PHOX2_ARATH
ID PHOX2_ARATH Reviewed; 751 AA.
AC O48802; Q8RWK1;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Protein CLMP1 {ECO:0000303|PubMed:22025705};
DE AltName: Full=CLUMPED CHLOROPLASTS 1 {ECO:0000303|PubMed:22025705};
DE AltName: Full=Protein MADB2 {ECO:0000303|PubMed:28096376};
DE AltName: Full=Protein PHOX2 {ECO:0000303|PubMed:20856808};
DE AltName: Full=Putative myosin adapter B2 {ECO:0000303|PubMed:28096376};
GN Name=CLMP1 {ECO:0000303|PubMed:22025705};
GN Synonyms=MADB2 {ECO:0000303|PubMed:28096376},
GN PHOX2 {ECO:0000303|PubMed:20856808};
GN OrderedLocusNames=At1g62390 {ECO:0000312|Araport:AT1G62390};
GN ORFNames=F2401.12 {ECO:0000312|EMBL:AAF70848.1};
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [5]
RP IDENTIFICATION BY 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 [6]
RP GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION BY HEAT.
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=22025705; DOI=10.1073/pnas.1106706108;
RA Yang Y., Sage T.L., Liu Y., Ahmad T.R., Marshall W.F., Shiu S.H.,
RA Froehlich J.E., Imre K.M., Osteryoung K.W.;
RT "CLUMPED CHLOROPLASTS 1 is required for plastid separation in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18530-18535(2011).
RN [8]
RP FUNCTION, INTERACTION WITH XI-K, 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: Required for plastid separation and partitioning during cell
CC division (PubMed:22025705). Not involved in plastid constriction or in
CC the organization of cytoplasmic actin cables (PubMed:22025705).
CC Contributes to polar growth of root hairs (PubMed:28096376).
CC {ECO:0000269|PubMed:22025705, ECO:0000269|PubMed:28096376}.
CC -!- SUBUNIT: Interacts with myosin XI-K. {ECO:0000269|PubMed:28096376}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22025705}.
CC Note=Localized to distinct foci in the cytoplasm, which frequently
CC colocalize with the cell periphery and with chloroplasts.
CC {ECO:0000269|PubMed:22025705}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, apex, flowers
CC and seeds (PubMed:20856808). Detected throughout the petiole in
CC juvenile and young leaves, but restricted to the petiole midvein in
CC older leaves (PubMed:22025705). Expressed in hydathodes, at the base of
CC the trichome, in the vascular cylinder of primary root and lateral
CC root, in emerging lateral root primordia, in pollen and in developing
CC embryos, but not in mature embryos (PubMed:22025705).
CC {ECO:0000269|PubMed:20856808, ECO:0000269|PubMed:22025705}.
CC -!- INDUCTION: Up-regulated by heat. {ECO:0000269|PubMed:20856808}.
CC -!- DISRUPTION PHENOTYPE: Normal constriction of plastids during division,
CC but impaired separation, resulting in plastid clustering. The clumped-
CC chloroplasts mutant phenotype is transient. In juvenile leaves,
CC clustered chloroplasts are observed in almost all cells of the petiole,
CC while in the oldest leaf, the phenotype is mostly absent
CC (PubMed:22025705). Phox1, phox2, phox3 and phox4 quadruple mutants show
CC a 70% reduction in root hair growth (PubMed:28096376).
CC {ECO:0000269|PubMed:22025705, ECO:0000269|PubMed:28096376}.
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DR EMBL; AC003113; AAF70848.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33961.1; -; Genomic_DNA.
DR EMBL; AY080782; AAL87265.1; -; mRNA.
DR EMBL; AY113996; AAM45044.1; -; mRNA.
DR EMBL; AY093038; AAM13037.1; -; mRNA.
DR PIR; T01449; T01449.
DR RefSeq; NP_564794.1; NM_104919.4.
DR AlphaFoldDB; O48802; -.
DR SMR; O48802; -.
DR IntAct; O48802; 1.
DR STRING; 3702.AT1G62390.1; -.
DR iPTMnet; O48802; -.
DR PaxDb; O48802; -.
DR PRIDE; O48802; -.
DR ProteomicsDB; 235108; -.
DR EnsemblPlants; AT1G62390.1; AT1G62390.1; AT1G62390.
DR GeneID; 842537; -.
DR Gramene; AT1G62390.1; AT1G62390.1; AT1G62390.
DR KEGG; ath:AT1G62390; -.
DR Araport; AT1G62390; -.
DR TAIR; locus:2027104; AT1G62390.
DR eggNOG; KOG4151; Eukaryota.
DR HOGENOM; CLU_014258_1_0_1; -.
DR InParanoid; O48802; -.
DR OMA; CLPARPM; -.
DR OrthoDB; 380896at2759; -.
DR PhylomeDB; O48802; -.
DR PRO; PR:O48802; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O48802; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
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; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..751
FT /note="Protein CLMP1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000440020"
FT REPEAT 51..84
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 89..124
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 125..158
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT DOMAIN 290..382
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REPEAT 434..468
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 481..514
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 536..570
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..402
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 82708 MW; 6131B59B632DD90B CRC64;
MGKSGGRKKK SGGSNSNSSQ VNSSETSGLS KPSTIVNGGV DFDASIFLKR AHELKEEGNK
KFQARDYVGA LEQYENGIKL IPKSHPDRAV FHSNRAACLM QMKPIDYESV ISECSMALKS
QPGFTRALLR RARAFEAVGK FDLAVQDVNV LLGSDPNHKD AGEISKRLKT ALGPHQDLQS
RPSPAALGAS AALGGPIAGL GPCLPSRNVH KKGVTSPVGS VSLPNASNGK VERPQVVNPV
TENGGSVSKG QASRVVLKPV SHSPKGSKVE ELGSSSVAVV GKVQEKRIRW RPLKFVYDHD
IRLGQMPVNC RFKELREIVS SRFPSSKAVL IKYKDNDGDL VTITSTAELK LAESAADCIL
TKEPDTDKSD SVGMLRLHVV DVSPEQEPML LEEEEEEVEE KPVIEEVISS PTESLSETEI
NTEKTDKEVE KEKASSSEDP ETKELEMDDW LFDFAHLFRT HVGIDPDAHI DLHELGMELC
SEALEETVTS EKAQPLFDKA SAKFQEVAAL AFFNWGNVHM CAARKRIPLD ESAGKEVVAA
QLQTAYEWVK ERYTLAKEKY EQALSIKPDF YEGLLALGQQ QFEMAKLHWS YLLAQKIDIS
GWDPSETLNL FDSAEAKMKD ATEMWEKLEE QRMDDLKNPN SNKKEEVSKR RKKQGGDGNE
EVSETITAEE AAEQATAMRS QIHLFWGNML FERSQVECKI GKDGWNKNLD SAVERFKLAG
ASEADIATVV KNHCSNEAAA TEGDEKKVPA P
