AURKC_MOUSE
ID AURKC_MOUSE Reviewed; 276 AA.
AC O88445; Q6P209; Q9JLC2;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Aurora kinase C;
DE EC=2.7.11.1;
DE AltName: Full=Aurora 3;
DE AltName: Full=Aurora/IPL1-related kinase 3;
DE Short=ARK-3;
DE Short=Aurora-related kinase 3;
DE AltName: Full=Aurora/IPL1/Eg2 protein 1;
DE AltName: Full=Serine/threonine-protein kinase 13;
DE AltName: Full=Serine/threonine-protein kinase aurora-C;
GN Name=Aurkc; Synonyms=Aie1, Aik3, Airk3, Ark3, Stk13;
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;
RX PubMed=9809744; DOI=10.1089/dna.1998.17.823;
RA Tseng T.-C., Chen S.-H., Hsu Y.-P.P., Tang T.K.;
RT "Protein kinase profile of sperm and eggs: cloning and characterization of
RT two novel testis-specific protein kinases (AIE1, AIE2) related to yeast and
RT fly chromosome segregation regulators.";
RL DNA Cell Biol. 17:823-833(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=11098217; DOI=10.1089/10445490050199063;
RA Hu H.M., Chuang C.K., Lee M.J., Tseng T.C., Tang T.K.;
RT "Genomic organization, expression, and chromosome localization of a third
RT aurora-related kinase gene, Aie1.";
RL DNA Cell Biol. 19:679-688(2000).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH64780.1};
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, MUTAGENESIS OF THR-171 AND THR-175, AND PHOSPHORYLATION AT
RP THR-171 BY PKA.
RX PubMed=11879579; DOI=10.1089/10445490252810302;
RA Chen S.H., Tang T.K.;
RT "Mutational analysis of the phosphorylation sites of the Aie1 (Aurora-C)
RT kinase in vitro.";
RL DNA Cell Biol. 21:41-46(2002).
RN [6]
RP FUNCTION.
RX PubMed=21613325; DOI=10.1242/dev.066381;
RA Fernandez-Miranda G., Trakala M., Martin J., Escobar B., Gonzalez A.,
RA Ghyselinck N.B., Ortega S., Canamero M., de Castro I.P., Malumbres M.;
RT "Genetic disruption of aurora B uncovers an essential role for aurora C
RT during early mammalian development.";
RL Development 138:2661-2672(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase component of the chromosomal
CC passenger complex (CPC), a complex that acts as a key regulator of
CC mitosis. The CPC complex has essential functions at the centromere in
CC ensuring correct chromosome alignment and segregation and is required
CC for chromatin-induced microtubule stabilization and spindle assembly.
CC Also plays a role in meiosis and more particularly in spermatogenesis.
CC Has redundant cellular functions with AURKB and can rescue an AURKB
CC knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and
CC 'Ser-28'. AURKC phosphorylates the CPC complex subunits BIRC5/survivin
CC and INCENP leading to increased AURKC activity. Phosphorylates TACC1,
CC another protein involved in cell division, at 'Ser-228'.
CC {ECO:0000269|PubMed:11879579, ECO:0000269|PubMed:21613325}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Okadaic acid, an inhibitor of protein phosphatase
CC 1 (PP1), protein phosphatase 2A (PP2A) and protein phosphatase 5 (PP5),
CC increases AURKC activity. AURKC is also stabilized through its
CC interaction with INCENP, which acts also as an activator (By
CC similarity). {ECO:0000250|UniProtKB:Q9UQB9}.
CC -!- SUBUNIT: Component of the chromosomal passenger complex (CPC) composed
CC of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC;
CC predominantly independent AURKB- and AURKC-containing complexes exist;
CC in the complex interacts directly with BIRC5/survivin and INCENP.
CC Interacts with TACC1. {ECO:0000250|UniProtKB:Q9UQB9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:Q9UQB9}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UQB9}. Note=Distributes
CC in the condensed chromosomes during prophase to metaphase. After
CC entering anaphase, there is a dissociation from separated chromosomes
CC and a redistribution to midzone microtubules, and finally remains in
CC the midbody during cytokinesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9UQB9}.
CC -!- TISSUE SPECIFICITY: Expressed only in testis.
CC -!- DEVELOPMENTAL STAGE: Expressed on day 14 dpc in prepubertal testis,
CC expression reached its plateau on day 21 dpc and remained at a high
CC level in adult.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AF054620; AAC25954.1; -; mRNA.
