ETAA1_MOUSE
ID ETAA1_MOUSE Reviewed; 877 AA.
AC Q5SVT3; Q8BZM6; Q8K332; Q9CS19; Q9D2Z9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ewing's tumor-associated antigen 1 homolog {ECO:0000250|UniProtKB:Q9NY74};
GN Name=Etaa1 {ECO:0000312|MGI:MGI:1915395};
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] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-852 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cecum, and Diencephalon;
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] (ISOFORM 1).
RC STRAIN=Czech II; 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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5SVT3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SVT3-2; Sequence=VSP_023538;
CC Name=3;
CC IsoId=Q5SVT3-3; Sequence=VSP_023537;
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 -!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AK018594; BAB31298.1; -; mRNA.
DR EMBL; AK034138; BAC28601.1; -; mRNA.
DR EMBL; AK019965; BAB31940.3; -; mRNA.
DR EMBL; AL627070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028916; AAH28916.1; -; mRNA.
DR CCDS; CCDS24452.1; -. [Q5SVT3-1]
DR RefSeq; NP_080852.2; NM_026576.3. [Q5SVT3-1]
DR RefSeq; XP_006514863.1; XM_006514800.3.
DR AlphaFoldDB; Q5SVT3; -.
DR SMR; Q5SVT3; -.
DR STRING; 10090.ENSMUSP00000075957; -.
DR iPTMnet; Q5SVT3; -.
DR PhosphoSitePlus; Q5SVT3; -.
DR PaxDb; Q5SVT3; -.
DR PRIDE; Q5SVT3; -.
DR ProteomicsDB; 275694; -. [Q5SVT3-1]
DR ProteomicsDB; 275695; -. [Q5SVT3-2]
DR ProteomicsDB; 275696; -. [Q5SVT3-3]
DR Antibodypedia; 47441; 57 antibodies from 19 providers.
DR DNASU; 68145; -.
DR Ensembl; ENSMUST00000076661; ENSMUSP00000075957; ENSMUSG00000016984. [Q5SVT3-1]
DR GeneID; 68145; -.
DR KEGG; mmu:68145; -.
DR UCSC; uc007icf.2; mouse. [Q5SVT3-1]
DR CTD; 54465; -.
DR MGI; MGI:1915395; Etaa1.
DR VEuPathDB; HostDB:ENSMUSG00000016984; -.
DR eggNOG; ENOG502QTMP; Eukaryota.
DR GeneTree; ENSGT00390000009597; -.
DR HOGENOM; CLU_015351_0_0_1; -.
DR InParanoid; Q5SVT3; -.
DR OMA; CITGSMS; -.
DR OrthoDB; 365628at2759; -.
DR PhylomeDB; Q5SVT3; -.
DR TreeFam; TF333863; -.
DR BioGRID-ORCS; 68145; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Etaa1; mouse.
DR PRO; PR:Q5SVT3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SVT3; protein.
DR Bgee; ENSMUSG00000016984; Expressed in primary oocyte and 231 other tissues.
DR Genevisible; Q5SVT3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 Alternative splicing; Coiled coil; DNA damage; DNA repair; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..877
FT /note="Ewing's tumor-associated antigen 1 homolog"
FT /id="PRO_0000280100"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..213
FT /evidence="ECO:0000255"
FT COILED 306..335
FT /evidence="ECO:0000255"
FT MOTIF 107..113
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 843..865
FT /note="RBM2 motif"
FT /evidence="ECO:0000250|UniProtKB:Q9NY74"
FT COMPBIAS 457..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..856
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 CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
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 510
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NY74"
FT VAR_SEQ 1..222
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023537"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023538"
FT CONFLICT 21
FT /note="A -> S (in Ref. 3; AAH28916)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="L -> V (in Ref. 1; BAB31940)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="D -> G (in Ref. 1; BAC28601)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="D -> G (in Ref. 1; BAC28601)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="V -> M (in Ref. 3; AAH28916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 877 AA; 96552 MW; 6A03F2B9F4ED2598 CRC64;
MQLKDGGTGM SRRRKHADSP ARRSTPHRAA AKNCRPAAEP WLRESRAACS SQLRRAGTRS
ARRAQRQAAA DGGRSPRGKE TPVQIVKMDL LSCTFSSPND PDGQTDIFWD QNSPMTKQLG
KGRKKQISSA YSDEISHIVN RIAPQDEKPV TNSMLGVWIG ETAIPCTPGV AKEKSRVKAS
CTKLKTKNRE KELMKLAQQF DKNMEELDVI QEQDGKNHDF IQMTSKMGHL DNHKDSVQKP
SGDVVPEITC TPVKKQMKGD SRISLAKAQD SSQKPFDQNV EAAFNAIFDG STQMCSGQLS
QDLLDAFLNN SKTSLRKKNA LLQEEIITTE TLLTENLLNK TPISLSPQID TTVILNSCVT
PCPKTPAAPD TQLDELTAND FEDDWESLLG SEPFLMENAE MLEFVPSTTA QDTCQKAICT
SVGENDTITS RTNMNLGGRL RDSKVTLDLP SKTRNGELRN AGEHRFSSHP GDESRKVPFT
GNKVSFEKSV TSIVSKDEDY VAVSNLEKVK EDSRNKCILN KHSSNKSSSY TRYPSKQSSE
LGVNLPLQVP TTDPFDSVFL GKENIVCSTN QSHGSKLNSS FDDWNDPLLA SEMVEACHRL
EATWDAGEVD DDLFCQACDD IERLTQQENK GSEESESVSY TSTRGSRSSS TASKQASQSA
PSKHWNVVSS AVPLSLANKS QMSKPVTVQK RGRCGDGPNI LDATNLSVCS KNSSDNKRGP
VQVNSSKFVL GGSSNLNVNL GLMSTKIATN MKLSTQQLSH NSLADTAQND NKILKLPKFT
FKKKNPQLNQ NHLVGSVPVG KISEDLGKRE TVNSLLEANQ QQSSINYSES LKPSSPDEEE
RNRKYSPEEI QRKRQEALVR RKAKALHTVQ SAPISLP
