OPS_ARATH
ID OPS_ARATH Reviewed; 685 AA.
AC Q9SS80;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Protein OCTOPUS {ECO:0000303|PubMed:22395740};
GN Name=OPS {ECO:0000303|PubMed:22395740};
GN OrderedLocusNames=At3g09070 {ECO:0000312|Araport:AT3G09070};
GN ORFNames=MZB10.10 {ECO:0000312|EMBL:AAD56323.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 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 FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=22395740; DOI=10.1242/dev.072629;
RA Truernit E., Bauby H., Belcram K., Barthelemy J., Palauqui J.C.;
RT "OCTOPUS, a polarly localised membrane-associated protein, regulates phloem
RT differentiation entry in Arabidopsis thaliana.";
RL Development 139:1306-1315(2012).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-319, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25049386; DOI=10.1073/pnas.1407337111;
RA Rodriguez-Villalon A., Gujas B., Kang Y.H., Breda A.S., Cattaneo P.,
RA Depuydt S., Hardtke C.S.;
RT "Molecular genetic framework for protophloem formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11551-11556(2014).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH VCC.
RC STRAIN=cv. Columbia;
RX PubMed=25149602; DOI=10.1104/pp.114.246314;
RA Roschzttardtz H., Paez-Valencia J., Dittakavi T., Jali S., Reyes F.C.,
RA Baisa G., Anne P., Gissot L., Palauqui J.-C., Masson P.H., Bednarek S.Y.,
RA Otegui M.S.;
RT "The VASCULATURE COMPLEXITY AND CONNECTIVITY gene encodes a plant-specific
RT protein required for embryo provasculature development.";
RL Plant Physiol. 166:889-902(2014).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-318 AND GLU-319,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-318, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=28652362; DOI=10.1073/pnas.1703258114;
RA Breda A.S., Hazak O., Hardtke C.S.;
RT "Phosphosite charge rather than shootward localization determines OCTOPUS
RT activity in root protophloem.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E5721-E5730(2017).
CC -!- FUNCTION: Potentiates primary root protophloem differentiation
CC (PubMed:22395740, PubMed:25049386, PubMed:28652362). Required, together
CC with VCC, for embryo provasculature development and cotyledon vascular
CC complexity and connectivity (PubMed:25149602). Regulates roots
CC architecture (PubMed:25049386). Mediates the recruitment of ASK7/BIN2
CC to the plasma membrane (PubMed:28652362). {ECO:0000269|PubMed:22395740,
CC ECO:0000269|PubMed:25049386, ECO:0000269|PubMed:25149602,
CC ECO:0000269|PubMed:28652362}.
CC -!- SUBUNIT: Interacts with VCC. {ECO:0000269|PubMed:25149602}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22395740,
CC ECO:0000269|PubMed:28652362}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:28652362}. Note=Polar localization at the apical
CC side of the plasma membrane, shootward oriented, in developing root
CC protophloem cells (PubMed:22395740, PubMed:28652362). Also found in the
CC cytoplasm in the early, dividing. protophloem cells (PubMed:28652362).
CC {ECO:0000269|PubMed:22395740, ECO:0000269|PubMed:28652362}.
CC -!- TISSUE SPECIFICITY: Expressed in provascular cells and phloem initials
CC (e.g. protophloem, metaphloem, sieve element precursor cells and sieve
CC element procambium precursor cells). {ECO:0000269|PubMed:22395740,
CC ECO:0000269|PubMed:25049386}.
CC -!- DEVELOPMENTAL STAGE: First expressed in provascular cells, and upon
CC vascular cell type specification becomes restricted to the phloem cell
CC lineage. {ECO:0000269|PubMed:22395740}.
CC -!- PTM: Phosphorylation at Ser-318 amplifies the promotion of protophloem
CC differentiation. {ECO:0000269|PubMed:28652362}.
CC -!- DISRUPTION PHENOTYPE: Short roots associated with both reduced cell
CC division in the root meristem and altered root cell elongation. Early
CC emergence of lateral roots at the root-hypocotyl junction
CC (PubMed:22395740, PubMed:25049386, PubMed:28652362). Reductions in the
CC complexity of vascular networks in cotyledons and discontinuous phloem
CC differentiation (PubMed:25149602, PubMed:22395740, PubMed:25049386,
CC PubMed:28652362). Impaired primary root protophloem differentiation
CC during root development leading to altered phloem long-distance
CC transport (PubMed:22395740). The double mutant vcc ops exhibits a
CC complete loss of high-complexity vascular networks (PubMed:25149602).
CC The double mutant brx ops double mutant has strongly reduced root
CC length and meristem size, with missing protophloem strands
CC (PubMed:28652362). {ECO:0000269|PubMed:22395740,
CC ECO:0000269|PubMed:25049386, ECO:0000269|PubMed:25149602,
CC ECO:0000269|PubMed:28652362}.
CC -!- SIMILARITY: Belongs to the OCTOPUS family. {ECO:0000305}.
