CHRD1_MOUSE
ID CHRD1_MOUSE Reviewed; 331 AA.
AC Q9D1P4; Q9CSI5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cysteine and histidine-rich domain-containing protein 1;
DE AltName: Full=CHORD domain-containing protein 1;
DE Short=CHORD-containing protein 1;
DE Short=Chp-1;
DE AltName: Full=Protein morgana;
GN Name=Chordc1; Synonyms=Chp1, Morgana;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=12965203; DOI=10.1016/s0014-5793(03)00892-5;
RA Brancaccio M., Menini N., Bongioanni D., Ferretti R., De Acetis M.,
RA Silengo L., Tarone G.;
RT "Chp-1 and melusin, two CHORD containing proteins in vertebrates.";
RL FEBS Lett. 551:47-52(2003).
RN [4]
RP INTERACTION WITH HSP90AB1.
RX PubMed=15642353; DOI=10.1016/j.febslet.2004.12.005;
RA Wu J., Luo S., Jiang H., Li H.;
RT "Mammalian CHORD-containing protein 1 is a novel heat shock protein 90-
RT interacting protein.";
RL FEBS Lett. 579:421-426(2005).
RN [5]
RP INTERACTION WITH HSP90AA1 AND PPP5C, FUNCTION, AND INDUCTION.
RX PubMed=16083881; DOI=10.1016/j.febslet.2005.07.024;
RA Hahn J.-S.;
RT "Regulation of Nod1 by Hsp90 chaperone complex.";
RL FEBS Lett. 579:4513-4519(2005).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17253150; DOI=10.1007/s11064-006-9271-z;
RA Gerstner J.R., Landry C.F.;
RT "The zinc-binding protein chordc1 undergoes complex diurnal changes in mRNA
RT expression during mouse brain development.";
RL Neurochem. Res. 32:241-250(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP FUNCTION.
RX PubMed=20493909; DOI=10.1016/j.bbamcr.2010.05.005;
RA Michowski W., Ferretti R., Wisniewska M.B., Ambrozkiewicz M.,
RA Beresewicz M., Fusella F., Skibinska-Kijek A., Zablocka B., Brancaccio M.,
RA Tarone G., Kuznicki J.;
RT "Morgana/CHP-1 is a novel chaperone able to protect cells from stress.";
RL Biochim. Biophys. Acta 1803:1043-1049(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
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).
CC -!- FUNCTION: Regulates centrosome duplication, probably by inhibiting the
CC kinase activity of ROCK2 (PubMed:20230755). Proposed to act as co-
CC chaperone for HSP90 (PubMed:16083881). May play a role in the
CC regulation of NOD1 via a HSP90 chaperone complex (PubMed:16083881). In
CC vitro, has intrinsic chaperone activity (PubMed:20230755). This
CC function may be achieved by inhibiting association of ROCK2 with NPM1
CC (PubMed:20230755). Plays a role in ensuring the localization of the
CC tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures
CC the subsequent regulation of EGFR activity and EGF-induced actin
CC cytoskeleton remodeling (By similarity). Involved in stress response
CC (PubMed:20493909). Prevents tumorigenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9UHD1, ECO:0000269|PubMed:16083881,
CC ECO:0000269|PubMed:20230755, ECO:0000269|PubMed:20493909}.
CC -!- SUBUNIT: Interacts with HSP90AA1, HSP90AB1 and PPP5C. Interacts with
CC ROCK1 and ROCK2 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in spleen,
CC lung and brain (at protein level). Expressed in proliferating myoblasts
CC and its expression remained steady after. Its expression undergoes
CC diurnal and circadian changes in hypothalamus. Highly expressed during
CC the dark-light transition (ZT20.5 (zeitgeber time 20.5) and ZT2.5).
CC {ECO:0000269|PubMed:12965203, ECO:0000269|PubMed:17253150}.
CC -!- DEVELOPMENTAL STAGE: Weakly expressed at ZT8.5 and highly expressed at
CC ZT14.5 at P6. At P6 highly expressed at ZT14.5 in hippocampus,
CC prefrontal cortex and cerebellum. First detected and widely distributed
CC at P1 and that continued throughout postnatal development. Expression
CC is evident in the cortical plate (CP) at 17 dpc. Lower levels of
CC expression is also evident in intermediate (IZ) and subventricular
CC (SVZ) zones at this age. A more diffuse expression pattern is evident
CC in early postnatal cortex with only slight differences in intensity
CC throughout cortical layers. By P14, a more laminated distribution
CC pattern becomes evident with a punctate distribution apparent in deep
CC cortical layers. {ECO:0000269|PubMed:17253150}.
CC -!- INDUCTION: By Heat shock in a HSF1-dependent manner.
