CHUP1_ARATH
ID CHUP1_ARATH Reviewed; 1004 AA.
AC Q9LI74; A0A1I9LT47;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Protein CHUP1, chloroplastic;
DE AltName: Full=Protein CHLOROPLAST UNUSUAL POSITIONING 1;
GN Name=CHUP1; OrderedLocusNames=At3g25690; ORFNames=T5M7.14;
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 [MRNA], AND FUNCTION.
RX PubMed=12490952; DOI=10.1038/nature01213;
RA Kasahara M., Kagawa T., Oikawa K., Suetsugu N., Miyao M., Wada M.;
RT "Chloroplast avoidance movement reduces photodamage in plants.";
RL Nature 420:829-832(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=14615600; DOI=10.1105/tpc.016428;
RA Oikawa K., Kasahara M., Kiyosue T., Kagawa T., Suetsugu N., Takahashi F.,
RA Kanegae T., Niwa Y., Kadota A., Wada M.;
RT "Chloroplast unusual positioning1 is essential for proper chloroplast
RT positioning.";
RL Plant Cell 15:2805-2815(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18193273; DOI=10.1007/s00425-007-0688-7;
RA Schmidt von Braun S., Schleiff E.;
RT "The chloroplast outer membrane protein CHUP1 interacts with actin and
RT profilin.";
RL Planta 227:1151-1159(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-4; SER-12 AND
RP ARG-20.
RX PubMed=18715957; DOI=10.1104/pp.108.123075;
RA Oikawa K., Yamasato A., Kong S.-G., Kasahara M., Nakai M., Takahashi F.,
RA Ogura Y., Kagawa T., Wada M.;
RT "Chloroplast outer envelope protein CHUP1 is essential for chloroplast
RT anchorage to the plasma membrane and chloroplast movement.";
RL Plant Physiol. 148:829-842(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, 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).
CC -!- FUNCTION: Required for the positioning and movement of chloroplasts.
CC Interacts with profilin and actin independent of its polymerization
CC status. Regulates chloroplast localization by anchoring chloroplasts to
CC the plasma membrane and forming a bridge to the actin cytoskeleton.
CC {ECO:0000269|PubMed:12490952, ECO:0000269|PubMed:14615600,
CC ECO:0000269|PubMed:18193273, ECO:0000269|PubMed:18715957}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:14615600, ECO:0000269|PubMed:18193273,
CC ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:18715957}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14615600,
CC ECO:0000269|PubMed:18193273, ECO:0000269|PubMed:18431481,
CC ECO:0000269|PubMed:18715957}; Cytoplasmic side
CC {ECO:0000269|PubMed:14615600, ECO:0000269|PubMed:18193273,
CC ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:18715957}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LI74-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in cauline leaves, rosette leaves, stems
CC and flowers, but not in roots. {ECO:0000269|PubMed:14615600}.
CC -!- DOMAIN: The N-terminal region (1-25) is necessary and sufficient for
CC targeting and anchoring the protein in the chloroplast envelope
CC membrane.
CC -!- DOMAIN: The coiled coil domain(123-341) interacts with the plasma
CC membrane and anchors chloroplasts firmly on the plasma membrane.
CC -!- DOMAIN: The actin binding motif (346-356) can function in vitro as an
CC actin binding site.
CC -!- DOMAIN: The proline-rich domain (648-705) mediates the interaction with
CC profilin.
CC -!- DISRUPTION PHENOTYPE: Defective in chloroplast photorelocation
CC movement, leading to damage of the photosynthetic apparatus and
CC subsequent bleaching of leaf color and necrosis under high light
CC conditions. Chloroplasts gathered at the bottom of cells, regardless of
CC the light conditions. {ECO:0000269|PubMed:14615600}.
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DR EMBL; AB087408; BAC55960.1; -; mRNA.
DR EMBL; AP001313; BAB03089.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77051.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77052.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65754.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65755.1; -; Genomic_DNA.
DR RefSeq; NP_001189974.1; NM_001203045.1. [Q9LI74-1]
DR RefSeq; NP_001327701.1; NM_001338763.1. [Q9LI74-1]
DR RefSeq; NP_001327702.1; NM_001338761.1. [Q9LI74-1]
DR RefSeq; NP_189197.2; NM_113468.5. [Q9LI74-1]
DR AlphaFoldDB; Q9LI74; -.
DR SMR; Q9LI74; -.
DR BioGRID; 7488; 1.
DR STRING; 3702.AT3G25690.2; -.
DR iPTMnet; Q9LI74; -.
DR PaxDb; Q9LI74; -.
DR PRIDE; Q9LI74; -.
DR ProteomicsDB; 246968; -. [Q9LI74-1]
DR EnsemblPlants; AT3G25690.1; AT3G25690.1; AT3G25690. [Q9LI74-1]
DR EnsemblPlants; AT3G25690.2; AT3G25690.2; AT3G25690. [Q9LI74-1]
DR EnsemblPlants; AT3G25690.4; AT3G25690.4; AT3G25690. [Q9LI74-1]
DR EnsemblPlants; AT3G25690.6; AT3G25690.6; AT3G25690. [Q9LI74-1]
DR GeneID; 822157; -.
