HOP2_RAT
ID HOP2_RAT Reviewed; 217 AA.
AC Q91ZY6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Homologous-pairing protein 2 homolog;
DE AltName: Full=Nuclear receptor coactivator GT198;
DE AltName: Full=PSMC3-interacting protein;
DE AltName: Full=Proteasome 26S ATPase subunit 3-interacting protein;
GN Name=Psmc3ip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NR3C1; ESR2; THRB AND RXRA,
RP REGION, PHOSPHORYLATION, AND FUNCTION.
RC TISSUE=Pituitary;
RX PubMed=11739747; DOI=10.1128/mcb.22.1.357-369.2002;
RA Ko L., Cardona G.R., Henrion-Caude A., Chin W.W.;
RT "Identification and characterization of a tissue-specific coactivator,
RT GT198, that interacts with the DNA-binding domains of nuclear receptors.";
RL Mol. Cell. Biol. 22:357-369(2002).
CC -!- FUNCTION: Plays an important role in meiotic recombination. Stimulates
CC DMC1-mediated strand exchange required for pairing homologous
CC chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA,
CC stimulates the recombinase activity of DMC1 as well as DMC1 D-loop
CC formation from double-strand DNA. This complex stabilizes presynaptic
CC RAD51 and DMC1 filaments formed on single strand DNA to capture double-
CC strand DNA. This complex stimulates both synaptic and presynaptic
CC critical steps in RAD51 and DMC1-promoted homologous pairing. May
CC inhibit HIV-1 viral protein TAT activity and modulate the activity of
CC proteasomes through association with PSMC3 (By similarity). Plays a
CC role as a coactivator in nuclear receptor-mediated transcription.
CC {ECO:0000250, ECO:0000269|PubMed:11739747}.
CC -!- SUBUNIT: Forms a stable heterodimer with MND1. Interacts with
CC PSMC3/TBP1 (By similarity). Interacts with the DNA-binding domain of
CC the nuclear receptors NR3C1/GR, ESR2/ER-beta, THRB and RXRA.
CC {ECO:0000250, ECO:0000269|PubMed:11739747}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated by PKA, PKC and MAPK.
CC {ECO:0000269|PubMed:11739747}.
CC -!- SIMILARITY: Belongs to the HOP2 family. {ECO:0000305}.
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DR EMBL; AF352812; AAL23906.1; -; mRNA.
DR RefSeq; NP_604453.2; NM_134458.2.
DR AlphaFoldDB; Q91ZY6; -.
DR SMR; Q91ZY6; -.
DR BioGRID; 250872; 1.
DR CORUM; Q91ZY6; -.
DR STRING; 10116.ENSRNOP00000027159; -.
DR iPTMnet; Q91ZY6; -.
DR PhosphoSitePlus; Q91ZY6; -.
DR PaxDb; Q91ZY6; -.
DR GeneID; 140938; -.
DR KEGG; rno:140938; -.
DR UCSC; RGD:621885; rat.
DR CTD; 29893; -.
DR RGD; 621885; Psmc3ip.
DR eggNOG; KOG4603; Eukaryota.
DR InParanoid; Q91ZY6; -.
DR OrthoDB; 1498024at2759; -.
DR PhylomeDB; Q91ZY6; -.
DR PRO; PR:Q91ZY6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR GO; GO:0120231; C:DNA recombinase auxiliary factor complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0050692; F:DNA binding domain binding; IDA:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IDA:RGD.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:RGD.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IDA:RGD.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:RGD.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:RGD.
DR GO; GO:0120230; F:recombinase activator activity; IBA:GO_Central.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IBA:GO_Central.
DR GO; GO:0000709; P:meiotic joint molecule formation; IBA:GO_Central.
DR GO; GO:0010774; P:meiotic strand invasion involved in reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:RGD.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR040461; Hop2.
DR InterPro; IPR010776; Hop2_WH_dom.
DR InterPro; IPR040661; LZ3wCH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR15938; PTHR15938; 1.
DR Pfam; PF18517; LZ3wCH; 1.
DR Pfam; PF07106; TBPIP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA recombination; DNA-binding; Meiosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..217
FT /note="Homologous-pairing protein 2 homolog"
FT /id="PRO_0000314137"
FT REGION 89..117
FT /note="Interaction with NR3C1, homodimerization and
FT transcriptional activation almost abolished when missing"
FT /evidence="ECO:0000269|PubMed:11739747"
FT REGION 118..182
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 118..182
FT /note="Interaction with NR3C1 decreased when missing"
FT COILED 93..153
FT /evidence="ECO:0000255"
SQ SEQUENCE 217 AA; 24768 MW; 422C1F1ED22EAD63 CRC64;
MSKSRAEAAA GAPGIVLRYL QEQNRPYSAQ DVFGNLQKEH GLGKAAVVKA LDQLAQQGKI
KEKTYGKQKI YFADQDQFDT VSDADLHSLD ASIMALTAKV QGLQQSCRHM EAELKELTSA
LTTPEMQTEI QELKKECARY TERLKNIKAA TNHVTPEEKE KVYRERQKYC KEWRKRKRMT
TELCDAILEG YPKSKKQFFE EVGIETDEDH NVTLPNP
