PCH2_MOUSE
ID PCH2_MOUSE Reviewed; 432 AA.
AC Q3UA06; A0JNT8; Q05CL4; Q3UQG6; Q9CWW8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Pachytene checkpoint protein 2 homolog;
DE AltName: Full=Thyroid hormone receptor interactor 13;
DE AltName: Full=Thyroid receptor-interacting protein 13;
DE Short=TR-interacting protein 13;
DE Short=TRIP-13;
GN Name=Trip13; Synonyms=Pch2;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Heart, and Stomach;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17696610; DOI=10.1371/journal.pgen.0030130;
RA Li X.C., Schimenti J.C.;
RT "Mouse pachytene checkpoint 2 (trip13) is required for completing meiotic
RT recombination but not synapsis.";
RL PLoS Genet. 3:E130-E130(2007).
RN [6]
RP FUNCTION.
RX PubMed=19851446; DOI=10.1371/journal.pgen.1000702;
RA Wojtasz L., Daniel K., Roig I., Bolcun-Filas E., Xu H., Boonsanay V.,
RA Eckmann C.R., Cooke H.J., Jasin M., Keeney S., McKay M.J., Toth A.;
RT "Mouse HORMAD1 and HORMAD2, two conserved meiotic chromosomal proteins, are
RT depleted from synapsed chromosome axes with the help of TRIP13 AAA-
RT ATPase.";
RL PLoS Genet. 5:E1000702-E1000702(2009).
RN [7]
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).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20711356; DOI=10.1371/journal.pgen.1001062;
RA Roig I., Dowdle J.A., Toth A., de Rooij D.G., Jasin M., Keeney S.;
RT "Mouse TRIP13/PCH2 is required for recombination and normal higher-order
RT chromosome structure during meiosis.";
RL PLoS Genet. 6:E1001062-E1001062(2010).
RN [9]
RP INTERACTION WITH PSMA8.
RX PubMed=31437213; DOI=10.1371/journal.pgen.1008316;
RA Gomez-H L., Felipe-Medina N., Condezo Y.B., Garcia-Valiente R., Ramos I.,
RA Suja J.A., Barbero J.L., Roig I., Sanchez-Martin M., de Rooij D.G.,
RA Llano E., Pendas A.M.;
RT "The PSMA8 subunit of the spermatoproteasome is essential for proper
RT meiotic exit and mouse fertility.";
RL PLoS Genet. 15:E1008316-E1008316(2019).
CC -!- FUNCTION: Plays a key role in chromosome recombination and chromosome
CC structure development during meiosis. Required at early steps in
CC meiotic recombination that leads to non-crossovers pathways. Also
CC needed for efficient completion of homologous synapsis by influencing
CC crossover distribution along the chromosomes affecting both crossovers
CC and non-crossovers pathways. Also required for development of higher-
CC order chromosome structures and is needed for synaptonemal-complex
CC formation. In males, required for efficient synapsis of the sex
CC chromosomes and for sex body formation. Promotes early steps of the DNA
CC double-strand breaks (DSBs) repair process upstream of the assembly of
CC RAD51 complexes. Required for depletion of HORMAD1 and HORMAD2 from
CC synapsed chromosomes (PubMed:17696610, PubMed:19851446,
CC PubMed:20711356). Plays a role in mitotic spindle assembly checkpoint
CC (SAC) activation (By similarity). {ECO:0000250|UniProtKB:Q15645,
CC ECO:0000269|PubMed:17696610, ECO:0000269|PubMed:19851446,
CC ECO:0000269|PubMed:20711356}.
CC -!- SUBUNIT: Specifically interacts with the ligand binding domain of the
CC thyroid receptor (TR). This interaction does not require the presence
CC of thyroid hormone for its interaction (By similarity). Interacts with
CC proteasome subunit PSMA8; to participate in meiosis progression during
CC spermatogenesis (PubMed:31437213). {ECO:0000250,
CC ECO:0000269|PubMed:31437213}.
CC -!- INTERACTION:
CC Q3UA06; Q99LG4: Ttc5; NbExp=2; IntAct=EBI-308990, EBI-21183045;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UA06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UA06-2; Sequence=VSP_041559;
CC -!- TISSUE SPECIFICITY: Widely expressed, including in testis.
CC {ECO:0000269|PubMed:20711356}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally without obvious somatic
CC defects but males and females are sterile due to meiotic disruption in
CC meiocytes. Homozygous mutants display small gonads and females have few
CC or no follicles, due to oocyte elimination between pachynema and
CC dictyate. Mutant testes display reduced populated tubules and
CC spermatogenesis is mainly arrested at spermatocyte stages of epithelial
CC stage IV, corresponding to pachynema. Different phenotypes are observed
CC in the different knockout experiments tested. In Trip13(RRB047) mutant
CC mice, also named Trip13(mod) allele for moderate, the number of
CC crossovers are not affected and meiocytes undergo homologous chromosome
CC synapsis despide the presence of unrepaired DSBs in pachynema. Using a
CC more severe mutant allele, named Trip13(sev) for severe, additional
CC defects are observed: the numbers of crossovers and chiasmata are
CC reduced in the absence of TRIP13, and their distribution along the
CC chromosomes is altered (PubMed:20711356). Autosomal bivalents in
CC meiocytes frequently display pericentric synaptic forks and other
CC defects (PubMed:20711356). Recombination defects are evident very early
CC in meiotic prophase, soon after DSB formation (PubMed:20711356). These
CC results suggest that the absence of defects in the number of crossovers
CC observed in Trip13(RRB047) mutant is due to the use of a weak
CC hypomorphic mutant allele. {ECO:0000269|PubMed:17696610,
CC ECO:0000269|PubMed:20711356}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. PCH2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK010336; BAB26861.1; -; mRNA.
