PHOX1_ARATH
ID PHOX1_ARATH Reviewed; 745 AA.
AC F4IRM4; Q9SIR4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Protein PHOX1 {ECO:0000303|PubMed:20856808};
DE AltName: Full=Protein MADB1 {ECO:0000303|PubMed:28096376};
DE AltName: Full=Putative myosin adapter B1 {ECO:0000303|PubMed:28096376};
GN Name=PHOX1 {ECO:0000303|PubMed:20856808};
GN Synonyms=MADB1 {ECO:0000303|PubMed:28096376};
GN OrderedLocusNames=At2g25290 {ECO:0000312|Araport:AT2G25290};
GN ORFNames=T22F11.12 {ECO:0000312|EMBL:AEC07680.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 GENE FAMILY, NOMENCLATURE, AND FUNCTION.
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 [4]
RP DISRUPTION PHENOTYPE.
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH XI-1 AND XI-K, AND
RP 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 -!- SUBUNIT: Interacts with myosin XI-1 and XI-K.
CC {ECO:0000269|PubMed:28096376}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:28096376}; Peripheral membrane protein
CC {ECO:0000269|PubMed:28096376}.
CC -!- DISRUPTION PHENOTYPE: No clumped-chloroplasts phenotype
CC (PubMed:22025705). 31% reduction in root hair growth (PubMed:28096376).
CC Phox1 and phox4 double mutants show no clumped-chloroplasts phenotype,
CC but a 46% reduction in root hair growth (PubMed:22025705,
CC PubMed:28096376). 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:22025705,
CC ECO:0000269|PubMed:28096376}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD23662.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007070; AAD23662.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07680.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07681.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07682.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61435.1; -; Genomic_DNA.
DR PIR; F84646; F84646.
DR RefSeq; NP_001154534.1; NM_001161062.2.
DR RefSeq; NP_001189599.1; NM_001202670.1.
DR RefSeq; NP_001323652.1; NM_001335984.1.
DR RefSeq; NP_180101.4; NM_128086.6.
DR AlphaFoldDB; F4IRM4; -.
DR SMR; F4IRM4; -.
DR STRING; 3702.AT2G25290.2; -.
DR iPTMnet; F4IRM4; -.
DR PaxDb; F4IRM4; -.
DR PRIDE; F4IRM4; -.
DR ProteomicsDB; 235107; -.
DR EnsemblPlants; AT2G25290.1; AT2G25290.1; AT2G25290.
DR EnsemblPlants; AT2G25290.2; AT2G25290.2; AT2G25290.
DR EnsemblPlants; AT2G25290.3; AT2G25290.3; AT2G25290.
DR EnsemblPlants; AT2G25290.4; AT2G25290.4; AT2G25290.
DR GeneID; 817067; -.
DR Gramene; AT2G25290.1; AT2G25290.1; AT2G25290.
DR Gramene; AT2G25290.2; AT2G25290.2; AT2G25290.
DR Gramene; AT2G25290.3; AT2G25290.3; AT2G25290.
DR Gramene; AT2G25290.4; AT2G25290.4; AT2G25290.
DR KEGG; ath:AT2G25290; -.
DR Araport; AT2G25290; -.
DR TAIR; locus:2059546; AT2G25290.
DR eggNOG; KOG4151; Eukaryota.
DR HOGENOM; CLU_014258_0_0_1; -.
DR InParanoid; F4IRM4; -.
DR OMA; EHAKLSW; -.
DR OrthoDB; 260600at2759; -.
DR PRO; PR:F4IRM4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IRM4; baseline and differential.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0080115; F:myosin XI tail binding; IDA:TAIR.
DR Gene3D; 1.25.40.10; -; 2.
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; 3.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Membrane; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..745
FT /note="Protein PHOX1"
FT /id="PRO_0000440019"
FT REPEAT 52..85
FT /note="TPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 90..125
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 126..159
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT DOMAIN 280..359
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REPEAT 406..441
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 443..472
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 494..528
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 553..586
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 84222 MW; A7E7C9FF79797286 CRC64;
MGKPTGKKKN NNYTEMPPTE SSTTGGGKTG KSFDRSATKS FDDDMTIFIN RALELKEEGN
KLFQKRDYEG AMFRYDKAVK LLPRDHGDVA YLRTSMASCY MQMGLGEYPN AINECNLALE
ASPRFSKALL KRARCYEALN KLDFAFRDSR VVLNMEPENV SANEIFERVK KVLVGKGIDV
DEMEKNLVNV QPVGAARLRK IVKERLRKKK KKSMTMTNGG NDGERKSVEA VVEDAKVDNG
EEVDSGRKGK AIEEKKLEDK VAVMDKEVIA SEIKEDATVT RTVKLVHGDD IRWAQLPLDS
SVVLVRDVIK DRFPALKGFL IKYRDSEGDL VTITTTDELR LAASTREKLG SFRLYIAEVS
PNQEPTYDVI DNDESTDKFA KGSSSVADNG SVGDFVESEK ASTSLEHWIF QFAQLFKNHV
GFDSDSYLEL HNLGMKLYTE AMEDIVTGED AQELFDIAAD KFQEMAALAM FNWGNVHMSK
ARRQIYFPED GSRETILEKV EAGFEWAKNE YNKAAEKYEG AVKIKSDFYE ALLALGQQQF
EQAKLCWYHA LSGEVDIESD ASQDVLKLYN KAEESMEKGM QIWEEMEERR LNGISNFDKH
KELLQKLGLD GIFSEASDEE SAEQTANMSS QINLLWGSLL YERSIVEYKL GLPTWDECLE
VAVEKFELAG ASATDIAVMV KNHCSSDNAL EGMGFKIDEI VQAWNEMYDA KRWQIGVPSF
RLEPLFRRRS PKLHDILENV FSGPQ
