S29A3_RAT
ID S29A3_RAT Reviewed; 475 AA.
AC Q80WK7; Q6AZ86;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Equilibrative nucleoside transporter 3;
DE AltName: Full=Solute carrier family 29 member 3;
GN Name=Slc29a3; Synonyms=Ent3;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Toan S.-V., Ward J.L., Tse C.-M.;
RT "Molecular cloning of rat equilibrative nucleoside transporter type 3
RT isoform.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Testis;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=15701636; DOI=10.1074/jbc.m414337200;
RA Baldwin S.A., Yao S.Y.M., Hyde R.J., Ng A.M.L., Foppolo S., Barnes K.,
RA Ritzel M.W.L., Cass C.E., Young J.D.;
RT "Functional characterization of novel human and mouse equilibrative
RT nucleoside transporters (hENT3 and mENT3) located in intracellular
RT membranes.";
RL J. Biol. Chem. 280:15880-15887(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Mediates both influx and efflux of nucleosides across the
CC membrane (equilibrative transporter). Mediates transport of adenine,
CC adenosine and uridine (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Late
CC endosome membrane. Lysosome membrane. Note=Intracellular localization
CC shows a partial overlap with late endosomes/lysosomes. Not detected at
CC the cell surface (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart and liver
CC (at protein level). {ECO:0000269|PubMed:15701636}.
CC -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC {ECO:0000305}.
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DR EMBL; AY273196; AAP23232.1; -; mRNA.
DR EMBL; BC078678; AAH78678.1; -; mRNA.
DR RefSeq; NP_853670.2; NM_181639.3.
DR AlphaFoldDB; Q80WK7; -.
DR SMR; Q80WK7; -.
DR STRING; 10116.ENSRNOP00000000689; -.
DR GlyGen; Q80WK7; 1 site.
DR iPTMnet; Q80WK7; -.
DR PhosphoSitePlus; Q80WK7; -.
DR PaxDb; Q80WK7; -.
DR Ensembl; ENSRNOT00000113968; ENSRNOP00000082643; ENSRNOG00000000568.
DR GeneID; 353307; -.
DR KEGG; rno:353307; -.
DR UCSC; RGD:727811; rat.
DR CTD; 55315; -.
DR RGD; 727811; Slc29a3.
DR eggNOG; KOG1479; Eukaryota.
DR GeneTree; ENSGT00950000182898; -.
DR HOGENOM; CLU_021611_6_1_1; -.
DR InParanoid; Q80WK7; -.
DR OMA; FWNLGDL; -.
DR OrthoDB; 559763at2759; -.
DR PhylomeDB; Q80WK7; -.
DR Reactome; R-RNO-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR PRO; PR:Q80WK7; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000568; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; Q80WK7; RN.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IMP:RGD.
DR GO; GO:0015858; P:nucleoside transport; IMP:RGD.
DR InterPro; IPR030193; ENT3.
DR InterPro; IPR002259; Eqnu_transpt.
DR PANTHER; PTHR10332; PTHR10332; 1.
DR PANTHER; PTHR10332:SF17; PTHR10332:SF17; 1.
DR Pfam; PF01733; Nucleoside_tran; 1.
DR PIRSF; PIRSF016379; ENT; 1.
DR PRINTS; PR01130; DERENTRNSPRT.
PE 1: Evidence at protein level;
KW Endosome; Glycoprotein; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..475
FT /note="Equilibrative nucleoside transporter 3"
FT /id="PRO_0000209345"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..475
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 272..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99P65"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 142
FT /note="S -> P (in Ref. 1; AAP23232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 51677 MW; 014B34E12CCA6303 CRC64;
MAFASEDIAY HSSNAVYRVP SNRHEADQEA LLGKPLDYPA PGLQRPEDRF NGAYIIFFCL
GIGGLLPWNF FVTAKEYWAF KLRNCSSPAS GKDPEDADIL NYFESYLAVA STVPSLLFLV
ANFLLVNRIR VHVRVLASLS VSLAIFVVMA VLVRVDTSSW TRGFFSIAMA CMAIISSSST
IFNSSVYGLT GSFPMRNAQA LISGGAMGGT VSAVASLVDL AASSDVRDSA LAFFLTAAVF
LGLCVGLYLL LPQLEYARYY MRPVVPIHVF SSEDSPPRDA PSTSSVAPAS RAVHTPPLGP
ILKKTAGLGF CAVFLYFITA LIFPAISTNI QPMHKGTGSP WTSKFYVPLT VFLLFNFADL
CGRQVTAWIQ VPGPRSKLLP ILAVSRVCLV PLFLLCNYQP RSHLTLVLFQ SDIYPILFTC
LLGLSNGYLS TLVLMYGPKI VPRELAEATS VVMLFYMSLG LMLGSACAAL LEHFI
