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Protein

Equilibrative nucleoside transporter 3

Gene

Slc29a3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). Mediates transport of adenine, adenosine and uridine (By similarity).By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiR-MMU-83936. Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Equilibrative nucleoside transporter 3
Short name:
mENT3
Alternative name(s):
Solute carrier family 29 member 3
Gene namesi
Name:Slc29a3
Synonyms:Ent3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1918529. Slc29a3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5151CytoplasmicSequence analysisAdd
BLAST
Transmembranei52 – 7221HelicalSequence analysisAdd
BLAST
Topological domaini73 – 10533ExtracellularSequence analysisAdd
BLAST
Transmembranei106 – 12621HelicalSequence analysisAdd
BLAST
Topological domaini127 – 1348CytoplasmicSequence analysis
Transmembranei135 – 15521HelicalSequence analysisAdd
BLAST
Topological domaini156 – 1627ExtracellularSequence analysis
Transmembranei163 – 18321HelicalSequence analysisAdd
BLAST
Topological domaini184 – 19916CytoplasmicSequence analysisAdd
BLAST
Transmembranei200 – 22021HelicalSequence analysisAdd
BLAST
Topological domaini221 – 23010ExtracellularSequence analysis
Transmembranei231 – 25121HelicalSequence analysisAdd
BLAST
Topological domaini252 – 30554CytoplasmicSequence analysisAdd
BLAST
Transmembranei306 – 32621HelicalSequence analysisAdd
BLAST
Topological domaini327 – 34014ExtracellularSequence analysisAdd
BLAST
Transmembranei341 – 36121HelicalSequence analysisAdd
BLAST
Topological domaini362 – 37716CytoplasmicSequence analysisAdd
BLAST
Transmembranei378 – 39821HelicalSequence analysisAdd
BLAST
Topological domaini399 – 41517ExtracellularSequence analysisAdd
BLAST
Transmembranei416 – 43621HelicalSequence analysisAdd
BLAST
Topological domaini437 – 45014CytoplasmicSequence analysisAdd
BLAST
Transmembranei451 – 47121HelicalSequence analysisAdd
BLAST
Topological domaini472 – 4754ExtracellularSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475Equilibrative nucleoside transporter 3PRO_0000209344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphoserineCombined sources
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ99P65.
MaxQBiQ99P65.
PaxDbiQ99P65.
PeptideAtlasiQ99P65.
PRIDEiQ99P65.

PTM databases

iPTMnetiQ99P65.
PhosphoSiteiQ99P65.

Expressioni

Gene expression databases

BgeeiQ99P65.
ExpressionAtlasiQ99P65. baseline and differential.
GenevisibleiQ99P65. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000112685.

Structurei

3D structure databases

ProteinModelPortaliQ99P65.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1479. Eukaryota.
ENOG410Y3MT. LUCA.
GeneTreeiENSGT00390000002232.
HOGENOMiHOG000007684.
HOVERGENiHBG108444.
InParanoidiQ99P65.
KOiK15014.
OMAiVMSFYLC.
OrthoDBiEOG7PP56W.
PhylomeDBiQ99P65.
TreeFamiTF313950.

Family and domain databases

InterProiIPR030193. ENT3.
IPR002259. Eqnu_transpt.
[Graphical view]
PANTHERiPTHR10332. PTHR10332. 1 hit.
PTHR10332:SF17. PTHR10332:SF17. 1 hit.
PfamiPF01733. Nucleoside_tran. 1 hit.
[Graphical view]
PIRSFiPIRSF016379. ENT. 1 hit.
PRINTSiPR01130. DERENTRNSPRT.

Sequencei

Sequence statusi: Complete.

