MTRM_DROME
ID MTRM_DROME Reviewed; 217 AA.
AC Q23973; B6UX71; B6UX75; B6UX76; B6UX77; B6UX82; B6UX83; B6UX94; Q9VSJ7;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein matrimony {ECO:0000303|PubMed:14573476};
DE AltName: Full=Cell cycle arrest protein D52;
GN Name=mtrm {ECO:0000303|PubMed:14573476}; Synonyms=anon-D52;
GN ORFNames=CG18543;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sevelin {ECO:0000305}; TISSUE=Embryo {ECO:0000305};
RA Edgar B.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-89 INS; GLN-GLN-89 INS;
RP MET-113 AND THR-190.
RC STRAIN=MW11, MW27, MW56, MW6, MW63, NC301, NC303, NC304, NC306, NC319,
RC NC322, NC335, NC336, NC357, NC358, NC359, NC361, NC362, NC390, NC397,
RC NC399, NC732, NC740, and NC774;
RX PubMed=18984573; DOI=10.1534/genetics.108.093807;
RA Anderson J.A., Gilliland W.D., Langley C.H.;
RT "Molecular population genetics and evolution of Drosophila meiosis genes.";
RL Genetics 181:177-185(2009).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6] {ECO:0000305}
RP SEQUENCE REVISION.
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14573476; DOI=10.1093/genetics/165.2.637;
RA Harris D., Orme C., Kramer J., Namba L., Champion M., Palladino M.J.,
RA Natzle J., Hawley R.S.;
RT "A deficiency screen of the major autosomes identifies a gene (matrimony)
RT that is haplo-insufficient for achiasmate segregation in Drosophila
RT oocytes.";
RL Genetics 165:637-652(2003).
RN [8]
RP FUNCTION, INTERACTION WITH POLO, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF THR-40 AND SER-124.
RX PubMed=18052611; DOI=10.1371/journal.pbio.0050323;
RA Xiang Y., Takeo S., Florens L., Hughes S.E., Huo L.J., Gilliland W.D.,
RA Swanson S.K., Teeter K., Schwartz J.W., Washburn M.P., Jaspersen S.L.,
RA Hawley R.S.;
RT "The inhibition of polo kinase by matrimony maintains G2 arrest in the
RT meiotic cell cycle.";
RL PLoS Biol. 5:E323-E323(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-66, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [10]
RP DEGRADATION, INTERACTION WITH CORT, AND MUTAGENESIS OF LEU-21; ARG-95;
RP GLY-170 AND ARG-193.
RX PubMed=24019759; DOI=10.1371/journal.pbio.1001648;
RA Whitfield Z.J., Chisholm J., Hawley R.S., Orr-Weaver T.L.;
RT "A meiosis-specific form of the APC/C promotes the oocyte-to-embryo
RT transition by decreasing levels of the Polo kinase inhibitor matrimony.";
RL PLoS Biol. 11:E1001648-E1001648(2013).
CC -!- FUNCTION: Polo kinase inhibitor required to maintain G2 arrest in the
CC meiotic cell cycle in females (PubMed:18052611). Holds
CC heterochromatically paired homologs together from the end of pachytene
CC until metaphase I (PubMed:14573476). Haploinsufficient locus for
CC homologous achiasmate segregation and may be required for the
CC maintenance of heterochromatic pairings (PubMed:14573476).
CC {ECO:0000269|PubMed:14573476, ECO:0000269|PubMed:18052611}.
CC -!- SUBUNIT: Interacts with polo (PubMed:18052611). Interacts with cort
CC (PubMed:24019759). {ECO:0000269|PubMed:18052611,
CC ECO:0000269|PubMed:24019759}.
CC -!- INTERACTION:
CC Q23973; Q960N3: cort; NbExp=3; IntAct=EBI-166563, EBI-3423056;
CC Q23973; P52304: polo; NbExp=4; IntAct=EBI-166563, EBI-163922;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14573476}. Chromosome
CC {ECO:0000269|PubMed:14573476}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the end of pachytene until the
CC completion of meiosis I. {ECO:0000269|PubMed:18052611}.
CC -!- PTM: Probably ubiquitinated: degraded during the oocyte-to-embryo
CC transition by the anaphase promoting complex/cyclosome (APC/C)
CC containing cort protein. {ECO:0000305|PubMed:24019759}.
CC -!- DISRUPTION PHENOTYPE: Mutants exhibit a strong dominant effect on
CC achiasmate segregation, inducing both X and fourth chromosome non-
CC disjunction in females (PubMed:14573476). Precocious nuclear envelope
CC breakdown in oocytes, due to defects in meiotic arrest in G2
CC (PubMed:18052611). {ECO:0000269|PubMed:14573476,
CC ECO:0000269|PubMed:18052611}.
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DR EMBL; U03288; AAA03463.1; -; Genomic_DNA.
DR EMBL; FJ219119; ACI97170.1; -; Genomic_DNA.
DR EMBL; FJ219123; ACI97174.1; -; Genomic_DNA.
DR EMBL; FJ219124; ACI97175.1; -; Genomic_DNA.
DR EMBL; FJ219125; ACI97176.1; -; Genomic_DNA.
DR EMBL; FJ219126; ACI97177.1; -; Genomic_DNA.
DR EMBL; FJ219127; ACI97178.1; -; Genomic_DNA.
DR EMBL; FJ219128; ACI97179.1; -; Genomic_DNA.
DR EMBL; FJ219129; ACI97180.1; -; Genomic_DNA.
