CTF18_MOUSE
ID CTF18_MOUSE Reviewed; 969 AA.
AC Q8BIW9; Q8R1R7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Chromosome transmission fidelity protein 18 homolog;
GN Name=Chtf18; Synonyms=Ctf18;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Chromosome cohesion factor involved in sister chromatid
CC cohesion and fidelity of chromosome transmission. Component of one of
CC the cell nuclear antigen loader complexes, CTF18-replication factor C
CC (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and
CC RFC5. The CTF18-RFC complex binds to single-stranded and primed DNAs
CC and has weak ATPase activity that is stimulated by the presence of
CC primed DNA, replication protein A (RPA) and by proliferating cell
CC nuclear antigen (PCNA). The CTF18-RFC complex catalyzes the ATP-
CC dependent loading of PCNA onto primed and gapped DNA. Interacts with
CC and stimulates DNA polymerase POLH. During DNA repair synthesis,
CC involved in loading DNA polymerase POLE at the sites of local damage.
CC {ECO:0000250|UniProtKB:Q8WVB6}.
CC -!- SUBUNIT: Component of the CTF18-RFC complex, which consists of CTF18,
CC CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. During assembly of the CTF18-RFC
CC complex, CTF18 may first assemble into a subcomplex with RFC2, RFC3,
CC RFC4 and RFC5. CTF18 then interacts directly with CTF8, which in turn
CC interacts with DCC1. The CTF18-RFC complex associates with PCNA and
CC with DNA polymerase POLH. The CTF18-RFC complex does not interact with
CC the Rad9/Rad1/Hus1 complex. CTF18 interacts with SMC1A and RAD21.
CC Interacts with DDX11. {ECO:0000250|UniProtKB:Q8WVB6}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with chromatin during S
CC phase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family. CTF18
CC subfamily. {ECO:0000305}.
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DR EMBL; AK077947; BAC37079.1; -; mRNA.
DR EMBL; BC024142; AAH24142.1; -; mRNA.
DR CCDS; CCDS28523.1; -.
DR RefSeq; NP_663384.2; NM_145409.2.
DR AlphaFoldDB; Q8BIW9; -.
DR BioGRID; 229573; 6.
DR STRING; 10090.ENSMUSP00000043896; -.
DR iPTMnet; Q8BIW9; -.
DR PhosphoSitePlus; Q8BIW9; -.
DR EPD; Q8BIW9; -.
DR jPOST; Q8BIW9; -.
DR MaxQB; Q8BIW9; -.
DR PaxDb; Q8BIW9; -.
DR PeptideAtlas; Q8BIW9; -.
DR PRIDE; Q8BIW9; -.
DR ProteomicsDB; 283977; -.
DR DNASU; 214901; -.
DR GeneID; 214901; -.
DR KEGG; mmu:214901; -.
DR UCSC; uc008bbk.2; mouse.
DR CTD; 63922; -.
DR MGI; MGI:2384887; Chtf18.
DR eggNOG; KOG1969; Eukaryota.
DR InParanoid; Q8BIW9; -.
DR OrthoDB; 307415at2759; -.
DR PhylomeDB; Q8BIW9; -.
DR TreeFam; TF314392; -.
DR Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
DR BioGRID-ORCS; 214901; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q8BIW9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BIW9; protein.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA: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; ISO:MGI.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISO:MGI.
DR GO; GO:0007059; P:chromosome segregation; IMP:MGI.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0007281; P:germ cell development; IMP:MGI.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:MGI.
DR GO; GO:0051985; P:negative regulation of chromosome segregation; IMP:MGI.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; ISS:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; DNA replication; DNA-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..969
FT /note="Chromosome transmission fidelity protein 18 homolog"
FT /id="PRO_0000340082"
FT REGION 30..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 369..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVB6"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVB6"
FT CONFLICT 880
FT /note="G -> E (in Ref. 2; AAH24142)"
FT /evidence="ECO:0000305"
FT CONFLICT 885
FT /note="A -> V (in Ref. 1; BAC37079)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="K -> T (in Ref. 1; BAC37079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 969 AA; 108137 MW; E0269C507AF514BD CRC64;
MEDYEEDLYG VEDDFQNQFA AELEVLAELE GTRDQAPPGT LQTPASRPPL TFEEAIAGGD
TVPRPCPAGS PGNVNRNTRK NVRRDQPAPS SPMVKRPRLD VVKKLNFEPD MEELLYPDSP
PGDITPPPSP EVFPEMLDAG YSDANADKDL MQTLPSPRNR NPVLRRPPIL EDYINVTSTS
GERAFLVLRA DLIGPGVQNP LLDVHWRGCG QLDLLGVPFA SLKEQVDSKR RQQLLEDAQQ
LSDTLHSLRS EGEEAVLEGP PAEEPAPGQN TAQHCLWVDE FAPQHYTELL SDDFTNRCLL
KWLKLWDLVV FGRERPARKP RPGVETTRVG KEATAPGKWK SHEQALEEML EAELDPSQRP
RQKVALLCGP PGLGKTTLAH VVARHAGYCV VEMNASDDRS PEAFRTRIEA ATQMESVLGV
GGRPNCLVID EIDGAPTAAI NVLLGILNRK GPQEADQGGT AVAAGGRRRR AEGGLLTRPI
ICICNDQFTP SLRQLKQQAL LLHVPPTLPS RLVQRLQEIS LQHGMRSDPG ALVALCEKTD
NDIRACINTL QFLYGRGRRE LSVKAVQTTH VGLKDQRKGL FSVWQEVFQL PRTQRRIVGQ
DLMLPAHALL LSNGDKGSLT LASQRFYHIL RVTTSAGEHE KVVQGLFDNF LRLRLRDSSL
STVCCALDWL AFDDLLEQAA HRGQSFQLLC YLPFVPAAFH VLFASSHVPR ITFPSSQQEA
QTRMSQTRNH IQTLVSGMAP TTRSRATPQA LVLDTLCLLL DVLAPKLRPV STQLYSAHEK
QQLSCLVGTM LAYSLTYHQE RTPDGQYLYK LEPNVEEVCR FPELPARKPL TYQAKQLIAR
EIEMEKMRRA EALAWARSGP QVDQGSSGPA SLWTDSGEKG TRQPAPRNHE QRLEHIMKRA
TVQEQPERDF FGRVVIRKVA VPSREVEAPQ KDADEWRMGV AVGRSEVWFR FNEGVSNAVR
RSLYIRDLL
