HOP2_MOUSE
ID HOP2_MOUSE Reviewed; 217 AA.
AC O35047; Q3V035;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Homologous-pairing protein 2 homolog;
DE AltName: Full=PSMC3-interacting protein;
DE AltName: Full=Proteasome 26S ATPase subunit 3-interacting protein;
DE AltName: Full=Tat-binding protein 1-interacting protein;
DE Short=TBP-1-interacting protein;
GN Name=Psmc3ip; Synonyms=Hop2, Tbpip;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PSMC3, TISSUE SPECIFICITY, AND
RP FUNCTION.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=9345291; DOI=10.1006/bbrc.1997.7447;
RA Tanaka T., Nakamura T., Takagi H., Sato M.;
RT "Molecular cloning and characterization of a novel TBP-1 interacting
RT protein (TBPIP): enhancement of TBP-1 action on Tat by TBPIP.";
RL Biochem. Biophys. Res. Commun. 239:176-181(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
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).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=14667414; DOI=10.1016/s1534-5807(03)00369-1;
RA Petukhova G.V., Romanienko P.J., Camerini-Otero R.D.;
RT "The Hop2 protein has a direct role in promoting interhomolog interactions
RT during mouse meiosis.";
RL Dev. Cell 5:927-936(2003).
RN [7]
RP FUNCTION, AND DNA-BINDING REGION.
RX PubMed=15192114; DOI=10.1074/jbc.m402481200;
RA Enomoto R., Kinebuchi T., Sato M., Yagi H., Shibata T., Kurumizaka H.,
RA Yokoyama S.;
RT "Positive role of the mammalian TBPIP/HOP2 protein in DMC1-mediated
RT homologous pairing.";
RL J. Biol. Chem. 279:35263-35272(2004).
RN [8]
RP FUNCTION, DNA-BINDING REGION, MUTAGENESIS OF GLU-136, AND INTERACTION WITH
RP MND1.
RX PubMed=16675459; DOI=10.1074/jbc.m601073200;
RA Pezza R.J., Petukhova G.V., Ghirlando R., Camerini-Otero R.D.;
RT "Molecular activities of meiosis-specific proteins Hop2, Mnd1, and the
RT Hop2-Mnd1 complex.";
RL J. Biol. Chem. 281:18426-18434(2006).
RN [9]
RP FUNCTION.
RX PubMed=17639080; DOI=10.1101/gad.1563007;
RA Chi P., San Filippo J., Sehorn M.G., Petukhova G.V., Sung P.;
RT "Bipartite stimulatory action of the Hop2-Mnd1 complex on the Rad51
RT recombinase.";
RL Genes Dev. 21:1747-1757(2007).
RN [10]
RP FUNCTION.
RX PubMed=17639081; DOI=10.1101/gad.1562907;
RA Pezza R.J., Voloshin O.N., Vanevski F., Camerini-Otero R.D.;
RT "Hop2/Mnd1 acts on two critical steps in Dmc1-promoted homologous
RT pairing.";
RL Genes Dev. 21:1758-1766(2007).
RN [11]
RP FUNCTION.
RX PubMed=17426123; DOI=10.1093/nar/gkm174;
RA Ploquin M., Petukhova G.V., Morneau D., Dery U., Bransi A., Stasiak A.,
RA Camerini-Otero R.D., Masson J.-Y.;
RT "Stimulation of fission yeast and mouse Hop2-Mnd1 of the Dmc1 and Rad51
RT recombinases.";
RL Nucleic Acids Res. 35:2719-2733(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC {ECO:0000269|PubMed:15192114, ECO:0000269|PubMed:16675459,
CC ECO:0000269|PubMed:17426123, ECO:0000269|PubMed:17639080,
CC ECO:0000269|PubMed:17639081, ECO:0000269|PubMed:9345291}.
CC -!- SUBUNIT: Interacts with the DNA-binding domain of the nuclear receptors
CC NR3C1/GR, ESR2/ER-beta, THRB and RXRA (By similarity). Forms a stable
CC heterodimer with MND1. Interacts with PSMC3/TBP1. {ECO:0000250,
CC ECO:0000269|PubMed:16675459, ECO:0000269|PubMed:9345291}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11739747}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and more specifically in
CC spermatocytes. Detected in spleen, ovary and thymus.
CC {ECO:0000269|PubMed:11739747, ECO:0000269|PubMed:9345291}.
