ID   S29A2_HUMAN             Reviewed;         456 AA.
AC   Q14542; B3KPY7; O43530; Q52M84; Q96R00; Q9UPE0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   25-MAY-2022, entry version 185.
DE   RecName: Full=Equilibrative nucleoside transporter 2;
DE   AltName: Full=36 kDa nucleolar protein HNP36;
DE   AltName: Full=Delayed-early response protein 12;
DE   AltName: Full=Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter;
DE            Short=Equilibrative NBMPR-insensitive nucleoside transporter;
DE   AltName: Full=Hydrophobic nucleolar protein, 36 kDa;
DE   AltName: Full=Nucleoside transporter, ei-type;
DE   AltName: Full=Solute carrier family 29 member 2;
GN   Name=SLC29A2; Synonyms=DER12, ENT2, HNP36;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Heart;
RX   PubMed=7639753; DOI=10.1006/bbrc.1995.2133;
RA   Williams J.B., Lanahan A.A.;
RT   "A mammalian delayed-early response gene encodes HNP36, a novel, conserved
RT   nucleolar protein.";
RL   Biochem. Biophys. Res. Commun. 213:325-333(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND TISSUE SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=9396714; DOI=10.1042/bj3280739;
RA   Griffiths M., Yao S.Y., Abidi F., Phillips S.E., Cass C.E., Young J.D.,
RA   Baldwin S.A.;
RT   "Molecular cloning and characterization of a nitrobenzylthioinosine-
RT   insensitive (ei) equilibrative nucleoside transporter from human
RT   placenta.";
RL   Biochem. J. 328:739-743(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND RESPONSE TO NBMPR.
RX   PubMed=9478986; DOI=10.1074/jbc.273.9.5288;
RA   Crawford C.R., Patel D.H., Naeve C., Belt J.A.;
RT   "Cloning of the human equilibrative, nitrobenzylmercaptopurine riboside
RT   (NBMPR)-insensitive nucleoside transporter ei by functional expression in a
RT   transport-deficient cell line.";
RL   J. Biol. Chem. 273:5288-5293(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LEU-455 AND
RP   LEU-456.
RX   PubMed=12527552; DOI=10.1152/ajprenal.00215.2002;
RA   Mangravite L.M., Xiao G., Giacomini K.M.;
RT   "Localization of human equilibrative nucleoside transporters, hENT1 and
RT   hENT2, in renal epithelial cells.";
RL   Am. J. Physiol. 284:F902-F910(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   [9]
RP   GLYCOSYLATION AT ASN-48 AND ASN-57.
RX   PubMed=12590919; DOI=10.1016/s0003-9861(02)00718-x;
RA   Ward J.L., Leung G.P., Toan S.V., Tse C.-M.;
RT   "Functional analysis of site-directed glycosylation mutants of the human
RT   equilibrative nucleoside transporter-2.";
RL   Arch. Biochem. Biophys. 411:19-26(2003).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
RP   VARIANTS TYR-5; LYS-68; LEU-94 AND 184-SER--VAL-186 DELINS MET.
RX   PubMed=16214850; DOI=10.1124/dmd.105.006270;
RA   Owen R.P., Lagpacan L.L., Taylor T.R., De La Cruz M., Huang C.C.,
RA   Kawamoto M., Johns S.J., Stryke D., Ferrin T.E., Giacomini K.M.;
RT   "Functional characterization and haplotype analysis of polymorphisms in the
RT   human equilibrative nucleoside transporter, ENT2.";
RL   Drug Metab. Dispos. 34:12-15(2006).