DR Gramene; AT3G25690.1; AT3G25690.1; AT3G25690. [Q9LI74-1]
DR Gramene; AT3G25690.2; AT3G25690.2; AT3G25690. [Q9LI74-1]
DR Gramene; AT3G25690.4; AT3G25690.4; AT3G25690. [Q9LI74-1]
DR Gramene; AT3G25690.6; AT3G25690.6; AT3G25690. [Q9LI74-1]
DR KEGG; ath:AT3G25690; -.
DR Araport; AT3G25690; -.
DR TAIR; locus:2102385; AT3G25690.
DR eggNOG; ENOG502QQ13; Eukaryota.
DR InParanoid; Q9LI74; -.
DR PhylomeDB; Q9LI74; -.
DR PRO; PR:Q9LI74; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LI74; baseline and differential.
DR Genevisible; Q9LI74; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IBA:GO_Central.
DR GO; GO:0009902; P:chloroplast relocation; IMP:TAIR.
DR InterPro; IPR040265; CHUP1-like.
DR PANTHER; PTHR31342; PTHR31342; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Coiled coil; Membrane; Phosphoprotein;
KW Plastid; Plastid outer membrane; Reference proteome; Repeat.
FT CHAIN 1..1004
FT /note="Protein CHUP1, chloroplastic"
FT /id="PRO_0000378107"
FT REGION 1..25
FT /note="Required for chloroplast localization"
FT REGION 22..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..290
FT /note="Leucine-zipper 1"
FT REGION 398..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..823
FT /note="Leucine-zipper 2"
FT REGION 979..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 123..341
FT /evidence="ECO:0000255"
FT COMPBIAS 33..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 4
FT /note="R->A: No effect on targeting. Loss of targeting;
FT when associated with A-12 and/or A-20."
FT /evidence="ECO:0000269|PubMed:18715957"
FT MUTAGEN 12
FT /note="S->A: No effect on targeting. Loss of targeting;
FT when associated with A-4 and/or A-20."
FT /evidence="ECO:0000269|PubMed:18715957"
FT MUTAGEN 20
FT /note="R->A: No effect on targeting. Loss of targeting;
FT when associated with A-4 and/or A-12."
FT /evidence="ECO:0000269|PubMed:18715957"
SQ SEQUENCE 1004 AA; 111912 MW; 2D85F5C3E68AE8DA CRC64;
MFVRIGFVVA ASIAAVTVKR LNVKPSKPSK PSDNGEGGDK EQSVDPDYNL NDKNLQEEEE
EEEEEVKLIN SVINQTRGSF SDYLDDDILP EFEDLLSGEI EYPLPDDDNN LEKAEKERKY
EVEMAYNDGE LERLKQLVKE LEEREVKLEG ELLEYYGLKE QESDIVELQR QLKIKTVEID
MLNITINSLQ AERKKLQEEL SQNGIVRKEL EVARNKIKEL QRQIQLDANQ TKGQLLLLKQ
HVSSLQMKEE EAMNKDTEVE RKLKAVQDLE VQVMELKRKN RELQHEKREL SIKLDSAEAR
IATLSNMTES DKVAKVREEV NNLKHNNEDL LKQVEGLQMN RFSEVEELVY LRWVNACLRY
ELRNYQTPAG KISARDLSKN LSPKSQAKAK RLMLEYAGSE RGQGDTDLES NYSQPSSPGS
DDFDNASMDS STSRFSSFSK KPGLIQKLKK WGKSKDDSSV QSSPSRSFYG GSPGRLSSSM
NKQRGPLESL MIRNAGESVA ITTFGQVDQE SPGTPETPNL PRIRTQQQAS SPGEGLNSVA
ASFHVMSKSV DNVLDEKYPA YKDRHKLAVE REKHIKHKAD QARAERFGGN VALPPKLAQL
KEKRVVVPSV ITATGDQSNE SNESNEGKAS ENAATVTKMK LVDIEKRPPR VPRPPPRSAG
GGKSTNLPSA RPPLPGGGPP PPPPPPGGGP PPPPGGGPPP PPPPPGALGR GAGGGNKVHR
APELVEFYQS LMKRESKKEG APSLISSGTG NSSAARNNMI GEIENRSTFL LAVKADVETQ
GDFVQSLATE VRASSFTDIE DLLAFVSWLD EELSFLVDER AVLKHFDWPE GKADALREAA
FEYQDLMKLE KQVTSFVDDP NLSCEPALKK MYKLLEKVEQ SVYALLRTRD MAISRYKEFG
IPVDWLSDTG VVGKIKLSSV QLAKKYMKRV AYELDSVSGS DKDPNREFLL LQGVRFAFRV
HQFAGGFDAE SMKAFEELRS RAKTESGDNN NNNNNNSNEE ESVN