Q99P65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFASEDNVY HSSNAVYRAP SNHQEADQEA LLGKLLDYPA PGLQRPEDRF
60 70 80 90 100
NGAYIIFFCL GIGGLLPWNF FVTAKEYWAY KLRNCSSPAS GEDPEDMDIL
110 120 130 140 150
NYFESYLAVA STVPSLLFLV ANFLLVNRVQ VHVRVLASLS VSLAIFVVMI
160 170 180 190 200
VLVKVDTSSW TRGFFSLTIA CMAIISSSST IFNSSVYGLT GSFPMRNAQA
210 220 230 240 250
LISGGAMGGT VSAVALLVDL AASSDVRDST LAFFLMAAVF LGLCMGLYLL
260 270 280 290 300
LSQLEYARYY MRPVAPVRVF SGEDNPSQDA PSASSVAPAS RVMHTPPLGP
310 320 330 340 350
ILKKTASLGF CAVSLYFVTA FIIPAISTNI QSMHKGTGSP WTSKFFVPLT
360 370 380 390 400
VFLLFNFADL CGRQVTAWIQ VPGPRSKLLP GLVVSRFCLV PLFLLCNYQP
410 420 430 440 450
RSHLTKVLFQ SDIYPVLFTC LLGLSNGYLS TLVLIYGPKI VPRELAEATS
460 470
VVMLFYMSVG LMLGSACAAL LEHFI
Length:475
Mass (Da):51,719
Last modified:June 1, 2001 - v1
Checksum:iF593D5D03C6CBB52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF326986 mRNA. Translation: AAK00957.1.
AK034133 mRNA. Translation: BAC28600.1.
CH466553 Genomic DNA. Translation: EDL32166.1.
BC137864 mRNA. Translation: AAI37865.1.
CCDSiCCDS48571.1.
RefSeqiNP_076085.1. NM_023596.3.
UniGeneiMm.284462.

Genome annotation databases

EnsembliENSMUST00000117513; ENSMUSP00000112685; ENSMUSG00000020100.
GeneIDi71279.
KEGGimmu:71279.
UCSCiuc007ffb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF326986 mRNA. Translation: AAK00957.1.
AK034133 mRNA. Translation: BAC28600.1.
CH466553 Genomic DNA. Translation: EDL32166.1.
BC137864 mRNA. Translation: AAI37865.1.
CCDSiCCDS48571.1.
RefSeqiNP_076085.1. NM_023596.3.
UniGeneiMm.284462.

3D structure databases

ProteinModelPortaliQ99P65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000112685.

PTM databases

iPTMnetiQ99P65.
PhosphoSiteiQ99P65.

Proteomic databases

EPDiQ99P65.
MaxQBiQ99P65.
PaxDbiQ99P65.
PeptideAtlasiQ99P65.
PRIDEiQ99P65.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000117513; ENSMUSP00000112685; ENSMUSG00000020100.
GeneIDi71279.
KEGGimmu:71279.
UCSCiuc007ffb.1. mouse.

Organism-specific databases

CTDi55315.
MGIiMGI:1918529. Slc29a3.

Phylogenomic databases

eggNOGiKOG1479. Eukaryota.
ENOG410Y3MT. LUCA.
GeneTreeiENSGT00390000002232.
HOGENOMiHOG000007684.
HOVERGENiHBG108444.
InParanoidiQ99P65.
KOiK15014.
OMAiVMSFYLC.
OrthoDBiEOG7PP56W.
PhylomeDBiQ99P65.
TreeFamiTF313950.

Enzyme and pathway databases

ReactomeiR-MMU-83936. Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.

Miscellaneous databases

PROiQ99P65.
SOURCEiSearch...

Gene expression databases

BgeeiQ99P65.
ExpressionAtlasiQ99P65. baseline and differential.
GenevisibleiQ99P65. MM.

Family and domain databases

InterProiIPR030193. ENT3.
IPR002259. Eqnu_transpt.
[Graphical view]
PANTHERiPTHR10332. PTHR10332. 1 hit.
PTHR10332:SF17. PTHR10332:SF17. 1 hit.
PfamiPF01733. Nucleoside_tran. 1 hit.
[Graphical view]
PIRSFiPIRSF016379. ENT. 1 hit.
PRINTSiPR01130. DERENTRNSPRT.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ENT family of eukaryote nucleoside and nucleobase transporters: recent advances in the investigation of structure/function relationships and the identification of novel isoforms."
    Hyde R.J., Cass C.E., Young J.D., Baldwin S.A.
    Mol. Membr. Biol. 18:53-63(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Diencephalon.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Spleen.

Entry informationi

Entry nameiS29A3_MOUSE
AccessioniPrimary (citable) accession number: Q99P65
Secondary accession number(s): B2RQD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.