ZHP4_CAEEL
ID ZHP4_CAEEL Reviewed; 283 AA.
AC Q8MYP1;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Zip homologous protein 4 {ECO:0000312|WormBase:Y39B6A.16};
GN Name=zhp-4 {ECO:0000312|WormBase:Y39B6A.16};
GN ORFNames=Y39B6A.16 {ECO:0000312|WormBase:Y39B6A.16};
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, INTERACTION WITH ZHP-3, 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 [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-26; 56-ILE--GLN-286
RP AND 160-GLN--GLN-283.
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-3 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:29521627, PubMed:30379819). In the early stages
CC of pachytene, in complex with zhp-4, recruited by the zhp-1-zhp-2
CC heterodimer to designated crossover sites along the recombination
CC intermediate to stabilize other pro-crossover factors such as rmh-1,
CC msh-5 and cosa-1 (PubMed:29521627, PubMed:30379819). This in turn
CC facilitates crossover and promotes the formation of chiasma in each
CC meiotic nucleus at the late pachytene stage of meiosis
CC (PubMed:29521627, PubMed:30379819). Negatively regulates double strand
CC break formation to promote formation of the crossover intermediate
CC (PubMed:30379819). {ECO:0000269|PubMed:29521627,
CC ECO:0000269|PubMed:30379819}.
CC -!- SUBUNIT: Interacts with zhp-3; 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:29521627,
CC ECO:0000269|PubMed:30379819}. Note=Co-localizes with zhp-3 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 from early prophase to mid-
CC pachytene (PubMed:29521627, PubMed:30379819). At late pachytene,
CC localization at chromosomes is not dependent on syp-1
CC (PubMed:29521627). From mid-pachytene, co-localizes with cosa-1 at
CC crossover sites of recombination intermediates, and gradually
CC disassociates from syp-1 along both chromosome arms (PubMed:29521627,
CC PubMed:30379819). {ECO:0000269|PubMed:29521627,
CC ECO:0000269|PubMed:30379819}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline.
CC {ECO:0000269|PubMed:29521627}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284605; CAD31814.1; -; Genomic_DNA.
DR RefSeq; NP_741682.1; NM_171592.3.
DR AlphaFoldDB; Q8MYP1; -.
DR SMR; Q8MYP1; -.
DR ComplexPortal; CPX-5802; ZHP-3-ZHP-4 meiotic pro-crossover complex.
DR IntAct; Q8MYP1; 2.
DR STRING; 6239.Y39B6A.16; -.
DR PaxDb; Q8MYP1; -.
DR EnsemblMetazoa; Y39B6A.16.1; Y39B6A.16.1; WBGene00012678.
DR GeneID; 3565475; -.
DR KEGG; cel:CELE_Y39B6A.16; -.
DR UCSC; Y39B6A.16; c. elegans.
DR CTD; 3565475; -.
DR WormBase; Y39B6A.16; CE29858; WBGene00012678; zhp-4.
DR eggNOG; KOG4739; Eukaryota.
DR GeneTree; ENSGT00740000115581; -.
DR HOGENOM; CLU_1166772_0_0_1; -.
DR InParanoid; Q8MYP1; -.
DR OMA; PANPPHM; -.
DR OrthoDB; 1325661at2759; -.
DR PhylomeDB; Q8MYP1; -.
DR PRO; PR:Q8MYP1; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00012678; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005694; C:chromosome; IC:ComplexPortal.
DR GO; GO:0000795; C:synaptonemal complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; IBA:GO_Central.
DR GO; GO:0051026; P:chiasma assembly; IC:ComplexPortal.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IBA:GO_Central.
DR GO; GO:0045132; P:meiotic chromosome segregation; IC:ComplexPortal.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IC:ComplexPortal.
DR InterPro; IPR042123; Zip3/RNF212-like.
DR PANTHER; PTHR22663; PTHR22663; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA recombination; Meiosis; Metal-binding; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..283
FT /note="Zip homologous protein 4"
FT /id="PRO_0000450698"
FT ZN_FING 6..50
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 149..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 26
FT /note="H->A: In vv138; 75% embryonic lethality and 35% of
FT surviving progeny are male. Chromosome segregation defects
FT due to impaired recruitment to the synaptonemal complex
FT between homologous chromosome pairs during pachytene.
FT Defective localization of the scaffolding protein rmh-1 and
FT cosa-1 at crossover sites. Reduced number of crossovers
FT that form are competent to initiate chromosome remodeling.
FT 95% embryonic lethality, 43% of surviving progeny are male
FT and abolished recruitment to chromosomes at any meiotic
FT stage in a zhp-3 vv137 mutant background."
FT /evidence="ECO:0000269|PubMed:30379819"
FT MUTAGEN 56..283
FT /note="Missing: In vv103; 95% embryonic lethality and 35%
FT of surviving progeny are male. Abolishes localization of
FT zhp-3 to chromosomes throughout meiotic prophase and
FT defective chiasmata formation during meiotic recombination.
FT Impairs localization of rmh-1, msh-5 and cosa-1 at
FT crossover sites resulting in defective crossovers and
FT chromosome remodeling and segregation. Increased rad-51
FT positive nuclei at late pachytene indicative of increased
FT double strand break formation. This is futher increased in
FT a rad-54 RNAi-mediated knockdown background."
FT /evidence="ECO:0000269|PubMed:30379819"
FT MUTAGEN 160..283
FT /note="Missing: In vv96; 95% embryonic lethality and 35% of
FT surviving progeny are male. Defective chiasmata formation
FT during meiotic recombination. Reduces localization of zhp-3
FT to chromosomes during late pachytene. Impairs localization
FT of rmh-1, msh-5 and cosa-1 at crossover sites resulting in
FT defective crossovers and chromosome remodeling and
FT segregation. No bivalent chromosomes are formed at
FT diakinesis in a rmh-1 jf92 mutant background."
FT /evidence="ECO:0000269|PubMed:30379819"
SQ SEQUENCE 283 AA; 32838 MW; EEEA0FEBE64A09CF CRC64;
MEAVHCFRCY KFPSKQIEFY LTNCMHMFCI ECERLCHPPE EEPLKCIQCS KTPIRIVKMG
PELPMTIKSM FTPISEEINQ YTRDLTRVLT FQHRQRASLS TFLERKVAAF DRLRDAYSEE
KTKKEHYKKQ LEEAYHLLKS KEHEISKLKK QLAEQAPPPQ TPPRSNSLKV ASSRSLETPS
MMRVFSDSMY ETPVQIQRRF TKAQAKAEAE AEAPAKSPGS KAQTTKCTSN YQSHPPASFE
TPIHHPPKTS MGFTTPANPP HMFPYLKKHE AQREKHKEHR NSQ
