ZHP2_CAEEL
ID ZHP2_CAEEL Reviewed; 240 AA.
AC Q9U3L0;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Zip homologous protein 2 {ECO:0000312|WormBase:D1081.9};
GN Name=zhp-2 {ECO:0000312|WormBase:D1081.9};
GN ORFNames=D1081.9 {ECO:0000312|WormBase:D1081.9};
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-1, 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-1 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-1, 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-1, 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-1; the interaction is required for their
CC chromosome association and stability. {ECO:0000269|PubMed:29521627}.
CC -!- INTERACTION:
CC Q9U3L0; Q95R14: zhp-1; NbExp=3; IntAct=EBI-2415382, EBI-2415375;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:29521627}. Note=In
CC association with zhp-1, 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; CAB54207.1; -; Genomic_DNA.
DR PIR; T20319; T20319.
DR RefSeq; NP_492301.1; NM_059900.3.
DR AlphaFoldDB; Q9U3L0; -.
DR SMR; Q9U3L0; -.
DR ComplexPortal; CPX-5801; ZHP-1-ZHP-2 complex.
DR IntAct; Q9U3L0; 2.
DR STRING; 6239.D1081.9; -.
DR EPD; Q9U3L0; -.
DR PaxDb; Q9U3L0; -.
DR EnsemblMetazoa; D1081.9.1; D1081.9.1; WBGene00008387.
DR GeneID; 172637; -.
DR UCSC; D1081.9; c. elegans.
DR CTD; 172637; -.
DR WormBase; D1081.9; CE23619; WBGene00008387; zhp-2.
DR eggNOG; KOG4739; Eukaryota.
DR GeneTree; ENSGT00740000115581; -.
DR HOGENOM; CLU_1157309_0_0_1; -.
DR InParanoid; Q9U3L0; -.
DR OMA; SDWIHCN; -.
DR OrthoDB; 1325661at2759; -.
DR PhylomeDB; Q9U3L0; -.
DR PRO; PR:Q9U3L0; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00008387; Expressed in germ line (C elegans) and 4 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 Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042123; Zip3/RNF212-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22663; PTHR22663; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA recombination; Meiosis; Metal-binding; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..240
FT /note="Zip homologous protein 2"
FT /id="PRO_0000450696"
FT ZN_FING 6..44
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 152..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 240 AA; 27841 MW; 69F05194D7623360 CRC64;
MDWIQCNHCG IKPNQTKLYL TACGHVFCQN CTKAAFNSQC YLCKKPLKVD EINKNLRPDL
MELFKDPRQL ASDLVNELKQ VVAFQAKQRE IYVKCKNAEA KKDTERFAEA RSKHVEKTQE
IEKRKKAFLE DNVKLKNAKE EKNQLMARLK ELREQPSQNL SVNKRRSNTR TEPPFSKISR
TGPPSVMRKA SHEFSLNLRD QSTSKILTST PLSNIDYSRR DHRNRLFGAG LEHPSPILRQ
