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ENT4_ARATH
ID   ENT4_ARATH              Reviewed;         418 AA.
AC   Q9M0Y2;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Equilibrative nucleotide transporter 4;
DE            Short=AtENT4;
DE   AltName: Full=Nucleoside transporter ENT4;
GN   Name=ENT4; OrderedLocusNames=At4g05130; ORFNames=C17L7.50, 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, AND BIOPHYSICOCHEMICAL PROPERTIES.
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=49.1 uM for adenosine {ECO:0000269|PubMed:15228386};
CC         KM=27.8 uM for uridine {ECO:0000269|PubMed:15228386};
CC         KM=7.3 uM for guanosine {ECO:0000269|PubMed:15228386};
CC         KM=94.2 uM for cytidine {ECO:0000269|PubMed:15228386};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000305}. Note=Plasma membrane.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and at lowe levels in stems and
CC       flowers. {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}.
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DR   EMBL; AF426401; AAL25097.1; -; mRNA.
DR   EMBL; AF162444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161502; CAB81055.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82482.1; -; Genomic_DNA.
DR   PIR; E85064; E85064.
DR   RefSeq; NP_192422.1; NM_116752.2.
DR   AlphaFoldDB; Q9M0Y2; -.
DR   SMR; Q9M0Y2; -.
DR   STRING; 3702.AT4G05130.1; -.
DR   PaxDb; Q9M0Y2; -.
DR   PRIDE; Q9M0Y2; -.
DR   EnsemblPlants; AT4G05130.1; AT4G05130.1; AT4G05130.
DR   GeneID; 825858; -.
DR   Gramene; AT4G05130.1; AT4G05130.1; AT4G05130.
DR   KEGG; ath:AT4G05130; -.
DR   Araport; AT4G05130; -.
DR   TAIR; locus:2115753; AT4G05130.
DR   eggNOG; KOG1479; Eukaryota.
DR   HOGENOM; CLU_021611_5_1_1; -.
DR   OMA; CGNLVGR; -.
DR   OrthoDB; 674800at2759; -.
DR   PhylomeDB; Q9M0Y2; -.
DR   PRO; PR:Q9M0Y2; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9M0Y2; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 4"
FT                   /id="PRO_0000419157"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..169
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;  46294 MW;  DBC6BF090A18752D CRC64;
     MADGYENHAP ENLQGKYQAM VVCCILGIGS LFSWNSMLTI ADYYYQVFPD YHPSRVFTLI
     YQPIALGTIM ILAYRESKIS TRKRILTGYI LFTISTFLLI VLDLTTKGHG GIGHYIVLCT
     IVASFGLADA TVKGGLVGDL SLMCPELIQS YMAGSGMAGA LTSVLRLITK AAFEKSNNSL
     RKGAMIFLAI STFIELLCVI LYAYVFPKLP IVKYYRRKAA SEGSKTVVAD LAAAGIQNLS
     DLSDDDSKNQ MLRKKELLLQ NIDHAVNLFL IYVLTLSIFP GFLYENTGQH GLGDWYALIL
     VATYNFWDLF GRYAPLVKWL KLENRKALTI AVLTRYFLVP AFYFTAKYGD KGWMIMLVSI
     LGLTTGHLTV CIMTIAPNGY KGPEKNALGN LLVVFILGGA VVGISLGWLW LIGKKYAF
 
 
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