CORT_DROME
ID CORT_DROME Reviewed; 483 AA.
AC Q960N3; Q9VMA1;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein cortex {ECO:0000303|PubMed:11252055};
GN Name=cort {ECO:0000303|PubMed:11252055}; ORFNames=CG11330;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF TYR-303 AND 431-TRP--ARG-483.
RX PubMed=11252055; DOI=10.1002/gene.1017;
RA Chu T., Henrion G., Haegeli V., Strickland S.;
RT "Cortex, a Drosophila gene required to complete oocyte meiosis, is a member
RT of the Cdc20/fizzy protein family.";
RL Genesis 29:141-152(2001).
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] OF 10-483.
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=10683177; DOI=10.1242/dev.127.6.1243;
RA Chen B., Harms E., Chu T., Henrion G., Strickland S.;
RT "Completion of meiosis in Drosophila oocytes requires transcriptional
RT control by grauzone, a new zinc finger protein.";
RL Development 127:1243-1251(2000).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=10924478; DOI=10.1093/genetics/155.4.1831;
RA Harms E., Chu T., Henrion G., Strickland S.;
RT "The only function of Grauzone required for Drosophila oocyte meiosis is
RT transcriptional activation of the cortex gene.";
RL Genetics 155:1831-1839(2000).
RN [7]
RP FUNCTION.
RX PubMed=17251266; DOI=10.1242/dev.02784;
RA Swan A., Schuepbach T.;
RT "The Cdc20 (Fzy)/Cdh1-related protein, Cort, cooperates with Fzy in cyclin
RT destruction and anaphase progression in meiosis I and II in Drosophila.";
RL Development 134:891-899(2007).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, DEGRADATION, INTERACTION WITH CDC16 AND
RP CDC27, AND MUTAGENESIS OF 424-ARG--ASN-432.
RX PubMed=18020708; DOI=10.1371/journal.pgen.0030202;
RA Pesin J.A., Orr-Weaver T.L.;
RT "Developmental role and regulation of cortex, a meiosis-specific anaphase-
RT promoting complex/cyclosome activator.";
RL PLoS Genet. 3:E202-E202(2007).
RN [9]
RP INTERACTION WITH MTRM.
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: Female meiosis-specific activator of the anaphase promoting
CC complex/cyclosome (APC/C) (PubMed:17251266, PubMed:18020708). Required
CC for the completion of meiosis in oocytes (PubMed:11252055,
CC PubMed:10683177, PubMed:10924478, PubMed:17251266, PubMed:18020708).
CC Activates the ubiquitin ligase activity and substrate specificity of
CC APC/C and triggers the sequential degradation of mitotic cyclins in
CC meiosis (PubMed:17251266, PubMed:18020708). Promotes the ubiquitination
CC and degradation of CycA early in meiosis I and the degradation of CycB
CC and CycB3 after egg activation (PubMed:18020708). Promotes degradation
CC of mtrm at the oocyte-to-embryo transition (PubMed:24019759).
CC {ECO:0000269|PubMed:10683177, ECO:0000269|PubMed:10924478,
CC ECO:0000269|PubMed:11252055, ECO:0000269|PubMed:17251266,
CC ECO:0000269|PubMed:18020708, ECO:0000269|PubMed:24019759}.
CC -!- SUBUNIT: Interacts with anaphase promoting complex/cyclosome (APC/C)
CC subunits Cdc16 and Cdc27 (PubMed:18020708). Interacts with mtrm
CC (PubMed:24019759). {ECO:0000269|PubMed:18020708,
CC ECO:0000269|PubMed:24019759}.
CC -!- INTERACTION:
CC Q960N3; Q23973: mtrm; NbExp=3; IntAct=EBI-3423056, EBI-166563;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11252055}.
CC -!- TISSUE SPECIFICITY: Highly expressed in ovaries. Expressed in nurse
CC cells from stage 6 to stage 12 egg chambers. As oocyte matures, it is
CC transferred from the nurse cells to the oocyte.
CC {ECO:0000269|PubMed:11252055}.
CC -!- DEVELOPMENTAL STAGE: Undetectable in early stage 1-8 egg chambers and
CC present at very low levels in stages 9-10B egg chambers. Strongly
CC increases in stage 12-13 egg chambers and remains high in mature stage
CC 14 oocytes (PubMed:18020708). Protein levels drop dramatically by the
CC time meiosis is completed in unfertilized eggs (at protein level)
CC (PubMed:18020708). {ECO:0000269|PubMed:18020708}.
CC -!- INDUCTION: Transcription is activated by grauzone (grau), which binds
CC to its promoter region. {ECO:0000269|PubMed:10683177,
CC ECO:0000269|PubMed:10924478}.
CC -!- PTM: Probably ubiquitinated: degraded following egg activation by the
CC anaphase promoting complex/cyclosome (APC/C).
CC {ECO:0000305|PubMed:18020708}.
