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ENT6_ARATH
ID   ENT6_ARATH              Reviewed;         418 AA.
AC   Q944N8; Q9M0Y4;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Equilibrative nucleotide transporter 6;
DE            Short=AtENT6;
DE   AltName: Full=Nucleoside transporter ENT6;
GN   Name=ENT6; OrderedLocusNames=At4g05110; ORFNames=C17L7.30, T32N4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=12810710; DOI=10.1074/jbc.m304768200;
RA   Li G., Liu K., Baldwin S.A., Wang D.;
RT   "Equilibrative nucleoside transporters of Arabidopsis thaliana. cDNA
RT   cloning, expression pattern, and analysis of transport activities.";
RL   J. Biol. Chem. 278:35732-35742(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX   PubMed=15228386; DOI=10.1042/bj20040389;
RA   Wormit A., Traub M., Floerchinger M., Neuhaus H.E., Moehlmann T.;
RT   "Characterization of three novel members of the Arabidopsis thaliana
RT   equilibrative nucleoside transporter (ENT) family.";
RL   Biochem. J. 383:19-26(2004).
CC   -!- FUNCTION: Nucleoside transporter that can mediate uptake of adenosine,
CC       uridine, guanosine or cytidine when expressed in a heterologous system
CC       (yeast). {ECO:0000269|PubMed:15228386}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.0 uM for adenosine {ECO:0000269|PubMed:15228386};
CC         KM=6.4 uM for uridine {ECO:0000269|PubMed:15228386};
CC         KM=11.5 uM for guanosine {ECO:0000269|PubMed:15228386};
CC         KM=21.2 uM for cytidine {ECO:0000269|PubMed:15228386};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15228386};
CC       Multi-pass membrane protein {ECO:0000305|PubMed:15228386}. Note=Plasma
CC       membrane.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and siliques.
CC       {ECO:0000269|PubMed:12810710}.
CC   -!- INDUCTION: By nitrogen deficiency and 5-fluorouracil plus methotrexate.
CC       {ECO:0000269|PubMed:12810710}.
CC   -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB81053.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF426402; AAL25098.1; -; mRNA.
DR   EMBL; AF162444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161502; CAB81053.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82480.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67036.1; -; Genomic_DNA.
DR   PIR; C85064; C85064.
DR   RefSeq; NP_001328891.1; NM_001340533.1.
DR   RefSeq; NP_192420.2; NM_116750.4.
DR   AlphaFoldDB; Q944N8; -.
DR   SMR; Q944N8; -.
DR   BioGRID; 11167; 1.
DR   IntAct; Q944N8; 1.
DR   STRING; 3702.AT4G05110.1; -.
DR   iPTMnet; Q944N8; -.
DR   PaxDb; Q944N8; -.
DR   ProteomicsDB; 221899; -.
DR   EnsemblPlants; AT4G05110.1; AT4G05110.1; AT4G05110.
DR   EnsemblPlants; AT4G05110.3; AT4G05110.3; AT4G05110.
DR   GeneID; 825856; -.
DR   Gramene; AT4G05110.1; AT4G05110.1; AT4G05110.
DR   Gramene; AT4G05110.3; AT4G05110.3; AT4G05110.
DR   KEGG; ath:AT4G05110; -.
DR   Araport; AT4G05110; -.
DR   TAIR; locus:2115718; AT4G05110.
DR   eggNOG; KOG1479; Eukaryota.
DR   HOGENOM; CLU_021611_5_1_1; -.
DR   OMA; RIMHEDA; -.
DR   OrthoDB; 559763at2759; -.
DR   PhylomeDB; Q944N8; -.
DR   PRO; PR:Q944N8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q944N8; baseline and differential.
DR   Genevisible; Q944N8; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005337; F:nucleoside transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015858; P:nucleoside transport; IDA:UniProtKB.
DR   InterPro; IPR002259; Eqnu_transpt.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR10332; PTHR10332; 1.
DR   Pfam; PF01733; Nucleoside_tran; 1.
DR   PIRSF; PIRSF016379; ENT; 1.
DR   PRINTS; PR01130; DERENTRNSPRT.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..418
FT                   /note="Equilibrative nucleotide transporter 6"
FT                   /id="PRO_0000419159"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   418 AA;  46225 MW;  85BDC0CFBB512F1A CRC64;
     MADIYEHQVP EKLRGKYQAM IVYCILGFGS LISWNSMLTT ADYYYKVFPD YHPSRVLTLV
     YQPFAFGAIV ILAYHESKTS TRKRNLIGYI LYTISTFLLI VLDLATKGRG GFGPYTGLCA
     VVAAFGLADA TVQGGMFGDL SLMCPELVQS YMGGMAVAGA LTSALRLITK AAFEKSNNGL
     RKGAMMFLAI STCIELLSVM LYAYVLPKLP IVMYYRRKAA SQGSKTVSAD LAAAGIQNQS
     DLSDDDSKNQ RLSKKELLFQ NIDHAVNLFL IYVCTLSIFP GFLYENTGQH GLGAWYALVL
     VAMYNCWDLV GRYTPLVKWL NIENRKLITI AVLSRYLLIP AFYFTAKYGD QGWMIMLVSV
     LGLTNGHLTV CIMTIAPKGY KGPEQNALGN LLVIFLLGGI FAGVALDWLW LIGKKNAF
 
 
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