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DR EMBL; AC009326; AAD56323.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74716.1; -; Genomic_DNA.
DR EMBL; AK226807; BAE98903.1; -; mRNA.
DR RefSeq; NP_187519.1; NM_111741.3.
DR AlphaFoldDB; Q9SS80; -.
DR BioGRID; 5394; 3.
DR STRING; 3702.AT3G09070.1; -.
DR iPTMnet; Q9SS80; -.
DR PaxDb; Q9SS80; -.
DR PRIDE; Q9SS80; -.
DR ProteomicsDB; 248816; -.
DR EnsemblPlants; AT3G09070.1; AT3G09070.1; AT3G09070.
DR GeneID; 820060; -.
DR Gramene; AT3G09070.1; AT3G09070.1; AT3G09070.
DR KEGG; ath:AT3G09070; -.
DR Araport; AT3G09070; -.
DR TAIR; locus:2095254; AT3G09070.
DR eggNOG; ENOG502QR95; Eukaryota.
DR HOGENOM; CLU_021226_0_0_1; -.
DR InParanoid; Q9SS80; -.
DR OMA; VHRHVTR; -.
DR OrthoDB; 604708at2759; -.
DR PhylomeDB; Q9SS80; -.
DR PRO; PR:Q9SS80; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SS80; baseline and differential.
DR Genevisible; Q9SS80; AT.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0010588; P:cotyledon vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0010088; P:phloem development; IMP:UniProtKB.
DR GO; GO:0010233; P:phloem transport; IMP:TAIR.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:0022622; P:root system development; IMP:TAIR.
DR InterPro; IPR008004; OCTOPUS-like.
DR PANTHER; PTHR31659; PTHR31659; 1.
DR Pfam; PF05340; DUF740; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; Developmental protein;
KW Differentiation; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..685
FT /note="Protein OCTOPUS"
FT /id="PRO_0000311122"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 549..578
FT /evidence="ECO:0000255"
FT COMPBIAS 179..202
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28652362"
FT MUTAGEN 318
FT /note="S->A: Reduced activity. Normal plasma membrane
FT localization. Complements the ops mutant."
FT /evidence="ECO:0000269|PubMed:28652362"
FT MUTAGEN 318
FT /note="S->E: Slightly reduced activity. Normal plasma
FT membrane localization. Complements the ops mutant."
FT /evidence="ECO:0000269|PubMed:28652362"
FT MUTAGEN 318
FT /note="S->K: Slightly increased activity. Normal plasma
FT membrane localization. Complements the ops and brx mutants.
FT Strongly increased activity; when associated with K-319."
FT /evidence="ECO:0000269|PubMed:28652362"
FT MUTAGEN 319
FT /note="E->K: Gain-of-function allele that partially rescues
FT roots defects phenotype associated with the lack of BRX.
FT Normal plasma membrane localization. Complements the ops
FT and brx mutants. Strongly increased activity; when
FT associated with K-318."
FT /evidence="ECO:0000269|PubMed:25049386,
FT ECO:0000269|PubMed:28652362"
FT MUTAGEN 319
FT /note="E->R: Slightly increased activity. Normal plasma
FT membrane localization. Complements the ops and brx
FT mutants."
FT /evidence="ECO:0000269|PubMed:28652362"
SQ SEQUENCE 685 AA; 75441 MW; 88E3B134DB6BCCA0 CRC64;
MNPATDPVSA AAAALAPPPQ PPQPHRLSTS CNRHPEERFT GFCPSCLCER LSVLDQTNNG
GSSSSSKKPP TISAAALKAL FKPSGNNGVG GVNTNGNGRV KPGFFPELRR TKSFSASKNN
EGFSGVFEPQ RRSCDVRLRS SLWNLFSQDE QRNLPSNVTG GEIDVEPRKS SVAEPVLEVN
DEGEAESDDE ELEEEEEEDY VEAGDFEILN DSGELMREKS DEIVEVREEI EEAVKPTKGL
SEEELKPIKD YIDLDSQTKK PSVRRSFWSA ASVFSKKLQK WRQNQKMKKR RNGGDHRPGS
ARLPVEKPIG RQLRDTQSEI ADYGYGRRSC DTDPRFSLDA GRFSLDAGRF SVDIGRISLD
DPRYSFDEPR ASWDGSLIGR TMFPPAARAP PPPSMLSVVE DAPPPVHRHV TRADMQFPVE
EPAPPPPVVN QTNGVSDPVI IPGGSIQTRD YYTDSSSRRR KSLDRSSSSM RKTAAAVVAD
MDEPKLSVSS AISIDAYSGS LRDNNNYAVE TADNGSFREP AMMIGDRKVN SNDNNKKSRR
WGKWSILGLI YRKSVNKYEE EEEEEEDRYR RLNGGMVERS LSESWPELRN GGGGGGGPRM
VRSNSNVSWR SSGGGSARKV NGLDRRNKSS RYSPKNGENG MLKFYLPHMK ASRRMSGTGG
AGGGGGGGWA NSHGHSIARS VMRLY
