISCELLANEOUS: Whether ABCG4 is an LXR target gene, is still under
CC debate. Studies performed in monocytes, and in one astrocyte cell line
CC indicated that ABCG4 expression could be up-regulated by oxysterols and
CC other LXR ligands (By similarity). However, subsequent observations in
CC a number of different cell types (primary mouse cells, oligodendrocytes
CC and neuron-like cell lines) have not confirmed this observation (By
CC similarity) (PubMed:21972082). {ECO:0000250|UniProtKB:Q91WA9,
CC ECO:0000250|UniProtKB:Q9H172, ECO:0000269|PubMed:21972082}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR EMBL; AC112557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473975; EDL95289.1; -; Genomic_DNA.
DR RefSeq; NP_001100286.1; NM_001106816.1.
DR AlphaFoldDB; D3ZCM3; -.
DR SMR; D3ZCM3; -.
DR STRING; 10116.ENSRNOP00000012534; -.
DR PhosphoSitePlus; D3ZCM3; -.
DR PaxDb; D3ZCM3; -.
DR GeneID; 300664; -.
DR KEGG; rno:300664; -.
DR CTD; 64137; -.
DR RGD; 1305840; Abcg4.
DR VEuPathDB; HostDB:ENSRNOG00000008862; -.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_6_1; -.
DR InParanoid; D3ZCM3; -.
DR OMA; VTDVDHI; -.
DR OrthoDB; 324553at2759; -.
DR PhylomeDB; D3ZCM3; -.
DR TreeFam; TF105210; -.
DR Reactome; R-RNO-1369062; ABC transporters in lipid homeostasis.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000008862; Expressed in frontal cortex and 15 other tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0034041; F:ABC-type sterol transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0071403; P:cellular response to high density lipoprotein particle stimulus; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0033344; P:cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISO:RGD.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0015918; P:sterol transport; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Cytoplasmic vesicle; Endosome; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..650
FT /note="ATP-binding cassette subfamily G member 4"
FT /id="PRO_0000453166"
FT TOPO_DOM 1..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..507
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..621
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..650
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 61..301
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 650 AA; 72491 MW; 625E6982F6FCA3EF CRC64;
MAEKALEAVG CGLGPGAVAM AVALEDGAEP PVLTTHLKKV ENHITEAQRF SHLPKRSAVD
IEFVELSYSV REGPCWRKRG YKTLLKCLSG KFCRRELIGI MGPSGAGKST FMNILAGYRE
SGMKGQILVN GRPRDLRTFR KMSCYIMQDD MLLPHLTVLE AMMVSANLKL SEKQEVKKEL
VTEILTALGL MSCSHTRTAL LSGGQRKRLA IALELVNNPP VMFFDEPTSG LDSASCFQVV
SLMKSLAHGG RTVICTIHQP SAKLFEMFDK LYILSQGQCI FKGVVTNLIP YLKGLGLHCP
TYHNPADFII EVASGEYGDL NPMLFRAVQN GLCTMAEKKS SPEKNEVPAH CPTCPPELDP
IESHTFATST LTQFCILFRR TFLSILRDTV LTHLRFMSHV LIGVLIGLLY LHIGDDASKV
FNNTGFLFFS MLFLMFAALM PTVLTCELIC LAKMAVFMRE HLNYWYSLKA YYLAKTMADV
PFQVVCPVVY CSIVYWMTGQ PAETSRFLLF SALSIATALV AQSLGLLIGA ASTSLQVATF
VGPVTAIPVL LFSGFFVSFK TIPTYLQWSS YLSYVRYGFE GLILTIYGME RGHLTCLEDH
CPFRDPQIIL HELDVEEAKL YMDFLVLGIF FLALRLLAYL VLRYRVKSER
