YEMA_DROME
ID YEMA_DROME Reviewed; 1002 AA.
AC P25992; Q6AWM5; Q9VAP4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=yemanuclein {ECO:0000312|FlyBase:FBgn0005596};
DE AltName: Full=Yemanuclein-alpha {ECO:0000303|PubMed:1606021};
GN Name=yem {ECO:0000312|FlyBase:FBgn0005596};
GN Synonyms=yema {ECO:0000312|FlyBase:FBgn0005596},
GN yemalpha {ECO:0000303|PubMed:1606021}, yG4.5;
GN ORFNames=CG14513 {ECO:0000312|FlyBase:FBgn0005596};
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=1606021; DOI=10.1016/0925-4773(92)90016-d;
RA Ait-Ahmed O., Bellon B., Capri M., Joblet C., Thomas-Delaage M.;
RT "The yemanuclein-alpha: a new Drosophila DNA binding protein specific for
RT the oocyte nucleus.";
RL Mech. Dev. 37:69-80(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685; SER-689; SER-885;
RP SER-886 AND SER-887, AND 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF VAL-478.
RX PubMed=21080953; DOI=10.1186/1471-2156-11-104;
RA Meyer R.E., Delaage M., Rosset R., Capri M., Ait-Ahmed O.;
RT "A single mutation results in diploid gamete formation and parthenogenesis
RT in a Drosophila yemanuclein-alpha meiosis I defective mutant.";
RL BMC Genet. 11:104-104(2010).
CC -!- FUNCTION: May play a key role in egg organization. May be a
CC transcriptional regulator having a role in chromatin remodeling in
CC concert with Hira, a histone chaperone. Involved in chromosome
CC segregation by affecting kinetochores function in the first meiotic
CC division. {ECO:0000269|PubMed:1606021, ECO:0000269|PubMed:21080953}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Chromosome. Chromosome,
CC centromere, kinetochore. Note=Abundant in the nucleoplasm. Only a
CC fraction of the protein is associated with the chromosomes. Localizes
CC to the chromosome arms and coexpresses with cid at the centromere.
CC -!- TISSUE SPECIFICITY: Oocyte specific. {ECO:0000269|PubMed:1606021,
CC ECO:0000269|PubMed:21080953}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed at all oogenic stages. {ECO:0000269|PubMed:1606021}.
CC -!- PTM: The N-terminus is blocked.
CC -!- DISRUPTION PHENOTYPE: Females exhibit disrupted chromosome segregation
CC in the first meiotic division and produce very low numbers of viable
CC progeny. This female sterility is partially suppressed when some
CC oocytes undergo precocious anaphase. Analysis of the X chromosome of
CC these progeny demonstrates they have inherited the two maternal X-
CC chromosome homologs and have no paternal chromosome markers. This
CC suggests that they developed from diploid gametes that underwent
CC gynogenesis, a form of parthenogenesis that requires fertilization.
CC {ECO:0000269|PubMed:21080953}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT94452.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X63503; CAA45074.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56858.2; -; Genomic_DNA.
DR EMBL; BT015223; AAT94452.1; ALT_FRAME; mRNA.
DR PIR; A56678; A56678.
DR RefSeq; NP_476893.1; NM_057545.4.
DR AlphaFoldDB; P25992; -.
DR BioGRID; 68310; 11.
DR DIP; DIP-21793N; -.
DR IntAct; P25992; 10.
DR STRING; 7227.FBpp0084784; -.
DR iPTMnet; P25992; -.
DR PaxDb; P25992; -.
DR EnsemblMetazoa; FBtr0085415; FBpp0084784; FBgn0005596.
DR GeneID; 43439; -.
DR KEGG; dme:Dmel_CG14513; -.
DR CTD; 43439; -.
DR FlyBase; FBgn0005596; yem.
DR VEuPathDB; VectorBase:FBgn0005596; -.
DR eggNOG; KOG4786; Eukaryota.
DR HOGENOM; CLU_282458_0_0_1; -.
