ID   ASCC3_RAT               Reviewed;        2197 AA.
AC   F1LPQ2;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Activating signal cointegrator 1 complex subunit 3;
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:Q8N3C0};
GN   Name=Ascc3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
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, as part of the ribosome quality control trigger
CC       (RQT) complex. Part of the ASC-1 complex that enhances NF-kappa-B, SRF
CC       and AP1 transactivation. {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   -!- SUBUNIT: Identified in the ASCC complex that contains ASCC1, ASCC2 and
CC       ASCC3. Functions as scaffolding subunit that interacts directly with
CC       both ASCC1 and ASCC2. Interacts directly with ALKBH3, and thereby
CC       recruits ALKBH3 to the ASCC complex. Part of the ASC-1/TRIP4 complex,
CC       that contains TRIP4, ASCC1, ASCC2 and ASCC3. Identified in the RQT
CC       (ribosome quality control trigger) complex, that contains ASCC2, ASCC3
CC       and TRIP4. Interacts with ASCC2. Interacts with TRIP4. Interacts with
CC       ZCCHC4. Interacts with ZNF598. Interacts with RPS3. Associates with
CC       ribosomes (By similarity). {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   AlphaFoldDB; F1LPQ2; -.
DR   SMR; F1LPQ2; -.
DR   STRING; 10116.ENSRNOP00000053848; -.
DR   iPTMnet; F1LPQ2; -.
DR   PhosphoSitePlus; F1LPQ2; -.
DR   jPOST; F1LPQ2; -.
DR   PaxDb; F1LPQ2; -.
DR   PRIDE; F1LPQ2; -.
DR   UCSC; RGD:1307995; rat.
DR   RGD; 1307995; Ascc3.
DR   eggNOG; KOG0952; Eukaryota.
DR   InParanoid; F1LPQ2; -.
DR   TreeFam; TF105778; -.
DR   PRO; PR:F1LPQ2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0099053; C:activating signal cointegrator 1 complex; ISO:RGD.
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: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   Gene3D; 1.10.10.10; -; 2.
DR   Gene3D; 2.60.40.150; -; 2.
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; IPR014756; Ig_E-set.
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; 2.
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   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 2.
PE   3: Inferred from homology;
KW   Acetylation; ATP-binding; Coiled coil; Cytoplasm; DNA damage; DNA repair;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation.
FT   CHAIN           1..2197
FT                   /note="Activating signal cointegrator 1 complex subunit 3"
FT                   /id="PRO_0000416916"
FT   DOMAIN          487..670
FT                   /note="Helicase ATP-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          697..915
FT                   /note="Helicase C-terminal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          979..1288
FT                   /note="SEC63 1"
FT   DOMAIN          1337..1512
FT                   /note="Helicase ATP-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1565..1739
FT                   /note="Helicase C-terminal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          1812..2175
FT                   /note="SEC63 2"
FT   COILED          18..80
