CHRD1_DROME
ID CHRD1_DROME Reviewed; 354 AA.
AC Q9VCC0; Q9U4A3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cysteine and histidine-rich domain-containing protein morgana {ECO:0000303|PubMed:20230755};
GN Name=mora {ECO:0000303|PubMed:20230755, ECO:0000312|FlyBase:FBgn0029503};
GN Synonyms=CHORD {ECO:0000303|PubMed:10571178};
GN ORFNames=CG6198 {ECO:0000312|FlyBase:FBgn0029503};
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].
RX PubMed=10571178; DOI=10.1016/s0092-8674(00)81522-6;
RA Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C., Schulze-Lefert P.;
RT "A novel class of eukaryotic zinc-binding proteins is required for disease
RT resistance signaling in barley and development in C. elegans.";
RL Cell 99:355-366(1999).
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;
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 DISRUPTION PHENOTYPE.
RX PubMed=20230755; DOI=10.1016/j.devcel.2009.12.020;
RA Ferretti R., Palumbo V., Di Savino A., Velasco S., Sbroggio M.,
RA Sportoletti P., Micale L., Turco E., Silengo L., Palumbo G., Hirsch E.,
RA Teruya-Feldstein J., Bonaccorsi S., Pandolfi P.P., Gatti M., Tarone G.,
RA Brancaccio M.;
RT "Morgana/chp-1, a ROCK inhibitor involved in centrosome duplication and
RT tumorigenesis.";
RL Dev. Cell 18:486-495(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-339, 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 [8]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 172-MET--ASP-354.
RX PubMed=24643112; DOI=10.1038/srep04415;
RA Shimono K., Fujishima K., Nomura T., Ohashi M., Usui T., Kengaku M.,
RA Toyoda A., Uemura T.;
RT "An evolutionarily conserved protein CHORD regulates scaling of dendritic
RT arbors with body size.";
RL Sci. Rep. 4:4415-4415(2014).
RN [9]
RP FUNCTION, INTERACTION WITH HSP83, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=31907206; DOI=10.1242/jcs.236786;
RA Palumbo V., Tariq A., Borgal L., Metz J., Brancaccio M., Gatti M.,
RA Wakefield J.G., Bonaccorsi S.;
RT "Drosophila Morgana is an Hsp90-interacting protein with a direct role in
RT microtubule polymerisation.";
RL J. Cell Sci. 133:0-0(2020).
CC -!- FUNCTION: Regulates centrosome duplication and mitotic spindle dynamics
CC (PubMed:20230755, PubMed:31907206). Also involved in controlling the
CC size of dendritic arbors (PubMed:24643112). May act as co-chaperone for
CC Hsp83 (PubMed:31907206). During mitotic spindle assembly, regulates
CC microtubule (MT) dynamics by binding to MTs and promoting MT
CC polymerisation (PubMed:31907206). Promotes the elongation and
CC retraction of terminal branches in response to changes in body size,
CC possibly acting downstream of the TORC2 pathway to enable proportional
CC scaling of dendritic arbors (PubMed:24643112).
CC {ECO:0000269|PubMed:20230755, ECO:0000269|PubMed:24643112,
CC ECO:0000269|PubMed:31907206}.
CC -!- SUBUNIT: Interacts with Hsp83. {ECO:0000269|PubMed:31907206}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31907206}. Nucleus
CC {ECO:0000269|PubMed:31907206}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:31907206}. Note=In syncytial embryos, mostly
CC cytoplasmic during interphase, with enrichment in the perinuclear area
CC and a weak nuclear localization. Upon nuclear envelope breakdown,
CC localizes to the spindles and remains associated with the spindle
CC microtubules throughout mitosis. {ECO:0000269|PubMed:31907206}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (PubMed:31907206). Expressed
CC in larvae (PubMed:24643112). {ECO:0000269|PubMed:24643112,
CC ECO:0000269|PubMed:31907206}.