CC   -!- FUNCTION: Mediates equilibrative transport of purine, pyrimidine
CC       nucleosides and the purine base hypoxanthine. Very less sensitive than
CC       SLC29A1 to inhibition by nitrobenzylthioinosine (NBMPR), dipyridamole,
CC       dilazep and draflazine. {ECO:0000269|PubMed:9396714}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.2 mM for uridine {ECO:0000269|PubMed:12527552,
CC         ECO:0000269|PubMed:9396714};
CC         KM=0.75 mM for adenosine {ECO:0000269|PubMed:12527552,
CC         ECO:0000269|PubMed:9396714};
CC         Note=Vmax for adenosine uptake is about the same for SLC29A1 and
CC         SLC29A2.;
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000269|PubMed:12527552}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:12527552}. Nucleus membrane
CC       {ECO:0000269|PubMed:12527552}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:12527552}. Note=Localized at the basolateral cell
CC       membrane in polarized MDCK cells.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Long;
CC         IsoId=Q14542-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short, HNP36;
CC         IsoId=Q14542-2; Sequence=VSP_040728, VSP_040729;
CC       Name=3;
CC         IsoId=Q14542-3; Sequence=VSP_040730, VSP_040731;
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, liver, lung,
CC       placenta, brain, heart, kidney and ovarian tissues.
CC       {ECO:0000269|PubMed:12527552, ECO:0000269|PubMed:9396714}.
CC   -!- INDUCTION: By PDGF/platelet derived growth factor and fibroblast growth
CC       factor (FGF).
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA60380.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR   EMBL; X86681; CAA60380.1; ALT_SEQ; mRNA.
DR   EMBL; AF029358; AAC39526.1; -; mRNA.
DR   EMBL; AF034102; AAB97834.1; -; mRNA.
DR   EMBL; AK057041; BAG51849.1; -; mRNA.
DR   EMBL; AF401235; AAK92533.1; -; mRNA.
DR   EMBL; AP001107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW74521.1; -; Genomic_DNA.
DR   EMBL; CH471076; EAW74519.1; -; Genomic_DNA.
DR   EMBL; BC093634; AAH93634.1; -; mRNA.
DR   CCDS; CCDS8137.1; -. [Q14542-1]
DR   PIR; JC4196; JC4196.
DR   RefSeq; NP_001287797.1; NM_001300868.1. [Q14542-1]
DR   RefSeq; NP_001523.2; NM_001532.2. [Q14542-1]
DR   RefSeq; XP_016873121.1; XM_017017632.1. [Q14542-1]
DR   AlphaFoldDB; Q14542; -.
DR   SMR; Q14542; -.
DR   BioGRID; 109419; 24.
DR   IntAct; Q14542; 2.
DR   MINT; Q14542; -.
DR   STRING; 9606.ENSP00000350024; -.
DR   BindingDB; Q14542; -.
DR   ChEMBL; CHEMBL3509606; -.
DR   DrugBank; DB00640; Adenosine.
DR   DrugBank; DB00993; Azathioprine.
DR   DrugBank; DB00900; Didanosine.
DR   DrugBank; DB00898; Ethanol.
DR   DrugBank; DB00441; Gemcitabine.
DR   DrugBank; DB01033; Mercaptopurine.
DR   DrugBank; DB09327; Tegafur-uracil.
DR   DrugBank; DB00432; Trifluridine.
DR   DrugBank; DB00943; Zalcitabine.
DR   DrugBank; DB00495; Zidovudine.
DR   TCDB; 2.A.57.1.8; the equilibrative nucleoside transporter (ent) family.
DR   GlyGen; Q14542; 3 sites.
DR   iPTMnet; Q14542; -.
DR   PhosphoSitePlus; Q14542; -.
DR   BioMuta; SLC29A2; -.
DR   DMDM; 116242781; -.
DR   EPD; Q14542; -.
DR   jPOST; Q14542; -.
DR   MassIVE; Q14542; -.
DR   MaxQB; Q14542; -.
DR   PaxDb; Q14542; -.
DR   PeptideAtlas; Q14542; -.
DR   PRIDE; Q14542; -.
DR   ProteomicsDB; 60037; -. [Q14542-1]
DR   ProteomicsDB; 60039; -. [Q14542-3]
DR   Antibodypedia; 16257; 140 antibodies from 23 providers.
