CCNA1_MOUSE
ID CCNA1_MOUSE Reviewed; 421 AA.
AC Q61456; Q8C5U1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cyclin-A1;
GN Name=Ccna1;
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].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=8565853; DOI=10.1242/dev.122.1.53;
RA Sweeney C., Murphy M., Kubelka M., Ravnik S.E., Hawkins C.F.,
RA Wolgemuth D.J., Carrington M.;
RT "A distinct cyclin A is expressed in germ cells in the mouse.";
RL Development 122:53-64(1996).
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 MRNA].
RC TISSUE=Brain;
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 FUNCTION.
RX PubMed=9843212; DOI=10.1038/3855;
RA Liu D., Matzuk M.M., Sung W.K., Guo Q., Wang P., Wolgemuth D.J.;
RT "Cyclin A1 is required for meiosis in the male mouse.";
RL Nat. Genet. 20:377-380(1998).
RN [5]
RP FUNCTION.
RC STRAIN=Swiss Webster;
RX PubMed=10068472; DOI=10.1006/dbio.1998.9156;
RA Ravnik S.E., Wolgemuth D.J.;
RT "Regulation of meiosis during mammalian spermatogenesis: the A-type cyclins
RT and their associated cyclin-dependent kinases are differentially expressed
RT in the germ-cell lineage.";
RL Dev. Biol. 207:408-418(1999).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH CDK2; CABLES1 AND CCNE1.
RX PubMed=11585773;
RA Wu C.-L., Kirley S.D., Xiao H., Chuang Y., Chung D.C., Zukerberg L.R.;
RT "Cables enhances cdk2 tyrosine 15 phosphorylation by Wee1, inhibits cell
RT growth, and is lost in many human colon and squamous cancers.";
RL Cancer Res. 61:7325-7332(2001).
CC -!- FUNCTION: May be involved in the control of the cell cycle at the G1/S
CC (start) and G2/M (mitosis) transitions. May primarily function in the
CC control of the germline meiotic cell cycle and additionally in the
CC control of mitotic cell cycle in some somatic cells.
CC {ECO:0000269|PubMed:10068472, ECO:0000269|PubMed:9843212}.
CC -!- SUBUNIT: Interacts with INCA1 and KLHDC9 (By similarity). Interacts
CC with the CDK2 and CDC2 protein kinases to form a serine/threonine
CC kinase holoenzyme complex. The cyclin subunit imparts substrate
CC specificity to the complex. Found in a complex with CDK2, CABLES1 and
CC CCNE1. {ECO:0000250|UniProtKB:P78396, ECO:0000269|PubMed:11585773}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle. Note=In oocytes at least, it associates with the spindle
CC during metaphase.
CC -!- TISSUE SPECIFICITY: Testis and ovaries.
CC -!- DEVELOPMENTAL STAGE: In male germ cells just prior to or during the
CC first, but not the second meiotic division.
CC -!- PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the anaphase-
CC promoting complex (APC/C), leading to its degradation by the
CC proteasome. Deubiquitinated and stabilized by USP37 enables entry into
CC S phase (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: CCNA1 -/- males are sterile due to a block of
CC spermatogenesis before the first meiotic division, whereas females are
CC normal.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; X84311; CAA59053.1; -; mRNA.
DR EMBL; AK077114; BAC36619.1; -; mRNA.
DR EMBL; BC120518; AAI20519.1; -; mRNA.
DR EMBL; BC125436; AAI25437.1; -; mRNA.
DR CCDS; CCDS17356.1; -.
DR RefSeq; NP_001292150.1; NM_001305221.1.
DR RefSeq; NP_031654.2; NM_007628.3.
DR RefSeq; XP_006501012.1; XM_006500949.2.
DR RefSeq; XP_006501013.1; XM_006500950.3.
DR RefSeq; XP_006501014.1; XM_006500951.2.
DR RefSeq; XP_006501015.1; XM_006500952.2.
