AURK_PATPE
ID AURK_PATPE Reviewed; 407 AA.
AC D7UQM5;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Aurora kinase {ECO:0000312|EMBL:BAJ10384.1};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:O14965};
DE AltName: Full=ApAurora {ECO:0000303|PubMed:21048162};
GN Name=aur {ECO:0000312|EMBL:BAJ10384.1};
OS Patiria pectinifera (Starfish) (Asterina pectinifera).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC Valvatacea; Valvatida; Asterinidae; Patiria.
OX NCBI_TaxID=7594;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAJ10384.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ASP-290.
RC TISSUE=Oocyte {ECO:0000269|PubMed:21048162};
RX PubMed=21048162; DOI=10.1242/jcs.076315;
RA Abe Y., Okumura E., Hosoya T., Hirota T., Kishimoto T.;
RT "A single starfish Aurora kinase performs the combined functions of Aurora-
RT A and Aurora-B in human cells.";
RL J. Cell Sci. 123:3978-3988(2010).
CC -!- FUNCTION: Serine/threonine protein kinase that contributes to the
CC regulation of cell cycle progression. Involved in meiotic apparatus
CC formation and polar body extrusion. Contributes to Plk1 activation and
CC phosphorylation of histone H3 at 'Ser-10' during meiosis I. Required
CC for accurate progression of early embryonic M phase. Involved in
CC chromosome alignment and cleavage furrow formation during early
CC embryonic cycles. May be involved in mitotic spindle formation and
CC cytokinesis. {ECO:0000269|PubMed:21048162}.
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 Evidence={ECO:0000250|UniProtKB:O14965};
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; Evidence={ECO:0000250|UniProtKB:O14965};
CC -!- ACTIVITY REGULATION: Cdc2 activity is required for activation.
CC {ECO:0000269|PubMed:21048162}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:21048162}. Midbody {ECO:0000269|PubMed:21048162}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:21048162}. Nucleus {ECO:0000269|PubMed:21048162}.
CC Chromosome {ECO:0000269|PubMed:21048162}. Chromosome, centromere
CC {ECO:0000269|PubMed:21048162}. Note=Localized to cytoplasm in immature
CC oocytes. After 1-methyladenine-induced oocyte maturation during meiosis
CC I, becomes localized initially to the chromosomes, then to both
CC chromosomes and the meiotic spindle, and subsequently relocates from
CC the chromosomes to the midzone at anaphase onset.
CC {ECO:0000269|PubMed:21048162}.
CC -!- DEVELOPMENTAL STAGE: Expressed in immature oocytes. Expressed at
CC constant levels during meiosis and early embryonic cycles (at protein
CC level). {ECO:0000269|PubMed:21048162}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB530259; BAJ10384.1; -; mRNA.
DR AlphaFoldDB; D7UQM5; -.
DR SMR; D7UQM5; -.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; 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:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR030616; Aur.
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 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; Developmental protein; Kinase; Meiosis; Mitosis;
KW Nucleotide-binding; Nucleus; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..407
FT /note="Aurora kinase"
FT /id="PRO_0000415403"
FT DOMAIN 147..399
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 272
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14965,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O14965,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O14965,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 224..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O14965,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O14965,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 290
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:21048162"
SQ SEQUENCE 407 AA; 45947 MW; 1A9DC847213E7216 CRC64;
MTPTGPSHHS MAPKRVLPAA SQSNMYGNIR SASTTSTTAS TSSQALRLLQ NAKTSKNADN
RIAHAERQGP PSAHPAAMQK PAARVAPSNE NRPDPAARQH QHQQQLQQQK ATGHDRVLKE
SQAGNSTTTT MTSTQSKEAN KWSLANFDIG RPLGKGKFGN VYLAREKKSK FIVALKVLFK
SQLQKAKVEH QLRREIEIQS HLRHDHILRL YGYFYDDTRV YLILEYAARG ELYKEMQAQK
AGHFDEDRSA VYIYQLAKAL LYCHEKKVIH RDIKPENLLL DLKGDLKIAD FGWSVHAPSS
RRATLCGTLD YLPPEMIEGK THDEKVDLWS LGVLCYEFLV GKPPFESQGN TETYRKITKV
EFTFPKHVSE GARDLICKLL KHNPSHRLSL EGVIAHAWIQ EKISQRS
