REPI1_MOUSE
ID REPI1_MOUSE Reviewed; 545 AA.
AC Q5U4E2; Q8BTQ5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Replication initiator 1;
DE AltName: Full=Zinc finger protein 464;
DE Short=Zfp-464;
GN Name=Repin1; Synonyms=Zfp464;
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=NOD; TISSUE=Thymus;
RX PubMed=12466851; DOI=10.1038/nature01266;
RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S.,
RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H.,
RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T.,
RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J., Schriml L.M.,
RA Kanapin A., Matsuda H., Batalov S., Beisel K.W., Blake J.A., Bradt D.,
RA Brusic V., Chothia C., Corbani L.E., Cousins S., Dalla E., Dragani T.A.,
RA Fletcher C.F., Forrest A., Frazer K.S., Gaasterland T., Gariboldi M.,
RA Gissi C., Godzik A., Gough J., Grimmond S., Gustincich S., Hirokawa N.,
RA Jackson I.J., Jarvis E.D., Kanai A., Kawaji H., Kawasawa Y.,
RA Kedzierski R.M., King B.L., Konagaya A., Kurochkin I.V., Lee Y.,
RA Lenhard B., Lyons P.A., Maglott D.R., Maltais L., Marchionni L.,
RA McKenzie L., Miki H., Nagashima T., Numata K., Okido T., Pavan W.J.,
RA Pertea G., Pesole G., Petrovsky N., Pillai R., Pontius J.U., Qi D.,
RA Ramachandran S., Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z.,
RA Ringwald M., Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K.,
RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M., Verardo R.,
RA Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C., Wilming L.G.,
RA Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L., Yuan Z., Zavolan M.,
RA Zhu Y., Zimmer A., Carninci P., Hayatsu N., Hirozane-Kishikawa T.,
RA Konno H., Nakamura M., Sakazume N., Sato K., Shiraki T., Waki K., Kawai J.,
RA Aizawa K., Arakawa T., Fukuda S., Hara A., Hashizume W., Imotani K.,
RA Ishii Y., Itoh M., Kagawa I., Miyazaki A., Sakai K., Sasaki D., Shibata K.,
RA Shinagawa A., Yasunishi A., Yoshino M., Waterston R., Lander E.S.,
RA Rogers J., Birney E., Hayashizaki Y.;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Sequence-specific double-stranded DNA-binding protein
CC required for initiation of chromosomal DNA replication. Binds on 5'-
CC ATT-3' reiterated sequences downstream of the origin of bidirectional
CC replication (OBR) and a second, homologous ATT sequence of opposite
CC orientation situated within the OBR zone. Facilitates DNA bending (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimers and homomultimers. Found in a complex with RIP60
CC and RIP100 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC40716.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK089041; BAC40716.1; ALT_FRAME; mRNA.
DR EMBL; BC085128; AAH85128.1; -; mRNA.
DR CCDS; CCDS39480.1; -.
DR RefSeq; NP_001073370.2; NM_001079901.1.
DR RefSeq; NP_001073371.2; NM_001079902.1.
DR RefSeq; NP_001073372.2; NM_001079903.1.
DR RefSeq; NP_001073373.2; NM_001079904.1.
DR RefSeq; NP_001073374.1; NM_001079905.1.
DR RefSeq; NP_780308.2; NM_175099.3.
DR AlphaFoldDB; Q5U4E2; -.
DR SMR; Q5U4E2; -.
DR STRING; 10090.ENSMUSP00000113548; -.
DR iPTMnet; Q5U4E2; -.
DR PhosphoSitePlus; Q5U4E2; -.
DR EPD; Q5U4E2; -.
DR MaxQB; Q5U4E2; -.
DR PaxDb; Q5U4E2; -.
DR PeptideAtlas; Q5U4E2; -.
DR PRIDE; Q5U4E2; -.
DR ProteomicsDB; 253211; -.
DR Antibodypedia; 32865; 68 antibodies from 17 providers.
DR DNASU; 58887; -.
DR Ensembl; ENSMUST00000009420; ENSMUSP00000009420; ENSMUSG00000052751.
DR Ensembl; ENSMUST00000163452; ENSMUSP00000132365; ENSMUSG00000052751.
DR GeneID; 58887; -.
DR KEGG; mmu:58887; -.
DR UCSC; uc009buv.1; mouse.
DR CTD; 29803; -.
DR MGI; MGI:1889817; Repin1.
DR VEuPathDB; HostDB:ENSMUSG00000052751; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162588; -.
DR HOGENOM; CLU_002678_36_0_1; -.
DR InParanoid; Q5U4E2; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5U4E2; -.
DR TreeFam; TF326846; -.
DR BioGRID-ORCS; 58887; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Repin1; mouse.
DR PRO; PR:Q5U4E2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q5U4E2; protein.
DR Bgee; ENSMUSG00000052751; Expressed in ascending aorta and 255 other tissues.
DR ExpressionAtlas; Q5U4E2; baseline and differential.
DR Genevisible; Q5U4E2; MM.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:MGI.
DR GO; GO:0005811; C:lipid droplet; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0043035; F:chromatin insulator sequence binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:MGI.
DR GO; GO:2000191; P:regulation of fatty acid transport; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR039705; REPIN1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24406:SF10; PTHR24406:SF10; 1.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 1: Evidence at protein level;
KW Acetylation; DNA replication; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..545
FT /note="Replication initiator 1"
FT /id="PRO_0000274913"
FT ZN_FING 52..74
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 80..102
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 111..133
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 140..162
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 172..194
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 229..251
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 257..279
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 285..307
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 353..375
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 381..403
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 409..431
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..459
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..487
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 493..515
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 521..543
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWE0"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWE0"
FT CONFLICT 33
FT /note="G -> R (in Ref. 1; BAC40716)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="L -> Q (in Ref. 1; BAC40716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 61830 MW; CC62C2AA5501C989 CRC64;
MLEQRCRGPT AMGPAQPWLF SGPSQESSQP DRGLRYQGKS AQPRGQTPGK VHRCAHCRKR
FPGWVALWLH ARRCQARLPL PCHECNQRFR HAPFLALHLQ VHASAVPDLG FICHLCGHSF
RGWVALVLHL RAHSASKRPI TCPECDRRFW RQKQLRAHLR RCQPPVPEAR PFICGNCGRS
FAQWDQLVVH KRVHVAEALE EAAAKALGPR PRGRPAAPRP GGDAVDRPFQ CACCGKRFRH
KPNLIAHRRV HTGERPHQCP ECGKRFTNKP YLTSHRRIHT GEKPYPCTEC GRRFRHKPNL
LSHSKIHKRL EVSAQAAPHP ESHQIAAEPM AQPALGVPLG SPRTPAEAPA LLHSCSDCGR
SFRLERFLRL HQRQHTGERP FACTECGKNF GKKTHLVAHS RVHSGERPFA CEECGRRFSQ
GSHLAAHRRD HAPERPFVCP DCGKAFRHKP YLAAHRRIHT GEKPYVCPDC GKAFSQKSNL
VSHRRIHTGE RPYACPDCDR SFSQKSNLIT HRKSHIRDGA FCCAICGQTF DDEDRLLMHQ
KKHDA