DR RefSeq; XP_011238305.1; XM_011240003.2.
DR AlphaFoldDB; Q61456; -.
DR SMR; Q61456; -.
DR BioGRID; 198544; 6.
DR ComplexPortal; CPX-2061; Cyclin A1-CDK1 complex.
DR ComplexPortal; CPX-2065; Cyclin A1-CDK2 complex.
DR CORUM; Q61456; -.
DR STRING; 10090.ENSMUSP00000029368; -.
DR iPTMnet; Q61456; -.
DR PhosphoSitePlus; Q61456; -.
DR PaxDb; Q61456; -.
DR PRIDE; Q61456; -.
DR ProteomicsDB; 281335; -.
DR Antibodypedia; 4520; 542 antibodies from 37 providers.
DR DNASU; 12427; -.
DR Ensembl; ENSMUST00000029368; ENSMUSP00000029368; ENSMUSG00000027793.
DR Ensembl; ENSMUST00000197238; ENSMUSP00000142692; ENSMUSG00000027793.
DR Ensembl; ENSMUST00000198320; ENSMUSP00000143447; ENSMUSG00000027793.
DR GeneID; 12427; -.
DR KEGG; mmu:12427; -.
DR UCSC; uc008pfy.3; mouse.
DR CTD; 8900; -.
DR MGI; MGI:108042; Ccna1.
DR VEuPathDB; HostDB:ENSMUSG00000027793; -.
DR eggNOG; KOG0654; Eukaryota.
DR GeneTree; ENSGT00940000157940; -.
DR HOGENOM; CLU_020695_3_2_1; -.
DR InParanoid; Q61456; -.
DR OMA; YKSSKYC; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; Q61456; -.
DR TreeFam; TF101002; -.
DR Reactome; R-MMU-1538133; G0 and Early G1.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR Reactome; R-MMU-68911; G2 Phase.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-MMU-69563; p53-Dependent G1 DNA Damage Response.
DR Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR BioGRID-ORCS; 12427; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q61456; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q61456; protein.
DR Bgee; ENSMUSG00000027793; Expressed in spermatid and 36 other tissues.
DR ExpressionAtlas; Q61456; baseline and differential.
DR Genevisible; Q61456; MM.
DR GO; GO:0097123; C:cyclin A1-CDK2 complex; IDA:MGI.
DR GO; GO:0097124; C:cyclin A2-CDK2 complex; IBA:GO_Central.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR032447; Cyclin-A_N.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF16500; Cyclin_N2; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cyclin; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Meiosis; Mitosis; Nucleus;
KW Reference proteome; Spermatogenesis; Ubl conjugation.
FT CHAIN 1..421
FT /note="Cyclin-A1"
FT /id="PRO_0000080334"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 176
FT /note="R -> P (in Ref. 1; CAA59053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 47772 MW; FF717D0065B954E9 CRC64;
MHRQSSKSGV ALPPVGQGPD ACQMLSRAQL GQDPPQRTVL GVLTENEQYR RTCGQEITAI
RCFSGSENVF PAAGKKVLSD HGVNEPAKRG FDIYMDDPEQ GDRDTCSGKE GIIFEDVYEV
DTSMLKSDLH FLLDFNTVSP MLVDPTTHAQ SEEATDFGSD VINVTEYAEE IHRYLREAEV
RHRPKAHYMR KQPDITEGMR AILVDWLVEV GEEYKLRTET LYLAVNFLDR FLSCMSVLRG
KLQLVGTAAI LLASKYEEIY PPDVDEFVYI TDDTYTKRQL LRMEHLLLKV LAFDLTVPTT
NQFLLQYLRR QGVCIRTENL AKYVAELSLL EADPFLKYLP SLVAAAAYCL ANYIVNRHFW
PETLAAFTGY SLNEIVPCLS ELHKACLSIP HRPQQAIREK YKASKYLHVS LMEPPVVLPL
Q