ID A0A0A0MY43_RAT Unreviewed; 2201 AA.
AC A0A0A0MY43;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 3 {ECO:0000256|ARBA:ARBA00014590};
GN Name=Ascc3 {ECO:0000313|Ensembl:ENSRNOP00000053848.4,
GN ECO:0000313|RGD:1307995};
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 {ECO:0000313|Ensembl:ENSRNOP00000053848.4, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000053848.4, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000053848.4,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
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).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000053848.4}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000053848.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the helicase family.
CC {ECO:0000256|ARBA:ARBA00008708}.
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DR RefSeq; NP_001263986.1; NM_001277057.1.
DR RefSeq; XP_006256664.1; XM_006256602.3.
DR RefSeq; XP_006256665.1; XM_006256603.3.
DR RefSeq; XP_008771214.1; XM_008772992.2.
DR RefSeq; XP_008771215.1; XM_008772993.2.
DR SMR; A0A0A0MY43; -.
DR IntAct; A0A0A0MY43; 2.
DR jPOST; A0A0A0MY43; -.
DR Ensembl; ENSRNOT00000057016.5; ENSRNOP00000053848.4; ENSRNOG00000037604.5.
DR GeneID; 309887; -.
DR KEGG; rno:309887; -.
DR CTD; 10973; -.
DR RGD; 1307995; Ascc3.
DR GeneTree; ENSGT00940000155377; -.
DR OMA; MCSATEF; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000037604; Expressed in liver and 19 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0010467; P:gene expression; IEA:UniProt.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR CDD; cd18020; DEXHc_ASCC3_1; 1.
DR CDD; cd18022; DEXHc_ASCC3_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
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 PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF13; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 2.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0A0MY43};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT DOMAIN 487..670
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 697..915
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1337..1512
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1545..1740
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 2201 AA; 250530 MW; 09B555E86A7C68A5 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 SMNKPAFQAI RSHSPAKPVL
IFVSSRRQTR LTALELIAFL ATEEDPKQWL NMDEQEMENI IATVRDSNLK LTLAFGIGMH
HAGLHERDRK TVEELFVNCK VQVLIATSTL AWGVNFPAHL VIIKGTEYYD GKTRRYVDFP
ITDVLQMMGR AGRPQFDDQG KAVILVHDIK KDFYKKFLYE PFPVESSLLG VLSDHLNAEI
AGGTITSKQD ALDYITWTYF FRRLIMNPSY YNLGDVSQDA INKFLSHLIG QSLVELELSH
CIEVGEDNRS IEPLTCGRIA SYYYLKHKTV KMFKDRLKPE CSTEELLSIL SDAEEYTDLP
VRHNEDHTNN ELAKCLPIEL NPHSFDSPHT KAHLLLQAHL SRAMLPCPDY DTDTKTVLDQ
ALRVCQAMLD VAASQGWLVT TLNITHLIQM VIQGRWLKDS SLLTIPNIEQ HHLHLFRKWK
PPVKGPHAKC RTSIECLPEL IHACEGKEHV FSSMVEKELQ PAKTKQAWNF LSHLPVINVG
ISVKGSWDDS VEGHNELSIS TLTADKRDEN TWIKLHADQQ YVLQVSLQRV HFEFHKVKHE
SHAVTPRFPK LKDEGWFLIL GEVDKRELVA VKRVGFVRTH HEASISFFTP EAPGRYIFTL
YLMSDCYLGL DQQYDIFLNV TKADISTQIN TEVPDVSTDL A
//
