ID   PCH2_CANLF              Reviewed;         432 AA.
AC   E2R222;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 65.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer;
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q3UA06}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. PCH2 subfamily.
CC       {ECO:0000305}.
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DR   RefSeq; NP_001300798.1; NM_001313869.1.
DR   AlphaFoldDB; E2R222; -.
DR   SMR; E2R222; -.
DR   STRING; 9615.ENSCAFP00000015956; -.
DR   PaxDb; E2R222; -.
DR   Ensembl; ENSCAFT00030015334; ENSCAFP00030013372; ENSCAFG00030008325.
DR   Ensembl; ENSCAFT00040046358; ENSCAFP00040040455; ENSCAFG00040024866.
DR   Ensembl; ENSCAFT00845047843; ENSCAFP00845037534; ENSCAFG00845027144.
DR   GeneID; 609426; -.
DR   KEGG; cfa:609426; -.
DR   CTD; 9319; -.
DR   VEuPathDB; HostDB:ENSCAFG00845027144; -.
DR   eggNOG; KOG0744; Eukaryota.
DR   GeneTree; ENSGT00390000017432; -.
DR   HOGENOM; CLU_028208_0_1_1; -.
DR   InParanoid; E2R222; -.
DR   OMA; VQIHVEV; -.
DR   OrthoDB; 1036414at2759; -.
DR   TreeFam; TF313507; -.
DR   Proteomes; UP000002254; Chromosome 34.
DR   Bgee; ENSCAFG00000010838; Expressed in keratinocyte and 50 other tissues.
DR   GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR   GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0007144; P:female meiosis I; IEA:Ensembl.
DR   GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR   GO; GO:0051598; P:meiotic recombination checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:Ensembl.
DR   GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
DR   GO; GO:0048477; P:oogenesis; ISS:UniProtKB.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; ISS:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   GO; GO:0007130; P:synaptonemal complex assembly; ISS: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   3: Inferred from homology;
KW   Acetylation; ATP-binding; Differentiation; Meiosis; Nucleotide-binding;
KW   Oogenesis; Reference proteome; Spermatogenesis.
FT   CHAIN           1..432
FT                   /note="Pachytene checkpoint protein 2 homolog"
FT                   /id="PRO_0000410921"
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"
SQ   SEQUENCE   432 AA;  48435 MW;  2B8CC6512A30E3AE CRC64;
     MDEAVGDLKQ ALPCVAEAPT VHVEVHQRSC STAKKEDIKL SVRKLLNRHN IVFGDYKWNE
     FDDPFLARNV QSVSIVDTEL KVKDPQPIDL GACTIALHVF QLNEGGPSSE TLEEETENIT
     AASHWVLPAA EFHGLWDSLV YDVEVKSHLL DYVMTTLLFS DKNVDSNLIA WNRVVLLHGP
     PGTGKTSLCK ALAQKLTIRL SSRYQYGQLI EINSHSLFSK WFSESGKLVT KMFQKIQDLI
     DDKDALVFVL IDEVESLTAA RNACRAGTEP SDAIRVVNAV LTQIDQIKRH CNVVILTTSN
     ITERIDVAFV DRADIRQYIG PPSAAAIFKI YLSCLEELMK CQIIYPRQQL LTLRELEMIG
     FIENNVSKLS LLLSEISRKS EGLSGRVLRK LPFLAHALYI QAPTVTIEGF LQALSLAVDK
     QFEERKKLSS CI