S43A3_MOUSE
ID S43A3_MOUSE Reviewed; 502 AA.
AC A2AVZ9; A6PX00; Q5FW65; Q8C345; Q9JLF3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Equilibrative nucleobase transporter 1 {ECO:0000250|UniProtKB:Q8NBI5};
DE AltName: Full=Embryonic epithelia gene 1 protein;
DE AltName: Full=Solute carrier family 43 member 3;
GN Name=Slc43a3; Synonyms=Eeg1, Enbt1 {ECO:0000250|UniProtKB:Q8NBI5};
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=11704567; DOI=10.1152/ajprenal.2001.281.6.f1148;
RA Stuart R.O., Pavlova A., Beier D., Li Z., Krijanovski Y., Nigam S.K.;
RT "EEG1, a putative transporter expressed during epithelial organogenesis:
RT comparison with embryonic transporter expression during nephrogenesis.";
RL Am. J. Physiol. 281:F1148-F1156(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
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=Heart, Lung, Pancreas, and 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).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=32217606; DOI=10.1194/jlr.ra119000294;
RA Hasbargen K.B., Shen W.J., Zhang Y., Hou X., Wang W., Shuo Q.,
RA Bernlohr D.A., Azhar S., Kraemer F.B.;
RT "Slc43a3 is a regulator of free fatty acid flux.";
RL J. Lipid Res. 61:734-745(2020).
CC -!- FUNCTION: Sodium-independent purine-selective nucleobase transporter
CC which mediates the equilibrative transport of extracellular purine
CC nucleobases such as adenine, guanine and hypoxanthine (By similarity).
CC May regulate fatty acid (FA) transport in adipocytes, acting as a
CC positive regulator of FA efflux and as a negative regulator of FA
CC uptake (PubMed:32217606). {ECO:0000250|UniProtKB:Q8NBI5,
CC ECO:0000269|PubMed:32217606}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q8NBI5}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AVZ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AVZ9-2; Sequence=VSP_028193;
CC -!- TISSUE SPECIFICITY: High expression in the heart, followed by the lung,
CC liver, spleen and kidney (PubMed:11704567). Highly expressed in adipose
CC tissue (PubMed:32217606). {ECO:0000269|PubMed:11704567,
CC ECO:0000269|PubMed:32217606}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the early embryo. High
CC expression at embryonic day 7 and later in the fetal liver, lung,
CC placenta and kidney.
CC -!- INDUCTION: Induced during the differentiation of adipocytes.
CC {ECO:0000269|PubMed:32217606}.
CC -!- SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26303.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF188622; AAF26303.1; ALT_FRAME; mRNA.
DR EMBL; AK086962; BAC39774.1; -; mRNA.
DR EMBL; AL935159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089603; AAH89603.1; -; mRNA.
DR CCDS; CCDS38164.1; -. [A2AVZ9-1]
DR RefSeq; NP_067373.2; NM_021398.3. [A2AVZ9-1]
DR RefSeq; XP_006500020.1; XM_006499957.2. [A2AVZ9-1]
DR RefSeq; XP_006500021.1; XM_006499958.3. [A2AVZ9-1]
DR RefSeq; XP_006500022.1; XM_006499959.2. [A2AVZ9-1]
DR RefSeq; XP_006500023.1; XM_006499960.2. [A2AVZ9-1]
DR RefSeq; XP_006500024.1; XM_006499961.1. [A2AVZ9-1]
DR AlphaFoldDB; A2AVZ9; -.
DR STRING; 10090.ENSMUSP00000088227; -.
DR GlyGen; A2AVZ9; 2 sites.
DR iPTMnet; A2AVZ9; -.
DR PhosphoSitePlus; A2AVZ9; -.
DR SwissPalm; A2AVZ9; -.
DR EPD; A2AVZ9; -.
DR jPOST; A2AVZ9; -.
DR MaxQB; A2AVZ9; -.
DR PaxDb; A2AVZ9; -.
DR PeptideAtlas; A2AVZ9; -.
DR PRIDE; A2AVZ9; -.
DR ProteomicsDB; 260903; -. [A2AVZ9-1]
DR ProteomicsDB; 260904; -. [A2AVZ9-2]
DR Antibodypedia; 14150; 76 antibodies from 18 providers.
DR DNASU; 58207; -.
DR Ensembl; ENSMUST00000090726; ENSMUSP00000088227; ENSMUSG00000027074. [A2AVZ9-1]
DR GeneID; 58207; -.
DR KEGG; mmu:58207; -.
DR UCSC; uc008kjn.2; mouse. [A2AVZ9-1]
DR UCSC; uc008kjo.1; mouse. [A2AVZ9-2]
DR CTD; 29015; -.
DR MGI; MGI:1931054; Slc43a3.
DR VEuPathDB; HostDB:ENSMUSG00000027074; -.
DR eggNOG; ENOG502QRYG; Eukaryota.
DR GeneTree; ENSGT00940000157622; -.
DR HOGENOM; CLU_035676_1_1_1; -.
DR InParanoid; A2AVZ9; -.
DR OMA; VCYEQEL; -.
DR OrthoDB; 639867at2759; -.
DR PhylomeDB; A2AVZ9; -.
DR TreeFam; TF328358; -.
DR BioGRID-ORCS; 58207; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Caprin2; mouse.
DR PRO; PR:A2AVZ9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AVZ9; protein.
DR Bgee; ENSMUSG00000027074; Expressed in right lung lobe and 201 other tissues.
DR ExpressionAtlas; A2AVZ9; baseline and differential.
DR Genevisible; A2AVZ9; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015207; F:adenine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015208; F:guanine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0035344; P:hypoxanthine transport; ISS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR027197; SLC43A3.
DR PANTHER; PTHR20765; PTHR20765; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Lipid transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..502
FT /note="Equilibrative nucleobase transporter 1"
FT /id="PRO_0000305037"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 237..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 225..502
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028193"
FT CONFLICT 81
FT /note="N -> S (in Ref. 1; AAH89603)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="Y -> H (in Ref. 1; AAH89603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 56034 MW; 4A268F1F2B786C8F CRC64;
MASKGLPLYL ATLLTGLLEC IGFAGVLFGW TSLLFVFKAE NYFSEPCEQD CLLQSNVTGP
SDLKAQDEKF SLIFTLASFM NNFMTFPTGY IFDRFKTTVA RLIAIFFYTC ATIIIAFTSA
NTAMLLFLAM PMLAVGGILF LITNLQIGNL FGKHRSTIIT LYNGAFDSSS AVFLVIKLLY
EQGISLRSSF IFMSVCSVWH IARTFLLMPK GHIPYPLPPN YSYGLCSRFG ASKKENKAAE
HETKELRSKE CLPPKEENSG PEQQQQQEQQ QQQQQQQEQH EQHSFRRCAL SRRFILHVVW
LSIIQLWHYL FIGTLNSLLT KLSGGDKVEV SAYTNAFAIT QFFGVLCAPW NGLLMDRLKQ
KYQKAAKRTG SSSEAVALCS MVPSLALTSL LSLGFALCAS IPVMQLQYAT FILQVVSRSF
LYGCNAAFLT LAFPSEHFGK LFGLVMALSA IVSLLQFPLF KVSPESNAVY VSMGLAIFLT
LVHPFLVYRE CRAEKTKSSV DA