DR InParanoid; P25992; -.
DR OMA; RSRDMCG; -.
DR OrthoDB; 349398at2759; -.
DR PhylomeDB; P25992; -.
DR BioGRID-ORCS; 43439; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43439; -.
DR PRO; PR:P25992; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0005596; Expressed in secondary oocyte and 41 other tissues.
DR ExpressionAtlas; P25992; baseline and differential.
DR Genevisible; P25992; DM.
DR GO; GO:0042585; C:germinal vesicle; IDA:FlyBase.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:0001940; C:male pronucleus; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IBA:GO_Central.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0035042; P:fertilization, exchange of chromosomal proteins; IMP:FlyBase.
DR InterPro; IPR014840; HRD.
DR InterPro; IPR026947; UBN_middle_dom.
DR Pfam; PF08729; HUN; 1.
DR Pfam; PF14075; UBN_AB; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromosome; DNA-binding; Kinetochore; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1002
FT /note="yemanuclein"
FT /id="PRO_0000066201"
FT REPEAT 230..241
FT /note="1"
FT REPEAT 242..253
FT /note="2"
FT REGION 193..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..253
FT /note="2 X 12 AA tandem repeats"
FT REGION 395..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 80..85
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 217..259
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 698
FT /note="S -> L"
FT MUTAGEN 478
FT /note="V->E: Displays defects in aligning on the meiotic
FT spindle."
FT /evidence="ECO:0000269|PubMed:21080953"
SQ SEQUENCE 1002 AA; 109311 MW; EE69A384EBA24D2F CRC64;
MSKGGEHKRV TLTSIIQGDA GFSRFGSNIL EPDAASAAPD NSSKPTTKTA KCIRIKLDLF
ETDSNKYPEF NYSRLLYLEK KKTKKLKQVS TTNGSASTDP FADNDDDVAR IVKELEAKYG
NSYATGRGKS KKDDYRDIGM GYDESDSFID NTEAYDEIIP EEAETLEGGF YINCGALEFK
NLTKKSYTTR TDAIIKMPER SRKRMVSSSS ESSSSSSGDD DENDDGNNEE DDESDSEDDS
EENDESDSED DSESESLEDE DSAATAKSSS KYKDNHQAKR AKVIVTGKSK PSSSSLTSGK
KPPTKPITTS SSSNSPRPST VEISDTEDGQ DPIQTQPSSQ LQSLPQSQAQ AQALKKVVKT
TTVKDMLKAK RDSFLKSQSG TAAVKGVGNG ELKCVSTDVS SSDSSDMESE HGRADRQAGQ
HGKDGQENLR TADTLLPTTL DADIVTAVNS FKEAVKSRDM CGKKFNLDVK LSPLLLRVYE
AVLCTDRNER NMVFSHIEYQ LQLPKYYMLR KGKQVRAKEE KRKSTIMLEK LRRAVAVVMP
KAVANYETEL RTFAEQAAAD VNSELPPKMP RKKFQWTSEL RHLLYDVYQA RWTSYAFLAK
RKESLEEFIN WYLKEKVVEL WPPGWMRLDE LQREITRYKN AKLKAKEKPK APPASASPKP
VGVVSAPEQM PPASSYLKAV EDPRSRGNSD TDSATSASSN SLKRKLKEMP KQTSKPPKKK
VAKQVPLQPQ LTPHPQFQLA PAATAAVSIP AISNNNNHLP HLDTLLSMPS TSAQAAALNA
AAVAAASTVL DLASPSRKID LNTSNNFYNL ITAASLAASG NPSPHSGDGQ AKVIVGARPS
PHVINLDDYQ CTSDILQTSK QLAATTTVIT AISKAAQTTS VARESSSESD GVEIVGVFPA
SKPQKKVQSK PKNKTQNRGR SSLGAVGQVN GSLGYSANNM YIYNSPRTLG PVYDLTDPHI
MKTMSNLKEM EKQFIQAAFS PNSVKGASGG MGSSAPSTPT RQ
