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Q7RTT9

- S29A4_HUMAN

UniProt

Q7RTT9 - S29A4_HUMAN

Protein

Equilibrative nucleoside transporter 4

Gene

SLC29A4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      Previous versions | rss
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    Functioni

    Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia.4 Publications

    GO - Molecular functioni

    1. nucleoside transmembrane transporter activity Source: InterPro

    GO - Biological processi

    1. transmembrane transport Source: Reactome

    Keywords - Biological processi

    Transport

    Enzyme and pathway databases

    ReactomeiREACT_1206. Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.

    Protein family/group databases

    TCDBi2.A.57.1.5. the equilibrative nucleoside transporter (ent) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Equilibrative nucleoside transporter 4
    Short name:
    hENT4
    Alternative name(s):
    Plasma membrane monoamine transporter
    Solute carrier family 29 member 4
    Gene namesi
    Name:SLC29A4
    Synonyms:ENT4, PMAT
    ORF Names:PSEC0113
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:23097. SLC29A4.

    Subcellular locationi

    Cell membrane Curated; Multi-pass membrane protein Curated. Apical cell membrane Curated; Multi-pass membrane protein Curated
    Note: Located to the plasma membranes of ventricular myocytes and vascular endothelial cells. Targeted to the apical membranes of differentiated kidney epithelial cells.2 Publications

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi91 – 911D → A: No significant change in cationic transport activity. 1 Publication
    Mutagenesisi107 – 1071D → A: Loss of cationic transport activity. 1 Publication
    Mutagenesisi128 – 1281E → A: No significant change in cationic transport activity. 1 Publication
    Mutagenesisi154 – 1541D → A: Loss of cationic transport activity; increase in uridine uptake. 1 Publication
    Mutagenesisi163 – 1631D → A: Loss of cationic transport activity. 1 Publication
    Mutagenesisi206 – 2061E → A: Loss of cationic transport activity. 2 Publications
    Mutagenesisi206 – 2061E → D: No loss of cationic transporter activity; no activity towards uridine. 2 Publications
    Mutagenesisi206 – 2061E → Q: Loss of cationic transporter activity; increase in uridine uptake. 2 Publications
    Mutagenesisi206 – 2061E → R: Loss of cationic transporter activity. 2 Publications
    Mutagenesisi220 – 2201T → A: Reduced cationic transport activity. 1 Publication
    Mutagenesisi220 – 2201T → I: Loss of cationic transporter activity. 1 Publication
    Mutagenesisi220 – 2201T → S: Reduced cationic transport activity. 1 Publication
    Mutagenesisi227 – 2271E → A: Functional with slight increased cationic transport activity. 1 Publication
    Mutagenesisi242 – 2421E → A: Reduced cationic transport activity. 1 Publication
    Mutagenesisi336 – 3361W → A: Loss of cationic transport activity. 1 Publication
    Mutagenesisi375 – 3751E → A: Functional with slight increased cationic transport activity. 2 Publications
    Mutagenesisi375 – 3751E → Q: No change in cationic activity and pH sensitivity. 2 Publications

    Organism-specific databases

    PharmGKBiPA134976472.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 530530Equilibrative nucleoside transporter 4PRO_0000326251Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi523 – 5231N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ7RTT9.
    PRIDEiQ7RTT9.

    PTM databases

    PhosphoSiteiQ7RTT9.

    Expressioni

    Tissue specificityi

    Expressed abundantly in the heart, in both cardiomyocytes and vascular endothelial cells (at protein level). Highly expressed in brain, kidney and skeletal muscle. In the brain expressed in cerebellum, cerebral cortex, medulla, occipital pole, frontal and temporal lobes putamen and in the spinal cord. Lower expression in liver, pancreas, and liver. Expressed in endometrial tissue, exclusively in the stroma. Expression is high in the proliferative phase, decreases during the secretory phase, and is no longer detectable in the menstrual phase.4 Publications

    Gene expression databases

    ArrayExpressiQ7RTT9.
    BgeeiQ7RTT9.
    CleanExiHS_SLC29A4.
    GenevestigatoriQ7RTT9.

