MOR1_ARATH
ID MOR1_ARATH Reviewed; 1978 AA.
AC Q94FN2; Q56XA7; Q9ZQN6;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Protein MOR1;
DE AltName: Full=Protein GEM1;
DE AltName: Full=Protein GEMINI POLLEN 1;
DE AltName: Full=Protein MICROTUBULE ORGANIZATION 1;
DE AltName: Full=Protein RID5;
DE AltName: Full=Protein ROOT INITIATION DEFECTIVE 5;
GN Name=MOR1; Synonyms=GEM1, RID5; OrderedLocusNames=At2g35630;
GN ORFNames=T20F21.17;
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], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LEU-174 AND GLU-195.
RC STRAIN=cv. Columbia;
RX PubMed=11385579; DOI=10.1038/35079128;
RA Whittington A.T., Vugrek O., Wei K.J., Hasenbein N.G., Sugimoto K.,
RA Rashbrooke M.C., Wasteneys G.O.;
RT "MOR1 is essential for organizing cortical microtubules in plants.";
RL Nature 411:610-613(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. No-0;
RX PubMed=12198497; DOI=10.1038/ncb844;
RA Twell D., Park S.K., Hawkins T.J., Schubert D., Schmidt R., Smertenko A.,
RA Hussey P.J.;
RT "MOR1/GEM1 has an essential role in the plant-specific cytokinetic
RT phragmoplast.";
RL Nat. Cell Biol. 4:711-714(2002).
RN [3]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1537-1978.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=12782733; DOI=10.1105/tpc.011593;
RA Sugimoto K., Himmelspach R., Williamson R.E., Wasteneys G.O.;
RT "Mutation or drug-dependent microtubule disruption causes radial swelling
RT without altering parallel cellulose microfibril deposition in Arabidopsis
RT root cells.";
RL Plant Cell 15:1414-1429(2003).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-96.
RX PubMed=14522871; DOI=10.1242/dev.00794;
RA Konishi M., Sugiyama M.;
RT "Genetic analysis of adventitious root formation with a novel series of
RT temperature-sensitive mutants of Arabidopsis thaliana.";
RL Development 130:5637-5647(2003).
RN [8]
RP FUNCTION.
RX PubMed=14617086; DOI=10.1046/j.1365-313x.2003.01906.x;
RA Himmelspach R., Williamson R.E., Wasteneys G.O.;
RT "Cellulose microfibril alignment recovers from DCB-induced disruption
RT despite microtubule disorganization.";
RL Plant J. 36:565-575(2003).
RN [9]
RP FUNCTION.
RX PubMed=15753108; DOI=10.1093/pcp/pci068;
RA Eleftheriou E.P., Baskin T.I., Hepler P.K.;
RT "Aberrant cell plate formation in the Arabidopsis thaliana microtubule
RT organization 1 mutant.";
RL Plant Cell Physiol. 46:671-675(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15860013; DOI=10.1111/j.1365-313x.2005.02393.x;
RA Korolev A.V., Chan J., Naldrett M.J., Doonan J.H., Lloyd C.W.;
RT "Identification of a novel family of 70 kDa microtubule-associated proteins
RT in Arabidopsis cells.";
RL Plant J. 42:547-555(2005).
RN [11]
RP FUNCTION.
RX PubMed=16608453; DOI=10.1111/j.1469-8137.2006.01671.x;
RA Collings D.A., Lill A.W., Himmelspach R., Wasteneys G.O.;
RT "Hypersensitivity to cytoskeletal antagonists demonstrates microtubule-
RT microfilament cross-talk in the control of root elongation in Arabidopsis
RT thaliana.";
RL New Phytol. 170:275-290(2006).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16377747; DOI=10.1104/pp.105.069989;
RA Kawamura E., Himmelspach R., Rashbrooke M.C., Whittington A.T., Gale K.R.,
RA Collings D.A., Wasteneys G.O.;
RT "MICROTUBULE ORGANIZATION 1 regulates structure and function of microtubule
RT arrays during mitosis and cytokinesis in the Arabidopsis root.";
RL Plant Physiol. 140:102-114(2006).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19033380; DOI=10.1242/jcs.039065;
RA Kawamura E., Wasteneys G.O.;
RT "MOR1, the Arabidopsis thaliana homologue of Xenopus MAP215, promotes rapid
RT growth and shrinkage, and suppresses the pausing of microtubules in vivo.";
RL J. Cell Sci. 121:4114-4123(2008).
RN [14]
RP IDENTIFICATION BY 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: Microtubule-binding protein that is essential for cortical
CC microtubules organization and function. Essential for maintaining the
CC interphase cortical array and for correct morphogenesis. Promotes rapid
CC growth and shrinkage of microtubules and suppresses the pausing of
CC interphase microtubules. Regulates the structure and function of
CC microtubule arrays during mitosis and cytokinesis. Probably not
CC required for cellulose microfibrils alignment in roots.
