CNTD1_MOUSE
ID CNTD1_MOUSE Reviewed; 334 AA.
AC Q9D995; Q9D9L8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cyclin N-terminal domain-containing protein 1 {ECO:0000305};
GN Name=Cntd1 {ECO:0000312|MGI:MGI:1923965}; Synonyms=Cntd;
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].
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 [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 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 [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=24891606; DOI=10.1083/jcb.201401122;
RA Holloway J.K., Sun X., Yokoo R., Villeneuve A.M., Cohen P.E.;
RT "Mammalian CNTD1 is critical for meiotic crossover maturation and
RT deselection of excess precrossover sites.";
RL J. Cell Biol. 205:633-641(2014).
RN [5]
RP ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY (ISOFORM 2),
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH CDC34; RFC3 AND RFC4.
RX PubMed=32640224; DOI=10.1016/j.celrep.2020.107858;
RA Gray S., Santiago E.R., Chappie J.S., Cohen P.E.;
RT "Cyclin N-Terminal Domain-Containing-1 Coordinates Meiotic Crossover
RT Formation with Cell-Cycle Progression in a Cyclin-Independent Manner.";
RL Cell Rep. 32:107858-107858(2020).
RN [6]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH PRR19.
RX PubMed=32555348; DOI=10.1038/s41467-020-16885-3;
RA Bondarieva A., Raveendran K., Telychko V., Rao H.B.D.P., Ravindranathan R.,
RA Zorzompokou C., Finsterbusch F., Dereli I., Papanikos F., Traenkner D.,
RA Schleiffer A., Fei J.F., Klimova A., Ito M., Kulkarni D.S., Roeder I.,
RA Hunter N., Toth A.;
RT "Proline-rich protein PRR19 functions with cyclin-like CNTD1 to promote
RT meiotic crossing over in mouse.";
RL Nat. Commun. 11:3101-3101(2020).
CC -!- FUNCTION: Plays a role in the different steps of crossover formation
CC during meiotic recombination (PubMed:24891606, PubMed:32640224,
CC PubMed:32555348). Participates in the crossover differentiation step of
CC crossover-specific recombination intermediates through its interaction
CC with PRR19 (PubMed:32555348). In addition, stimulates crossover
CC formation through the interactions with RFC3 and RFC4 and
CC simultaneously regulates cell-cycle progression through interactions
CC with CDC34 and subsequent ubiquitination of WEE1 (PubMed:32640224). May
CC also participates in an active deselection process that destabilizes or
CC removes excess pre-CO intermediates (PubMed:24891606).
CC {ECO:0000269|PubMed:24891606, ECO:0000269|PubMed:32555348,
CC ECO:0000269|PubMed:32640224}.
CC -!- SUBUNIT: Interacts with PRR19; this interaction promotes crossover
CC formation (PubMed:32555348). Interacts with RFC3 and RFC4; these
CC interactions facilitate crossover formation (PubMed:32640224).
CC Interacts with CDC34; this interaction regulates the cell-cycle
CC progression (PubMed:32640224). {ECO:0000269|PubMed:32555348,
CC ECO:0000269|PubMed:32640224}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32640224}. Cytoplasm
CC {ECO:0000269|PubMed:32640224}. Chromosome
CC {ECO:0000269|PubMed:32555348}. Note=Shuttles between the nucleus and
CC cytoplasm in a stage-specific manner of prophase I cells
CC (PubMed:32640224). Co-localized at crossover sites with PRR19
CC (PubMed:32555348). {ECO:0000269|PubMed:32555348,
CC ECO:0000269|PubMed:32640224}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D995-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:32640224};
CC IsoId=Q9D995-3; Sequence=VSP_061282;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in spermatocyte.
CC {ECO:0000269|PubMed:32640224}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice for CNTD1 are grossly
CC similar to wild-type, surviving into adulthood and exhibiting
CC appropriate mating behavior. Males are sterile with a decreased testis
CC size. Females are also sterile. {ECO:0000269|PubMed:24891606}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24728.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AK006754; BAB24728.1; ALT_SEQ; mRNA.
DR EMBL; AK007245; BAB24912.1; -; mRNA.
DR EMBL; AK049116; BAC33551.1; -; mRNA.
DR EMBL; AL590969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006866; AAH06866.1; -; mRNA.
DR CCDS; CCDS25461.1; -. [Q9D995-1]
DR RefSeq; NP_080838.1; NM_026562.2.
DR AlphaFoldDB; Q9D995; -.
DR BioGRID; 212659; 1.
DR STRING; 10090.ENSMUSP00000099396; -.
DR PhosphoSitePlus; Q9D995; -.
DR PaxDb; Q9D995; -.
DR PRIDE; Q9D995; -.
DR ProteomicsDB; 283659; -.
DR Antibodypedia; 17117; 96 antibodies from 20 providers.
DR Ensembl; ENSMUST00000103107; ENSMUSP00000099396; ENSMUSG00000078653. [Q9D995-1]
DR GeneID; 68107; -.
DR KEGG; mmu:68107; -.
DR UCSC; uc007loi.1; mouse. [Q9D995-1]
DR CTD; 124817; -.
DR MGI; MGI:1923965; Cntd1.
DR VEuPathDB; HostDB:ENSMUSG00000078653; -.
DR eggNOG; ENOG502QVK8; Eukaryota.
DR GeneTree; ENSGT00440000033966; -.
DR HOGENOM; CLU_072822_0_0_1; -.
DR InParanoid; Q9D995; -.
DR OMA; VTEDYML; -.
DR OrthoDB; 1572593at2759; -.
DR PhylomeDB; Q9D995; -.
DR TreeFam; TF342669; -.
DR BioGRID-ORCS; 68107; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9D995; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D995; protein.
DR Bgee; ENSMUSG00000078653; Expressed in spermatocyte and 118 other tissues.
DR Genevisible; Q9D995; MM.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:MGI.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR InterPro; IPR039890; CNTD1.
DR InterPro; IPR036915; Cyclin-like_sf.
DR PANTHER; PTHR21615; PTHR21615; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Cytoplasm; Meiosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..334
FT /note="Cyclin N-terminal domain-containing protein 1"
FT /id="PRO_0000313716"
FT DOMAIN 29..180
FT /note="Cyclin N-terminal"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:32640224"
FT /id="VSP_061282"
FT CONFLICT 178
FT /note="Q -> E (in Ref. 1; BAB24728)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="S -> R (in Ref. 1; BAB24728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37222 MW; B40F366F062779A4 CRC64;
MNMEGPLRPR LVNCSDFQFG VVTTETIENA LLHLAQQNEQ AVKEAAGRTG SFRETRIVEF
VFLLSEQWCL EKSVSYQAVE ILERFMLKQA EDICRQATLQ LRGKDTELQS WRAMKEQLVN
KFILRLVSCV QLASKLSFHY KIVSNITVLN FLQALGYVHT KEELLESELD ILKSLNFQIN
LPTPLAYVEM LLEVLGYNGC LVPATQLHAT CLTLLDLVYL LHEPIYESLL RASIENSTPS
QLQGEKFLSV KEDFMLLAVG IIAASAFIQN HECWSQVIGH LQSITGIASE SIAEFSYAIL
THSVGANTPG PQQPVPHKAA RALRTAAAAA SSNT
