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ANTR2_ARATH
ID   ANTR2_ARATH             Reviewed;         541 AA.
AC   Q8GX78; O23065;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Ascorbate transporter, chloroplastic {ECO:0000303|PubMed:25557369};
DE   AltName: Full=Phosphate transporter PHT4;4;
DE            Short=AtPHT4;4;
DE   AltName: Full=Probable anion transporter 2;
DE   Flags: Precursor;
GN   Name=PHT4;4; Synonyms=ANTR2; OrderedLocusNames=At4g00370;
GN   ORFNames=A_IG005I10_nn, F5I10.7;
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=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   [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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
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   [5]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY,
RP   AND NOMENCLATURE.
RX   PubMed=14564522; DOI=10.1007/s00425-003-1121-5;
RA   Roth C., Menzel G., Petetot J.M., Rochat-Hacker S., Poirier Y.;
RT   "Characterization of a protein of the plastid inner envelope having
RT   homology to animal inorganic phosphate, chloride and organic-anion
RT   transporters.";
RL   Planta 218:406-416(2004).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18353780; DOI=10.1074/jbc.m709371200;
RA   Pavon L.R., Lundh F., Lundin B., Mishra A., Persson B.L., Spetea C.;
RT   "Arabidopsis ANTR1 is a thylakoid Na+-dependent phosphate transporter:
RT   functional characterization in Escherichia coli.";
RL   J. Biol. Chem. 283:13520-13527(2008).
RN   [7]
RP   FUNCTION.
RX   PubMed=18086223; DOI=10.1111/j.1469-8137.2007.02331.x;
RA   Guo B., Jin Y., Wussler C., Blancaflor E.B., Motes C.M., Versaw W.K.;
RT   "Functional analysis of the Arabidopsis PHT4 family of intracellular
RT   phosphate transporters.";
RL   New Phytol. 177:889-898(2008).
RN   [8]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=19513231; DOI=10.4161/psb.3.10.6666;
RA   Guo B., Irigoyen S., Fowler T.B., Versaw W.K.;
RT   "Differential expression and phylogenetic analysis suggest specialization
RT   of plastid-localized members of the PHT4 phosphate transporter family for
RT   photosynthetic and heterotrophic tissues.";
RL   Plant Signal. Behav. 3:784-790(2008).
RN   [9]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, TISSUE
RP   SPECIFICITY, INDUCTION BY LIGHT, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=25557369; DOI=10.1038/ncomms6928;
RA   Miyaji T., Kuromori T., Takeuchi Y., Yamaji N., Yokosho K., Shimazawa A.,
RA   Sugimoto E., Omote H., Ma J.F., Shinozaki K., Moriyama Y.;
RT   "AtPHT4;4 is a chloroplast-localized ascorbate transporter in
RT   Arabidopsis.";
RL   Nat. Commun. 6:5928-5928(2015).
CC   -!- FUNCTION: Inorganic phosphate and probable anion transporter
CC       (PubMed:18086223). Ascorbate transporter bridging the chloroplast
CC       envelope. Transports ascorbate from the cytosol into the chloroplast.
CC       Requires chloride ions and the presence of an electrochemical potential
CC       across the membrane for activity (PubMed:25557369).
CC       {ECO:0000269|PubMed:18086223, ECO:0000269|PubMed:25557369}.
CC   -!- ACTIVITY REGULATION: Insensitive to dehydroascorbate, p-isoascorbate,
CC       inorganic phosphate, glutamate, ATP, p-aminohippuric acid or
CC       tetraethylammonium. {ECO:0000269|PubMed:25557369}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.2 mM for ascorbate {ECO:0000269|PubMed:25557369};
CC         Vmax=520 nmol/min/mg enzyme {ECO:0000269|PubMed:25557369};
CC         Note=Ascorbate uptake shows an absolute requirement for Cl(-).
CC         {ECO:0000269|PubMed:25557369};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC       {ECO:0000269|PubMed:14564522, ECO:0000269|PubMed:18353780,
CC       ECO:0000269|PubMed:25557369}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14564522, ECO:0000269|PubMed:18353780}.
CC   -!- TISSUE SPECIFICITY: Expressed in stems, developing siliques, leaf
CC       mesophyll cells and sepals of mature flowers. Not detected in roots.
CC       Detected in palisade tissue rather than spongy tissue from the leaves
CC       (PubMed:25557369). {ECO:0000269|PubMed:14564522,
CC       ECO:0000269|PubMed:19513231, ECO:0000269|PubMed:25557369}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing embryo at the
CC       upturned-U stage. {ECO:0000269|PubMed:14564522}.
