ID   ASCC3_DANRE             Reviewed;        1534 AA.
AC   E7F8F4; E7F5Q7;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Activating signal cointegrator 1 complex subunit 3;
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:Q8N3C0};
GN   Name=ascc3;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: 3'-5' DNA helicase involved in repair of alkylated DNA.
CC       Promotes DNA unwinding to generate single-stranded substrate needed for
CC       alkbh3, enabling alkbh3 to process alkylated N3-methylcytosine (3mC)
CC       within double-stranded regions. Also involved in activation of the
CC       ribosome quality control (RQC) pathway, a pathway that degrades nascent
CC       peptide chains during problematic translation. Drives the splitting of
CC       stalled ribosomes. {ECO:0000250|UniProtKB:Q8N3C0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000250|UniProtKB:Q8N3C0};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N3C0}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:Q8N3C0}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q8N3C0}. Note=Colocalizes with alkbh3 and ascc2
CC       in nuclear foci when cells have been exposed to alkylating agents that
CC       cause DNA damage. {ECO:0000250|UniProtKB:Q8N3C0}.
CC   -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR   EMBL; CABZ01076009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01076010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01076011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01076012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01076013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01076014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01076015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01076016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01076017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABZ01076018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU468254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU915569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E7F8F4; -.
DR   SMR; E7F8F4; -.
DR   STRING; 7955.ENSDARP00000106925; -.
DR   PaxDb; E7F8F4; -.
DR   PeptideAtlas; E7F8F4; -.
DR   PRIDE; E7F8F4; -.
DR   ZFIN; ZDB-GENE-130214-2; ascc3.
DR   eggNOG; KOG0952; Eukaryota.
DR   InParanoid; E7F8F4; -.
DR   PhylomeDB; E7F8F4; -.
DR   PRO; PR:E7F8F4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; ISS:UniProtKB.
DR   GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR   GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR   GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 2.
DR   Gene3D; 2.60.40.150; -; 1.
DR   Gene3D; 3.40.50.300; -; 4.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 2.
DR   Pfam; PF02889; Sec63; 4.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00973; Sec63; 2.
DR   SUPFAM; SSF46785; SSF46785; 2.
DR   SUPFAM; SSF52540; SSF52540; 3.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA repair; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1534
FT                   /note="Activating signal cointegrator 1 complex subunit 3"
FT                   /id="PRO_0000416918"
FT   DOMAIN          83..267
FT                   /note="Helicase ATP-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          294..500
FT                   /note="Helicase C-terminal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          576..849
FT                   /note="SEC63 1"
FT   DOMAIN          898..1073
FT                   /note="Helicase ATP-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1106..1313
FT                   /note="Helicase C-terminal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          1374..1481
FT                   /note="SEC63 2"
FT   MOTIF           209..212
FT                   /note="DEVH box"
FT   MOTIF           1015..1018
FT                   /note="DEIH box"
FT   BINDING         96..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         911..918
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1534 AA;  175219 MW;  48438FEBFAC54FF3 CRC64;
     MVDVNDVIHA NEKAQIDFAQ MLLPEGIRRD NNKMYEEVEI PPNEPMPIGF EEKAVFVSEL
     DEIGQLVFKG MKRLNRIQSI VFETAYNTNE NLLICAPTGA GKTNIAMLTI LHEIRQHLQP
     GGVIRKDQFK IVYVAPMKAL AAEMTNYFSK RLEPLGIAVK ELTGDMQLTK GEILRTQMLV
     TTPEKWDVVT RKSVGDVALS QVVRLLILDE VHLLHEDRGP VLESLVARTL RQVESTQSMI
     RILGLSATLP NYLDVATFLH VNPFIGLFYF DSRFRPVPLG QSFVGIKTTN KVQQLHDMEE
     VCYEKVLKQI KAGHQVMVFV HARNSTVRTA MSLIEMAKNR GELSFFQVDQ GADYGQCEKQ
     IQRSRNKQMR EMFPDGFGIH HAGMLRQDRS LMESMFSRGY LKVLVCTATL AWGVNLPAHA
     VIIKGTNIYD AKRGTLVDLG ILDVMQIFGR AGRPQFDKYG EGTIITTHDK LSHYLTLLTQ
     QNPIESQFQQ SLADNLNAEI ALGTVTNVDE AVRWLSYTYL YVRMRANPLA YGINHKAYQM
     DPQLELYRKE LVVESGRKLD KARMIRFDER TGYFASTDLG RTASHFYIKY NTIESFNELF
     NAQNTEADVL SIVSKAEEFE QIKVRVQEED ADGKSSVQIL CGSHHTNAAR IMRALFEMAL
     RKRWPAMTYR LLNLCKVMDK RLWGWAHPLR QFNTLPASAL ARMEDKNLTI DKLRDMGKDE
     IGHMLHHVNI GLKVKQCVHQ IPAILLESSI QPITRTVLRV RLSITPDFRW NDQVHGSVGE
     PWWLWVEDPI NDHIYHSEYF LLQKKQVVSG EPQQVVFTIP IFEPMPSQYY IRAVSDRWLG
     SEAVCIINFQ HLILPERHPP HTELLDLQPL PITALGNREY ESLYKFTHYN PIQTQIFHTL
     YHTDTNVLLG APTGSGKTIA AEMAIFRVFN MYPTSKVVYI APLKALVRER IEDWKIRIEE
     KLGRKVVELT GDNTPDMRAI AQADLIVTTP EKWDGVSRSW QNRSYVQKVA ILIIDEIHLL
     GEDRGPVLEV IVSRTNFISS HTSKTVRVVG LSTALANARD LADWLGIGQV GLFNFRPSVR
     PVPLEVHIQG FPGQHYCPRM ATMNKPVFQA IRTHSPAKPV LIFVSSRRQT RLTALDLIAF
     LATEDDPKQW LHQDEREMTD IIATIRESNL KLTLAFGIGM HHAGLHERDR KTVEELFVNC
     KIQVLIATST LAWGVNFPAH LVIVKGTEYY DGKTRRYVDY PITDVLQMMG RAGRPQFDDQ
     GKAVILVHDI KKDFYKKFLY EPFPVESSLL SVLSDHLNAE IAAGTVTSKQ DAMDYITWTY
     FFRRLVMNPS YYNLDDISHE TINKYLSNLV ERSLRDLECS YCMEIQQDEQ TIEPLTYGRI
     SSYYYLKHQT IRMFKERLKP ELPVHELLAI LSLPCSDYGT DTKTVLDNAI RICQAMLDVV
     ANEGWLVSAL SLCNLVQMII QARWLHDSSL LTLPHIQKQE LYVFRRWSSR GVRAGCGHQG
     PIEGLPELIA ACDGKEDIFT SMVKEVLQPN QISQ