    Organism-specific databases

    HPAiHPA052829.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000297195.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7RTT9.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6868ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini90 – 10112CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini123 – 13917ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini161 – 1666CytoplasmicSequence Analysis
    Topological domaini188 – 23144ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini253 – 35199CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini373 – 3819ExtracellularSequence Analysis
    Topological domaini403 – 41614CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini438 – 45013ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini472 – 48615CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini510 – 53021ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei69 – 8921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei102 – 12221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei140 – 16021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei167 – 18721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei232 – 25221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei352 – 37221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei382 – 40221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei417 – 43721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei451 – 47121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei487 – 50923HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG249415.
    HOGENOMiHOG000048076.
    HOVERGENiHBG095787.
    InParanoidiQ7RTT9.
    KOiK03323.
    OMAiWPSFRAL.
    PhylomeDBiQ7RTT9.
    TreeFamiTF313950.

    Family and domain databases

    InterProiIPR002259. Eqnu_transpt.
    IPR016196. MFS_dom_general_subst_transpt.
    [Graphical view]
    PANTHERiPTHR10332. PTHR10332. 1 hit.
    PfamiPF01733. Nucleoside_tran. 1 hit.
    [Graphical view]
    PRINTSiPR01130. DERENTRNSPRT.
    SUPFAMiSSF103473. SSF103473. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7RTT9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGSVGSQRLE EPSVAGTPDP GVVMSFTFDS HQLEEAAEAA QGQGLRARGV    50
    PAFTDTTLDE PVPDDRYHAI YFAMLLAGVG FLLPYNSFIT DVDYLHHKYP 100
    GTSIVFDMSL TYILVALAAV LLNNVLVERL TLHTRITAGY LLALGPLLFI 150
    SICDVWLQLF SRDQAYAINL AAVGTVAFGC TVQQSSFYGY TGMLPKRYTQ 200
    GVMTGESTAG VMISLSRILT KLLLPDERAS TLIFFLVSVA LELLCFLLHL 250
    LVRRSRFVLF YTTRPRDSHR GRPGLGRGYG YRVHHDVVAG DVHFEHPAPA 300
    LAPNESPKDS PAHEVTGSGG AYMRFDVPRP RVQRSWPTFR ALLLHRYVVA 350
    RVIWADMLSI AVTYFITLCL FPGLESEIRH CILGEWLPIL IMAVFNLSDF 400
    VGKILAALPV DWRGTHLLAC SCLRVVFIPL FILCVYPSGM PALRHPAWPC 450
    IFSLLMGISN GYFGSVPMIL AAGKVSPKQR ELAGNTMTVS YMSGLTLGSA 500
    VAYCTYSLTR DAHGSCLHAS TANGSILAGL 530
    Length:530
    Mass (Da):58,059
    Last modified:December 15, 2003 - v1
    Checksum:i3FE5D5ED1D248A13
    GO
    Isoform 2 (identifier: Q7RTT9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         139-182: GYLLALGPLLFISICDVWLQLFSRDQAYAINLAAVGTVAFGCTV → ASATCGCSSSLGTRPTPSTWPLWAPWPSAA

    Note: No experimental confirmation available.

    Show »
    Length:516
    Mass (Da):56,401
    Checksum:i601976FF77817BFD
    GO

    Sequence cautioni

    The sequence BAC11612.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251S → C in BAC03836. (PubMed:14702039)Curated
    Sequence conflicti41 – 411Q → R in BAC03836. (PubMed:14702039)Curated
    Sequence conflicti196 – 1961K → R in BAC03836. (PubMed:14702039)Curated
    Sequence conflicti261 – 2611Y → H in BAC11612. (PubMed:14702039)Curated
    Sequence conflicti301 – 3011L → P in BAC03836. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791V → E.1 Publication
    Corresponds to variant rs17854505 [ dbSNP | Ensembl ].
    VAR_040044
    Natural varianti124 – 1241N → K.1 Publication
    Corresponds to variant rs17855675 [ dbSNP | Ensembl ].
    VAR_040045
    Natural varianti429 – 4291P → T.1 Publication
    Corresponds to variant rs17857336 [ dbSNP | Ensembl ].
    VAR_040046

