ABCG3_MOUSE
ID ABCG3_MOUSE Reviewed; 650 AA.
AC Q99P81; Q8BKI5;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ATP-binding cassette sub-family G member 3;
GN Name=Abcg3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=11178751; DOI=10.1007/s003350010237;
RA Mickley L., Jain P., Miyake K., Schriml L.M., Rao K., Fojo T., Bates S.,
RA Dean M.;
RT "An ATP-binding cassette gene (ABCG3) closely related to the multidrug
RT transporter ABCG2 (MXR/ABCP) has an unusual ATP-binding domain.";
RL Mamm. Genome 12:86-88(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBUNIT: May dimerize with another subunit to form a functional
CC transporter.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highest levels of expression in thymus and spleen.
CC Detected in lung and small intestine.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
CC -!- CAUTION: Seems to have a defective ATP-binding region. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF324242; AAK14241.1; -; mRNA.
DR EMBL; AK051880; BAC34799.1; -; mRNA.
DR EMBL; CH466529; EDL20215.1; -; Genomic_DNA.
DR EMBL; BC138772; AAI38773.1; -; mRNA.
DR EMBL; BC138773; AAI38774.1; -; mRNA.
DR CCDS; CCDS19488.1; -.
DR RefSeq; NP_084515.2; NM_030239.2.
DR AlphaFoldDB; Q99P81; -.
DR SMR; Q99P81; -.
DR IntAct; Q99P81; 13.
DR STRING; 10090.ENSMUSP00000031239; -.
DR iPTMnet; Q99P81; -.
DR PhosphoSitePlus; Q99P81; -.
DR EPD; Q99P81; -.
DR jPOST; Q99P81; -.
DR MaxQB; Q99P81; -.
DR PaxDb; Q99P81; -.
DR PRIDE; Q99P81; -.
DR ProteomicsDB; 285958; -.
DR Antibodypedia; 14577; 364 antibodies from 45 providers.
DR DNASU; 27405; -.
DR Ensembl; ENSMUST00000031239; ENSMUSP00000031239; ENSMUSG00000029299.
DR GeneID; 27405; -.
DR KEGG; mmu:27405; -.
DR UCSC; uc008ykt.1; mouse.
DR CTD; 27405; -.
DR MGI; MGI:1351624; Abcg3.
DR VEuPathDB; HostDB:ENSMUSG00000029299; -.
DR eggNOG; KOG0061; Eukaryota.
DR GeneTree; ENSGT00940000162658; -.
DR HOGENOM; CLU_000604_57_8_1; -.
DR InParanoid; Q99P81; -.
DR OMA; FKHERAC; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; Q99P81; -.
DR TreeFam; TF105211; -.
DR BioGRID-ORCS; 27405; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Abcg3; mouse.
DR PRO; PR:Q99P81; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99P81; protein.
DR Bgee; ENSMUSG00000029299; Expressed in dorsal pancreas and 45 other tissues.
DR ExpressionAtlas; Q99P81; baseline and differential.
DR Genevisible; Q99P81; MM.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015143; F:urate transmembrane transporter activity; ISO:MGI.
DR GO; GO:1990748; P:cellular detoxification; ISO:MGI.
DR GO; GO:0097744; P:renal urate salt excretion; ISO:MGI.
DR GO; GO:0032218; P:riboflavin transport; ISO:MGI.
DR GO; GO:0070633; P:transepithelial transport; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR GO; GO:0046415; P:urate metabolic process; ISO:MGI.
DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
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 SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..650
FT /note="ATP-binding cassette sub-family G member 3"
FT /id="PRO_0000093391"
FT TOPO_DOM 1..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..420
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..498
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..623
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 624..644
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 645..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..279
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 381..644
FT /note="ABC transmembrane type-2"
FT CONFLICT 550
FT /note="S -> P (in Ref. 1; AAK14241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 73613 MW; B9995BDBDFD945E1 CRC64;
MASNNDPTVI SMIERHLCDL PETNTSDLKT LTEEAVLSFH NISYQETVQS GFPLRKKAYV
IERLSNISGI MKPGLNAIMG PQDGSRSLLL DVLAARRDPR GLSGDILING KPRPANFKCT
SGYVPQNDVV LGTVTVRDNL EFSAALRLPV TITRDEKRRR INEVLELLHL NKEQNIKPRS
KELRKRTSIA MELVTEHPIL FLDDPTTGLD LRTTTDVILV LRRMSKKGRT IIFSINQPQY
SIFKFFDSLT LVASGKVMFH GPAQDALEYF RSAGYNYESH NNPADFFLDV INGGFSNILD
TEEDGHEDDK YEELFERQYQ VTGKLANMYA QSPLYSETRA ILDQLLGEQK LERSSAVETT
CVTPFCHQLK WIICQSFKNF KGFPWVTVIQ AIITVILATA VGTAFRVLKN DCIEVQMRAG
LLYLLTIFQC ITSVSAGELF VIDRVRFLHE HTSGYYRVSS YFFGKLLAEL IPRRLLPSTV
FSLITYVIAG VKMSMKCFFT MICTIMVLAY SASSLPLSIG AGENAVAVPT LLVTIYFVFM
LFFSGLSLYS GSFLPKLSWI QYFSIPHYGF RALLHNEFLG QNFCPEHNTE EVSRCHNYVI
CTGEEFLMIQ GIDLSSWGFW ENHLALVCTM IILLTITYVQ LLQVKNIRNF
