ZHP3_CAEEL
ID ZHP3_CAEEL Reviewed; 389 AA.
AC C6KRL6; P90905;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Zip homologous protein 3 {ECO:0000312|WormBase:K02B12.8b};
DE AltName: Full=Zip3-homologous protein {ECO:0000303|PubMed:15340062};
GN Name=zhp-3 {ECO:0000312|WormBase:K02B12.8b};
GN ORFNames=K02B12.8 {ECO:0000312|WormBase:K02B12.8b};
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|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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15340062; DOI=10.1128/mcb.24.18.7998-8006.2004;
RA Jantsch V., Pasierbek P., Mueller M.M., Schweizer D., Jantsch M., Loidl J.;
RT "Targeted gene knockout reveals a role in meiotic recombination for ZHP-3,
RT a Zip3-related protein in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 24:7998-8006(2004).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18949042; DOI=10.1371/journal.pgen.1000235;
RA Bhalla N., Wynne D.J., Jantsch V., Dernburg A.F.;
RT "ZHP-3 acts at crossovers to couple meiotic recombination with synaptonemal
RT complex disassembly and bivalent formation in C. elegans.";
RL PLoS Genet. 4:e1000235-e1000235(2008).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=23832114; DOI=10.1038/cdd.2013.68;
RA Silva N., Adamo A., Santonicola P., Martinez-Perez E., La Volpe A.;
RT "Pro-crossover factors regulate damage-dependent apoptosis in the
RT Caenorhabditis elegans germ line.";
RL Cell Death Differ. 20:1209-1218(2013).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ZHP-4, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=29521627; DOI=10.7554/elife.30789;
RA Zhang L., Koehler S., Rillo-Bohn R., Dernburg A.F.;
RT "A compartmentalized signaling network mediates crossover control in
RT meiosis.";
RL Elife 7:0-0(2018).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=30383754; DOI=10.1371/journal.pgen.1007653;
RA Janisiw E., Dello Stritto M.R., Jantsch V., Silva N.;
RT "BRCA1-BARD1 associate with the synaptonemal complex and pro-crossover
RT factors and influence RAD-51 dynamics during Caenorhabditis elegans
RT meiosis.";
RL PLoS Genet. 14:e1007653-e1007653(2018).
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-25.
RX PubMed=30379819; DOI=10.1371/journal.pgen.1007776;
RA Nguyen H., Labella S., Silva N., Jantsch V., Zetka M.;
RT "C. elegans ZHP-4 is required at multiple distinct steps in the formation
RT of crossovers and their transition to segregation competent chiasmata.";
RL PLoS Genet. 14:E1007776-E1007776(2018).
CC -!- FUNCTION: Recruited co-dependently with zhp-4 to the synaptonemal
CC complex between homologous chromosome pairs to regulate the formation
CC and number of crossover events between homologs during meiotic
CC recombination (PubMed:15340062, PubMed:18949042, PubMed:29521627,
CC PubMed:30379819). In the early stages of pachytene, in complex with
CC zhp-4, recruited by the zhp-1-zhp-2 heterodimer to designated crossover
CC sites along the homolog pair to stabilize other pro-crossover factors
CC such as rmh-1, msh-5 and cosa-1 (PubMed:29521627, PubMed:30379819).
CC This in turn facilitates crossover and promotes the formation of
CC chiasma in each meiotic nucleus at the late pachytene stage of meiosis
CC (PubMed:29521627, PubMed:30379819). Plays a role in the segregation of
CC homologous chromosomes following the completion of crossovers
CC (PubMed:18949042). Together with him-14 and msh-5 plays a role in the
CC activation of DNA damage-dependent apoptosis at the DNA damage
CC checkpoint in pachytene cells (PubMed:23832114).
CC {ECO:0000269|PubMed:15340062, ECO:0000269|PubMed:18949042,
CC ECO:0000269|PubMed:23832114, ECO:0000269|PubMed:29521627,
CC ECO:0000269|PubMed:30379819}.