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei139 – 18244GYLLA…FGCTV → ASATCGCSSSLGTRPTPSTW PLWAPWPSAA in isoform 2. 1 PublicationVSP_032647Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY485959 mRNA. Translation: AAS65965.1.
    AK075422 mRNA. Translation: BAC11612.1. Different initiation.
    AK092242 mRNA. Translation: BAC03836.1.
    CH471144 Genomic DNA. Translation: EAW87329.1.
    CH471144 Genomic DNA. Translation: EAW87330.1.
    BC025325 mRNA. Translation: AAH25325.1.
    BC047592 mRNA. Translation: AAH47592.1.
    BK000627 Genomic DNA. Translation: DAA00308.1.
    CCDSiCCDS5340.1. [Q7RTT9-1]
    RefSeqiNP_001035751.1. NM_001040661.1. [Q7RTT9-1]
    NP_694979.2. NM_153247.2. [Q7RTT9-1]
    XP_005249714.1. XM_005249657.1. [Q7RTT9-2]
    XP_005249715.1. XM_005249658.2. [Q7RTT9-2]
    XP_006715730.1. XM_006715667.1. [Q7RTT9-1]
    UniGeneiHs.4302.

    Genome annotation databases

    EnsembliENST00000297195; ENSP00000297195; ENSG00000164638. [Q7RTT9-1]
    ENST00000396872; ENSP00000380081; ENSG00000164638. [Q7RTT9-1]
    ENST00000406453; ENSP00000385845; ENSG00000164638. [Q7RTT9-2]
    GeneIDi222962.
    KEGGihsa:222962.
    UCSCiuc003soc.3. human. [Q7RTT9-1]
    uc003soe.3. human. [Q7RTT9-2]

    Polymorphism databases

    DMDMi74713147.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY485959 mRNA. Translation: AAS65965.1 .
    AK075422 mRNA. Translation: BAC11612.1 . Different initiation.
    AK092242 mRNA. Translation: BAC03836.1 .
    CH471144 Genomic DNA. Translation: EAW87329.1 .
    CH471144 Genomic DNA. Translation: EAW87330.1 .
    BC025325 mRNA. Translation: AAH25325.1 .
    BC047592 mRNA. Translation: AAH47592.1 .
    BK000627 Genomic DNA. Translation: DAA00308.1 .
    CCDSi CCDS5340.1. [Q7RTT9-1 ]
    RefSeqi NP_001035751.1. NM_001040661.1. [Q7RTT9-1 ]
    NP_694979.2. NM_153247.2. [Q7RTT9-1 ]
    XP_005249714.1. XM_005249657.1. [Q7RTT9-2 ]
    XP_005249715.1. XM_005249658.2. [Q7RTT9-2 ]
    XP_006715730.1. XM_006715667.1. [Q7RTT9-1 ]
    UniGenei Hs.4302.

    3D structure databases

    ProteinModelPortali Q7RTT9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000297195.

    Chemistry

    GuidetoPHARMACOLOGYi 1120.

    Protein family/group databases

    TCDBi 2.A.57.1.5. the equilibrative nucleoside transporter (ent) family.

    PTM databases

    PhosphoSitei Q7RTT9.

    Polymorphism databases

    DMDMi 74713147.

