MS5_ARATH
ID MS5_ARATH Reviewed; 434 AA.
AC Q9SUC3; O65310; Q9SBJ5;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein POLLENLESS 3 {ECO:0000303|Ref.2};
DE AltName: Full=Protein MALE STERILE 5 {ECO:0000303|PubMed:9750346};
DE AltName: Full=Protein THREE-DIVISION MUTANT 1 {ECO:0000303|PubMed:9451956};
GN Name=MS5 {ECO:0000303|PubMed:9750346};
GN Synonyms=TDM1 {ECO:0000303|PubMed:9451956};
GN OrderedLocusNames=At4g20900 {ECO:0000312|Araport:AT4G20900};
GN ORFNames=T13K14.60 {ECO:0000312|EMBL:CAB45885.1};
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 [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wassilewskija;
RX PubMed=9750346; DOI=10.1046/j.1365-313x.1998.00216.x;
RA Glover J., Grelon M., Craig S., Chaudhury A., Dennis E.;
RT "Cloning and characterization of MS5 from Arabidopsis: a gene critical in
RT male meiosis.";
RL Plant J. 15:345-356(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Landsberg erecta, and cv. Wassilewskija;
RX DOI=10.1007/s004970050158;
RA Sanders P.M., Bui A.Q., Weterings K., McIntire K.N., Hsu Y.-C., Lee P.Y.,
RA Truong M.T., Beals T.B., Goldberg R.B.;
RT "Anther developmental defects in Arabidopsis thaliana male-sterile
RT mutants.";
RL Sex. Plant Reprod. 11:297-322(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9451956; DOI=10.1023/a:1018497804129;
RA Ross K.J., Fransz P., Armstrong S.J., Vizir I., Mulligan B., Franklin F.C.,
RA Jones G.H.;
RT "Cytological characterization of four meiotic mutants of Arabidopsis
RT isolated from T-DNA-transformed lines.";
RL Chromosome Res. 5:551-559(1997).
RN [6]
RP REVIEW.
RX PubMed=10679449; DOI=10.1016/s1369-5266(99)00037-0;
RA Yang W.C., Sundaresan V.;
RT "Genetics of gametophyte biogenesis in Arabidopsis.";
RL Curr. Opin. Plant Biol. 3:53-57(2000).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21119056; DOI=10.1105/tpc.110.078378;
RA Bulankova P., Riehs-Kearnan N., Nowack M.K., Schnittger A., Riha K.;
RT "Meiotic progression in Arabidopsis is governed by complex regulatory
RT interactions between SMG7, TDM1, and the meiosis I-specific cyclin TAM.";
RL Plant Cell 22:3791-3803(2010).
CC -!- FUNCTION: Essential for male fertility, especially for microspore and
CC pollen grain production (PubMed:9750346, Ref.2). Involved in the
CC regulation of cell division after male meiosis I and II to facilitate
CC exit from meiosis and transition to G1 (PubMed:9451956,
CC PubMed:21119056). {ECO:0000269|PubMed:21119056,
CC ECO:0000269|PubMed:9451956, ECO:0000269|PubMed:9750346,
CC ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000303|PubMed:9750346}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels mostly in floral organs
CC during meiosis. Also barely detectable in leaves, stems and roots.
CC {ECO:0000269|PubMed:9750346, ECO:0000269|Ref.2}.
CC -!- DEVELOPMENTAL STAGE: Specifically localized within meiotic cells in the
CC anther locules, transiently, only during late meiosis.
CC {ECO:0000269|Ref.2}.
CC -!- DISRUPTION PHENOTYPE: Sterile plants with abnormal formation of polyads
CC during microsporogenesis, tetrads with more than four pools of
CC chromosomes, after male meiosis, due to an unusual and abnormal cell
CC division without further DNA or chromosome replication after meiosis I
CC and II, and leading to collapsed pollen in flattened anthers
CC (PubMed:9750346, Ref.2). Chromatin recondensation and stretching after
CC meiosis II characterized by a dense microtubule network connecting
CC haploid nuclei in the tetrad stage rearranged into four bipolar
CC spindles as chromatids recondense, as if haploid nuclei entered a third
CC meiotic division (PubMed:9451956, PubMed:21119056).
