CHRD1_CAEEL
ID CHRD1_CAEEL Reviewed; 321 AA.
AC G5EEI8;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Cysteine and histidine-rich domain-containing protein 1 {ECO:0000305};
DE AltName: Full=CHORD domain-containing protein 1 {ECO:0000305};
DE Short=CHORD-containing protein 1 {ECO:0000305};
DE AltName: Full=Protein CHORD {ECO:0000312|WormBase:Y110A7A.13};
GN Name=chp-1 {ECO:0000312|WormBase:Y110A7A.13};
GN Synonyms=chp {ECO:0000312|WormBase:Y110A7A.13};
GN ORFNames=Y110A7A.13 {ECO:0000312|WormBase:Y110A7A.13};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAF18435.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
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] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32053105; DOI=10.7554/elife.50986;
RA Haag A., Walser M., Henggeler A., Hajnal A.;
RT "The CHORD protein CHP-1 regulates EGF receptor trafficking and signaling
RT in C. elegans and in human cells.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Regulates centrosome duplication (By similarity). Controls
CC the secretion of the tyrosine kinase receptor let-23/EGFR from the
CC endoplasmic reticulum and is required for the localization of let-
CC 23/EGFR to the plasma membrane of vulval precursor cells
CC (PubMed:32053105). It thus plays a role in positively regulating
CC let/EGFR signaling, and anchor cell and vulval precursor cell alignment
CC (PubMed:32053105). Plays a role in vulval development and morphogenesis
CC (PubMed:10571178, PubMed:32053105). {ECO:0000250|UniProtKB:Q9D1P4,
CC ECO:0000269|PubMed:10571178, ECO:0000269|PubMed:32053105}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC fertility and in high levels of embryonic lethality with none of the
CC unhatched embryos reaching the comma stage of development
CC (PubMed:10571178). Among the 40% of embryos that hatch, 98% reach
CC adulthood, but have a reduced brood size, and the remaining 2% do not
CC survive beyond the L1 larval stage (PubMed:10571178). Surviving adults
CC have defects in vulval development, whereby 3-5% have a protruding
CC vulva (Pvl) phenotype and 1% have a multivulva (Mvl) phenotype
CC (PubMed:10571178). Occasionally, some adults have one missing gonadal
CC arm, but many adults have defects in the organization of the proximal
CC arm of the gonad, which are filled with smaller cells instead of full
CC sized oocytes (PubMed:10571178). RNAi-mediated knockdown results in
CC reduced plasma membrane localization and increased intracellular
CC accumulation of let-23 in vulval precursor cells P6.p and their
CC descendants (PubMed:32053105). RNAi-mediated knockdown does not affect
CC the membrane localization of lin-12, lin-18 or pat-3 (PubMed:32053105).
CC RNAi-mediated knockdown in vulval precursor cells results in the
CC intracellular accumulation of let-23 in 31% of cases (PubMed:32053105).
CC {ECO:0000269|PubMed:10571178, ECO:0000269|PubMed:32053105}.
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DR EMBL; AF192264; AAF18435.1; -; mRNA.
DR EMBL; BX284601; CCD66204.1; -; Genomic_DNA.
DR RefSeq; NP_491519.1; NM_059118.4.
DR AlphaFoldDB; G5EEI8; -.
DR SMR; G5EEI8; -.
DR IntAct; G5EEI8; 1.
DR STRING; 6239.Y110A7A.13; -.
DR EPD; G5EEI8; -.
DR PaxDb; G5EEI8; -.
DR PeptideAtlas; G5EEI8; -.
DR EnsemblMetazoa; Y110A7A.13.1; Y110A7A.13.1; WBGene00000502.
DR GeneID; 172138; -.
DR KEGG; cel:CELE_Y110A7A.13; -.
DR CTD; 172138; -.
DR WormBase; Y110A7A.13; CE23244; WBGene00000502; chp-1.
DR eggNOG; KOG1667; Eukaryota.
DR GeneTree; ENSGT00940000159429; -.
DR HOGENOM; CLU_040079_0_0_1; -.
DR InParanoid; G5EEI8; -.
DR OMA; TVRNDFY; -.
DR OrthoDB; 1163528at2759; -.
DR PhylomeDB; G5EEI8; -.
DR PRO; PR:G5EEI8; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000502; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..321
FT /note="Cysteine and histidine-rich domain-containing
FT protein 1"
FT /id="PRO_0000450441"
FT DOMAIN 9..68
FT /note="CHORD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 152..210
FT /note="CHORD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 218..308
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
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 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 47
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
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 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
SQ SEQUENCE 321 AA; 36007 MW; 8FF2228055BE2FBE CRC64;
MVDESKLQCY HKGCGLLFDP KENDNEACTY HPGGPYFHDA YKIWTCCDKK STDFGTWMNY
KGCTRGKHSN EKPVDIVKVA AVKEIRPEKE EDVIVWKGLN KSGKLDSKDA TKRIEQNLNV
EVTPGATAAI EKKLKEISEA AQSADIQIGA PCRNNGCSTE FDGSKNKENC QHHPGAAIFH
EGMKYWSCCN KKTSNFGAFL EQVGCTSGEH KFRNNEIVSK FREDWFSSNG FVTINVYCRG
ALPETANIVS DGHTVRVSMK HGFGNASVDL DYDLWDEVIP EESRVVIGER KVEISLKQKH
GTGWPRLKFD PELDAKNDEE A
