MBP2C_ARATH
ID MBP2C_ARATH Reviewed; 326 AA.
AC Q9LEZ4; A0A1P8BFS6; P92987;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein MICROTUBULE BINDING PROTEIN 2C {ECO:0000303|PubMed:17965274};
DE Short=AtMBP2C {ECO:0000303|PubMed:17965274};
DE AltName: Full=Movement protein binding protein 2C {ECO:0000303|PubMed:17965274};
GN Name=MBP2C {ECO:0000303|PubMed:17965274};
GN Synonyms=AT18 {ECO:0000303|PubMed:8893552};
GN OrderedLocusNames=At5g08120 {ECO:0000312|Araport:AT5G08120};
GN ORFNames=T22D6.60 {ECO:0000312|EMBL:CAB93713.1};
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 [MRNA] (ISOFORM 3), AND FUNCTION.
RX PubMed=8893552; DOI=10.1046/j.1365-313x.1996.10040761.x;
RA Xia G., Ramachandran S., Hong Y., Chan Y.-S., Simanis V., Chua N.-H.;
RT "Identification of plant cytoskeletal, cell cycle-related and polarity-
RT related proteins using Schizosaccharomyces pombe.";
RL Plant J. 10:761-769(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STM, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=17965274; DOI=10.1105/tpc.107.044354;
RA Winter N., Kollwig G., Zhang S., Kragler F.;
RT "MPB2C, a microtubule-associated protein, regulates non-cell-autonomy of
RT the homeodomain protein KNOTTED1.";
RL Plant Cell 19:3001-3018(2007).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=19074626; DOI=10.1104/pp.108.130450;
RA Ruggenthaler P., Fichtenbauer D., Krasensky J., Jonak C., Waigmann E.;
RT "Microtubule-associated protein AtMPB2C plays a role in organization of
RT cortical microtubules, stomata patterning, and tobamovirus infectivity.";
RL Plant Physiol. 149:1354-1365(2009).
CC -!- FUNCTION: Prevents homeodomain proteins (e.g. STM) association to
CC plasmodesmata and, consequently, cell-to-cell transport. Binds to RNA.
CC Alters STM RNA binding capacity (PubMed:17965274). Regulates
CC cytoskeleton (e.g. actin) organization that determinates cell shape
CC (PubMed:8893552, PubMed:19074626). Regulates stomata patterning and
CC drought tolerance (PubMed:19074626). Involved in restricting
CC tobamovirus (e.g. oilseed rape mosaic virus) infectivity, probably by
CC interfering with cell-to-cell virus movement (PubMed:19074626).
CC {ECO:0000269|PubMed:17965274, ECO:0000269|PubMed:19074626,
CC ECO:0000269|PubMed:8893552}.
CC -!- SUBUNIT: Interacts with STM. {ECO:0000269|PubMed:17965274}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17965274, ECO:0000269|PubMed:19074626}.
CC Note=Microtubule-associated and stabilizer (PubMed:17965274,
CC PubMed:19074626). Localized in cytosolic punctae when associated with
CC STM (PubMed:17965274). {ECO:0000269|PubMed:17965274,
CC ECO:0000269|PubMed:19074626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LEZ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LEZ4-2; Sequence=VSP_059023, VSP_059024;
CC Name=3;
CC IsoId=Q9LEZ4-3; Sequence=VSP_059022;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, flowers and
CC developing ovules. {ECO:0000269|PubMed:17965274}.
CC -!- DEVELOPMENTAL STAGE: In young seedlings, expressed in the vascular
CC tissues of cotyledons, leaf primordia, and shoot apical meristem (SAM).
CC In roots, confined to a limited number of epidermal cells in proximity
CC to the root apical meristem. In flowers, present in carpels and ovules.
CC In developing ovules, observed in the funiculus and integuments.
CC {ECO:0000269|PubMed:17965274}.
CC -!- SIMILARITY: Belongs to the microtubule binding protein 2C family.
