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PHOX3_ARATH
ID   PHOX3_ARATH             Reviewed;         809 AA.
AC   F4K487;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Protein PHOX3 {ECO:0000303|PubMed:20856808};
GN   Name=PHOX3 {ECO:0000303|PubMed:20856808};
GN   OrderedLocusNames=At5g20360 {ECO:0000312|Araport:AT5G20360};
GN   ORFNames=F5O24.250 {ECO:0000312|EMBL:AED92835.1};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [4]
RP   GENE FAMILY, NOMENCLATURE, FUNCTION, AND INDUCTION.
RX   PubMed=20856808; DOI=10.1371/journal.pone.0012761;
RA   Prasad B.D., Goel S., Krishna P.;
RT   "In silico identification of carboxylate clamp type tetratricopeptide
RT   repeat proteins in Arabidopsis and rice as putative co-chaperones of
RT   Hsp90/Hsp70.";
RL   PLoS ONE 5:E12761-E12761(2010).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28096376; DOI=10.1073/pnas.1620577114;
RA   Kurth E.G., Peremyslov V.V., Turner H.L., Makarova K.S., Iranzo J.,
RA   Mekhedov S.L., Koonin E.V., Dolja V.V.;
RT   "Myosin-driven transport network in plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:E1385-E1394(2017).
CC   -!- FUNCTION: Carboxylate clamp type tetratricopeptide repeat protein that
CC       may act as a potential Hsp90/Hsp70 co-chaperone (PubMed:20856808).
CC       Contributes to polar growth of root hairs (PubMed:28096376).
CC       {ECO:0000269|PubMed:28096376, ECO:0000305|PubMed:20856808}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. {ECO:0000305};
CC       Name=1;
CC         IsoId=F4K487-1; Sequence=Displayed;
CC   -!- INDUCTION: Up-regulated by abscisic acid treatment, and by cold and
CC       salt stress. {ECO:0000269|PubMed:20856808}.
CC   -!- DISRUPTION PHENOTYPE: Phox1, phox3 and phox4 triple mutants and phox1,
CC       phox2, phox3 and phox4 quadruple mutants show a 70% reduction in root
CC       hair growth (PubMed:28096376). {ECO:0000269|PubMed:28096376}.
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DR   EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92835.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM71141.1; -; Genomic_DNA.
DR   RefSeq; NP_001332690.1; NM_001343653.1. [F4K487-1]
DR   RefSeq; NP_197536.1; NM_122043.3. [F4K487-1]
DR   AlphaFoldDB; F4K487; -.
DR   SMR; F4K487; -.
DR   STRING; 3702.AT5G20360.1; -.
DR   iPTMnet; F4K487; -.
DR   PaxDb; F4K487; -.
DR   PRIDE; F4K487; -.
DR   ProteomicsDB; 234720; -. [F4K487-1]
DR   EnsemblPlants; AT5G20360.1; AT5G20360.1; AT5G20360. [F4K487-1]
DR   EnsemblPlants; AT5G20360.2; AT5G20360.2; AT5G20360. [F4K487-1]
DR   GeneID; 832158; -.
DR   Gramene; AT5G20360.1; AT5G20360.1; AT5G20360. [F4K487-1]
DR   Gramene; AT5G20360.2; AT5G20360.2; AT5G20360. [F4K487-1]
DR   KEGG; ath:AT5G20360; -.
DR   Araport; AT5G20360; -.
DR   TAIR; locus:2149174; AT5G20360.
DR   eggNOG; KOG4151; Eukaryota.
DR   HOGENOM; CLU_014258_0_0_1; -.
DR   InParanoid; F4K487; -.
DR   OrthoDB; 380896at2759; -.
DR   PhylomeDB; F4K487; -.
DR   PRO; PR:F4K487; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4K487; baseline and differential.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR044517; PHOX1-4.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR46183; PTHR46183; 1.
DR   Pfam; PF00564; PB1; 1.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS51745; PB1; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Reference proteome; Repeat;
KW   TPR repeat.
FT   CHAIN           1..809
FT                   /note="Protein PHOX3"
FT                   /id="PRO_0000440021"
FT   REPEAT          126..159
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00339"
FT   REPEAT          164..199
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          200..233
FT                   /note="TPR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REPEAT          235..265
FT                   /note="TPR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          274..311
FT                   /note="TPR 5"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          359..438
FT                   /note="PB1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT   REPEAT          508..541
FT                   /note="TPR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          563..597
FT                   /note="TPR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          615..648
FT                   /note="TPR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          709..741
FT                   /note="TPR 9"
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         298
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   809 AA;  91522 MW;  749615589D8126F5 CRC64;
     MEKQNEEIST DDAETSQSQL VDDSKVETLD DCVSKVETLD DCVSKVETLD DCVSKAETLA
     DCVSKVETLD DCVSKVKTLD DCVSKVENLD DCVPKVETLD DCVPKVETLD DCVSEVETLD
     DCVSKAQGLK EEGNKLFQKR DYDGAMFKYG EAIKILPKDH VEVSHVRANV ASCYMQLEPG
     EFAKAIHECD LALSVTPDHN KALLKRARCY EALNKLDLAL RDVCMVSKLD PKNPMASEIV
     EKLKRTLESK GLRINNSVIE LPPDYVEPVG ASPAALWAKL GKVRVKKTKK SNQVEEKSEG
     EGEDVEPEKK NNVLAEKGKE KIKMKVKGKQ SDKRSDTSKE QEKVIIEEEL LVIGVEDVNK
     DVKFVYSDDI RLAELPINCT LFKLREVVHE RFPSLRAVHI KYRDQEGDLV TITTDEELRM
     SEVSSRSQGT MRFYVVEVSP EQDPFFGRLV EMKKLKITAD SFKAKVNGRG GCKVEDWMIE
     FAHLFKIQAR IDSDRCLNLQ ELGMKLNSEA MEEVVTSDAA QGPFDRAAQQ FQEVAARSLL
     NLGYVHMSGA RKRLSLLQGV SGESVSEQVK TAYECAKKEH ANAKEKYEEA MKIKPECFEV
     FLALGLQQFE EARLSWYYVL VSHLDLKTWP YADVVQFYQS AESNIKKSME VLENLETGKE
     SEPSQAGKTD CLTHEKDLGS STQNNPAKEA GRLKSWIDIL LCAVLYERSI MEYKLDQPFW
     RESLEAAMEK FELAGTCKDD VVEIISEDYV AGNTLRDIRF HMEEIIQIFD EIYEAKHWTN
     GIPSDQLEEI LKRRAENIFH VPNIAIQRG
 
 
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