DR   DNASU; 3177; -.
DR   Ensembl; ENST00000357440.7; ENSP00000350024.2; ENSG00000174669.12.
DR   Ensembl; ENST00000540386.5; ENSP00000444870.1; ENSG00000174669.12. [Q14542-3]
DR   Ensembl; ENST00000541567.5; ENSP00000442116.1; ENSG00000174669.12. [Q14542-2]
DR   Ensembl; ENST00000544554.5; ENSP00000439456.1; ENSG00000174669.12.
DR   Ensembl; ENST00000546034.1; ENSP00000440329.1; ENSG00000174669.12.
DR   GeneID; 3177; -.
DR   KEGG; hsa:3177; -.
DR   MANE-Select; ENST00000357440.7; ENSP00000350024.2; NM_001532.3; NP_001523.2.
DR   UCSC; uc001oht.4; human. [Q14542-1]
DR   CTD; 3177; -.
DR   DisGeNET; 3177; -.
DR   GeneCards; SLC29A2; -.
DR   HGNC; HGNC:11004; SLC29A2.
DR   HPA; ENSG00000174669; Group enriched (skeletal muscle, tongue).
DR   MIM; 602110; gene.
DR   neXtProt; NX_Q14542; -.
DR   OpenTargets; ENSG00000174669; -.
DR   PharmGKB; PA191; -.
DR   VEuPathDB; HostDB:ENSG00000174669; -.
DR   eggNOG; KOG1479; Eukaryota.
DR   GeneTree; ENSGT00950000182898; -.
DR   HOGENOM; CLU_021611_6_0_1; -.
DR   InParanoid; Q14542; -.
DR   OMA; FNIMDWV; -.
DR   OrthoDB; 559763at2759; -.
DR   PhylomeDB; Q14542; -.
DR   TreeFam; TF313950; -.
DR   PathwayCommons; Q14542; -.
DR   Reactome; R-HSA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR   SignaLink; Q14542; -.
DR   BioGRID-ORCS; 3177; 15 hits in 1074 CRISPR screens.
DR   ChiTaRS; SLC29A2; human.
DR   GeneWiki; Equilibrative_nucleoside_transporter_2; -.
DR   GenomeRNAi; 3177; -.
DR   Pharos; Q14542; Tbio.
DR   PRO; PR:Q14542; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q14542; protein.
DR   Bgee; ENSG00000174669; Expressed in gastrocnemius and 186 other tissues.
DR   ExpressionAtlas; Q14542; baseline and differential.
DR   Genevisible; Q14542; HS.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0005337; F:nucleoside transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0015213; F:uridine transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0015853; P:adenine transport; IBA:GO_Central.
DR   GO; GO:0032238; P:adenosine transport; IDA:ARUK-UCL.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR   GO; GO:0015854; P:guanine transport; IBA:GO_Central.
DR   GO; GO:0035344; P:hypoxanthine transport; IBA:GO_Central.
DR   GO; GO:0007595; P:lactation; IEA:Ensembl.
DR   GO; GO:0098810; P:neurotransmitter reuptake; IMP:SynGO.
DR   GO; GO:0006836; P:neurotransmitter transport; IDA:ARUK-UCL.
DR   GO; GO:0001504; P:neurotransmitter uptake; ISS:ARUK-UCL.
DR   GO; GO:1901642; P:nucleoside transmembrane transport; IDA:ARUK-UCL.
DR   GO; GO:0015858; P:nucleoside transport; IDA:UniProtKB.
DR   GO; GO:0015860; P:purine nucleoside transmembrane transport; IDA:ARUK-UCL.
DR   GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; IDA:ARUK-UCL.
DR   GO; GO:0035364; P:thymine transport; IBA:GO_Central.
DR   GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR   GO; GO:0015862; P:uridine transport; IDA:ARUK-UCL.
DR   Gene3D; 1.20.1250.20; -; 1.