CC {ECO:0000269|PubMed:16083881}.
CC -!- DISRUPTION PHENOTYPE: Results in centrosome amplification and
CC lethality. Cells become polyploid or undergo apoptosis. Embryos are no
CC longer detected after 3.5 dpc. {ECO:0000269|PubMed:20230755}.
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DR EMBL; AK003259; BAB22675.1; -; mRNA.
DR EMBL; AK012747; BAB28444.1; -; mRNA.
DR EMBL; AK132696; BAE21307.1; -; mRNA.
DR EMBL; BC018374; AAH18374.1; -; mRNA.
DR CCDS; CCDS22842.1; -.
DR RefSeq; NP_080120.1; NM_025844.2.
DR AlphaFoldDB; Q9D1P4; -.
DR SMR; Q9D1P4; -.
DR BioGRID; 211809; 22.
DR IntAct; Q9D1P4; 1.
DR MINT; Q9D1P4; -.
DR STRING; 10090.ENSMUSP00000001825; -.
DR iPTMnet; Q9D1P4; -.
DR PhosphoSitePlus; Q9D1P4; -.
DR SwissPalm; Q9D1P4; -.
DR EPD; Q9D1P4; -.
DR jPOST; Q9D1P4; -.
DR MaxQB; Q9D1P4; -.
DR PaxDb; Q9D1P4; -.
DR PeptideAtlas; Q9D1P4; -.
DR PRIDE; Q9D1P4; -.
DR ProteomicsDB; 283833; -.
DR Antibodypedia; 31553; 209 antibodies from 28 providers.
DR DNASU; 66917; -.
DR Ensembl; ENSMUST00000001825; ENSMUSP00000001825; ENSMUSG00000001774.
DR GeneID; 66917; -.
DR KEGG; mmu:66917; -.
DR UCSC; uc009ogm.1; mouse.
DR CTD; 26973; -.
DR MGI; MGI:1914167; Chordc1.
DR VEuPathDB; HostDB:ENSMUSG00000001774; -.
DR eggNOG; KOG1667; Eukaryota.
DR GeneTree; ENSGT00940000154174; -.
DR HOGENOM; CLU_040079_0_0_1; -.
DR InParanoid; Q9D1P4; -.
DR OMA; MKQWSCC; -.
DR OrthoDB; 1163528at2759; -.
DR PhylomeDB; Q9D1P4; -.
DR TreeFam; TF105394; -.
DR BioGRID-ORCS; 66917; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Chordc1; mouse.
DR PRO; PR:Q9D1P4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D1P4; protein.
DR Bgee; ENSMUSG00000001774; Expressed in primitive streak and 268 other tissues.
DR ExpressionAtlas; Q9D1P4; baseline and differential.
DR Genevisible; Q9D1P4; MM.
DR GO; GO:0043531; F:ADP binding; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IDA:MGI.
DR GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
DR GO; GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:1900034; P:regulation of cellular response to heat; IDA:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007051; CHORD_dom.
DR InterPro; IPR039790; CHORD_protein.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR12621; PTHR12621; 1.
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 Acetylation; Chaperone; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Stress response; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD1"
FT CHAIN 2..331
FT /note="Cysteine and histidine-rich domain-containing
FT protein 1"
FT /id="PRO_0000317771"
FT DOMAIN 5..64
FT /note="CHORD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 157..216
FT /note="CHORD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 227..316
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 2..77
FT /note="Interaction with PPP5C"
FT /evidence="ECO:0000269|PubMed:16083881"
FT REGION 62..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..316
FT /note="Interaction with HSP90AA1 and HSP90AB1"
FT /evidence="ECO:0000269|PubMed:15642353,
FT ECO:0000269|PubMed:16083881"
FT COMPBIAS 64..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 27
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 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 157
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="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 179
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 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD1"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD1"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD1"
SQ SEQUENCE 331 AA; 37351 MW; 8E02FD5F4EB89BB9 CRC64;
MALLCYNRGC GQRFDPEANS DDACTYHPGV PVFHDALKGW SCCKRRTTDF SDFLSIVGCT
KGRHNSEKPP EPVKPEVKTT EKKELSELKP KFQEHIIQAP KPVEAIKRPS PDEPMTNLEL
KISASLKQAL DKLKLSSGSE EDKKEEDSDE IKIGTSCKNG GCSKTYQGLQ SLEEVCVYHS
GVPIFHEGMK YWSCCRRKTS DFNTFLAQEG CTRGKHVWTK KDAGKKVVPC RHDWHQTGGE
VTISVYAKNS LPELSQVEAN STLLNVHIVF EGEKEFHQNV KLWGVIDVKR SYVTMTATKI
EITMRKAEPM QWASLELPTT KKQEKQKDIA D
