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   27-MAR-2024, entry version 130.
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; 6.
DR   IntAct; Q3UA06; 10.
DR   MINT; Q3UA06; -.
DR   STRING; 10090.ENSMUSP00000022053; -.
DR   iPTMnet; Q3UA06; -.
DR   PhosphoSitePlus; Q3UA06; -.
DR   SwissPalm; Q3UA06; -.
DR   EPD; Q3UA06; -.
DR   MaxQB; Q3UA06; -.
DR   PaxDb; 10090-ENSMUSP00000022053; -.
DR   PeptideAtlas; Q3UA06; -.
DR   ProteomicsDB; 288070; -. [Q3UA06-1]
DR   ProteomicsDB; 288071; -. [Q3UA06-2]
DR   Pumba; Q3UA06; -.
DR   Antibodypedia; 8906; 366 antibodies from 33 providers.
DR   DNASU; 69716; -.
DR   Ensembl; ENSMUST00000022053.11; ENSMUSP00000022053.9; ENSMUSG00000021569.11. [Q3UA06-1]
DR   GeneID; 69716; -.
DR   KEGG; mmu:69716; -.
DR   UCSC; uc007rei.1; mouse. [Q3UA06-1]
DR   UCSC; uc011zbt.1; mouse. [Q3UA06-2]
DR   AGR; MGI:1916966; -.
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; NVCDSVQ; -.
DR   OrthoDB; 10402at2759; -.
DR   PhylomeDB; Q3UA06; -.
DR   TreeFam; TF313507; -.
DR   BioGRID-ORCS; 69716; 12 hits in 117 CRISPR screens.
DR   PRO; PR:Q3UA06; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q3UA06; Protein.
DR   Bgee; ENSMUSG00000021569; Expressed in respiratory primordium and 214 other cell types or tissues.
DR   ExpressionAtlas; Q3UA06; baseline and differential.
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   CDD; cd19508; RecA-like_Pch2-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; PACHYTENE CHECKPOINT PROTEIN 2; 1.
DR   PANTHER; PTHR45991:SF1; PACHYTENE CHECKPOINT PROTEIN 2 HOMOLOG; 1.
DR   Pfam; PF00004; AAA; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
DR   Genevisible; Q3UA06; MM.
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
//