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S29A3_MOUSE
ID   S29A3_MOUSE             Reviewed;         475 AA.
AC   Q99P65; B2RQD3;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Equilibrative nucleoside transporter 3;
DE            Short=mENT3;
DE   AltName: Full=Solute carrier family 29 member 3;
GN   Name=Slc29a3; Synonyms=Ent3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=11396612; DOI=10.1080/09687680118799;
RA   Hyde R.J., Cass C.E., Young J.D., Baldwin S.A.;
RT   "The ENT family of eukaryote nucleoside and nucleobase transporters: recent
RT   advances in the investigation of structure/function relationships and the
RT   identification of novel isoforms.";
RL   Mol. Membr. Biol. 18:53-63(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Mediates both influx and efflux of nucleosides across the
CC       membrane (equilibrative transporter). Mediates transport of adenine,
CC       adenosine and uridine (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Late
CC       endosome membrane. Lysosome membrane. Note=Intracellular localization
CC       shows a partial overlap with late endosomes/lysosomes. Not detected at
CC       the cell surface (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC       {ECO:0000305}.
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DR   EMBL; AF326986; AAK00957.1; -; mRNA.
DR   EMBL; AK034133; BAC28600.1; -; mRNA.
DR   EMBL; CH466553; EDL32166.1; -; Genomic_DNA.
DR   EMBL; BC137864; AAI37865.1; -; mRNA.
DR   CCDS; CCDS48571.1; -.
DR   RefSeq; NP_076085.1; NM_023596.3.
DR   AlphaFoldDB; Q99P65; -.
DR   SMR; Q99P65; -.
DR   STRING; 10090.ENSMUSP00000112685; -.
DR   GlyGen; Q99P65; 1 site.
DR   iPTMnet; Q99P65; -.
DR   PhosphoSitePlus; Q99P65; -.
DR   EPD; Q99P65; -.
DR   MaxQB; Q99P65; -.
DR   PaxDb; Q99P65; -.
DR   PeptideAtlas; Q99P65; -.
DR   PRIDE; Q99P65; -.
DR   ProteomicsDB; 260902; -.
DR   Antibodypedia; 68472; 107 antibodies from 19 providers.
DR   DNASU; 71279; -.
DR   Ensembl; ENSMUST00000117513; ENSMUSP00000112685; ENSMUSG00000020100.
DR   GeneID; 71279; -.
DR   KEGG; mmu:71279; -.
DR   UCSC; uc007ffb.1; mouse.
DR   CTD; 55315; -.
DR   MGI; MGI:1918529; Slc29a3.
DR   VEuPathDB; HostDB:ENSMUSG00000020100; -.
DR   eggNOG; KOG1479; Eukaryota.
DR   GeneTree; ENSGT00950000182898; -.
DR   HOGENOM; CLU_021611_6_1_1; -.
DR   InParanoid; Q99P65; -.
DR   OMA; FWNLGDL; -.
DR   OrthoDB; 559763at2759; -.
DR   PhylomeDB; Q99P65; -.
DR   TreeFam; TF313950; -.
DR   Reactome; R-MMU-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR   BioGRID-ORCS; 71279; 3 hits in 73 CRISPR screens.
DR   PRO; PR:Q99P65; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q99P65; protein.
DR   Bgee; ENSMUSG00000020100; Expressed in right kidney and 210 other tissues.
DR   ExpressionAtlas; Q99P65; baseline and differential.
DR   Genevisible; Q99P65; MM.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005337; F:nucleoside transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015858; P:nucleoside transport; ISO:MGI.
DR   InterPro; IPR030193; ENT3.
DR   InterPro; IPR002259; Eqnu_transpt.
DR   PANTHER; PTHR10332; PTHR10332; 1.
DR   PANTHER; PTHR10332:SF17; PTHR10332:SF17; 1.
DR   Pfam; PF01733; Nucleoside_tran; 1.
DR   PIRSF; PIRSF016379; ENT; 1.
DR   PRINTS; PR01130; DERENTRNSPRT.
PE   1: Evidence at protein level;
KW   Endosome; Glycoprotein; Lysosome; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..475
FT                   /note="Equilibrative nucleoside transporter 3"
FT                   /id="PRO_0000209344"
FT   TOPO_DOM        1..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..134
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..162
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..199
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        221..230
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..305
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..340
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        341..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        362..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        399..415
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        437..450
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        472..475
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   475 AA;  51719 MW;  F593D5D03C6CBB52 CRC64;
     MAFASEDNVY HSSNAVYRAP SNHQEADQEA LLGKLLDYPA PGLQRPEDRF NGAYIIFFCL
     GIGGLLPWNF FVTAKEYWAY KLRNCSSPAS GEDPEDMDIL NYFESYLAVA STVPSLLFLV
     ANFLLVNRVQ VHVRVLASLS VSLAIFVVMI VLVKVDTSSW TRGFFSLTIA CMAIISSSST
     IFNSSVYGLT GSFPMRNAQA LISGGAMGGT VSAVALLVDL AASSDVRDST LAFFLMAAVF
     LGLCMGLYLL LSQLEYARYY MRPVAPVRVF SGEDNPSQDA PSASSVAPAS RVMHTPPLGP
     ILKKTASLGF CAVSLYFVTA FIIPAISTNI QSMHKGTGSP WTSKFFVPLT VFLLFNFADL
     CGRQVTAWIQ VPGPRSKLLP GLVVSRFCLV PLFLLCNYQP RSHLTKVLFQ SDIYPVLFTC
     LLGLSNGYLS TLVLIYGPKI VPRELAEATS VVMLFYMSVG LMLGSACAAL LEHFI
 
 
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