ETAA1_BOVIN
ID ETAA1_BOVIN Reviewed; 899 AA.
AC Q08DI1;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Ewing's tumor-associated antigen 1 homolog {ECO:0000250|UniProtKB:Q9NY74};
GN Name=ETAA1 {ECO:0000250|UniProtKB:Q9NY74};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Replication stress response protein that accumulates at DNA
CC damage sites and promotes replication fork progression and integrity.
CC Recruited to stalled replication forks via interaction with the RPA
CC complex and directly stimulates ATR kinase activity independently of
CC TOPBP1. Probably only regulates a subset of ATR targets.
CC {ECO:0000250|UniProtKB:Q9NY74}.
CC -!- SUBUNIT: Interacts (via RBM1 motif) with RPA1. Interacts (via RBM2
CC motif) with RPA2. Interacts (via the ATR-activation domain motif) with
CC ATR. {ECO:0000250|UniProtKB:Q9NY74}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NY74}.
CC Note=Localizes at sites of DNA damage following replication stress.
CC Recruited to stalled replication forks via interaction with RPA1 and
CC RPA2 subunits of the RPA complex. {ECO:0000250|UniProtKB:Q9NY74}.
CC -!- DOMAIN: The RBM1 (RPA1-binding, also named RPA70N-binding) motif
CC mediates interaction with RPA1. The RBM2 (RPA2-binding, also named
CC RPA32C-binding) motif mediates interaction with RPA2.
CC {ECO:0000250|UniProtKB:Q9NY74}.
CC -!- DOMAIN: The ATR-activation domain (AAD) motif is required to bind and
CC activate ATR. {ECO:0000250|UniProtKB:Q9NY74}.
CC -!- PTM: Phosphorylated by ATR. {ECO:0000250|UniProtKB:Q9NY74}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC123739; AAI23740.1; -; mRNA.
DR RefSeq; NP_001068596.1; NM_001075128.1.
DR AlphaFoldDB; Q08DI1; -.
DR SMR; Q08DI1; -.
DR STRING; 9913.ENSBTAP00000015577; -.
DR PaxDb; Q08DI1; -.
DR PRIDE; Q08DI1; -.
DR Ensembl; ENSBTAT00000015577; ENSBTAP00000015577; ENSBTAG00000011727.
DR GeneID; 282224; -.
DR KEGG; bta:282224; -.
DR CTD; 54465; -.
DR VEuPathDB; HostDB:ENSBTAG00000011727; -.
DR VGNC; VGNC:28616; ETAA1.
DR eggNOG; ENOG502QTMP; Eukaryota.
DR GeneTree; ENSGT00390000009597; -.
DR HOGENOM; CLU_015351_0_0_1; -.
DR InParanoid; Q08DI1; -.
DR OMA; CITGSMS; -.
DR OrthoDB; 365628at2759; -.
DR TreeFam; TF333863; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000011727; Expressed in spermatid and 111 other tissues.
DR ExpressionAtlas; Q08DI1; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR InterPro; IPR029406; ETAA1.
DR PANTHER; PTHR16434; PTHR16434; 1.
DR Pfam; PF15350; ETAA1; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; DNA damage; DNA repair; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..899
FT /note="Ewing's tumor-associated antigen 1 homolog"
FT /id="PRO_0000280098"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..210
FT /evidence="ECO:0000255"
FT MOTIF 105..111
FT /note="ATR-activation domain (AAD)"
FT /evidence="ECO:0000250|UniProtKB:Q9NY74"
FT MOTIF 607..622
FT /note="RBM1 motif"
FT /evidence="ECO:0000250|UniProtKB:Q9NY74"
FT MOTIF 868..890
FT /note="RBM2 motif"
FT /evidence="ECO:0000250|UniProtKB:Q9NY74"
FT COMPBIAS 856..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NY74"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NY74"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NY74"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NY74"
FT CROSSLNK 485
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NY74"
FT CROSSLNK 539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NY74"
SQ SEQUENCE 899 AA; 99859 MW; 6B986979E1D3655A CRC64;
MSRRRKHGDS SGLKQTPRKA MATEEGSLVF ESGKRRLRAA RGSGPQGPGE RPPRPLPQQE
QPPVAASCRK SNTEERYETP KRMLQMDLLS STFSSPNDPD GQNDIFWDQN SPMTKQLDKG
RKKQLYTTDS DEISHIVNRI APQDEKPTTD SMLGVWIGDT AIPCTPSVAK GKSRTKLSCT
KLKSQNQEEE LMKLAKQFDK NMEELDVIQE QDKRNHDLIQ MISEAETSLN CRDNVQMQLL
CDTVPEIDKA LLKKPVKENT KISVVNDQTS SQKPFDQNAE AAFIAMFDGS TQKCSGQLSQ
DLSDSFLKTS NTTFGKKNTL KEEKIITNES VVTENLPSKT LGSLSHQVDN PGMTKSYVTF
CTKEPGTFNK HIDTFTTSDF EDDWENLLSN EPFVMQNIET SELFPAPKTI QIADQKEMCS
FNSKEAKSKS GMNKSVDVKL RDSKILQGLP SNTWNNELTD AEKYRFSPKP NDKPNKLSTT
GNKMKLEKSF NIVVNQDKIQ DCAVASNLTK VNEDTHTKFN CKVNASEKKS ALKPGCSNKS
IFNQSLKVPA NVKPFGSATL GSTTSVCNPD QTNGSKLGSF FDDWNDPSFT NEIVKACHQL
ENSWEADDVD DDILYQACDD IERLTQEQNI RVDSKTSESV LEINNSSKHG AKNVFTTPKQ
GSQFMQSKHL NLNSISAQTS SLANSLQINK SVKMERGEMY GNSPGFLGAT TNLSIYSKNS
DCQISNLHVS CNNPDVPKQV NSSKSVLTGS SSLNVGSHHM STEIAASKNR LSTLHLSKST
TRGKAQSDLN RAVRLSEYVF TKMKNCPMLS PFNNSSVTGS ISDTKIAQGL EKNKTVNPLP
GKAVQQQPLV KFSEPLKQPS KEEEEKNRKC SPEEIQRKRQ AALIRRMAKA QASSVKKGR
