S28A3_MOUSE
ID S28A3_MOUSE Reviewed; 703 AA.
AC Q9ERH8; Q3UM72; Q8BWE2; Q91VD7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Solute carrier family 28 member 3;
DE AltName: Full=Concentrative Na(+)-nucleoside cotransporter 3 {ECO:0000303|PubMed:11032837};
DE Short=CNT 3 {ECO:0000303|PubMed:11032837};
DE Short=mCNT3 {ECO:0000303|PubMed:11032837};
GN Name=Slc28a3; Synonyms=Cnt3 {ECO:0000303|PubMed:11032837};
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], FUNCTION, AND TRANSPORTER ACTIVITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=11032837; DOI=10.1074/jbc.m007746200;
RA Ritzel M.W.L., Ng A.M.L., Yao S.Y.M., Graham K., Loewen S.K., Smith K.M.,
RA Ritzel R.G., Mowles D.A., Carpenter P., Chen X.-Z., Karpinski E.,
RA Hyde R.J., Baldwin S.A., Cass C.E., Young J.D.;
RT "Molecular identification and characterization of novel human and mouse
RT concentrative Na+-nucleoside cotransporter proteins (hCNT3 and mCNT3)
RT broadly selective for purine and pyrimidine nucleosides (system cib).";
RL J. Biol. Chem. 276:2914-2927(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Sodium-dependent, pyrimidine- and purine-selective
CC (PubMed:11032837). Involved in the homeostasis of endogenous
CC nucleosides (PubMed:11032837). Exhibits the transport characteristics
CC of the nucleoside transport system cib or N3 subtype (N3/cib) (with
CC marked transport of both thymidine and inosine) (PubMed:11032837).
CC Employs a 2:1 sodium/nucleoside ratio (PubMed:11032837). Also able to
CC transport gemcitabine, 3'-azido-3'-deoxythymidine (AZT), ribavirin and
CC 3-deazauridine (By similarity). {ECO:0000250|UniProtKB:Q9HAS3,
CC ECO:0000269|PubMed:11032837}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Na(+)(out) + thymidine(out) = 2 Na(+)(in) + thymidine(in);
CC Xref=Rhea:RHEA:69899, ChEBI:CHEBI:17748, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:11032837};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(out) + 2 Na(+)(out) = cytidine(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:69903, ChEBI:CHEBI:17562, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:11032837};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Na(+)(out) + uridine(out) = 2 Na(+)(in) + uridine(in);
CC Xref=Rhea:RHEA:69907, ChEBI:CHEBI:16704, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:11032837};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(out) + 2 Na(+)(out) = adenosine(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:69911, ChEBI:CHEBI:16335, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:11032837};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(out) + 2 Na(+)(out) = guanosine(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:69915, ChEBI:CHEBI:16750, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:11032837};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=inosine(out) + 2 Na(+)(out) = inosine(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:69919, ChEBI:CHEBI:17596, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:11032837};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q9HAS3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9HAS3};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT)
CC (TC 2.A.41) family. {ECO:0000305}.
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DR EMBL; AF305211; AAG22552.1; -; mRNA.
DR EMBL; AK052784; BAC35145.1; -; mRNA.
DR EMBL; AK145077; BAE26226.1; -; mRNA.
DR EMBL; BC010472; AAH10472.1; -; mRNA.
DR EMBL; BC013783; AAH13783.1; -; mRNA.
DR CCDS; CCDS26572.1; -.
DR RefSeq; NP_071712.3; NM_022317.3.
DR AlphaFoldDB; Q9ERH8; -.
DR SMR; Q9ERH8; -.
DR STRING; 10090.ENSMUSP00000022036; -.
DR TCDB; 2.A.41.2.6; the concentrative nucleoside transporter (cnt) family.
DR PhosphoSitePlus; Q9ERH8; -.
DR PaxDb; Q9ERH8; -.
DR PRIDE; Q9ERH8; -.
DR ProteomicsDB; 256875; -.
DR Antibodypedia; 13126; 72 antibodies from 15 providers.
DR DNASU; 114304; -.
DR Ensembl; ENSMUST00000022036; ENSMUSP00000022036; ENSMUSG00000021553.
DR GeneID; 114304; -.
DR KEGG; mmu:114304; -.
DR UCSC; uc007qud.1; mouse.
DR CTD; 64078; -.
DR MGI; MGI:2137361; Slc28a3.
DR VEuPathDB; HostDB:ENSMUSG00000021553; -.
DR eggNOG; KOG3747; Eukaryota.
DR GeneTree; ENSGT00390000016025; -.
DR HOGENOM; CLU_016813_3_0_1; -.
DR InParanoid; Q9ERH8; -.
DR OMA; IMLYAMC; -.
DR OrthoDB; 471043at2759; -.
DR PhylomeDB; Q9ERH8; -.
DR TreeFam; TF314131; -.
DR Reactome; R-MMU-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR Reactome; R-MMU-9748787; Azathioprine ADME.
DR SABIO-RK; Q9ERH8; -.
DR BioGRID-ORCS; 114304; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Slc28a3; mouse.