DR EMBL; AF195272; AAF25838.1; -; Genomic_DNA.
DR EMBL; AC152418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064780; AAH64780.1; -; mRNA.
DR CCDS; CCDS85211.1; -.
DR RefSeq; NP_001074435.1; NM_001080966.1.
DR RefSeq; NP_065597.2; NM_020572.2.
DR RefSeq; XP_006539760.1; XM_006539697.3.
DR RefSeq; XP_006539764.1; XM_006539701.3.
DR RefSeq; XP_011248768.1; XM_011250466.2.
DR RefSeq; XP_017177568.1; XM_017322079.1.
DR RefSeq; XP_017177569.1; XM_017322080.1.
DR RefSeq; XP_017177570.1; XM_017322081.1.
DR AlphaFoldDB; O88445; -.
DR SMR; O88445; -.
DR STRING; 10090.ENSMUSP00000083426; -.
DR iPTMnet; O88445; -.
DR PhosphoSitePlus; O88445; -.
DR PaxDb; O88445; -.
DR PRIDE; O88445; -.
DR ProteomicsDB; 273431; -.
DR ProteomicsDB; 334427; -.
DR Antibodypedia; 33237; 510 antibodies from 30 providers.
DR DNASU; 20871; -.
DR Ensembl; ENSMUST00000086248; ENSMUSP00000083426; ENSMUSG00000070837.
DR Ensembl; ENSMUST00000207711; ENSMUSP00000146450; ENSMUSG00000070837.
DR Ensembl; ENSMUST00000208049; ENSMUSP00000147207; ENSMUSG00000070837.
DR GeneID; 20871; -.
DR KEGG; mmu:20871; -.
DR UCSC; uc009fcf.1; mouse.
DR CTD; 6795; -.
DR MGI; MGI:1321119; Aurkc.
DR VEuPathDB; HostDB:ENSMUSG00000070837; -.
DR eggNOG; KOG0580; Eukaryota.
DR GeneTree; ENSGT00940000161619; -.
DR InParanoid; O88445; -.
DR OMA; RRTWTIN; -.
DR BioGRID-ORCS; 20871; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Aurkc; mouse.
DR PRO; PR:O88445; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O88445; protein.
DR Bgee; ENSMUSG00000070837; Expressed in secondary oocyte and 23 other tissues.
DR ExpressionAtlas; O88445; baseline and differential.
DR GO; GO:0005694; C:chromosome; IDA:MGI.
DR GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:1990385; C:meiotic spindle midzone; IDA:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0031616; C:spindle pole centrosome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0048599; P:oocyte development; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:InterPro.
DR GO; GO:0051255; P:spindle midzone assembly; IEA:InterPro.
DR InterPro; IPR030616; Aur.
DR InterPro; IPR030613; AURKC.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24350; PTHR24350; 1.
DR PANTHER; PTHR24350:SF3; PTHR24350:SF3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Kinase; Meiosis; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..276
FT /note="Aurora kinase C"
FT /id="PRO_0000085661"
FT DOMAIN 16..266
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 171
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:11879579"
FT MUTAGEN 171
FT /note="T->A: Impairs kinase activity, when associated with
FT A-175."
FT /evidence="ECO:0000269|PubMed:11879579"
FT MUTAGEN 175
FT /note="T->A: Impairs kinase activity, when associated with
FT A-171."
FT /evidence="ECO:0000269|PubMed:11879579"
FT CONFLICT 74
FT /note="R -> P (in Ref. 2; AAF25838)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="C -> PCVHGAS (in Ref. 1; AAC25954 and 2; AAF25838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 276 AA; 32358 MW; 91530FF97594D63E CRC64;
MEPSTSTRKH FTINDFEIGR PLGRGKFGRV YLARLKENHF IVALKVLFKS EIEKEGLEHQ
LRREVEIQAH LQHRNILRLY NYFYDDTRIY LILEYAPGGE LYKELQRHQK LDQQRTATII
QELSDALTYC HEKKVIHRDI KPENLLLGLN GEVKISDFGW SVHTPSLRRK TMCGTLDYLP
PEMIAQKPYN EMVDLWCIGV LCYELLVGKP PFESSTSSET YRRIRQVDFK FPSSVPAGAQ
DLISKLLRYH PSERLSLAQV LKHPWVREHS RRVLPC
