ASCC3_BOVIN
ID ASCC3_BOVIN Reviewed; 2201 AA.
AC E1BNG3;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 3;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q8N3C0};
GN Name=ascc3;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
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 EMBL; DAAA02026160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001193047.1; NM_001206118.1.
DR AlphaFoldDB; E1BNG3; -.
DR SMR; E1BNG3; -.
DR STRING; 9913.ENSBTAP00000027294; -.
DR PaxDb; E1BNG3; -.
DR PRIDE; E1BNG3; -.
DR Ensembl; ENSBTAT00000027294; ENSBTAP00000027294; ENSBTAG00000020482.
DR GeneID; 538416; -.
DR KEGG; bta:538416; -.
DR CTD; 10973; -.
DR VEuPathDB; HostDB:ENSBTAG00000020482; -.
DR VGNC; VGNC:26205; ASCC3.
DR eggNOG; KOG0952; Eukaryota.
DR GeneTree; ENSGT00940000155377; -.
DR HOGENOM; CLU_000335_2_1_1; -.
DR InParanoid; E1BNG3; -.
DR OMA; GTHHAGM; -.
DR OrthoDB; 154891at2759; -.
DR TreeFam; TF105778; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000020482; Expressed in spiral colon and 108 other tissues.
DR ExpressionAtlas; E1BNG3; baseline and differential.
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; 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..2201
FT /note="Activating signal cointegrator 1 complex subunit 3"
FT /id="PRO_0000416914"
FT DOMAIN 486..669
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 696..914
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 978..1287
FT /note="SEC63 1"
FT DOMAIN 1336..1511
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1544..1739
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1812..2176
FT /note="SEC63 2"
FT COILED 18..81
FT /evidence="ECO:0000255"
FT COILED 328..356
FT /evidence="ECO:0000255"
FT MOTIF 611..614
FT /note="DEVH box"
FT MOTIF 1453..1456
FT /note="DEIH box"
FT BINDING 499..506
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1349..1356
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 572
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3C0"
SQ SEQUENCE 2201 AA; 250765 MW; 212EC92B798CF399 CRC64;
MALPRLTGAL RSFSNVTKQD NYNEEVADLQ MKRSKLHEQI VGLDLTWMKI VKFLNEKLEK
SEMQRVNEDL KAILQAAKQI VGTDNGKEAI ESAAAFLFKT FHLKDCVGHQ ETKAIKQMFG
PFPSSSATAA CDATNRITSH FCKDSLTALV QMTTDENGDR VLFGKNLAFS FDMHDLDHFD
ELPINGESQK TISLDYKKFL TDHLQDHSTL NRKPAEKTND SFLWCEVEKY LNATLNEMAE
ATRIEDLCCT LYDMLASVKS GDELQDELFE LLGPDGLELI EKLLQNRVTI VDRFLNSSND
HKLQALQDNC KKILGENAKP NYGCQVTIQS EQEKQLMKQY RREEKRIARR EKKAGEDGEA
TEGLLCFDPK ELRIHREQAL MNARNVPILS RQRDTDVEKI RYPHVYDSQA EAMRTSAFIA
GAKMILPEGI QRENNKIYEE VKIPYTEPMP IGFEEKPVYI QDLDEIGQLA FKGMRRLNRI
QSIVFETAYN TNENMLICAP TGAGKTNIAM LTVLHEIRQH FQQGVIKKNE FKIVYVAPMK
ALAAEMTNYF SKRLEPLGIV VKELTGDMQL SKNEILRTQM LVTTPEKWDV VTRKSVGDVA
LSQIVKLLIL DEVHLLHEDR GPVLESIVAR TLRQVESTQS MIRILGLSAT LPNYLDVATF
LHVNPCIGLF FFDGRFRPVP LGQTFLGIKS ANKVQQLNNM DEVCYESVLK QVKAGHQVMV
FVHARNATVR TAMSLIERAK NNGQICYFLP TQGPEYGHAE KQVQKSRNRQ VRELFPDGFS
IHHAGMLRQD RNLVESLFSN GHIKVLVCTA TLAWGVNLPA HAVIIKGTQI YAAKRGSFVD
LGILDVMQIF GRAGRPQFDK FGEGIIITTH DKLSHYLSLL TQQNPIESQF LESLADNLNA
EIALGTVTNV EEAVKWISYT YLYVRMRANP LVYGISHKAY QIDPTLAKHR EQLVIEVGRK
LDKARMIRFE ERTGYFSSTD LGRTASHYYI KYNTIETFNE LFDAHKTESD IFAIVSKAEE
FDQIKVREEE IEELDTLLSN FCELSAPGGV ENSYGKINIL LQTYISRGEV DSFSLISDSA
YVAQNAARIV RALFEIALRK RWPAMTYRLL NLSKVIDKRL WGWTSPLRQF SVLPPHILTR
LEEKNLTVDK LKDMRKDEIG HILHHVNIGL KVKQCVHQIP SVTMEASIQP ITRTVLRVTL
SISPDFSWND QVHGTVGEPW WIWVEDPTND HIYHSEYFLV LKKQVISKEA QLLVFTIPIF
EPLPSQYYIR AVSDRWLGAE AVCIINFQHL ILPERHPPHT ELLDLQPLPV TALGCEAYEA
LYNFSHFNPV QTQIFHTLYH TDCNVLLGAP TGSGKTVAAE LAIFRVFNKY PTSKAVYIAP
LKALVRERMD DWKVRIEEKL GKKVIELTGD VTPDMKSIAK ADLIVTTPEK WDGVSRSWQN
RNYVKQVTIL IIDEIHLLGE ERGPVLEVIV SRTNFISSHT EKPVRIVGLS TALANARDLA
DWLNIRQMGL FNFRPSVRPV PLEVHIQGFP GQHYCPRMAS MNKPTFQAIR SHSPAKPVLI
FVSSRRQTRL TALELIAFLA TEEDPKQWLN MDEREMENII GTIRDSNLKL TLAFGIGMHH
AGLHERDRKT VEELFVNCKI QVLIATSTLA WGVNFPAHLV IIKGTEYYDG KTRRYVDFPI
TDVLQMMGRA GRPQFDDQGK AVILVHDIKK DFYKKFLYEP FPVESSLLGV LSDHLNAEIA
GGTITSKQDA MDYITWTYFF RRLIMNPSYY NLSDVSHDSV NKFLSNLVEK SLVELEHSYC
IEIGEDNRSI EPLTYGRIAS YYYLKHQTVK MFKERLKPEC GTEELLSILS DAEEYTDLPV
RHNEDHMNSE LAKCLPLESN PHSFDSPHTK AHLLLQAHLS RTMLPCPDYD TDTKTVLDQA
LRVCQAMLDV AAHQGWLVTV LNITSLVQMV IQGRWLKDSS LLTIPHIENH HLHIFRKWSP
GMKGPHAGYH GSIECLPELI HACAGKDHVF SSMIEKELPA PKMKQAWNFL SHLPVIDVGL
SVKGWWDDAA EGHDEISITT VASDKHSDNR WVRLHADQEY VLQVSLQRVS LGFHKGKQDS
HAVTPRFPKS KDEGWFLILG EVDKRELIAL KRVGYVRSHH MVSISFYTPE VPGRYIYTLY
FMSDCYLGLD QQYDIHLHVT PASISAQADE ISDALTDLKV K
