ASCC3_CHICK
ID ASCC3_CHICK Reviewed; 2211 AA.
AC F1NTD6;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 3;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q8N3C0};
GN Name=ascc3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(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. {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; AADN02002229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02002230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02002231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02002232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02002233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02002234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001292140.1; NM_001305211.1.
DR AlphaFoldDB; F1NTD6; -.
DR SMR; F1NTD6; -.
DR STRING; 9031.ENSGALP00000024889; -.
DR PaxDb; F1NTD6; -.
DR PRIDE; F1NTD6; -.
DR Ensembl; ENSGALT00000024935; ENSGALP00000024889; ENSGALG00000015465.
DR GeneID; 421790; -.
DR KEGG; gga:421790; -.
DR CTD; 10973; -.
DR VEuPathDB; HostDB:geneid_421790; -.
DR eggNOG; KOG0952; Eukaryota.
DR GeneTree; ENSGT00940000155377; -.
DR HOGENOM; CLU_000335_2_1_1; -.
DR InParanoid; F1NTD6; -.
DR OMA; GTHHAGM; -.
DR OrthoDB; 154891at2759; -.
DR PRO; PR:F1NTD6; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000015465; Expressed in kidney and 13 other tissues.
DR GO; GO:0099053; C:activating signal cointegrator 1 complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:1990391; C:DNA repair complex; IEA:Ensembl.
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; 4.
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 ATP-binding; Cytoplasm; DNA damage; DNA repair; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..2211
FT /note="Activating signal cointegrator 1 complex subunit 3"
FT /id="PRO_0000416917"
FT DOMAIN 495..678
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 717..923
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 987..1296
FT /note="SEC63 1"
FT DOMAIN 1345..1520
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1553..1760
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1821..2184
FT /note="SEC63 2"
FT MOTIF 620..623
FT /note="DEVH box"
FT MOTIF 1462..1465
FT /note="DEIH box"
FT BINDING 508..515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1358..1365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 2211 AA; 251857 MW; 4C6E71A5A5AE2767 CRC64;
MALPRLTGAL RSFSNVTRHD DYSEELADLT TKRTKQQEQL LKSDLTWKKI IKFVDDNLDK
KEYQTVNGDL KTILQAAKQI VGAENGQEAI ESGAVFLFKT FHRKECVGHD ETKAIKQMFG
PFPSSSATAA CNATCRIASH FTEEQLTALI QMAEEQNGDN RVFFGKNIVF SFDMHDLDHS
EELPVNGEAD AQRIISLDYK KFLNNQLDHL KNCCDEKSDL KSLGKVDDSF LWSEVGKYLN
ESQGGTPGGP TTEDLCCTLY EMLASPKSGD ELQNELFELL GPEGFELIEK LLQNRSVIVE
RSLTCQNDNK FQTLQEQCKK FIGENAKPNY GCQVTIQSEQ EKLLMKQYRR EEKRNARREK
QAGEDGEVSG EGLLCFDPKE LRLQRELALL NARSVPILGR QREVDLERIH YPHVYDSRAE
AMKTSAFIGG AKVFLPESVQ RENNKMYEEV KIPHSEPMPI GIEEKIVYIK DLDEIGQLAF
KGMKRLNRIQ SIVFETAYNT NENMLICAPT GAGKTNIAML TVLHEIRQHV QHGVIKKDEF
KIVYVAPMKA LAAEMTNYFS KRLEPLGITV KELTGDMQLS KGEILRTQML VTTPEKWDVV
TRKSVGDVAL SQLVKLLILD EVHLLHEDRG PVLESIVART LRQVESTQSM IRILGLSATL
PNYLDVATFL HVNPYIGLFY FDSRFRPVPL GQTFIGIKTT NKVQQLNHMD EVCYENVLKQ
IMAGHQVMVF VHARNATVRT AMALREKAKN NGHICHFLSP QGSDYGQAEK QVQRSRNKQL
RELFPDGFSI HHAGMLRQDR SLVENLFSNG HIKVLVCTAT LAWGVNLPAH AVVIKGTQIY
AAKRGSFVDL GILDVMQIFG RAGRPQFDKF GEGIIITTHD KLSHYLTLLT QQNPIESQFL
ESLADNLNAE IALGTVTNVE EAVKWISYTY LYVRMRANPL VYGISHKAYQ MDPGLEKHRE
QLVIEVGRKL DKARMIRFEE RTGFFSSTDL GRTASHYYIK YNTIETFNEL FDAHKTEGDI
LAIVSKAEEF EQIKVREEEI EELDTLLNDF CELPAPGGVE NNYGKINILL QTYISRGELD
SFSLISDSAY VAQNAARIVR ALFEIALRKR WPAMTYRLLN LSKVIDKRLW GWVSPLRQFS
VLPPSVLSKL EEKNLTVDKM KDMRKDEIGH MLHHVKIGLK VKQCVHQIPS IAMEATIQPI
TRTVLRVRLN ITPDFTWNDQ VHGTVGEPWW IWVEDPTNDH IYHSEYFIIQ KKQVITKEPQ
LLVFTIPIFE PLPSQYYIRA VSDRWLGAEA VCIINFQHLI LPERHPPHTE LLDLQPLPVT
ALGHPEYEVL YKFTHFNPIQ TQIFHTLYHT DCNVLLGAPT GSGKTVAAEL AIFRVFNKYP
TSKAVYIAPL KALVRERIED WKVRIEEKLG KKVVELTGDV TPDMRAIAQA DLIVTTPEKW
DGVSRSWQNR SYVQKVSILI IDEIHLLGDE RGPVLEVIVS RTNFISSHTE KPVRVVGLST
ALANARDLAD WLNINQMGLF NFRPSVRPVP LEVHIQGFPG QHYCPRMARM NKPAFQAIRS
HSPAKPVLIF VSSRRQTRLT SLDLIAFLAT EDDPKQWLKM DEREMNDIIG TVRDSNLKLT
LAFGIGMHHA GLHERDRKTV EELFVNCKIQ VLIATSTLAW GVNFPAHLVI VKGTEYYDGK
TRRYVDYPIT DVLQMMGRAG RPQFDDQGKA VILVHDIKKD FYKKFLYEPF PVESSLLDVL
ADHLNAEIAA GTITSKQDAM DYITWTYFFR RLIMNPTYYN LDNVSHDTMN KYLSSLVEKS
LFDLECSYCI EIGEDNRTIE PLTYGRIASY YYLKHPTIGM FKDQLKPESS VEELLLILTN
ADEYTDLPVR HNEDQMNSEL AKHLPIEVNP HSFDSSHTKT HLLLQAHFSH AILPCPDYAT
DTKTVLDQAI RICQAMLDVT AHHGWLVAAL NITNLVQMVV QGRWIHDSSL LTVPNIEVQH
LYLFQKWSQQ KRKSVHGGYQ GPIECLPELM AACEGKEDVF ASIVDSELQT AHISQAWNFL
SRLPILNVSL SIKGCWDDPA QPQNEVPVPC LTADTRDNKR WIKLHADQEY VLQIHLQRTQ
MGYQGKQDSK AVAPRFPKVK DEGWFLILGE VDKKELIALK RTGYVRNRNT VSVAFYTPET
PGKCIYTLYL MSDSYLGMDQ QYDIYLNIIP TSTSAQATTE VSDAMSYLTL K