DR EMBL; AK142463; BAE25076.1; -; mRNA.
DR EMBL; AK146877; BAE27499.1; -; mRNA.
DR EMBL; AK151568; BAE30510.1; -; mRNA.
DR EMBL; CT010471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466563; EDL37076.1; -; Genomic_DNA.
DR EMBL; BC023834; AAH23834.1; -; mRNA.
DR EMBL; BC126946; AAI26947.1; -; mRNA.
DR CCDS; CCDS26637.1; -. [Q3UA06-1]
DR RefSeq; NP_081458.1; NM_027182.2. [Q3UA06-1]
DR AlphaFoldDB; Q3UA06; -.
DR SMR; Q3UA06; -.
DR BioGRID; 213633; 5.
DR IntAct; Q3UA06; 10.
DR MINT; Q3UA06; -.
DR STRING; 10090.ENSMUSP00000022053; -.
DR iPTMnet; Q3UA06; -.
DR PhosphoSitePlus; Q3UA06; -.
DR EPD; Q3UA06; -.
DR MaxQB; Q3UA06; -.
DR PaxDb; Q3UA06; -.
DR PeptideAtlas; Q3UA06; -.
DR PRIDE; Q3UA06; -.
DR ProteomicsDB; 288070; -. [Q3UA06-1]
DR ProteomicsDB; 288071; -. [Q3UA06-2]
DR Antibodypedia; 8906; 335 antibodies from 33 providers.
DR DNASU; 69716; -.
DR Ensembl; ENSMUST00000022053; ENSMUSP00000022053; ENSMUSG00000021569. [Q3UA06-1]
DR GeneID; 69716; -.
DR KEGG; mmu:69716; -.
DR UCSC; uc007rei.1; mouse. [Q3UA06-1]
DR UCSC; uc011zbt.1; mouse. [Q3UA06-2]
DR CTD; 9319; -.
DR MGI; MGI:1916966; Trip13.
DR VEuPathDB; HostDB:ENSMUSG00000021569; -.
DR eggNOG; KOG0744; Eukaryota.
DR GeneTree; ENSGT00390000017432; -.
DR HOGENOM; CLU_028208_0_1_1; -.
DR InParanoid; Q3UA06; -.
DR OMA; VQIHVEV; -.
DR OrthoDB; 1036414at2759; -.
DR PhylomeDB; Q3UA06; -.
DR TreeFam; TF313507; -.
DR BioGRID-ORCS; 69716; 12 hits in 112 CRISPR screens.
DR PRO; PR:Q3UA06; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3UA06; protein.
DR Bgee; ENSMUSG00000021569; Expressed in respiratory primordium and 210 other tissues.
DR ExpressionAtlas; Q3UA06; baseline and differential.
DR Genevisible; Q3UA06; MM.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0007144; P:female meiosis I; IMP:MGI.
DR GO; GO:0007141; P:male meiosis I; IMP:MGI.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IMP:MGI.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044539; Pch2-like.
DR PANTHER; PTHR45991; PTHR45991; 1.
DR Pfam; PF00004; AAA; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Differentiation; Meiosis;
KW Nucleotide-binding; Oogenesis; Reference proteome; Spermatogenesis.
FT CHAIN 1..432
FT /note="Pachytene checkpoint protein 2 homolog"
FT /id="PRO_0000084783"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15645"
FT VAR_SEQ 1..231
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041559"
FT CONFLICT 148
FT /note="H -> R (in Ref. 1; BAB26861)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="I -> F (in Ref. 1; BAB26861)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="G -> S (in Ref. 1; BAE25076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 48377 MW; 4427E94AF4D733DB CRC64;
MDEAVGDLKQ ALPCVAESPA VHVEVLQRSG STAKKEDIKS SVYRLLNRHN IVFGDYVWTE
FDDPFLSRNV QSVSIVDTEL KAKDPQPIDL SACTIALHIF QLNEEGPSSE NLDEETENII
AASHWVLPAA EFHGLWDSLV YDVEVKSHLL DYVMTTVLFS DKNVDSNLIT WNRVVLLHGP
PGTGKTSLCK ALAQKLTIRL SSRYRYGQLI EINSHSLFSK WFSESGKLVT KMFQKIQDLI
DDKEALVFVL IDEVESLTAA RNACRAGAEP SDAIRVVNAV LTQIDQIKRH SNVVILTTSN
ITEKIDVAFV DRADIKQYIG PPSAAAIFKI YLSCLEELMK CQIIYPRQQL LTLRELEMIG
FIENNVSKLS LLLSEISRKS EGLSGRVLRK LPFLAHALYI QAPSVTIEGF LQALSLAVDK
QFEEKKKLSA YV
