CHRD1_RAT
ID CHRD1_RAT Reviewed; 331 AA.
AC D4A4T9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Cysteine and histidine-rich domain-containing protein 1;
DE AltName: Full=CHORD domain-containing protein 1;
DE Short=CHP-1;
DE AltName: Full=Morgana;
GN Name=Chordc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates centrosome duplication, probably by inhibiting the
CC kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90.
CC May play a role in the regulation of NOD1 via a HSP90 chaperone
CC complex. In vitro, has intrinsic chaperone activity. This function may
CC be achieved by inhibiting association of ROCK2 with NPM1. Plays a role
CC in ensuring the localization of the tyrosine kinase receptor EGFR to
CC the plasma membrane, and thus ensures the subsequent regulation of EGFR
CC activity and EGF-induced actin cytoskeleton remodeling (By similarity).
CC Involved in stress response. Prevents tumorigenesis (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q9UHD1}.
CC -!- SUBUNIT: Interacts with HSP90AA1, HSP90AB1, PPP5C, ROCK1 and ROCK2.
CC {ECO:0000250}.
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DR EMBL; CH473993; EDL78419.1; -; Genomic_DNA.
DR RefSeq; NP_001101598.1; NM_001108128.1.
DR AlphaFoldDB; D4A4T9; -.
DR SMR; D4A4T9; -.
DR STRING; 10116.ENSRNOP00000030171; -.
DR iPTMnet; D4A4T9; -.
DR PhosphoSitePlus; D4A4T9; -.
DR jPOST; D4A4T9; -.
DR PaxDb; D4A4T9; -.
DR PeptideAtlas; D4A4T9; -.
DR PRIDE; D4A4T9; -.
DR GeneID; 315447; -.
DR KEGG; rno:315447; -.
DR UCSC; RGD:1304679; rat.
DR CTD; 26973; -.
DR RGD; 1304679; Chordc1.
DR VEuPathDB; HostDB:ENSRNOG00000026643; -.
DR eggNOG; KOG1667; Eukaryota.
DR HOGENOM; CLU_040079_0_0_1; -.
DR InParanoid; D4A4T9; -.
DR OMA; MKQWSCC; -.
DR OrthoDB; 1163528at2759; -.
DR PhylomeDB; D4A4T9; -.
DR TreeFam; TF105394; -.
DR PRO; PR:D4A4T9; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000026643; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; D4A4T9; RN.
DR GO; GO:0043531; F:ADP binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:1900034; P:regulation of cellular response to heat; ISS:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; ISS: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 3: Inferred from homology;
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_0000402802"
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:0000250"
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:0000250"
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; 37362 MW; 88100248DC1061C5 CRC64;
MALLCYNRGC GQRFDPEANA DDACTYHPGV PVFHDALKGW SCCKRRTTDF SDFLSIVGCT
KGRHNSEKPP EPVKPEVKTT EKKELSELKP KFQEHIIQAP KPVEAIKRPS PDEPMTNLEL
KISASLKQAL DKLKLSSGNE EDKKEEDSDE IKIGTSCKNG GCSKTYQGLQ SLEEVCVYHS
GVPIFHEGMK YWSCCRRKTS DFNTFLAQEG CTRGKHVWTK KDAGKKVVPC RHDWHQTGGE
VTISVYAKNS LPELSQVEAN STLLNVHIVF EGEKEFHQNV KLWGVIDVKR SYVTMTATKI
EITMRKAEPM QWASLELPTT KKQEKQKDIA D
