WEB1_ARATH
ID WEB1_ARATH Reviewed; 807 AA.
AC O48724; Q0WQC5;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Protein WEAK CHLOROPLAST MOVEMENT UNDER BLUE LIGHT 1;
DE Short=Protein WEB1;
GN Name=WEB1; OrderedLocusNames=At2g26570; ORFNames=T9J22.24;
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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, 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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP GENE FAMILY, AND INTERACTION WITH PMI2.
RX PubMed=20974974; DOI=10.1073/pnas.1007836107;
RA Kodama Y., Suetsugu N., Kong S.G., Wada M.;
RT "Two interacting coiled-coil proteins, WEB1 and PMI2, maintain the
RT chloroplast photorelocation movement velocity in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19591-19596(2010).
CC -!- FUNCTION: Required for the chloroplast avoidance response under high
CC intensity blue light. This avoidance response consists in the
CC relocation of chloroplasts on the anticlinal side of exposed cells.
CC Acts in association with PMI2 to maintain the velocity of chloroplast
CC photorelocation movement via cp-actin filaments regulation.
CC {ECO:0000269|PubMed:20974974}.
CC -!- SUBUNIT: Interacts with PMI2. {ECO:0000269|PubMed:20974974}.
CC -!- INTERACTION:
CC O48724; Q9C9N6: PMI2; NbExp=6; IntAct=EBI-4408440, EBI-4408425;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20974974}.
CC -!- TISSUE SPECIFICITY: Ubiquitous but preferentially in chloroplast-
CC containing tissues. {ECO:0000269|PubMed:20974974}.
CC -!- DISRUPTION PHENOTYPE: Deficient chloroplast response.
CC {ECO:0000269|PubMed:20974974}.
CC -!- SIMILARITY: Belongs to the WEB family. {ECO:0000305}.
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DR EMBL; AC002505; AAC14505.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07859.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63180.1; -; Genomic_DNA.
DR EMBL; AK228775; BAF00674.1; -; mRNA.
DR PIR; T00990; T00990.
DR RefSeq; NP_001325286.1; NM_001336076.1.
DR RefSeq; NP_180225.1; NM_128214.3.
DR AlphaFoldDB; O48724; -.
DR SMR; O48724; -.
DR BioGRID; 2550; 2.
DR IntAct; O48724; 1.
DR STRING; 3702.AT2G26570.1; -.
DR iPTMnet; O48724; -.
DR PaxDb; O48724; -.
DR PRIDE; O48724; -.
DR ProteomicsDB; 242487; -.
DR EnsemblPlants; AT2G26570.1; AT2G26570.1; AT2G26570.
DR EnsemblPlants; AT2G26570.2; AT2G26570.2; AT2G26570.
DR GeneID; 817198; -.
DR Gramene; AT2G26570.1; AT2G26570.1; AT2G26570.
DR Gramene; AT2G26570.2; AT2G26570.2; AT2G26570.
DR KEGG; ath:AT2G26570; -.
DR Araport; AT2G26570; -.
DR TAIR; locus:2066301; AT2G26570.
DR eggNOG; ENOG502QQFI; Eukaryota.
DR HOGENOM; CLU_008410_1_1_1; -.
DR InParanoid; O48724; -.
DR OMA; STENMSH; -.
DR OrthoDB; 380942at2759; -.
DR PhylomeDB; O48724; -.
DR PRO; PR:O48724; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48724; baseline and differential.
DR Genevisible; O48724; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009904; P:chloroplast accumulation movement; IMP:TAIR.
DR GO; GO:0009903; P:chloroplast avoidance movement; IMP:TAIR.
DR InterPro; IPR008545; Web.
DR Pfam; PF05701; WEMBL; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..807
FT /note="Protein WEAK CHLOROPLAST MOVEMENT UNDER BLUE LIGHT
FT 1"
FT /id="PRO_0000414038"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..429
FT /evidence="ECO:0000255"
FT COILED 457..489
FT /evidence="ECO:0000255"
FT COILED 516..621
FT /evidence="ECO:0000255"
FT COILED 664..724
FT /evidence="ECO:0000255"
FT COMPBIAS 27..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 558
FT /note="E -> A (in Ref. 3; BAF00674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 807 AA; 89294 MW; F83F0655E1371472 CRC64;
MEDLKTVEAS DNVVSDNVEK VNPELIDSTI RESNIQSATK VDNIPQSQTD TEETQQSQTD
TEETQQSQTD DTTGNAKIYV DDTFSPSDAA TAAVLTGKDS TSTTIVEEVM EPDEIGLPSV
KITEAATGTA RNGGGSPRTV SSPRFSGSPV STGTPKNVDS HRGLIDTAAP FESVKEAVSK
FGGITDWKSH RMQAVERRKL IEEELKKIHE EIPEYKTHSE TAEAAKLQVL KELESTKRLI
EQLKLNLDKA QTEEQQAKQD SELAKLRVEE MEQGIAEDVS VAAKAQLEVA KARHTTAITE
LSSVKEELET LHKEYDALVQ DKDVAVKKVE EAMLASKEVE KTVEELTIEL IATKESLESA
HASHLEAEEQ RIGAAMARDQ DTHRWEKELK QAEEELQRLN QQIHSSKDLK SKLDTASALL
LDLKAELVAY MESKLKQEAC DSTTNTDPST ENMSHPDLHA AVASAKKELE EVNVNIEKAA
AEVSCLKLAS SSLQLELEKE KSTLASIKQR EGMASIAVAS IEAEIDRTRS EIASVQSKEK
DAREKMVELP KQLQQAAEEA DEAKSLAEVA REELRKAKEE AEQAKAGAST MESRLFAAQK
EIEAAKASER LALAAIKALE ESESTLKAND TDSPRSVTLS LEEYYELSKR AHEAEELANA
RVAAAVSRIE EAKETEMRSL EKLEEVNRDM DARKKALKEA TEKAEKAKEG KLGVEQELRK
WRAEHEQKRK AGDGVNTEKN LKESFEGGKM EQSPEAVVYA SSPSESYGTE ENSETNLSPQ
TKSRKKKKKL SFPRFFMFLS KKKSHNN
