Q99808 (S29A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Equilibrative nucleoside transporter 1

Alternative name(s):
Equilibrative nitrobenzylmercaptopurine riboside-sensitive nucleoside transporter
Short name=Equilibrative NBMPR-sensitive nucleoside transporter
Nucleoside transporter, es-type
Solute carrier family 29 member 1

Gene names

Name:	SLC29A1
Synonyms:	ENT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). It is sensitive (ES) to low concentrations of the inhibitor nitrobenzylmercaptopurine riboside (NBMPR) and is sodium-independent. It has a higher affinity for adenosine. Inhibited by dipyridamole and dilazep (anticancer chemotherapeutics drugs).
Subcellular location	Basolateral cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Note: Predominantly localized in the basolateral membrane in polarized MDCK cells. Ref.5
Tissue specificity	Expressed in heart, brain, mammary gland, erythrocytes and placenta, and also in fetal liver and spleen. Ref.5
Post-translational modification	Glycosylated.
Sequence similarities	Belongs to the SLC29A/ENT transporter (TC 2.A.57) family. [View classification]
Biophysicochemical properties	Kinetic parameters: Vmax for adenosine uptake is about the same for SLC29A1 and SLC29A2. KM=0.62 mM for adenosine Ref.5

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara cellular response to hypoxia Inferred from electronic annotation. Source: Compara lactation Inferred from electronic annotation. Source: Compara nucleobase-containing compound metabolic process Traceable author statement Ref.1. Source: ProtInc nucleoside transport Inferred from direct assay Ref.5. Source: UniProtKB regulation of excitatory postsynaptic membrane potential Inferred from electronic annotation. Source: Compara sleep Inferred from electronic annotation. Source: Compara uridine transport Inferred from electronic annotation. Source: Compara
Cellular_component	apical plasma membrane Inferred from direct assay Ref.5. Source: UniProtKB basolateral plasma membrane Inferred from direct assay Ref.5. Source: UniProtKB integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	nucleoside transmembrane transporter activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STK19	P49842	1	EBI-347907,EBI-347581

