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UTR3_ARATH
ID   UTR3_ARATH              Reviewed;         331 AA.
AC   Q9M9S6; Q8L9F0; Q9FV57;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=UDP-galactose/UDP-glucose transporter 3 {ECO:0000303|PubMed:12042319};
DE            Short=AtUTr3 {ECO:0000303|PubMed:12042319};
GN   Name=UTR3 {ECO:0000303|PubMed:12042319};
GN   Synonyms=MSS4 {ECO:0000303|PubMed:10929106};
GN   OrderedLocusNames=At1g14360 {ECO:0000312|Araport:AT1G14360};
GN   ORFNames=F14L17.13 {ECO:0000312|EMBL:AAF43936.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 141-331, AND FUNCTION.
RX   PubMed=10929106; DOI=10.1046/j.1365-313x.2000.00809.x;
RA   Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.;
RT   "Functional identification of an Arabidopsis Snf4 ortholog by screening for
RT   heterologous multicopy suppressors of snf4 deficiency in yeast.";
RL   Plant J. 23:115-122(2000).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12042319; DOI=10.1074/jbc.m204081200;
RA   Norambuena L., Marchant L., Berninsone P., Hirschberg C.B., Silva H.,
RA   Orellana A.;
RT   "Transport of UDP-galactose in plants. Identification and functional
RT   characterization of AtUTr1, an Arabidopsis thaliana UDP-galactose/UDP-
RT   glucose transporter.";
RL   J. Biol. Chem. 277:32923-32929(2002).
RN   [7]
RP   GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=15456736; DOI=10.1093/glycob/cwh159;
RA   Bakker H., Routier F., Oelmann S., Jordi W., Lommen A., Gerardy-Schahn R.,
RA   Bosch D.;
RT   "Molecular cloning of two Arabidopsis UDP-galactose transporters by
RT   complementation of a deficient Chinese hamster ovary cell line.";
RL   Glycobiology 15:193-201(2005).
RN   [8]
RP   FUNCTION AS UDP-GLUCOSE TRANSPORTER, DISRUPTION PHENOTYPE, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. No-0;
RX   PubMed=19906043; DOI=10.1111/j.1365-313x.2009.04066.x;
RA   Reyes F., Leon G., Donoso M., Brandizzi F., Weber A.P., Orellana A.;
RT   "The nucleotide sugar transporters AtUTr1 and AtUTr3 are required for the
RT   incorporation of UDP-glucose into the endoplasmic reticulum, are essential
RT   for pollen development and are needed for embryo sac progress in
RT   Arabidopsis thaliana.";
RL   Plant J. 61:423-435(2010).
RN   [9]
RP   GENE FAMILY.
RX   PubMed=25053812; DOI=10.1073/pnas.1406073111;
RA   Rautengarten C., Ebert B., Moreno I., Temple H., Herter T., Link B.,
RA   Donas-Cofre D., Moreno A., Saez-Aguayo S., Blanco F., Mortimer J.C.,
RA   Schultink A., Reiter W.D., Dupree P., Pauly M., Heazlewood J.L.,
RA   Scheller H.V., Orellana A.;
RT   "The Golgi localized bifunctional UDP-rhamnose/UDP-galactose transporter
RT   family of Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:11563-11568(2014).
CC   -!- FUNCTION: Essential sugar transporter required for the transport of
CC       UDP-glucose from the cytoplasm into the Golgi and the endoplasmic
CC       reticulum. Essential for pollen development and involved in embryo sac
CC       progress. {ECO:0000269|PubMed:10929106, ECO:0000269|PubMed:19906043}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.4 uM for UDP-glucose {ECO:0000269|PubMed:19906043};
CC         Vmax=4.2 pmol/min/mg enzyme with UDP-glucose as substrate
CC         {ECO:0000269|PubMed:19906043};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:19906043}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:19906043}. Golgi apparatus membrane
CC       {ECO:0000269|PubMed:19906043}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:19906043}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in flowers, and, to a lower
CC       extent, in roots, stems and leaves. {ECO:0000269|PubMed:19906043}.
