S29A2_HUMAN
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 03-AUG-2022, entry version 186.
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; 142 antibodies from 23 providers.
DR DNASU; 3177; -.
DR Ensembl; ENST00000357440.7; ENSP00000350024.2; ENSG00000174669.12. [Q14542-1]
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. [Q14542-1]
DR Ensembl; ENST00000546034.1; ENSP00000440329.1; ENSG00000174669.12. [Q14542-1]
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 Reactome; R-HSA-9748787; Azathioprine ADME.
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 147 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: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 GO; GO:0006855; P:xenobiotic transmembrane transport; TAS:Reactome.
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