CC -!- DISRUPTION PHENOTYPE: Results in centrosome amplification and lethality
CC (PubMed:20230755). Cells become polyploid or undergo apoptosis
CC (PubMed:20230755). Homozygotes died as third instar larvae
CC (PubMed:20230755). RNAi-mediated knockdown in neuronal cells, results
CC in severe mitotic defects in the larval brain and is lethal at the
CC third-instar stage (PubMed:31907206). RNAi-mediated knockdown in the
CC female germline, results in embryos failing to hatch due to various
CC mitotic defects such as abnormal chromosome condensation and adherent
CC spindle formation (PubMed:31907206). However, in contrast to RNAi-
CC mediated knockdown in the brain, embryos do not exhibit centrosome
CC amplification (PubMed:31907206). {ECO:0000269|PubMed:20230755,
CC ECO:0000269|PubMed:31907206}.
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DR EMBL; AF192465; AAF18436.1; -; mRNA.
DR EMBL; AE014297; AAF56252.1; -; Genomic_DNA.
DR EMBL; AY070947; AAL48569.1; -; mRNA.
DR RefSeq; NP_651226.1; NM_142969.4.
DR AlphaFoldDB; Q9VCC0; -.
DR SMR; Q9VCC0; -.
DR BioGRID; 67806; 5.
DR IntAct; Q9VCC0; 1.
DR STRING; 7227.FBpp0083939; -.
DR iPTMnet; Q9VCC0; -.
DR PaxDb; Q9VCC0; -.
DR PRIDE; Q9VCC0; -.
DR DNASU; 42874; -.
DR EnsemblMetazoa; FBtr0084554; FBpp0083939; FBgn0029503.
DR GeneID; 42874; -.
DR KEGG; dme:Dmel_CG6198; -.
DR UCSC; CG6198-RA; d. melanogaster.
DR CTD; 42874; -.
DR FlyBase; FBgn0029503; mora.
DR VEuPathDB; VectorBase:FBgn0029503; -.
DR eggNOG; KOG1667; Eukaryota.
DR GeneTree; ENSGT00940000159429; -.
DR HOGENOM; CLU_040079_0_0_1; -.
DR InParanoid; Q9VCC0; -.
DR OMA; TVRNDFY; -.
DR OrthoDB; 1163528at2759; -.
DR PhylomeDB; Q9VCC0; -.
DR BioGRID-ORCS; 42874; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42874; -.
DR PRO; PR:Q9VCC0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0029503; Expressed in egg chamber and 26 other tissues.
DR Genevisible; Q9VCC0; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0051298; P:centrosome duplication; IMP:FlyBase.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
DR GO; GO:0008361; P:regulation of cell size; IMP:FlyBase.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:FlyBase.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007051; CHORD_dom.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR Pfam; PF04968; CHORD; 2.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51401; CHORD; 2.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..354
FT /note="Cysteine and histidine-rich domain-containing
FT protein morgana"
FT /id="PRO_0000402803"
FT DOMAIN 4..63
FT /note="CHORD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 140..199
FT /note="CHORD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 210..301
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT BINDING 4
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 172..354
FT /note="Missing: Early larval lethal. Homozygous neurons
FT (generated by mosaic analysis) display decreased
FT elongation/retraction rate of terminal branches, resulting
FT in small dendritic arbors regardless of pupal body size
FT and/or nutritional input. Also in both fed and starved
FT pupae, dendritic segment length is decreased without
FT simplifying the branching pattern."
FT /evidence="ECO:0000269|PubMed:24643112"
FT CONFLICT 288
FT /note="K -> T (in Ref. 1; AAF18436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40240 MW; D0EC003F1F70C63C CRC64;
MEQCYNRGCG QLFDPQTNND ESCRHHPGEP FFHDAYKGWS CCNKKSVDFT EFLNIKGCTL
AKHSNVKPPE PEKPVKDESD KDEVIEVRAP IREALPRPPI DSPLTVIQPT VAPALKDMVF
AVKTPAAQKS SDAIEVGTTC KNNGCTYSFT GNSSDFGECT YHPGVPIFHE GMKFWSCCQK
RTSDFSQFMA QKGCTYGEHK WVKENDDKKV VQCRYDWHQT ATNVVMAIYA KKYDYSQSVI
ELNPIRLHVN LVFPEQDNAR FDLDLELRGI VNVSNASAHM YGTKVEIKLP KLEPGSWSNL
NFPNKKLPVV KKSQVEEKKK QEESDEEFFD LDDIKAETSF RLSEMSMQSP NNLD