CC -!- DEVELOPMENTAL STAGE: Overexpressed at day 11 in the embryo.
CC {ECO:0000269|PubMed:11739747}.
CC -!- PTM: Phosphorylated by PKA, PKC and MAPK. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Infertility. Males exhibit testicular hypoplasia
CC with lack of spermatozoa. Spermatocytes arrest at the stage of
CC pachytene-like chromosome condensation and spermatogenesis is blocked
CC at prophase of meiosis I. Axial elements are fully developed, but
CC synapsis is limited. While meiotic double-stranded breaks are formed
CC and processed, they fail to be repaired. {ECO:0000269|PubMed:14667414}.
CC -!- SIMILARITY: Belongs to the HOP2 family. {ECO:0000305}.
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DR EMBL; AB000121; BAA23155.1; -; mRNA.
DR EMBL; AK133462; BAE21670.1; -; mRNA.
DR EMBL; BX255926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030169; AAH30169.1; -; mRNA.
DR CCDS; CCDS25448.1; -.
DR PIR; JC5710; JC5710.
DR RefSeq; NP_032975.1; NM_008949.3.
DR PDB; 2MH2; NMR; -; A=1-84.
DR PDBsum; 2MH2; -.
DR AlphaFoldDB; O35047; -.
DR BMRB; O35047; -.
DR SMR; O35047; -.
DR BioGRID; 202429; 1.
DR CORUM; O35047; -.
DR STRING; 10090.ENSMUSP00000019447; -.
DR PhosphoSitePlus; O35047; -.
DR EPD; O35047; -.
DR MaxQB; O35047; -.
DR PaxDb; O35047; -.
DR PRIDE; O35047; -.
DR ProteomicsDB; 273379; -.
DR Antibodypedia; 29297; 72 antibodies from 22 providers.
DR DNASU; 19183; -.
DR Ensembl; ENSMUST00000019447; ENSMUSP00000019447; ENSMUSG00000019303.
DR GeneID; 19183; -.
DR KEGG; mmu:19183; -.
DR UCSC; uc007lnh.2; mouse.
DR CTD; 29893; -.
DR MGI; MGI:1098610; Psmc3ip.
DR VEuPathDB; HostDB:ENSMUSG00000019303; -.
DR eggNOG; KOG4603; Eukaryota.
DR GeneTree; ENSGT00390000006890; -.
DR HOGENOM; CLU_063266_1_0_1; -.
DR InParanoid; O35047; -.
DR OMA; IETDEDC; -.
DR OrthoDB; 1498024at2759; -.
DR PhylomeDB; O35047; -.
DR TreeFam; TF328666; -.
DR BioGRID-ORCS; 19183; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Psmc3ip; mouse.
DR PRO; PR:O35047; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O35047; protein.
DR Bgee; ENSMUSG00000019303; Expressed in optic fissure and 204 other tissues.
DR ExpressionAtlas; O35047; baseline and differential.
DR Genevisible; O35047; MM.
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:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0050692; F:DNA binding domain binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0120230; F:recombinase activator activity; IBA:GO_Central.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0007131; P:reciprocal meiotic recombination; ISO:MGI.
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 3D-structure; Coiled coil; DNA recombination; DNA-binding; Meiosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..217
FT /note="Homologous-pairing protein 2 homolog"
FT /id="PRO_0000314136"
FT REGION 118..182
FT /note="DNA-binding"
FT COILED 84..152
FT /evidence="ECO:0000255"
FT MUTAGEN 136
FT /note="E->P: Alters PSMC3/MND1 formation."
FT /evidence="ECO:0000269|PubMed:16675459"
FT CONFLICT 80
FT /note="T -> K (in Ref. 2; BAE21670)"
FT /evidence="ECO:0000305"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:2MH2"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:2MH2"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:2MH2"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:2MH2"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2MH2"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2MH2"
SQ SEQUENCE 217 AA; 24748 MW; 18E834492C2609EC CRC64;
MSKSRAEAAA GAPGIILRYL QEQNRPYSAQ DVFGNLQKEH GLGKAAVVKA LDQLAQEGKI
KEKTYGKQKI YFADQNQFDT VSDADLHGLD ASIVALTAKV QSLQQSCRHM EAELKELTSA
LTTPEMQKEI QELKKECAQY TERLKNIKAA TNHVTPEEKE KVYRDRQKYC KEWRKRKRMT
TELCDAILEG YPKSKKQFFE EVGIETDEDH NVLLPDP