DR PRO; PR:Q9ERH8; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9ERH8; protein.
DR Bgee; ENSMUSG00000021553; Expressed in conjunctival fornix and 55 other tissues.
DR ExpressionAtlas; Q9ERH8; baseline and differential.
DR Genevisible; Q9ERH8; MM.
DR GO; GO:0031526; C:brush border membrane; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005415; F:nucleoside:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0015390; F:purine-specific nucleoside:sodium symporter activity; IDA:MGI.
DR GO; GO:0015389; F:pyrimidine- and adenine-specific:sodium symporter activity; IDA:MGI.
DR GO; GO:0015293; F:symporter activity; IBA:GO_Central.
DR GO; GO:0015213; F:uridine transmembrane transporter activity; ISO:MGI.
DR GO; GO:1901642; P:nucleoside transmembrane transport; ISO:MGI.
DR GO; GO:0015860; P:purine nucleoside transmembrane transport; IDA:MGI.
DR GO; GO:0015864; P:pyrimidine nucleoside transport; IDA:MGI.
DR GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; ISO:MGI.
DR GO; GO:0001895; P:retina homeostasis; ISO:MGI.
DR GO; GO:0015862; P:uridine transport; ISO:MGI.
DR InterPro; IPR008276; C_nuclsd_transpt.
DR InterPro; IPR018270; C_nuclsd_transpt_met_bac.
DR InterPro; IPR030211; CNT3.
DR InterPro; IPR011657; CNT_C_dom.
DR InterPro; IPR002668; CNT_N_dom.
DR InterPro; IPR011642; Gate_dom.
DR PANTHER; PTHR10590; PTHR10590; 1.
DR PANTHER; PTHR10590:SF18; PTHR10590:SF18; 1.
DR Pfam; PF07670; Gate; 1.
DR Pfam; PF07662; Nucleos_tra2_C; 1.
DR Pfam; PF01773; Nucleos_tra2_N; 1.
DR TIGRFAMs; TIGR00804; nupC; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..703
FT /note="Solute carrier family 28 member 3"
FT /id="PRO_0000324147"
FT TOPO_DOM 1..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..138
FT /note="Helical; Name=TM1"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 139..143
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 144..164
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 165..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 189..209
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 210..212
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..234
FT /note="Helical; Name=TM4"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 235..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 243..262
FT /note="Helical; Name=TM5"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 263..299
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 300..320
FT /note="Helical; Name=TM6"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 321..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 345..363
FT /note="Helical; Name=HP1"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 364..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 377..399
FT /note="Helical; Name=TM7"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 400..401
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 402..423
FT /note="Helical; Name=TM8"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 424..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 459..484
FT /note="Helical; Name=TM9"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 485..522
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 523..542
FT /note="Helical; Name=HP2"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 543..581
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 582..592
FT /note="Helical; Name=TM10"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 593..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 606..628
FT /note="Helical; Name=TM11"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 629..703
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 69
FT /note="D -> N (in Ref. 2; BAE26226)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="N -> S (in Ref. 3; AAH10472/AAH13783)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="D -> N (in Ref. 2; BAE26226)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="H -> P (in Ref. 2; BAC35145)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="K -> R (in Ref. 3; AAH10472/AAH13783)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="N -> D (in Ref. 2; BAE26226 and 3; AAH10472/
FT AAH13783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 703 AA; 78310 MW; 96D427BF15851C44 CRC64;
MSRADPGKNS EPSESKMSLE LRPTAPSDLG RSNEAFQDED LERQNTPGNS TVRNRVVQSG
EQGHAKQDDR QITIEQEPLG NKEDPEDDSE DEHQKGFLER KYDTICEFCR KHRVVLRSTI
WAVLLTGFLA LVIAACAINF HRALPLFVIT LVTIFFVIWD HLMAKYEQRI DDFLSPGRRL
LDRHWFWLKW VVWSSLILAI ILWLSLDTAK LGQQNLVSFG GLIMYLILLF LFSKHPTRVY
WRPVFWGIGL QFLLGLLILR TRPGFVAFDW MGRQVQTFLG YTDTGARFVF GEKYTDHFFA
FKILPIVVFF STVMSMLYYL GLMQWIIRKV GWLMLVTMGS SPIESVVAAG NIFIGQTESP
LLVQPYLPHV TKSELHTIMT AGFATIAGSV LGAYISFGVS STHLLTASVM SAPAALAVAK
LFWPETEKPK ITLKSAMKME NGDSRNLLEA ASQGASSSIP LVANIAANLI AFLALLSFVN
SALSWFGSMF NYPELSFELI CSYIFMPFSF MMGVDWQDSF MVAKLIGYKT FFNEFVAYDH
LSKLINLRKA AGPKFVNGVQ QYMSIRSETI ATYALCGFAN FGSLGIVIGG LTSIAPSRKR
DIASGAMRAL IAGTIACFMT ACIAGILSDT PVDINCHHVL ENGRVLSNTT EVVSCCQNLF
NSTVAKGPND VVPGGNFSLY ALKSCCNLLK PPTLNCNWIP NKL