CC -!- SUBUNIT: Interacts with zhp-4; the interaction is required for their
CC localization along paired chromosomes and stability, and for the
CC formation of chiasma during meiotic recombination.
CC {ECO:0000269|PubMed:29521627}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:15340062,
CC ECO:0000269|PubMed:18949042, ECO:0000269|PubMed:29521627,
CC ECO:0000269|PubMed:30379819}. Note=Co-localizes with zhp-4 to
CC chromosomes from mitosis to early diakinesis in the germline
CC (PubMed:29521627, PubMed:30379819). Co-localizes with syp-1, a
CC component of the synaptonemal complex, throughout the gonad from early
CC prophase to mid-pachytene (PubMed:15340062, PubMed:18949042,
CC PubMed:29521627, PubMed:30379819). In early pachytene, co-localizes
CC with syp-1 as puncta along chromosomes (PubMed:18949042). In pachytene
CC nuclei, localizes in linear arrays in the space in between synapsed
CC chromosomes (PubMed:15340062). Does not localize to unsynapsed
CC chromosomes (PubMed:18949042). From mid-pachytene, co-localizes with
CC cosa-1 at crossover sites of recombination intermediates, and gradually
CC disassociates from syp-1 along both chromosome arms (PubMed:15340062,
CC PubMed:18949042, PubMed:29521627, PubMed:30379819). Co-localizes with
CC brc-1 at crossover sites in mid-late pachytene nuclei
CC (PubMed:30383754). At late pachytene, localizes asymmetrically on
CC synapsed chromosomes (PubMed:18949042). At late pachytene and early
CC diplotene localizes to a single focus at the boundary between the long
CC and short arm of each pair of homologous chromosomes (PubMed:18949042).
CC At late pachytene, localization at chromosomes is not dependent on syp-
CC 1 (PubMed:18949042, PubMed:29521627). In diakinesis, does not localize
CC to chromosomes, but is dispersed between chromosomes (PubMed:15340062).
CC {ECO:0000269|PubMed:15340062, ECO:0000269|PubMed:18949042,
CC ECO:0000269|PubMed:29521627, ECO:0000269|PubMed:30379819,
CC ECO:0000269|PubMed:30383754}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:K02B12.8b};
CC IsoId=C6KRL6-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:K02B12.8a};
CC IsoId=C6KRL6-2; Sequence=VSP_060674;
CC -!- TISSUE SPECIFICITY: Expressed througout the gonad (at protein level)
CC (PubMed:18949042). Expressed in the germline (PubMed:15340062,
CC PubMed:29521627). {ECO:0000269|PubMed:15340062,
CC ECO:0000269|PubMed:18949042, ECO:0000269|PubMed:29521627}.
CC -!- DISRUPTION PHENOTYPE: High levels of embryonic lethality, but a small
CC proportion of the surviving progeny develop beyond the L3 larval stage
CC (PubMed:15340062, PubMed:18949042, PubMed:29521627). Of the surviving
CC progeny, there is a high incidence of males (him phenotype)
CC (PubMed:18949042, PubMed:29521627). Impaired meiotic recombination with
CC no chiasma formation between homologous chromosome pairs at diplotene
CC and diakinesis (PubMed:15340062). This is most likely due to an absence
CC of crossover recombination (PubMed:15340062). Disrupted rad-51
CC localization during meiosis, whereby rad-51-positive foci are present
CC in the gonad similarly to wild-type, however unlike in wild-type, they
CC disappear before the end of pachytene (PubMed:15340062).
CC {ECO:0000269|PubMed:15340062, ECO:0000269|PubMed:18949042,
CC ECO:0000269|PubMed:29521627}.
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DR EMBL; BX284601; CAB00037.3; -; Genomic_DNA.
DR EMBL; BX284601; CAZ65508.1; -; Genomic_DNA.
DR PIR; T23224; T23224.