CC -!- SIMILARITY: Belongs to the WD repeat CORT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93390.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY033478; AAK54464.1; -; mRNA.
DR EMBL; AE014134; AAF52421.1; -; Genomic_DNA.
DR EMBL; AY051966; AAK93390.1; ALT_INIT; mRNA.
DR RefSeq; NP_001260144.1; NM_001273215.1.
DR RefSeq; NP_523494.1; NM_078770.2.
DR AlphaFoldDB; Q960N3; -.
DR SMR; Q960N3; -.
DR BioGRID; 60090; 9.
DR DIP; DIP-60666N; -.
DR ELM; Q960N3; -.
DR IntAct; Q960N3; 8.
DR STRING; 7227.FBpp0078949; -.
DR PaxDb; Q960N3; -.
DR DNASU; 33937; -.
DR EnsemblMetazoa; FBtr0079320; FBpp0078949; FBgn0000351.
DR EnsemblMetazoa; FBtr0333350; FBpp0305542; FBgn0000351.
DR GeneID; 33937; -.
DR KEGG; dme:Dmel_CG11330; -.
DR UCSC; CG11330-RA; d. melanogaster.
DR CTD; 1325; -.
DR FlyBase; FBgn0000351; cort.
DR VEuPathDB; VectorBase:FBgn0000351; -.
DR eggNOG; KOG0305; Eukaryota.
DR HOGENOM; CLU_039771_0_0_1; -.
DR InParanoid; Q960N3; -.
DR OMA; SYWRQSG; -.
DR OrthoDB; 948748at2759; -.
DR PhylomeDB; Q960N3; -.
DR BioGRID-ORCS; 33937; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33937; -.
DR PRO; PR:Q960N3; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000351; Expressed in secondary oocyte and 10 other tissues.
DR ExpressionAtlas; Q960N3; baseline and differential.
DR Genevisible; Q960N3; DM.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IPI:FlyBase.
DR GO; GO:1990757; F:ubiquitin ligase activator activity; IBA:GO_Central.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; HMP:FlyBase.
DR GO; GO:0007343; P:egg activation; IMP:FlyBase.
DR GO; GO:0007144; P:female meiosis I; IGI:FlyBase.
DR GO; GO:0007147; P:female meiosis II; IMP:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0045143; P:homologous chromosome segregation; TAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007279; P:pole cell formation; HMP:FlyBase.
DR GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IMP:FlyBase.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IMP:FlyBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR033010; Cdc20/Fizzy.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19918; PTHR19918; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Meiosis; Oogenesis;
KW Reference proteome; Repeat; Ubl conjugation; WD repeat.
FT CHAIN 1..483
FT /note="Protein cortex"
FT /id="PRO_0000050941"
FT REPEAT 158..195
FT /note="WD 1"
FT REPEAT 196..237
FT /note="WD 2"
FT REPEAT 245..284
FT /note="WD 3"
FT REPEAT 287..326
FT /note="WD 4"
FT REPEAT 421..460
FT /note="WD 5"
FT MOTIF 424..432
FT /note="D-box"
FT /evidence="ECO:0000269|PubMed:18020708"
FT MUTAGEN 303
FT /note="Y->C: In QW55; abnormal arrest in female meiosis."
FT /evidence="ECO:0000269|PubMed:11252055"
FT MUTAGEN 424..432
FT /note="RGTLFLMWN->AGTAFLMWA: Prevents degradation following
FT egg activation."
FT /evidence="ECO:0000269|PubMed:18020708"
FT MUTAGEN 431..483
FT /note="Missing: In RH65; abnormal arrest in female
FT meiosis."
FT /evidence="ECO:0000269|PubMed:11252055"
SQ SEQUENCE 483 AA; 55575 MW; 007DD0190DE06735 CRC64;
MFVEMSVCDS PNKNSKLDKK SLTPFKKVRR KNWKQEAAYK SDTSKGQEVS YVGERFIPNR
FERENIEFNL KYIGKRKERD ILETGVTLTA SYWRQSGFIS NINRTFGIGE RRLFQFSSQQ
GTRSRVVDND SADSDWPCNP RARPYAIQNA THEMPGICSP VDYNMMDWSS GGMVAMSSGQ
DVMLWRNLDE STMVFSVESP TSLKYSPDGK HLAIGCMDRN YPVLDLWEVR SPTEFLVSYR
KLFFKSMGYI SCIEWSHDGK EVICGTQCGV IIVLAMPTLN TLMQLREHRH TVKKMKFAPT
HKYFASSDTD GKIFIFDAVL KVRLLKLDGR SIVFDWHPWT GEDLAVAERS PASIFIFNIP
RRQFVASYRR RDDRIVIKTL TYSKITGELL VNVIRRDDAD LAVCEILVLA SLNRVVDLMS
HQDRGTLFLM WNPDGTKIAT GGLDDTFSLW NFFPTYKREA ILRKQEQKAK DKCSSLSLYK
GIR