    Proteomic databases

    PaxDbi Q7RTT9.
    PRIDEi Q7RTT9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297195 ; ENSP00000297195 ; ENSG00000164638 . [Q7RTT9-1 ]
    ENST00000396872 ; ENSP00000380081 ; ENSG00000164638 . [Q7RTT9-1 ]
    ENST00000406453 ; ENSP00000385845 ; ENSG00000164638 . [Q7RTT9-2 ]
    GeneIDi 222962.
    KEGGi hsa:222962.
    UCSCi uc003soc.3. human. [Q7RTT9-1 ]
    uc003soe.3. human. [Q7RTT9-2 ]

    Organism-specific databases

    CTDi 222962.
    GeneCardsi GC07P005289.
    HGNCi HGNC:23097. SLC29A4.
    HPAi HPA052829.
    MIMi 609149. gene.
    neXtProti NX_Q7RTT9.
    PharmGKBi PA134976472.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249415.
    HOGENOMi HOG000048076.
    HOVERGENi HBG095787.
    InParanoidi Q7RTT9.
    KOi K03323.
    OMAi WPSFRAL.
    PhylomeDBi Q7RTT9.
    TreeFami TF313950.

    Enzyme and pathway databases

    Reactomei REACT_1206. Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.

    Miscellaneous databases

    ChiTaRSi SLC29A4. human.
    GeneWikii SLC29A4.
    GenomeRNAii 222962.
    NextBioi 91692.
    PROi Q7RTT9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7RTT9.
    Bgeei Q7RTT9.
    CleanExi HS_SLC29A4.
    Genevestigatori Q7RTT9.

    Family and domain databases

    InterProi IPR002259. Eqnu_transpt.
    IPR016196. MFS_dom_general_subst_transpt.
    [Graphical view ]
    PANTHERi PTHR10332. PTHR10332. 1 hit.
    Pfami PF01733. Nucleoside_tran. 1 hit.
    [Graphical view ]
    PRINTSi PR01130. DERENTRNSPRT.
    SUPFAMi SSF103473. SSF103473. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a novel monoamine transporter in the human brain."
      Engel K., Zhou M., Wang J.
      J. Biol. Chem. 279:50042-50049(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY.
      Tissue: Kidney.
    2. "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] (ISOFORM 1).
      Tissue: Teratocarcinoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 2), VARIANTS GLU-79; LYS-124 AND THR-429.
      Tissue: Brain and Eye.
    5. "Molecular evolution of the equilibrative nucleoside transporter family: identification of novel family members in prokaryotes and eukaryotes."
      Acimovic Y., Coe I.R.
      Mol. Biol. Evol. 19:2199-2210(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    6. "Distribution and functional characterization of equilibrative nucleoside transporter-4, a novel cardiac adenosine transporter activated at acidic pH."
      Barnes K., Dobrzynski H., Foppolo S., Beal P.R., Ismat F., Scullion E.R., Sun L., Tellez J., Ritzel M.W., Claycomb W.C., Cass C.E., Young J.D., Billeter-Clark R., Boyett M.R., Baldwin S.A.
      Circ. Res. 99:510-519(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-523, MUTAGENESIS OF GLU-206 AND GLU-375.
    7. "Membrane localization and pH-dependent transport of a newly cloned organic cation transporter (PMAT) in kidney cells."
      Xia L., Engel K., Zhou M., Wang J.
      Am. J. Physiol. 292:F682-F690(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TOPOLOGY, TISSUE SPECIFICITY.
    8. "Molecular determinants of substrate selectivity of a novel organic cation transporter (PMAT) in the SLC29 family."
      Zhou M., Xia L., Engel K., Wang J.
      J. Biol. Chem. 282:3188-3195(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-91; ASP-107; GLU-128; ASP-154; ASP-163; GLU-206; THR-220; GLU-227; GLU-242; TRP-336 AND GLU-375.
    9. "The organic cation transporters (OCT1, OCT2, EMT) and the plasma membrane monoamine transporter (PMAT) show differential distribution and cyclic expression pattern in human endometrium and early pregnancy decidua."
      Bottalico B., Noskova V., Pilka R., Larsson I., Domanski H., Casslen B., Hansson S.R.
      Mol. Reprod. Dev. 74:1303-1311(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiS29A4_HUMAN
    AccessioniPrimary (citable) accession number: Q7RTT9
    Secondary accession number(s): Q6PJ08
    , Q86WY8, Q8NAR3, Q8NBM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3