CC {ECO:0000269|PubMed:11385579, ECO:0000269|PubMed:12198497,
CC ECO:0000269|PubMed:12782733, ECO:0000269|PubMed:14522871,
CC ECO:0000269|PubMed:14617086, ECO:0000269|PubMed:15753108,
CC ECO:0000269|PubMed:16377747, ECO:0000269|PubMed:16608453,
CC ECO:0000269|PubMed:19033380}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16377747, ECO:0000269|PubMed:19033380}. Cytoplasm,
CC cytoskeleton, phragmoplast {ECO:0000269|PubMed:16377747}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:16377747}. Note=Associated
CC with microtubules in interphase arrays, preprophase bands, spindles,
CC and phragmoplasts. {ECO:0000269|PubMed:16377747}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, rosette leaves,
CC stems, open flowers and green siliques. {ECO:0000269|PubMed:11385579}.
CC -!- DISRUPTION PHENOTYPE: Homozygous lethal in gem1-1 mutant. No visible
CC phenotype under normal growth condition in mor1-1 and mor1-2 mutants,
CC but the restrictive temperature of 29 degrees Celsius causes cortical
CC microtubule shortening and disorganization, left-handed helical growth
CC of root, disrupts microtubule arrays during mitosis and cytokinesis and
CC alters plant morphology and organ development.
CC {ECO:0000269|PubMed:11385579, ECO:0000269|PubMed:12198497,
CC ECO:0000269|PubMed:14522871}.
CC -!- MISCELLANEOUS: Aberrant cytokinesis and cell division pattern during
CC pollen mitosis in heterozygous gem1-1 and gem1-2 mutants.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15450.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD93861.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF367246; AAK59871.1; -; mRNA.
DR EMBL; AY124770; AAM94170.1; -; Genomic_DNA.
DR EMBL; AC006068; AAD15450.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09133.1; -; Genomic_DNA.
DR EMBL; AK221769; BAD93861.1; ALT_INIT; mRNA.
DR PIR; A84771; A84771.
DR RefSeq; NP_565811.2; NM_129117.5.
DR AlphaFoldDB; Q94FN2; -.
DR BioGRID; 3476; 2.
DR STRING; 3702.AT2G35630.1; -.
DR iPTMnet; Q94FN2; -.
DR PaxDb; Q94FN2; -.
DR PRIDE; Q94FN2; -.
DR ProteomicsDB; 238264; -.
DR EnsemblPlants; AT2G35630.1; AT2G35630.1; AT2G35630.
DR GeneID; 818131; -.
DR Gramene; AT2G35630.1; AT2G35630.1; AT2G35630.
DR KEGG; ath:AT2G35630; -.
DR Araport; AT2G35630; -.
DR TAIR; locus:2058739; AT2G35630.
DR eggNOG; KOG1820; Eukaryota.
DR HOGENOM; CLU_000539_1_0_1; -.
DR InParanoid; Q94FN2; -.
DR OrthoDB; 33681at2759; -.
DR PhylomeDB; Q94FN2; -.
DR PRO; PR:Q94FN2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q94FN2; baseline and differential.
DR Genevisible; Q94FN2; AT.
DR GO; GO:0030981; C:cortical microtubule cytoskeleton; IDA:TAIR.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009574; C:preprophase band; IDA:TAIR.
DR GO; GO:0005819; C:spindle; IDA:TAIR.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0061863; F:microtubule plus end polymerase; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR GO; GO:0009920; P:cell plate formation involved in plant-type cell wall biogenesis; IMP:TAIR.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR GO; GO:0046785; P:microtubule polymerization; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 5.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR045110; XMAP215.
DR PANTHER; PTHR12609; PTHR12609; 1.
DR Pfam; PF12348; CLASP_N; 1.
DR SMART; SM01349; TOG; 5.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW Reference proteome; Repeat.
