MMD1_ARATH
ID MMD1_ARATH Reviewed; 704 AA.
AC Q7X6Y7; Q9C8D0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=PHD finger protein MALE MEIOCYTE DEATH 1 {ECO:0000303|PubMed:12782723};
GN Name=MMD1 {ECO:0000303|PubMed:12782723};
GN Synonyms=DUET {ECO:0000303|PubMed:14573517};
GN OrderedLocusNames=At1g66170 {ECO:0000312|Araport:AT1G66170};
GN ORFNames=F15E12.11 {ECO:0000312|EMBL:AAG51303.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14573517; DOI=10.1242/dev.00827;
RA Reddy T.V., Kaur J., Agashe B., Sundaresan V., Siddiqi I.;
RT "The DUET gene is necessary for chromosome organization and progression
RT during male meiosis in Arabidopsis and encodes a PHD finger protein.";
RL Development 130:5975-5987(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12782723; DOI=10.1105/tpc.010447;
RA Yang X., Makaroff C.A., Ma H.;
RT "The Arabidopsis MALE MEIOCYTE DEATH1 gene encodes a PHD-finger protein
RT that is required for male meiosis.";
RL Plant Cell 15:1281-1295(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=27385818; DOI=10.1105/tpc.16.00040;
RA Wang J., Niu B., Huang J., Wang H., Yang X., Dong A., Makaroff C., Ma H.,
RA Wang Y.;
RT "The PHD Finger Protein MMD1/DUET Ensures the Progression of Male Meiotic
RT Chromosome Condensation and Directly Regulates the Expression of the
RT Condensin Gene CAP-D3.";
RL Plant Cell 28:1894-1909(2016).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH JMJ16, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=32572214; DOI=10.1038/s41477-020-0697-0;
RA Wang J., Yu C., Zhang S., Ye J., Dai H., Wang H., Huang J., Cao X., Ma J.,
RA Ma H., Wang Y.;
RT "Cell-type-dependent histone demethylase specificity promotes meiotic
RT chromosome condensation in Arabidopsis.";
RL Nat. Plants 6:823-837(2020).
CC -!- FUNCTION: Probable transcription factor required for chromosome
CC organization and progression during male meiosis (e.g.
CC microsporogenesis) (PubMed:12782723, PubMed:14573517). Necessary for
CC fertility and meiotic progressive compaction of prophase I chromosomes
CC to metaphase I bivalents (PubMed:27385818). Together with JMJ16,
CC promotes gene expression in male meiocytes in an H3K9me3-dependent
CC manner, and contributes to meiotic chromosome condensation by
CC triggering some condensin promoters (e.g. CAP-D3 and CAP-H)
CC (PubMed:32572214, PubMed:27385818). {ECO:0000269|PubMed:12782723,
CC ECO:0000269|PubMed:14573517, ECO:0000269|PubMed:27385818,
CC ECO:0000269|PubMed:32572214}.
CC -!- SUBUNIT: Interacts with JMJ16 in the nucleus of male meiocytes,
CC especially on pachytene chromosomes. {ECO:0000269|PubMed:32572214}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12782723,
CC ECO:0000269|PubMed:32572214}.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescence, specifically in male
CC meiocytes. {ECO:0000269|PubMed:12782723, ECO:0000269|PubMed:14573517,
CC ECO:0000269|PubMed:27385818}.
CC -!- DEVELOPMENTAL STAGE: First detected in sporogenous cells at late anther
CC stage 4. Maximum levels observed in male meiocytes at anther stage 5,
CC prior to meiosis. Fades out at anther stage 6, during meiosis to
CC disappear later. Also present at low levels in the placenta of very
CC young pistils. {ECO:0000269|PubMed:12782723,
CC ECO:0000269|PubMed:14573517}.
CC -!- DISRUPTION PHENOTYPE: Male sterile that lacks pollen and undergoes an
CC aberrant male meiosis resulting in the formation of two uni- to tri-
CC nucleate cells instead of a normal tetrad, accompanied by aberrant
CC chromosomal organization from diplotene followed by metaphase 1 arrest.
CC After, male meiocytes exhibit signs of apoptosis, including defects in
CC chromosome behavior, cytoplasmic shrinkage, and chromatin
CC fragmentation, followed by cell death before cytokinesis. Reduced
CC expression of several condensin genes in meiocytes leading to defective
CC meiotic chromosome condensation in male meiocytes (PubMed:27385818,
CC PubMed:32572214). Increased H3K9me3 levels specifically in male
CC meiocytes leading to greater number of down-regulated than up-regulated
CC genes (PubMed:32572214). {ECO:0000269|PubMed:12782723,
CC ECO:0000269|PubMed:14573517, ECO:0000269|PubMed:27385818,
CC ECO:0000269|PubMed:32572214}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51303.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC026480; AAG51303.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34471.1; -; Genomic_DNA.
