ID CHRD1_MACFA Reviewed; 332 AA.
AC Q4R7U2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 62.
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; ORFNames=QtsA-14386;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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; AB168720; BAE00830.1; -; mRNA.
DR RefSeq; NP_001270158.1; NM_001283229.1.
DR AlphaFoldDB; Q4R7U2; -.
DR SMR; Q4R7U2; -.
DR STRING; 9541.ENSMFAP00000021389; -.
DR eggNOG; KOG1667; Eukaryota.
DR OrthoDB; 1360344at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
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 CDD; cd06488; p23_melusin_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 4.10.1130.20; -; 2.
DR InterPro; IPR007051; CHORD_dom.
DR InterPro; IPR039790; CHRD1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR12621; CYSTEINE AND HISTIDINE-RICH DOMAIN CHORD -CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12621:SF9; CYSTEINE AND HISTIDINE-RICH DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF04968; CHORD; 2.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS51401; CHORD; 2.
DR PROSITE; PS51203; CS; 1.
PE 2: Evidence at transcript 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..332
FT /note="Cysteine and histidine-rich domain-containing
FT protein 1"
FT /id="PRO_0000402800"
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 332 AA; 37602 MW; 91546BFAF62D4DC5 CRC64;
MALLCYNRAC GQRFDPETNS DDACTYHPGV PVFHDALKGW SCCKRRTTDF SDFLSIVGCT
KGRHNSEKPP EPVKPEVKTT EKKELSELKP KFQEHIIQAP KPVEAIKRPS PDEPMTNLEL
KISASLKQAL DKLKLSSGNE EDKKEEDNDE IKIGTSCKNG GCSKTYRGLE SLEEVCVYHS
GVPIFHEGMK YWSCCRRKTS DFNTFLAQEG CTKGRHMWTK KDAGKKVVPC RHDWHQTGGE
VTISVYAKNS LPELSRVEAN STLLNVHIVF EGEKEFDQNV KLWGVIDVKR SYVTMTATKI
EINMRKAEPM QWASLELPAA KKQEKQKDDT TD
//