DR EMBL; FJ219130; ACI97181.1; -; Genomic_DNA.
DR EMBL; FJ219131; ACI97182.1; -; Genomic_DNA.
DR EMBL; FJ219132; ACI97183.1; -; Genomic_DNA.
DR EMBL; FJ219133; ACI97184.1; -; Genomic_DNA.
DR EMBL; FJ219134; ACI97185.1; -; Genomic_DNA.
DR EMBL; FJ219135; ACI97186.1; -; Genomic_DNA.
DR EMBL; FJ219136; ACI97187.1; -; Genomic_DNA.
DR EMBL; FJ219137; ACI97188.1; -; Genomic_DNA.
DR EMBL; FJ219138; ACI97189.1; -; Genomic_DNA.
DR EMBL; FJ219139; ACI97190.1; -; Genomic_DNA.
DR EMBL; FJ219140; ACI97191.1; -; Genomic_DNA.
DR EMBL; FJ219141; ACI97192.1; -; Genomic_DNA.
DR EMBL; FJ219142; ACI97193.1; -; Genomic_DNA.
DR EMBL; FJ219143; ACI97194.1; -; Genomic_DNA.
DR EMBL; FJ219144; ACI97195.1; -; Genomic_DNA.
DR EMBL; FJ219145; ACI97196.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50422.1; -; Genomic_DNA.
DR EMBL; AY061524; AAL29072.3; -; mRNA.
DR RefSeq; NP_648223.1; NM_139966.3.
DR AlphaFoldDB; Q23973; -.
DR SMR; Q23973; -.
DR BioGRID; 64371; 7.
DR DIP; DIP-22904N; -.
DR IntAct; Q23973; 2.
DR STRING; 7227.FBpp0076340; -.
DR iPTMnet; Q23973; -.
DR PaxDb; Q23973; -.
DR PRIDE; Q23973; -.
DR DNASU; 38958; -.
DR EnsemblMetazoa; FBtr0076613; FBpp0076340; FBgn0010431.
DR GeneID; 38958; -.
DR KEGG; dme:Dmel_CG18543; -.
DR UCSC; CG18543-RA; d. melanogaster.
DR CTD; 38958; -.
DR FlyBase; FBgn0010431; mtrm.
DR VEuPathDB; VectorBase:FBgn0010431; -.
DR eggNOG; ENOG502RVWY; Eukaryota.
DR HOGENOM; CLU_1273428_0_0_1; -.
DR InParanoid; Q23973; -.
DR OMA; RNDEDCN; -.
DR OrthoDB; 1378366at2759; -.
DR PhylomeDB; Q23973; -.
DR SignaLink; Q23973; -.
DR BioGRID-ORCS; 38958; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38958; -.
DR PRO; PR:Q23973; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0010431; Expressed in secondary oocyte and 18 other tissues.
DR Genevisible; Q23973; DM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032837; P:distributive segregation; IMP:FlyBase.
DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP:FlyBase.
DR GO; GO:0045143; P:homologous chromosome segregation; IMP:UniProtKB.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IMP:FlyBase.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chromosome; DNA-binding; Meiosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..217
FT /note="Protein matrimony"
FT /id="PRO_0000096635"
FT DOMAIN 157..217
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184,
FT ECO:0000305"
FT REGION 83..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..41
FT /note="POLO box domain (PBD)-binding"
FT /evidence="ECO:0000269|PubMed:18052611"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 89
FT /note="Q -> QQ (in strain: NC335, NC390, NC397 and NC774)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 89
FT /note="Q -> QQQ (in strain: NC336 and MW6)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 113
FT /note="I -> M (in strain: MW11)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 190
FT /note="S -> T (in strain: NC303 and NC399)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT MUTAGEN 21
FT /note="L->A: Decreased degradation during the oocyte-to-
FT embryo transition."
FT /evidence="ECO:0000269|PubMed:24019759"
FT MUTAGEN 40
FT /note="T->A: Abolishes interaction with polo and ability to
FT maintain G2 arrest."
FT /evidence="ECO:0000269|PubMed:18052611"
FT MUTAGEN 95
FT /note="R->A: No effect on degradation during the oocyte-to-
FT embryo transition; when associated with A-193."
FT /evidence="ECO:0000269|PubMed:24019759"
FT MUTAGEN 124
FT /note="S->A: Does not affect interaction with polo."
FT /evidence="ECO:0000269|PubMed:18052611"
FT MUTAGEN 170
FT /note="G->A: No effect on degradation during the oocyte-to-
FT embryo transition."
FT /evidence="ECO:0000269|PubMed:24019759"
FT MUTAGEN 193
FT /note="R->A: No effect on degradation during the oocyte-to-
FT embryo transition; when associated with A-95."
FT /evidence="ECO:0000269|PubMed:24019759"
FT CONFLICT 98
FT /note="L -> F (in Ref. 1; AAA03463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 24780 MW; 5F630F759BB1362C CRC64;
MENSRTPTNK TKITLNRTPT LKERRWNTLK VNTSNVRCST PIFGNFRSPN LSPIENMGTK
GKSPVSPMRF ATFKKVPTKV HPKQQQQQQH QHCHRTQLKP PPFVLPKPQE EIIEPEREIK
SCSSPDTCSD DSNMETSLAL ESRRRSIKAS NHSYVVNHAA NVEQILMHMG LENYVTNFEE
AHIDLVELAS LERADLVKIG LNTDEDCNRI MDVLHTL
