RFC1_MOUSE
ID RFC1_MOUSE Reviewed; 1131 AA.
AC P35601;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Replication factor C subunit 1;
DE AltName: Full=A1-P145;
DE AltName: Full=Activator 1 140 kDa subunit;
DE Short=A1 140 kDa subunit;
DE AltName: Full=Activator 1 large subunit;
DE AltName: Full=Activator 1 subunit 1;
DE AltName: Full=Differentiation-specific element-binding protein;
DE AltName: Full=ISRE-binding protein;
DE AltName: Full=Replication factor C 140 kDa subunit;
DE Short=RF-C 140 kDa subunit;
DE Short=RFC140;
DE AltName: Full=Replication factor C large subunit;
GN Name=Rfc1; Synonyms=Ibf-1, Recc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=8265586; DOI=10.1073/pnas.90.24.11543;
RA Burbelo P.D., Utani A., Pan Z., Yamada Y.;
RT "Cloning of the large subunit of activator 1 (replication factor C) reveals
RT homology with bacterial DNA ligases.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11543-11547(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8114700; DOI=10.1128/mcb.14.3.1626-1634.1994;
RA Luckow B., Bunz F., Stillman B., Lichter P., Schuetz G.;
RT "Cloning, expression, and chromosomal localization of the 140-kilodalton
RT subunit of replication factor C from mice and humans.";
RL Mol. Cell. Biol. 14:1626-1634(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=SWR/J;
RX PubMed=7659092; DOI=10.1210/mend.9.4.7659092;
RA McGehee Habener J.F.;
RT "Differentiation-specific element binding protein (DSEB) binds to a defined
RT element in the promoter of the angiotensinogen gene required for the
RT irreversible induction of gene expression during differentiation of 3T3-L1
RT adipoblasts to adipocytes.";
RL Mol. Endocrinol. 9:487-501(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Haque S.J.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-565.
RC STRAIN=LAF1;
RA Lossie A.C., Haugen B.H., Wood W.M., Camper S.A., Gordon D.F.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 354-528.
RX PubMed=1691767; DOI=10.1089/jir.1990.10.31;
RA Haque S.J., Kumar A., Fischer T., Rutherford M.N., Williams B.R.;
RT "Evaluation of inter- and intramolecular primary structure homologies of
RT interferons by a Monte Carlo method.";
RL J. Interferon Res. 10:31-38(1990).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-70; SER-107 AND
RP THR-109, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-70; SER-107; THR-109;
RP SER-155; THR-160; SER-244; SER-250; SER-253; SER-535 AND SER-1090, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC delta and epsilon requires the action of the accessory proteins PCNA
CC and activator 1. This subunit binds to the primer-template junction.
CC -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC form a complex either with RFC1 or with RAD17. The former interacts
CC with PCNA in the presence of ATP, while the latter has ATPase activity
CC but is not stimulated by PCNA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35601-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35601-2; Sequence=VSP_008444;
CC -!- MISCELLANEOUS: [Isoform 2]: Alternative use of an acceptor site.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000305}.
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DR EMBL; U01222; AAA21643.1; -; mRNA.
DR EMBL; X72711; CAA51260.1; -; mRNA.
DR EMBL; U36441; AAA79698.1; -; mRNA.
DR EMBL; U07157; AAC52140.1; -; mRNA.
DR EMBL; U15037; AAB60452.1; -; mRNA.
DR CCDS; CCDS39096.1; -. [P35601-1]
DR CCDS; CCDS84884.1; -. [P35601-2]
DR PIR; A49393; A49393.
DR RefSeq; NP_035388.2; NM_011258.2.
DR AlphaFoldDB; P35601; -.
DR BMRB; P35601; -.
DR SMR; P35601; -.
DR BioGRID; 202846; 19.
DR ComplexPortal; CPX-472; DNA replication factor C complex.
DR CORUM; P35601; -.
DR STRING; 10090.ENSMUSP00000031092; -.
DR iPTMnet; P35601; -.
DR PhosphoSitePlus; P35601; -.
DR SwissPalm; P35601; -.
DR EPD; P35601; -.
DR jPOST; P35601; -.
DR MaxQB; P35601; -.
DR PaxDb; P35601; -.
DR PeptideAtlas; P35601; -.
DR PRIDE; P35601; -.
DR ProteomicsDB; 255290; -. [P35601-1]
DR ProteomicsDB; 255291; -. [P35601-2]
DR DNASU; 19687; -.
DR GeneID; 19687; -.
DR KEGG; mmu:19687; -.
DR CTD; 5981; -.
DR MGI; MGI:97891; Rfc1.
DR eggNOG; KOG1968; Eukaryota.
DR InParanoid; P35601; -.
DR PhylomeDB; P35601; -.
DR Reactome; R-MMU-110312; Translesion synthesis by REV1.
DR Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-MMU-110320; Translesion Synthesis by POLH.