FT CHAIN 1..1978
FT /note="Protein MOR1"
FT /id="PRO_0000409455"
FT REPEAT 48..86
FT /note="HEAT 1"
FT REPEAT 165..202
FT /note="HEAT 2"
FT REPEAT 322..359
FT /note="HEAT 3"
FT REPEAT 363..400
FT /note="HEAT 4"
FT REPEAT 442..479
FT /note="HEAT 5"
FT REPEAT 849..886
FT /note="HEAT 6"
FT REPEAT 890..928
FT /note="HEAT 7"
FT REPEAT 932..969
FT /note="HEAT 8"
FT REPEAT 1008..1045
FT /note="HEAT 9"
FT REPEAT 1230..1253
FT /note="HEAT 10"
FT REPEAT 1254..1286
FT /note="HEAT 11"
FT REPEAT 1287..1325
FT /note="HEAT 12"
FT REPEAT 1328..1365
FT /note="HEAT 13"
FT REPEAT 1535..1575
FT /note="HEAT 14"
FT REGION 230..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1837..1862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 96
FT /note="C->Y: In rid5; no formation of root primordia at
FT temperatures above 28 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:14522871"
FT MUTAGEN 174
FT /note="L->F: In mor1-1; short and disordered microtubules
FT at temperatures above 28 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11385579"
FT MUTAGEN 195
FT /note="E->K: In mor1-2; short and disordered microtubules
FT at temperatures above 28 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11385579"
SQ SEQUENCE 1978 AA; 217550 MW; 05D5B250F0717C71 CRC64;
MSTEDEKLLK EAKKLPWEDR LGHKNWKVRN EANVDLASVF DSITDPKDPR LRDFGHLFRK
TVADSNAPVQ EKALDALIAF LRAADSDAGR YAKEVCDAIA LKCLTGRKNT VDKAQAAFLL
WVELEAVDVF LDTMEKAIKN KVAKAVVPAV DVMFQALSEF GSKVIPPKRI LKMLPELFDH
QDQNVRASAK GVTLELCRWI GKDPVKSILF EKMRDTMKKE LEAELANVTA GAKPTRKIRS
EQDKEPEAEA SSDVVGDGPS EEAVADAPQE IDEYDLMDPV DILTPLEKSG FWDGVKATKW
SERKEAVAEL TKLASTKKIA PGDFSEICRT LKKLITDVNL AVAVEAIQAI GNLACGLRTH
FSASSRFMLP VLLEKLKEKK QSVTDPLTQT LQTMYKAGCL NLVDVIEDVK TAVKNKVPLV
RSSTLTWLTF CLETSNKALI LKAHKEYVPL CMECLNDGTP DVRDAAFSAL AAIAKSVGMR
PLERSLEKLD DVRKKKLSEM IAGSGGGDQA GTSSVTVQSS VGSTATGNSD ASFVRKSAAS
MLSGKRPAPS AQASKKVGTG KPGGGKKDGS VRNEGSKSVE PPEDVEPAEM GLEEIENRLG
SLVKPETVSQ LKSSVWKERL EATLALKEEI EGLQELDKSV EILVRLLCAV PGWNEKNVQV
QQQVIEIITY ISSTAAKFPK KCVVLCITGT SERVADIKTR ASAMKCLTAF CEAVGPGFVF
ERLFKIMKEH KNPKVLSEGL LWMVSAVDDF GVSLLKLKDL IDFCKDVGLQ SSTAATRNAT
IKLLGALHKF VGPDIKGFLN DVKPALLSAL DTEYEKNPFE GTAAPKRVVK TSVSTSTSSG
GLDSLPREDI STKITPNLLK GFESPDWKMR LESIEAVNKI LEEANKRIQP TGTGELFGGL
RGRLLDSNKN LVMQTLTTIG GVAAAMGPAV EKASKGILSD VLKCLGDNKK HMRECTLAAL
DLWLGAVHLD KMIPYIIIAL TDGKMGAEGR KDLFDWLTKQ LTGLSDFVDA IHLLKPASTA
MTDKSADVRK AAEGCISEIL RVSGQEMIEK NLKDIQGPAL ALVLEKVRPG FVQEPFESSK
AMAGPVSKGV TKISKSTSNG TLKQGNRSRA VPTKGSSQIT SVHDIAIQSQ ALLNTKDSNK
EDRERVVVRR IKFEELRPEQ IQDLENDMMK FFREDLQKRL LSPDFKKQVD GLEILQKALP
SVSKEIIEVL DVLLRWFVLQ FCKSNTTCLL KVLEFLPELF NTLRDEEYCM TEAEAAIFLP
CLAEKLGHNI EKVREKMREL MKQIIQAYSV GKTYPYILEG LRSKNNRTRI ECTDLIGYLL
ETCGTEIGGL LKYLNIVASL TAERDGELRK AALNTMATGY QILGADIWKY VGKLTDAQKS
MIDDRFKWKA KDMEKRREGK PGEARAALRR SVRDSGPEVA EQSGDISQTV PGPLFPRQSY
GISEQMLERT PVPRTIAGVN GPTDWNEALD IIMFGSPEQS VEGMKVVCHE LAQASNDPEE
SAIDELVKDA DGLVSCLANK VAKTFDVSLM GASSRSCKYV LNTLMQTFQN KKLAHAVKEG
TLESLITELL LWLLDERVPR MEDGSQLLKA LNVLMLKILD NADRTSSFVV LISLLRPLDP
SRWPSPATAE VYAVRNQKFS DLVVKCLIKL TKLLQSTIYE VDLDRLLQSI HVYLQDLGME
EIRRRAGADD KPLRMVKTVL HELVKLRGAA IKGHLSLVPI DMRPQPIILA YIDLNLETLA
AARMLTATGP VGQTHWTDST ANNPSPPANS ADVQLKQELG AIFKKIGDKQ TSTIGLYDLY
HITKSYPKVD IFSQLQNASE AFRTYIRDGL AQVEKNAAAG RTPSSLPLST PPPSSLALPS
PDIPSLSSLD VKPLMNPRSD LYTDDIRASN MNPGVMTGTL DAIRERMKNM QLASSEPVSK
PLMPTNDNLS MNQQSVPPSQ MGQETVHTHP VVLPMDEKAL SGLQARMERL KGGSLEHM