CC {ECO:0000305}.
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DR EMBL; U62744; AAB38778.1; -; mRNA.
DR EMBL; AL357612; CAB93713.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91249.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70463.1; -; Genomic_DNA.
DR EMBL; AF370224; AAK44039.1; -; mRNA.
DR EMBL; AY117260; AAM51335.1; -; mRNA.
DR PIR; T50497; T50497.
DR RefSeq; NP_001332071.1; NM_001342982.1. [Q9LEZ4-2]
DR RefSeq; NP_196429.1; NM_120894.5. [Q9LEZ4-1]
DR AlphaFoldDB; Q9LEZ4; -.
DR SMR; Q9LEZ4; -.
DR STRING; 3702.AT5G08120.1; -.
DR iPTMnet; Q9LEZ4; -.
DR PaxDb; Q9LEZ4; -.
DR PRIDE; Q9LEZ4; -.
DR ProteomicsDB; 238375; -. [Q9LEZ4-1]
DR DNASU; 830707; -.
DR EnsemblPlants; AT5G08120.1; AT5G08120.1; AT5G08120. [Q9LEZ4-1]
DR EnsemblPlants; AT5G08120.2; AT5G08120.2; AT5G08120. [Q9LEZ4-2]
DR GeneID; 830707; -.
DR Gramene; AT5G08120.1; AT5G08120.1; AT5G08120. [Q9LEZ4-1]
DR Gramene; AT5G08120.2; AT5G08120.2; AT5G08120. [Q9LEZ4-2]
DR KEGG; ath:AT5G08120; -.
DR Araport; AT5G08120; -.
DR TAIR; locus:2181534; AT5G08120.
DR eggNOG; ENOG502QS43; Eukaryota.
DR HOGENOM; CLU_078364_0_0_1; -.
DR InParanoid; Q9LEZ4; -.
DR OMA; QWEPMIS; -.
DR PhylomeDB; Q9LEZ4; -.
DR PRO; PR:Q9LEZ4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LEZ4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:TAIR.
DR GO; GO:0051607; P:defense response to virus; IMP:TAIR.
DR GO; GO:0051224; P:negative regulation of protein transport; IDA:UniProtKB.
DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IDA:UniProtKB.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0010375; P:stomatal complex patterning; IMP:TAIR.
DR InterPro; IPR040289; MBP2C.
DR PANTHER; PTHR35502; PTHR35502; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Plant defense;
KW Reference proteome; RNA-binding.
FT CHAIN 1..326
FT /note="Protein MICROTUBULE BINDING PROTEIN 2C"
FT /id="PRO_0000441029"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 132..183
FT /evidence="ECO:0000255"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 3)"
FT /id="VSP_059022"
FT VAR_SEQ 275..294
FT /note="LDDVDETDLRKMEEARLAYV -> LVSQRNHNPHLSFFLFFFFG (in
FT isoform 2)"
FT /id="VSP_059023"
FT VAR_SEQ 295..326
FT /note="Missing (in isoform 2)"
FT /id="VSP_059024"
SQ SEQUENCE 326 AA; 37349 MW; 7FC6FBF157198CF0 CRC64;
MYEQQQHFMD LQSDSGFGDD SSWLAGDDDL RLSPHQSAAG TNSGNENLDR RLLKDLVEMV
PLIEHYMEHK ERSSFKRRGS MIYTKMPSKE SLSRRGRNAS QTVPGRKKRD QEGNDDVMNN
SREDDENAKA LAGAEKEEMS RLREQVNDLQ TKLSEKEEVL KSMEMSKNQV NEIQEKLEAT
NRLVAEKDML IKSMQLQLSD TKIKLADKQA ALEKTQWEAK TTGTRAIKLQ EQLDAVEGDI
STFTRVFETL AKTDSKKPDR DYDAVPYEFD HLPYLDDVDE TDLRKMEEAR LAYVAAVNTA
KEREDEESLV MAAQARAYLQ SLAFTY