CC   -!- INDUCTION: Expressed with a circadian rhythm showing a peak during the
CC       middle of the day (under long day conditions) (PubMed:19513231). Up-
CC       regulated by light (PubMed:25557369). {ECO:0000269|PubMed:19513231,
CC       ECO:0000269|PubMed:25557369}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, but decreased reduced
CC       ascorbate content in leaves and decreased xanthophyll cycle for heat
CC       dissipation of excessive energy in photosynthesis.
CC       {ECO:0000269|PubMed:25557369}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC       cotransporter (TC 2.A.1.14) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB62846.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF02804.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80795.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF013293; AAB62846.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF195115; AAF02804.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161471; CAB80795.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE81870.1; -; Genomic_DNA.
DR   EMBL; AK118390; BAC43000.1; -; mRNA.
DR   EMBL; BT009663; AAP78931.1; -; mRNA.
DR   PIR; T01534; T01534.
DR   RefSeq; NP_567175.2; NM_116261.4.
DR   AlphaFoldDB; Q8GX78; -.
DR   SMR; Q8GX78; -.
DR   BioGRID; 13199; 4.
DR   IntAct; Q8GX78; 5.
DR   STRING; 3702.AT4G00370.1; -.
DR   TCDB; 2.A.1.14.45; the major facilitator superfamily (mfs).
DR   PaxDb; Q8GX78; -.
DR   PRIDE; Q8GX78; -.
DR   ProteomicsDB; 244469; -.
DR   EnsemblPlants; AT4G00370.1; AT4G00370.1; AT4G00370.
DR   GeneID; 827908; -.
DR   Gramene; AT4G00370.1; AT4G00370.1; AT4G00370.
DR   KEGG; ath:AT4G00370; -.
DR   Araport; AT4G00370; -.
DR   TAIR; locus:2126066; AT4G00370.
DR   eggNOG; KOG2532; Eukaryota.
DR   HOGENOM; CLU_001265_5_11_1; -.
DR   InParanoid; Q8GX78; -.
DR   OMA; LDRFCSK; -.
DR   OrthoDB; 497052at2759; -.
DR   PhylomeDB; Q8GX78; -.
DR   PRO; PR:Q8GX78; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8GX78; baseline and differential.
DR   Genevisible; Q8GX78; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0009706; C:chloroplast inner membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; IDA:TAIR.
DR   GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0015229; F:L-ascorbic acid transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0015882; P:L-ascorbic acid transmembrane transport; IDA:TAIR.
DR   GO; GO:0010028; P:xanthophyll cycle; IMP:TAIR.
DR   CDD; cd17380; MFS_SLC17A9_like; 1.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR044777; SLC17A9-like.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Membrane; Plastid; Plastid inner membrane; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..28
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..541
FT                   /note="Ascorbate transporter, chloroplastic"
FT                   /id="PRO_0000331535"
FT   TRANSMEM        133..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        430..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        481..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        515..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   541 AA;  59614 MW;  26BA44B8649FA351 CRC64;
     MALGGLISNR NFGSFIGSGN GCQRLGKSGA EVSKLFPNAL LCRNHQPLQA SLHHESGHMR
     RSFGCFLQPR MDSVIRFRNS IKINRSRAYY KSEESDITEG VVPSADGSAE AILVEGNLQN
     ASPWWQQFPR RWVIVLLCFS SFLLCNMDRV NMSIAILPMS QEYNWSSATV GLIQSSFFWG
     YLLTQILGGI WADKFGGKVV LGFGVVWWSF ATIMTPIAAR LGLPFLLVVR AFMGIGEGVA
     MPAMNNMLSK WIPVSERSRS LALVYSGMYL GSVTGLAFSP MLITKFGWPS VFYSFGSLGS
     IWFLLWLKFA YSSPKDDPDL SEEEKKVILG GSKPREPVTV IPWKLILSKP PVWALIISHF
     CHNWGTFILL TWMPTYYNQV LKFNLTESGL LCVLPWLTMA VFANIGGWIA DTLVSRGLSI
     TNVRKIMQSI GFLGPAFFLS QLSHVKTPAM AVLCMACSQG SDAFSQSGLY SNHQDIGPRY
     AGVLLGLSNT AGVLAGVFGT AATGYILQRG SWDDVFKVAV ALYLIGTLVW NLFATGEKIL
     D
 
 
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