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   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Membrane; Nucleus;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..456
FT                   /note="Equilibrative nucleoside transporter 2"
FT                   /id="PRO_0000209340"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        360..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        432..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12590919"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12590919"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         93..202
FT                   /note="VPETVRILGSLLAILLLFALTAALVKVDMSPGPFFSITMASVCFINSFSAVL
FT                   QGSLFGQLGTMPSTYSTLFLSGQGLAGIFAALAMLLSMASGVDAETSALGYFITPCVG
FT                   -> AGQGGHEPRTLLLHHHGLRLLHQLLQCSPTGQPLRAAGHHALHLQHPLPQRPGPGW
FT                   DLCCPCHAPVHGQWRGRRDLCPGVLYHALCGHPHVHRVLPEPASPEVCPLLPGQ (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:7639753"
FT                   /id="VSP_040728"
FT   VAR_SEQ         203..456
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:7639753"
FT                   /id="VSP_040729"
FT   VAR_SEQ         290..301
FT                   /note="IWLTALCLVLVF -> SPCPSSPPSQPW (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12527552"
FT                   /id="VSP_040730"
FT   VAR_SEQ         302..456
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12527552"
FT                   /id="VSP_040731"
FT   VARIANT         5
FT                   /note="D -> Y (in dbSNP:rs8187643)"
FT                   /evidence="ECO:0000269|PubMed:16214850"
FT                   /id="VAR_029289"
FT   VARIANT         68
FT                   /note="N -> K (in dbSNP:rs8187644)"
FT                   /evidence="ECO:0000269|PubMed:16214850"
FT                   /id="VAR_029290"
FT   VARIANT         94
FT                   /note="P -> L (in dbSNP:rs8187648)"
FT                   /evidence="ECO:0000269|PubMed:16214850"
FT                   /id="VAR_029291"
FT   VARIANT         184..186
FT                   /note="SGV -> M"
FT                   /evidence="ECO:0000269|PubMed:16214850"
FT                   /id="VAR_036822"
FT   MUTAGEN         455
FT                   /note="L->R: Reduces drastically localization at the cell
FT                   surface. No effect on uptake of adenosine and thymidine.
FT                   Reduces drastically localization at the cell surface and
FT                   induces an significant reduction of adenosine or thymidine
FT                   uptake; when associated with R-456."
FT                   /evidence="ECO:0000269|PubMed:12527552"
FT   MUTAGEN         456
FT                   /note="L->R: Reduces drastically localization at the cell
FT                   surface and induces an significant reduction of adenosine
FT                   or thymidine uptake; when associated with R-455."
FT                   /evidence="ECO:0000269|PubMed:12527552"
FT   CONFLICT        200
FT                   /note="C -> Y (in Ref. 1; CAA60380 and 2; AAC39526)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   456 AA;  50113 MW;  ABCBD244306708E1 CRC64;
     MARGDAPRDS YHLVGISFFI LGLGTLLPWN FFITAIPYFQ ARLAGAGNST ARILSTNHTG
     PEDAFNFNNW VTLLSQLPLL LFTLLNSFLY QCVPETVRIL GSLLAILLLF ALTAALVKVD
     MSPGPFFSIT MASVCFINSF SAVLQGSLFG QLGTMPSTYS TLFLSGQGLA GIFAALAMLL
     SMASGVDAET SALGYFITPC VGILMSIVCY LSLPHLKFAR YYLANKSSQA QAQELETKAE
     LLQSDENGIP SSPQKVALTL DLDLEKEPES EPDEPQKPGK PSVFTVFQKI WLTALCLVLV
     FTVTLSVFPA ITAMVTSSTS PGKWSQFFNP ICCFLLFNIM DWLGRSLTSY FLWPDEDSRL
     LPLLVCLRFL FVPLFMLCHV PQRSRLPILF PQDAYFITFM LLFAVSNGYL VSLTMCLAPR
     QVLPHEREVA GALMTFFLAL GLSCGASLSF LFKALL
//