REPI1_RAT
ID REPI1_RAT Reviewed; 548 AA.
AC Q68H95;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Replication initiator 1;
GN Name=Repin1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BB/OK;
RA Kloting N., Kloting I.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AY691175; AAT99579.1; -; mRNA.
DR RefSeq; NP_001005893.1; NM_001005893.1.
DR RefSeq; XP_006236490.1; XM_006236428.3.
DR RefSeq; XP_006236491.1; XM_006236429.3.
DR AlphaFoldDB; Q68H95; -.
DR SMR; Q68H95; -.
DR STRING; 10116.ENSRNOP00000011032; -.
DR PaxDb; Q68H95; -.
DR Ensembl; ENSRNOT00000117289; ENSRNOP00000088288; ENSRNOG00000008239.
DR GeneID; 445541; -.
DR KEGG; rno:445541; -.
DR UCSC; RGD:1549707; rat.
DR CTD; 29803; -.
DR RGD; 1549707; Repin1.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162588; -.
DR HOGENOM; CLU_002678_36_0_1; -.
DR InParanoid; Q68H95; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q68H95; -.
DR TreeFam; TF326846; -.
DR PRO; PR:Q68H95; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Genevisible; Q68H95; RN.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0005811; C:lipid droplet; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:2000191; P:regulation of fatty acid transport; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; DNA replication; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..548
FT /note="Replication initiator 1"
FT /id="PRO_0000274914"
FT ZN_FING 53..75
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 81..103
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 112..134
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 141..163
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 173..195
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 232..254
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 260..282
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 288..310
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..490
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 524..546
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
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:0000250|UniProtKB:Q5U4E2"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWE0"
SQ SEQUENCE 548 AA; 61951 MW; B69186A5DE3918EF CRC64;
MLERRCRGPT AMGPAHPWLF SGPSQESSQP NRGLRYQGKS VAQPGGPAPV KVHRCAHCRK
RFPGWVALWL HTRRCQARLP LPCHECNQRF RHAPFLALHL QVHASAVPDL GFICHLCGHS
FRGWVALVLH LRAHSASKRP ITCPECNKRF WRQKQLRAHL RRCQPPAPEA RPFICGNCGR
SFAQWDQLVV HKRVHVAEAL EEAAAKALGP RPRGRPSVTA PRPGGDAVDR PFQCACCGKR
FRHKPNLIAH RRVHTGERPH QCPECGKRFT NKPYLTSHRR IHTGEKPYPC TECGRRFRHK
PNLLSHSKIH KRSEVSAQAA SHTGSHLIAA EPMAQPALGV PLGSLRTPAE APASLHSCTD
CGRSFRLERF LRLHQRQHTG ERPFTCTECG KNFGKKTHLV AHSRVHSGER PFACEECGRR
FSQGSHLAAH RRDHAPERPF VCPDCGKAFR HKPYLAAHRR IHTGEKPYVC PDCGKAFSQK
SNLVSHRRIH TGERPYACPD CDRSFSQKSN LITHRKSHIR DGAFCCAICG QTFDDEDRLL
MHQKKHDA