CC {ECO:0000269|PubMed:21119056, ECO:0000269|PubMed:9451956,
CC ECO:0000269|PubMed:9750346, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the MS5 protein family.
CC {ECO:0000305|PubMed:9750346, ECO:0000305|Ref.2}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE84373.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB45885.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79090.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF031607; AAC72541.1; -; Genomic_DNA.
DR EMBL; AF060248; AAC97106.1; -; Genomic_DNA.
DR EMBL; AL080282; CAB45885.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161553; CAB79090.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84373.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; ANM66435.1; -; Genomic_DNA.
DR PIR; T10632; T10632.
DR RefSeq; NP_001328331.1; NM_001341460.1.
DR RefSeq; NP_193822.1; NM_118208.1.
DR AlphaFoldDB; Q9SUC3; -.
DR SMR; Q9SUC3; -.
DR STRING; 3702.AT4G20900.1; -.
DR iPTMnet; Q9SUC3; -.
DR PaxDb; Q9SUC3; -.
DR PRIDE; Q9SUC3; -.
DR EnsemblPlants; AT4G20900.2; AT4G20900.2; AT4G20900.
DR GeneID; 827838; -.
DR Gramene; AT4G20900.2; AT4G20900.2; AT4G20900.
DR KEGG; ath:AT4G20900; -.
DR Araport; AT4G20900; -.
DR TAIR; locus:2133099; AT4G20900.
DR eggNOG; ENOG502QQBN; Eukaryota.
DR HOGENOM; CLU_013792_0_0_1; -.
DR InParanoid; Q9SUC3; -.
DR OrthoDB; 579132at2759; -.
DR PRO; PR:Q9SUC3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUC3; baseline and differential.
DR Genevisible; Q9SUC3; AT.
DR GO; GO:0005634; C:nucleus; ISS:TAIR.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0009556; P:microsporogenesis; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR044961; MS5/SDI1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR36326; PTHR36326; 1.
DR SMART; SM00028; TPR; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; Developmental protein; Meiosis;
KW Nucleus; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..434
FT /note="Protein POLLENLESS 3"
FT /id="PRO_0000430653"
FT REPEAT 95..131
FT /note="TPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 133..164
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 191..224
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 241..274
FT /note="TPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REGION 13..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..166
FT /evidence="ECO:0000255"
FT COILED 408..434
FT /evidence="ECO:0000255"
FT MOTIF 34..37
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000303|PubMed:9750346"
FT MOTIF 377..380
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000303|PubMed:9750346"
FT COMPBIAS 394..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 25
FT /note="H -> D (in Ref. 1; AAC72541)"
FT CONFLICT 410..411
FT /note="DI -> NF (in Ref. 2; AAC97106)"
SQ SEQUENCE 434 AA; 49216 MW; A65CF0C7E91F9BD7 CRC64;
MCPCVERRAP PGVYYTPPPA RTSDHVAAMP MTERRRPPYS CSSSSERRDP FHIVHKVPSG
DSPYVRAKHA QLIDKDPNRA ISLFWTAINA GDRVDSALKD MAVVMKQLGR SDEGIEAIKS
FRYLCSFESQ DSIDNLLLEL YKKSGRIEEE AVLLEHKLQT LEQGMGFGGR VSRAKRVQGK
HVIMTIEQEK ARILGNLGWV HLQLHNYGIA EQHYRRALGL ERDKNKLCNL AICLMRMSRI
PEAKSLLDDV RDSPAESECG DEPFAKSYDR AVEMLAEIES KKPEADLSEK FYAGCSFVNR
MKENIAPGTA NKNYSDVSSS PASVRPNSAG LYTQPRRCRL FEEETRGAAR KLLFGKPQPF
GSEQMKILER GEEEPMKRKK LDQNMIQYLH EFVKDTADGP KSESKKSWAD IAEEEEAEEE
EEERLQGELK TAEM