DR Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-MMU-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-MMU-5655862; Translesion synthesis by POLK.
DR Reactome; R-MMU-5656121; Translesion synthesis by POLI.
DR Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-69091; Polymerase switching.
DR BioGRID-ORCS; 19687; 26 hits in 107 CRISPR screens.
DR ChiTaRS; Rfc1; mouse.
DR PRO; PR:P35601; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P35601; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005663; C:DNA replication factor C complex; ISO:MGI.
DR GO; GO:0031391; C:Elg1 RFC-like complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR GO; GO:0061860; F:DNA clamp unloader activity; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0090618; P:DNA clamp unloading; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR Gene3D; 3.40.50.10190; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012178; RFC1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08519; RFC1; 1.
DR PIRSF; PIRSF036578; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ATP-binding; DNA replication; DNA-binding;
KW Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1131
FT /note="Replication factor C subunit 1"
FT /id="PRO_0000121773"
FT DOMAIN 399..489
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 14..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..528
FT /note="Interferon-stimulated-response-element binding
FT region"
FT REGION 491..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1104..1108
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 18..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1093
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 635..642
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35251"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35251"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 162
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35251"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35251"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35251"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35251"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35251"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35251"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35251"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P35251"
FT VAR_SEQ 614
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7659092, ECO:0000303|Ref.4"
FT /id="VSP_008444"
FT CONFLICT 66
FT /note="Y -> N (in Ref. 3; AAA79698)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="E -> EPDFCLSCLIFFGIQ (in Ref. 4; AAC52140)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="V -> A (in Ref. 5; AAB60452)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="N -> S (in Ref. 4; AAC52140)"
FT /evidence="ECO:0000305"
FT CONFLICT 945
FT /note="S -> N (in Ref. 1; AAA21643)"
FT /evidence="ECO:0000305"
FT CONFLICT 1071
FT /note="T -> A (in Ref. 3; AAA79698)"
FT /evidence="ECO:0000305"
FT CONFLICT 1104
FT /note="K -> KQ (in Ref. 4; AAC52140)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1131 AA; 125985 MW; A6F4F970A7F9EE94 CRC64;
MDIRKFFGVI SSGKKPVNET VKNEKTKASE GTVKGKKGVK EAKVNNSGKE DASKPKQHSK
KKRIIYDSDS ESEETVQVKN AKKKSEKLSL SYKPGKVSQK DPVTYVSETD EDDDFVCKKA
ASKSKENGVS TNSYLGTSNV KKNEENVKTK NKPLSPIKLT PTSVLDYFGT ESVQRSGKKM
VTSKRKESSQ NTEDSRLNDE AIAKQLQLDE DAELERQLHE DEEFARTLAL LDEEPKIKKA
RKDSEEGEES FSSVQDDLSK AEKQKSPNKA ELFSTARKTY SPAKHGKGRA SEDAKQPCKS
AHRKEACSSP KASAKLALMK AKEESSYNET ELLAARRKES ATEPKGEKTT PKKTKVSPTK
RESVSPEDSE KKRTNYQAYR SYLNREGPKA LGSKEIPKGA ENCLEGLTFV ITGVLESIER
DEAKSLIERY GGKVTGNVSK KTNYLVMGRD SGQSKSDKAA ALGTKILDED GLLDLIRTMP
GKRSKYEMAA EAEMKKEKSK LERTPQKNDQ GKRKISPAKK ESESKKCKLT LLKNSPMKAV
KKEASTCPRG LDVKETHGNR SSNKEECLLW VDKYKPASLK NIIGQQGDQS CANKLLRWLR
NWHKSSPEEK KHAAKFGKLA SKDDGSSFKA ALLSGPPGVG KTTTASLVCQ ELGYSYVELN
ASDTRSKNSL KAVVAESLNN TSIKGFYTSG AAPSVSARHA LIMDEVDGMA GNEDRGGIQE
LIGLIKHTKI PIICMCNDRN HPKIRSLVHY CFDLRFQRPR VEQIKSAMLS IAFKEGLKIP
PPAMNEIILG ANQDVRQVLH NLSMWCAQSK ALTYDQAKAD SQRAKKDIRL GPFDVTRKVF
AAGEETAHMS LMDKSDLFFH DYSIAPLFVQ ENYLHVKPVA AGGDMKKHLM LLSRAADSIC
DGDLVDNQIR SKQNWSLLPT QAIYASVLPG ELMRGYMTQF PSFPSWLGKH SSTGKHDRIV
QDLSLHMSLR TYSSKRTVNM DYLSHIRDAL VRPLTSQGVE GAQHVIKLMD TYYLMKEDFE
NIMEVSSWGG KPSAFSKLDP KVKAAFTRAY NKEAHLTPYS LQVVKTSRLS TGPALDSEYS
EEFQEDDTQS EKEQDAVETD AMIKKKTRSS KPSKSEREKE SKKGKGKNWK K
