S29A2_RAT
ID S29A2_RAT Reviewed; 456 AA.
AC O54699;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Equilibrative nucleoside transporter 2;
DE AltName: Full=Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter;
DE Short=Equilibrative NBMPR-insensitive nucleoside transporter;
DE AltName: Full=Nucleoside transporter, ei-type;
DE AltName: Full=Solute carrier family 29 member 2;
GN Name=Slc29a2; Synonyms=Ent2;
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=Jejunum;
RX PubMed=9353301; DOI=10.1074/jbc.272.45.28423;
RA Yao S.Y.M., Ng A.M.L., Muzyka W.R., Griffiths M., Cass C.E., Baldwin S.A.,
RA Young J.D.;
RT "Molecular cloning and functional characterization of
RT nitrobenzylthioinosine (NBMPR)-sensitive (es) and NBMPR-insensitive (ei)
RT equilibrative nucleoside transporter proteins (rENT1 and rENT2) from rat
RT tissues.";
RL J. Biol. Chem. 272:28423-28430(1997).
CC -!- FUNCTION: Mediates both influx and efflux of nucleosides across the
CC membrane (equilibrative transporter). It is insensitive (EI) to low
CC concentrations of the inhibitor nitrobenzylmercaptopurine riboside
CC (NBMPR) and is sodium-independent. Specific for nucleosides, but may
CC also transport hypoxanthine. May also play a role in the efflux of
CC inosine and hypoxanthine from muscle cells during the net degradation
CC of purine nucleotides that occurs during strenuous exercise and/or in
CC the reuptake of these purines during the recovery process (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Resistant to dipyridamole and dilazep inhibition
CC (anticancer chemotherapeutics drugs).
CC -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC {ECO:0000305}.
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DR EMBL; AF015305; AAB88050.1; -; mRNA.
DR RefSeq; NP_113926.1; NM_031738.1.
DR RefSeq; XP_017445770.1; XM_017590281.1.
DR RefSeq; XP_017459751.1; XM_017604262.1.
DR AlphaFoldDB; O54699; -.
DR SMR; O54699; -.
DR STRING; 10116.ENSRNOP00000027178; -.
DR BindingDB; O54699; -.
DR ChEMBL; CHEMBL1287614; -.
DR DrugCentral; O54699; -.
DR TCDB; 2.A.57.1.4; the equilibrative nucleoside transporter (ent) family.
DR GlyGen; O54699; 2 sites.
DR PaxDb; O54699; -.
DR GeneID; 65194; -.
DR KEGG; rno:65194; -.
DR UCSC; RGD:69296; rat.
DR CTD; 3177; -.
DR RGD; 69296; Slc29a2.
DR VEuPathDB; HostDB:ENSRNOG00000020025; -.
DR eggNOG; KOG1479; Eukaryota.
DR HOGENOM; CLU_021611_6_0_1; -.
DR InParanoid; O54699; -.
DR OMA; FNIMDWV; -.
DR OrthoDB; 559763at2759; -.
DR PhylomeDB; O54699; -.
DR TreeFam; TF313950; -.
DR Reactome; R-RNO-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR Reactome; R-RNO-9748787; Azathioprine ADME.
DR PRO; PR:O54699; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020025; Expressed in skeletal muscle tissue and 16 other tissues.
DR Genevisible; O54699; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; ISO:RGD.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015213; F:uridine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015853; P:adenine transport; IDA:RGD.
DR GO; GO:0032238; P:adenosine transport; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0015854; P:guanine transport; IMP:RGD.
DR GO; GO:0035344; P:hypoxanthine transport; IMP:RGD.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0098810; P:neurotransmitter reuptake; ISO:RGD.
DR GO; GO:0006836; P:neurotransmitter transport; ISO:RGD.
DR GO; GO:0001504; P:neurotransmitter uptake; ISO:RGD.
DR GO; GO:1901642; P:nucleoside transmembrane transport; ISO:RGD.
DR GO; GO:0015858; P:nucleoside transport; IDA:RGD.
DR GO; GO:0015860; P:purine nucleoside transmembrane transport; ISO:RGD.
DR GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; ISO:RGD.
DR GO; GO:0035364; P:thymine transport; IDA:RGD.
DR GO; GO:0015862; P:uridine transport; IMP:RGD.
DR InterPro; IPR034764; ENT1/ENT2.
DR InterPro; IPR030197; ENT2.
DR InterPro; IPR002259; Eqnu_transpt.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR10332; PTHR10332; 1.
DR PANTHER; PTHR10332:SF8; PTHR10332:SF8; 1.
DR Pfam; PF01733; Nucleoside_tran; 1.
DR PIRSF; PIRSF016379; ENT; 1.
DR PRINTS; PR01130; DERENTRNSPRT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00939; 2a57; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..456
FT /note="Equilibrative nucleoside transporter 2"
FT /id="PRO_0000209342"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..68
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..456
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14542"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 456 AA; 50265 MW; DA97C2C578E1EE9D CRC64;
MAHGNAPRDS YHLVGISFFI LGLGTLLPWN FFITAIPYFQ GRLAGTNSSA ETPSTNHTSP
TDTFNFNNWV TLLSQLPLLL FTLLNSFLYQ CIPESVRILG SLLAILLLFA LTAALVKVDL
SPGLFFSITM ASVWFINSFC AVLQGSLFGQ LGTMPSTYST LFLSGQGLAG IFAALAMLTS
LASGVDPQTS ALGYFITPCV GILLSIICYL SLPHLKFARY YLTKKPQAPV QELETKAELL
GADEKNGIPV SPQQAGPTLD LDPEKELELG LEEPQKPGKP SVFVVFRKIW LTALCLVLVF
TVTLSVFPAI TAMVTTSSNS PGKWSQFFNP ICCFLLFNVM DWLGRSLTSY FLWPDEDSQL
LPLLVCLRFL FVPLFMLCHV PQRARLPIIF WQDAYFITFM LLFAISNGYF VSLTMCLAPR
QVLPHEREVA GALMTFFLAL GLSCGASLSF LFKALL
