ZHP1_CAEEL
ID ZHP1_CAEEL Reviewed; 220 AA.
AC Q95R14;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Zip homologous protein 1 {ECO:0000312|WormBase:F55A12.10};
GN Name=zhp-1 {ECO:0000312|WormBase:F55A12.10};
GN ORFNames=F55A12.10 {ECO:0000312|WormBase:F55A12.10};
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-2, 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).
CC -!- FUNCTION: Recruited co-dependently with zhp-2 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). Together with zhp-2, promotes the
CC accumulation of pro-crossover proteins, including zhp-3 and zhp-4, at a
CC designated crossover site along the recombination intermediate
CC (PubMed:29521627). Limits the number of crossover sites along a
CC recombination intermediate by restricting the association of these pro-
CC crossover proteins with other recombination sites during late prophase
CC (PubMed:29521627). Also, together with zhp-2, plays a role in
CC chromosome remodeling following crossover formation to promote two
CC successive rounds of chromosome segregation during meiosis
CC (PubMed:29521627). {ECO:0000269|PubMed:29521627}.
CC -!- SUBUNIT: Interacts with zhp-2; the interaction is required for their
CC chromosome association and stability. {ECO:0000269|PubMed:29521627}.
CC -!- INTERACTION:
CC Q95R14; Q9U3L0: zhp-2; NbExp=3; IntAct=EBI-2415375, EBI-2415382;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:29521627}. Note=In
CC association with zhp-2, localizes to chromosomes from pachytene to
CC early diakinesis in the germ line (PubMed:29521627). Co-localizes with
CC syp-1, a component of the synaptonemal complex from early prophase to
CC mid-pachytene (PubMed:29521627). From mid-pachytene to diplotene, co-
CC localizes with syp-1 on one side of each crossover site
CC (PubMed:29521627). Remains co-localized with syp-1 along the short arm
CC of homologous chromosomes through to late diakinesis (PubMed:29521627).
CC At late pachytene, localization at chromosomes is not dependent on syp-
CC 1 (PubMed:29521627). {ECO:0000269|PubMed:29521627}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline.
CC {ECO:0000269|PubMed:29521627}.
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DR EMBL; BX284601; CCD65448.1; -; Genomic_DNA.
DR RefSeq; NP_491578.1; NM_059177.3.
DR AlphaFoldDB; Q95R14; -.
DR ComplexPortal; CPX-5801; ZHP-1-ZHP-2 complex.
DR IntAct; Q95R14; 2.
DR STRING; 6239.F55A12.10; -.
DR PaxDb; Q95R14; -.
DR EnsemblMetazoa; F55A12.10.1; F55A12.10.1; WBGene00018867.
DR EnsemblMetazoa; F55A12.10.2; F55A12.10.2; WBGene00018867.
DR GeneID; 172186; -.
DR KEGG; cel:CELE_F55A12.10; -.
DR UCSC; F55A12.10; c. elegans.
DR CTD; 172186; -.
DR WormBase; F55A12.10; CE28451; WBGene00018867; zhp-1.
DR eggNOG; KOG4739; Eukaryota.
DR GeneTree; ENSGT00740000115581; -.
DR HOGENOM; CLU_1251651_0_0_1; -.
DR InParanoid; Q95R14; -.
DR OMA; FCETCRT; -.
DR OrthoDB; 1325661at2759; -.
DR PhylomeDB; Q95R14; -.
DR PRO; PR:Q95R14; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00018867; 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:0007129; P:homologous chromosome pairing at meiosis; IBA:GO_Central.
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; Coiled coil; DNA recombination; Meiosis; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..220
FT /note="Zip homologous protein 1"
FT /id="PRO_0000450695"
FT ZN_FING 6..44
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 166..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 124..155
FT /evidence="ECO:0000255"
FT COMPBIAS 169..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 220 AA; 24839 MW; 9FFD74F24407BE78 CRC64;
MEFIVCNGCG CSPSKRQFFI TACSHVFCET CRTTPTADFC HLCKIPTKTL KMDASLPKNV
KKMFGDVGVM STDIHKRLAR VIGFQKIQKS IQLKMENKKS VMRKEQTKKV EKKTEEMHCQ
LSKLTSFEEN NRKKLEDIER ENEKLRNLIS ALELKVASSR DIDDDEFFMQ GTPTSSNPSV
AGSDVDNDEL LDYDLLGLRN RSDSSSSNCS SQSNRGGSLF