FT                   /evidence="ECO:0000255"
FT   COILED          328..356
FT                   /evidence="ECO:0000255"
FT   MOTIF           612..615
FT                   /note="DEVH box"
FT   MOTIF           1454..1457
FT                   /note="DEIH box"
FT   BINDING         500..507
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         1350..1357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N3C0"
FT   MOD_RES         573
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N3C0"
SQ   SEQUENCE   2197 AA;  250220 MW;  C8A73337406E5F8D CRC64;
     MALPRLTGAL RSFSNVTKQD NYNEEVADLK LKRSKLHEQA LDFGLSWKKI VKFLNEKLEK
     NKMQTINEDL KDILQAAKQI VGTDNGNEAI ESGAAFLFMT FHMTDSVGYT ETKAIRQMFG
     PFPSSSATSA CNATSRIISH FSQDDLTALV QATENQCNDR VVFGRNLAFS FDMHDLDHFD
     ELPVNGEAQK TISLDYKKFL NEQFQEPYTP ELKPVEKSNG SLLWCEVEKY LNATLKEMTE
     APRVEDLCCT LYDMLASAKS GDELQDELFE LLGPGGLDLI EKLLQNRITI VDRFLNSSSD
     HKFQVLQDNC KKILGENAKP NYGCQVTIQS EQEKQLMKQY RREEKRIARR EKKAGEDGEV
     SGEGLLPFDP KELRLQREHA LLNARSAPIL GRQRDTEVEK IRYPHVYDSQ AAARETSAFI
     AGAKMILPEG IQRENTKLYE EVRIPYSEPM PVGFEEKPVY IQDLDEVGQL AFKGMKRLNR
     IQSIVFDTAY NTNENMLICA PTGAGKTNIA MLTVLHEIRQ HFHQGVLKKN EFKIVYVAPM
     KALAAEMTNY FSKRLEPLGI VVKELTGDMQ LSKSEILRTQ MLVTTPEKWD VVTRKSVGDV
     ALSQIVKLLI LDEVHLLHED RGPVLESIVA RTLRQVESTQ SMIRILGLSA TLPNYLDVAT
     FLHVNPYIGL FYFDGRFRPV PLGQTFLGIK SANKMQQLNN MDEVCYESVL KQVKAGHQVM
     VFVHARNATV RTAMSLIERA KNSGQISCFL PTQGPEYGHA LKQVQKSRNK QVRELFSDGF
     SIHHAGMLRQ DRNLVENLFS NGHIKVLVCT ATLAWGVNLP AHAVIIKGTQ IYAAKRGSFV
     DLGILDVMQI FGRAGRPQFD KFGEGIIITT HDKLSHYLSL LTQQNPIESQ FLESLADNLN
     AEIALGTVTN VEEAVKWMSY TYLYVRMRAN PLAYGISHKA YQMDPTLRKH REQLLIEVGQ
     KLDKARMIRF EERTGYFSST DLGRTASHYY IKYNTIETFN ELFDAHKTEG DIFAIVSKAE
     EFDQIKVREE EIEELDALLN NFCELSAPGG VENSYGKINI LLQTYISRGE MDSFSLISDS
     AYVAQNAARI VRALFEIALR KRWPTMTYRL LNLSKVIDKR LWGWASPLRQ FSVLPPHILT
     RLEEKNLTVD KLKDMRKDEI GHILHHVNIG LKVKQCVHQI PSVTMEASIQ PITRTVLRVS
     LNIYPDFSWN DQVHGTVGEP WWIWVEDPTN DHIYHSEYFL ALKKQVINKE AQLLVFTIPI
     FEPLPSQYYI RAVSDRWLGA EAVCIINFQH LILPERHPPH TELLDLQPLP VTALGCKAYE
     ALYNFSHFNP VQTQIFHTLY HTDCNVLLGA PTGSGKTVAA ELAIFRVFNK YPTSKAVYIA
     PLKALVRERM DDWKIRIEEK LGKKVIELTG DVTPDMKSIA KADLIVTTPE KWDGVSRSWQ
     NRSYVQQVNI LIIDEIHLLG EERGPVLEVI VSRTNFISSH TEKPVRIVGL STALANARDL
     ADWLNIKQMG LFNFRPSVRP VPLEVHIQGF PGQHYCPRMA SMNKPAFQES HTHCPDRPCL
     LLPERMLSSM TKLELIAFLA TEEDPKQWLN MDEQEMENII ATVRDSNLKL TLAFGIGMHH
     AGLHERDRKT VEELFVNCKV QVLIATSTLA WGVNFPAHLV IIKGTEYYDG KTRRYVDFPI
     TDVLQMMGRA GRPQFDDQGK AVILVHDIKK DFYKKFLYEP FPVESSLLGV LSDHLNAEIA
     GGTITSKQDA LDYITWTYFF RRLIMNPSYY NLGDVSQDAI NKFLSHLIGQ SLVELELSHC
     IEVGEDNRSI EPLTCGRIAS YYYLKHKTVK MFKDRLKPEC STEELLSILS DAEEYTDLPV
     RHNEDHTNNE LAKCLPIELN PHSFDSPHTK AHLLLQAHLS RAMLPCPDYD TDTKTVLDQA
     LRVCQAMLDV AASQGWLVTT LNITHLIQMV IQGRWLKDSS LLTIPNIEQH HLHLFRKWKP
     PVKGPHAKCR TSIECLPELI HACEGKEHVF SSMVEKELQP AKTKQAWNFL SHLPVINVGI
     SVKGSWDDSV EGHNELSIST LTADKRDENT WIKLHADQQY VLQVSLQRVH FEFHKVKHES
     HAVTPRFPKL KDEGWFLILG EVDKRELVAV KRVGFVRTHH EASISFFTPE APGRYIFTLY
     LMSDCYLGLD QQYDIFLNVT KADISTQINT EVPDVST