DR EMBL; AY305007; AAP69944.1; -; mRNA.
DR EMBL; AY158082; AAO16873.1; -; mRNA.
DR PIR; E96686; E96686.
DR RefSeq; NP_176791.2; NM_105288.2.
DR AlphaFoldDB; Q7X6Y7; -.
DR STRING; 3702.AT1G66170.1; -.
DR PaxDb; Q7X6Y7; -.
DR PRIDE; Q7X6Y7; -.
DR EnsemblPlants; AT1G66170.1; AT1G66170.1; AT1G66170.
DR GeneID; 842932; -.
DR Gramene; AT1G66170.1; AT1G66170.1; AT1G66170.
DR KEGG; ath:AT1G66170; -.
DR Araport; AT1G66170; -.
DR TAIR; locus:2013845; AT1G66170.
DR eggNOG; KOG1844; Eukaryota.
DR HOGENOM; CLU_012141_0_0_1; -.
DR InParanoid; Q7X6Y7; -.
DR OMA; GCPINPT; -.
DR OrthoDB; 659181at2759; -.
DR PhylomeDB; Q7X6Y7; -.
DR PRO; PR:Q7X6Y7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7X6Y7; baseline and differential.
DR Genevisible; Q7X6Y7; AT.
DR GO; GO:0000791; C:euchromatin; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IPI:TAIR.
DR GO; GO:1990188; F:euchromatin binding; IDA:TAIR.
DR GO; GO:0042393; F:histone binding; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:TAIR.
DR GO; GO:0007060; P:male meiosis chromosome segregation; IMP:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:TAIR.
DR GO; GO:0051321; P:meiotic cell cycle; IGI:TAIR.
DR GO; GO:0010032; P:meiotic chromosome condensation; IMP:UniProtKB.
DR GO; GO:0000212; P:meiotic spindle organization; IGI:TAIR.
DR GO; GO:0048235; P:pollen sperm cell differentiation; IMP:UniProtKB.
DR GO; GO:1905821; P:positive regulation of chromosome condensation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Meiosis; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..704
FT /note="PHD finger protein MALE MEIOCYTE DEATH 1"
FT /id="PRO_0000405994"
FT ZN_FING 606..656
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 609
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 611
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 627
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 632
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 635
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 653
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
SQ SEQUENCE 704 AA; 80812 MW; AD1B2ACFA6A399C4 CRC64;
MPVPIIETCR KRKRKPKVYN LQRFGEDGFP IQRNGAFRDQ IRVFLRDCAE IEDYDIRGMT
VWCTLLSHET KSSLIPLYIV EENVKHSSEP YCDHCRCTGW SNHFVSKRKY HFIIPIDTEW
SLPLEDDAFD SQSHVLHGLI HCNGFGHLVC VNGMESGSKY LCGREIVDFW DRLCNSLGAR
MITVEDLAKK RSVELRLLYG VAYGHSWFGR WGYKFCCGSF GVTKNEYENA IEALGSLEID
QIEFDFGELR QSKEINQVFR YYREMSEGHL KTFRDLLRFM LIIKSHASPQ KLLPVTPPLL
TDSPHQKRSS RLLLKKSDVA DNDKSPKYRN YSTVAANLGS RWPVRRLIFA AEVIVESLKE
MKALKQNGMT RQDVRDSARL HIGDTGLLDY VLKSMNNVVV GDVLVRRYVD PITRILHYTI
QDLDDAVKAK EPKKKEAVVL EEITPLRILT PLKPGADVYG DLLLLYTNVL LNYPESELVR
SATQAILDSK HFIKEWPIWD NNDTVLQFLC RINPSLVDVR SEQTTELPPG ELVTVPLQAT
VYDLKQAIEE TFRDTYCILS NFVVTEIDEV EEDMSLIGSC SALTVRGHGI DLESKLKCQG
GCDTWMVKCI CRARDDDGER MISCDVCEVW QHTRCCGIDD SDTLPPLFVC SNCCEEFAEQ
QRKVLQPKYE FPSSENVFLL ESADDFFGDQ RCLGMIFPEE NYLL