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 456	455	Equilibrative nucleoside transporter 1		PRO_0000209337
Regions
	Topological domain	2 – 12	11	Cytoplasmic Potential
	Transmembrane	13 – 29	17	Helical; Potential
	Topological domain	30 – 82	53	Extracellular Potential
	Transmembrane	83 – 107	25	Helical; Potential
	Topological domain	108 – 111	4	Cytoplasmic Potential
	Transmembrane	112 – 130	19	Helical; Potential
	Topological domain	131 – 138	8	Extracellular Potential
	Transmembrane	139 – 157	19	Helical; Potential
	Topological domain	158 – 174	17	Cytoplasmic Potential
	Transmembrane	175 – 199	25	Helical; Potential
	Topological domain	200 – 206	7	Extracellular Potential
	Transmembrane	207 – 227	21	Helical; Potential
	Topological domain	228 – 291	64	Cytoplasmic Potential
	Transmembrane	292 – 311	20	Helical; Potential
	Topological domain	312 – 323	12	Extracellular Potential
	Transmembrane	324 – 342	19	Helical; Potential
	Topological domain	343 – 359	17	Cytoplasmic Potential
	Transmembrane	360 – 378	19	Helical; Potential
	Topological domain	379 – 393	15	Extracellular Potential
	Transmembrane	394 – 413	20	Helical; Potential
	Topological domain	414 – 431	18	Cytoplasmic Potential
	Transmembrane	432 – 452	21	Helical; Potential
	Topological domain	453 – 456	4	Extracellular Potential
Amino acid modifications
	Glycosylation	48	1	N-linked (GlcNAc...) Ref.10
Natural variations
	Natural variant	216	1	I → T. Corresponds to variant rs45573936 [ dbSNP | Ensembl ].		VAR_053668
	Natural variant	293	1	A → T in a colorectal cancer sample; somatic mutation. Ref.11		VAR_036221
	Natural variant	391	1	E → K. Corresponds to variant rs45458701 [ dbSNP | Ensembl ].		VAR_053669
	Natural variant	455	1	I → V in a colorectal cancer sample; somatic mutation. Ref.11		VAR_036222
Experimental info
	Mutagenesis	453 – 456	4	Missing: No effect on subcellular localization and inosine transport. Ref.5
	Mutagenesis	453	1	R → A: No effect on subcellular localization and inosine transport. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q99808 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F18535A95DEBC95D	FASTA	456	50,219
	10 20 30 40 50 60 MTTSHQPQDR YKAVWLIFFM LGLGTLLPWN FFMTATQYFT NRLDMSQNVS LVTAELSKDA 70 80 90 100 110 120 QASAAPAAPL PERNSLSAIF NNVMTLCAML PLLLFTYLNS FLHQRIPQSV RILGSLVAIL 130 140 150 160 170 180 LVFLITAILV KVQLDALPFF VITMIKIVLI NSFGAILQGS LFGLAGLLPA SYTAPIMSGQ 190 200 210 220 230 240 GLAGFFASVA MICAIASGSE LSESAFGYFI TACAVIILTI ICYLGLPRLE FYRYYQQLKL 250 260 270 280 290 300 EGPGEQETKL DLISKGEEPR AGKEESGVSV SNSQPTNESH SIKAILKNIS VLAFSVCFIF 310 320 330 340 350 360 TITIGMFPAV TVEVKSSIAG SSTWERYFIP VSCFLTFNIF DWLGRSLTAV FMWPGKDSRW 370 380 390 400 410 420 LPSLVLARLV FVPLLLLCNI KPRRYLTVVF EHDAWFIFFM AAFAFSNGYL ASLCMCFGPK 430 440 450 KVKPAEAETA GAIMAFFLCL GLALGAVFSF LFRAIV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a human nucleoside transporter implicated in the cellular uptake of adenosine and chemotherapeutic drugs." Griffiths M., Beaumont N., Yao S.Y.M., Sundaram M., Boumah C.E., Davies A., Kwong F.Y.P., Coe I., Cass C.E., Young J.D., Baldwin S.A. Nat. Med. 3:89-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-22. Tissue: Placenta.
[2]	"Genomic sequence of the human equilibrative nucleoside transporter 1 (hENT1)." Graham K.A., Coe I.R., Carpenter P., Baldwin S.A., Young J.D., Cass C.E. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Human intestinal es nucleoside transporter: molecular characterization and nucleoside inhibitory profiles." Lum P.Y., Ngo L.Y., Bakken A.H., Unadkat J.D. Cancer Chemother. Pharmacol. 45:273-278(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Jejunum and Small intestine.
[4]	"Comparative genomic analysis of equilibrative nucleoside transporters suggests conserved protein structure despite limited sequence identity." Sankar N., Machado J., Abdulla P., Hilliker A.J., Coe I.R. Nucleic Acids Res. 30:4339-4350(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Localization of human equilibrative nucleoside transporters, hENT1 and hENT2, in renal epithelial cells." Mangravite L.M., Xiao G., Giacomini K.M. Am. J. Physiol. 284:F902-F910(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-453 AND 453-ARG--VAL-456.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: Colon and Muscle.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-293 AND VAL-455.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U81375 mRNA. Translation: AAC51103.1. AF190884 Genomic DNA. Translation: AAF02777.1. AF079117 mRNA. Translation: AAC62495.1. AF495730 Genomic DNA. Translation: AAM11785.1. AK090615 mRNA. Translation: BAG52197.1. AL139392 Genomic DNA. Translation: CAI20093.1. BC001382 mRNA. Translation: AAH01382.1. BC008954 mRNA. Translation: AAH08954.1.
IPI	IPI00939219.
RefSeq	NP_001071642.1. NM_001078174.1. NP_001071643.1. NM_001078175.2. NP_001071644.1. NM_001078176.2. NP_001071645.1. NM_001078177.1. NP_004946.1. NM_004955.2.
UniGene	Hs.25450.
3D structure databases
ProteinModelPortal	Q99808.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99808. 2 interactions.
MINT	MINT-1034227.
STRING	9606.ENSP00000360773.
Protein family/group databases
TCDB	2.A.57.1.1. equilibrative nucleoside transporter (ENT) family.
PTM databases
PhosphoSite	Q99808.
Polymorphism databases
DMDM	9296956.
Proteomic databases
PaxDb	Q99808.
PRIDE	Q99808.
Protocols and materials databases
DNASU	2030.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371708; ENSP00000360773; ENSG00000112759. ENST00000371713; ENSP00000360778; ENSG00000112759. ENST00000371724; ENSP00000360789; ENSG00000112759. ENST00000371731; ENSP00000360796; ENSG00000112759. ENST00000371740; ENSP00000360805; ENSG00000112759. ENST00000371755; ENSP00000360820; ENSG00000112759. ENST00000393841; ENSP00000377424; ENSG00000112759. ENST00000393844; ENSP00000377427; ENSG00000112759. ENST00000427851; ENSP00000392668; ENSG00000112759.
GeneID	2030.
KEGG	hsa:2030.
UCSC	uc003owu.1. human.
Organism-specific databases
CTD	2030.
GeneCards	GC06P044187.
HGNC	HGNC:11003. SLC29A1.
HPA	HPA012383. HPA012384.
MIM	602193. gene.
neXtProt	NX_Q99808.
PharmGKB	PA154.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG249415.
HOGENOM	HOG000007684.
HOVERGEN	HBG074626.
InParanoid	Q99808.
KO	K15014.
OrthoDB	EOG48PMKH.
PhylomeDB	Q99808.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	Q99808.
Bgee	Q99808.
CleanEx	HS_SLC29A1.
Genevestigator	Q99808.
GermOnline	ENSG00000112759. Homo sapiens.
Family and domain databases
InterPro	IPR002259. Eqnu_transpt. [Graphical view]
PANTHER	PTHR10332. PTHR10332. 1 hit.
Pfam	PF01733. Nucleoside_tran. 1 hit. [Graphical view]
PIRSF	PIRSF016379. ENT. 1 hit.
PRINTS	PR01130. DERENTRNSPRT.
TIGRFAMs	TIGR00939. 2a57. 1 hit.
ProtoNet	Search...
Other
BindingDB	Q99808.
ChEMBL	CHEMBL1997.
DrugBank	DB00197. Troglitazone.
GenomeRNAi	2030.
NextBio	8235.
SOURCE	Search...

Entry information

Entry name

S29A1_HUMAN

Accession

Primary (citable) accession number: Q99808
Secondary accession number(s): B3KQY5, Q5T9W9, Q9UJY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.