CC   -!- INDUCTION: Up-regulated by stimuli that trigger unfolded protein
CC       accumulation in the ER (UPR) (e.g. DTT or tunicamycin).
CC       {ECO:0000269|PubMed:19906043}.
CC   -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC       for type I membrane proteins. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000269|PubMed:19906043}.
CC   -!- MISCELLANEOUS: Suppressor of the Yeast snf4 mutation that is impaired
CC       in sugar trophism.
CC   -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. UDP-
CC       galactose:UMP antiporter (TC 2.A.7.11) subfamily. {ECO:0000305}.
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DR   EMBL; AC012188; AAF43936.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29152.1; -; Genomic_DNA.
DR   EMBL; AF332450; AAG48813.1; -; mRNA.
DR   EMBL; AY059942; AAL24424.1; -; mRNA.
DR   EMBL; AY114599; AAM47918.1; -; mRNA.
DR   EMBL; AY088469; AAM66005.1; -; mRNA.
DR   EMBL; AF250341; AAG10147.1; -; mRNA.
DR   PIR; A86278; A86278.
DR   RefSeq; NP_563949.1; NM_101303.4.
DR   AlphaFoldDB; Q9M9S6; -.
DR   BioGRID; 23238; 77.
DR   IntAct; Q9M9S6; 77.
DR   STRING; 3702.AT1G14360.1; -.
DR   PaxDb; Q9M9S6; -.
DR   PRIDE; Q9M9S6; -.
DR   ProteomicsDB; 228567; -.
DR   EnsemblPlants; AT1G14360.1; AT1G14360.1; AT1G14360.
DR   GeneID; 837998; -.
DR   Gramene; AT1G14360.1; AT1G14360.1; AT1G14360.
DR   KEGG; ath:AT1G14360; -.
DR   Araport; AT1G14360; -.
DR   TAIR; locus:2012482; AT1G14360.
DR   eggNOG; KOG1581; Eukaryota.
DR   HOGENOM; CLU_036019_0_1_1; -.
DR   InParanoid; Q9M9S6; -.
DR   OMA; VCSNMAL; -.
DR   OrthoDB; 1220063at2759; -.
DR   PhylomeDB; Q9M9S6; -.
DR   SABIO-RK; Q9M9S6; -.
DR   PRO; PR:Q9M9S6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9M9S6; baseline and differential.
DR   Genevisible; Q9M9S6; AT.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005459; F:UDP-galactose transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005460; F:UDP-glucose transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0009553; P:embryo sac development; IMP:UniProtKB.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEP:UniProtKB.
DR   GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR   GO; GO:0072334; P:UDP-galactose transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR013657; UAA.
DR   PANTHER; PTHR10778; PTHR10778; 1.
DR   Pfam; PF08449; UAA; 1.
PE   1: Evidence at protein level;
KW   Antiport; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW   Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..331
FT                   /note="UDP-galactose/UDP-glucose transporter 3"
FT                   /id="PRO_0000415962"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           327..331
FT                   /note="Di-lysine motif"
FT   CONFLICT        158
FT                   /note="S -> I (in Ref. 4; AAM66005)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323..325
FT                   /note="QRM -> L (in Ref. 4; AAM66005)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   331 AA;  36717 MW;  45ADF9D1506C8EF2 CRC64;
     MESHGSGLRR VLLLSFCVAG IWAAYIYQGI LQETLSTKKF GEDGKRFEHL AFLNLAQNVI
     CLVWSYIMIK LWSNGGSGGA PWWTYWSAGI TNTIGPAMGI EALKYISYPA QVLAKSSKMI
     PVMLMGSLVY GIRYTLPEYL CTFLVAGGVS MFALLKTSSK TISKLAHPNA PLGYGLCFLN
     LAFDGFTNAT QDSITARYPK TNAWDIMLGM NLWGTIYNMV YMFGLPHGSG FEAVQFCKQH
     PEAAWDILMY CLCGAVGQNF IFLTISRFGS LANTTITTTR KFVSIVVSSV LSGNPLSSKQ
     WGCVSMVFGG LSYQIYLKWR KLQRMQKKKK A
 
 
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