DR RefSeq; NP_001250801.1; NM_001263872.1. [C6KRL6-2]
DR RefSeq; NP_001250802.1; NM_001263873.1. [C6KRL6-1]
DR AlphaFoldDB; C6KRL6; -.
DR ComplexPortal; CPX-5802; ZHP-3-ZHP-4 meiotic pro-crossover complex.
DR IntAct; C6KRL6; 1.
DR STRING; 6239.K02B12.8b; -.
DR PaxDb; C6KRL6; -.
DR EnsemblMetazoa; K02B12.8a.1; K02B12.8a.1; WBGene00006976. [C6KRL6-2]
DR EnsemblMetazoa; K02B12.8b.1; K02B12.8b.1; WBGene00006976. [C6KRL6-1]
DR GeneID; 172644; -.
DR KEGG; cel:CELE_K02B12.8; -.
DR UCSC; K02B12.8; c. elegans.
DR CTD; 172644; -.
DR WormBase; K02B12.8a; CE34201; WBGene00006976; zhp-3. [C6KRL6-2]
DR WormBase; K02B12.8b; CE43850; WBGene00006976; zhp-3. [C6KRL6-1]
DR eggNOG; KOG4739; Eukaryota.
DR GeneTree; ENSGT00740000115581; -.
DR HOGENOM; CLU_700632_0_0_1; -.
DR InParanoid; C6KRL6; -.
DR OMA; HSMANQT; -.
DR OrthoDB; 1325661at2759; -.
DR PRO; PR:C6KRL6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006976; Expressed in embryo and 3 other tissues.
DR ExpressionAtlas; C6KRL6; baseline and differential.
DR GO; GO:0005694; C:chromosome; IC:ComplexPortal.
DR GO; GO:0000795; C:synaptonemal complex; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; ISO:WormBase.
DR GO; GO:0051026; P:chiasma assembly; IC:ComplexPortal.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IBA:GO_Central.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:WormBase.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IC:ComplexPortal.
DR GO; GO:0070194; P:synaptonemal complex disassembly; IMP:WormBase.
DR InterPro; IPR042123; Zip3/RNF212-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22663; PTHR22663; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; DNA recombination; Meiosis;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..389
FT /note="Zip homologous protein 3"
FT /id="PRO_0000450697"
FT ZN_FING 6..43
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 366..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 123..164
FT /evidence="ECO:0000255"
FT VAR_SEQ 245..246
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060674"
FT MUTAGEN 25
FT /note="H->A: In vv137; 3% embryonic lethality and 3% of
FT surviving progeny are male. Does not abolish zhp-4
FT recruitment to the synaptonemal complex between homologous
FT chromosome pairs during pachytene. 95% embryonic lethality,
FT 43% of surviving progeny are male and abolishes recruitment
FT to chromosomes at any meiotic stage in a zhp-4 vv138 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:30379819"
SQ SEQUENCE 389 AA; 43623 MW; D31EB8C7010901B8 CRC64;
MDFVHCNKCF NRKPPDGFFI SSCFHIFCTK CAKADLAVCL ICKKNVRLVR LDGNISSGIK
IYFADPIKMV ADSLAKIQKK IDFQQSTRDH LVKYLTKEKE KKRQMEVYFR TKGQEFDSQR
KKLAEATAWI QMAEKKLQAS EEERVKAERE IEECQAKLKS MTNLMSADTL GMNSQTPFPF
SLAESQETAP SLVESSANST FNMVSPLVSS PASSPNSINY NSFFENGSRT RPESLNEEAM
FNTMLQSSGQ SANANTSESS AFSVAFNNIF TPSRNNMGDS SMINKTTANQ TIMDKTSMSL
ENWRQNRANS FGVHDISKRD SSLPTGGGSA IRVHHFKQNS RITPIAQNRR SAAGFDRQQI
QEMRRISSQP GYLAQRKPIN GRSFIGPAD
