REPI1_BOVIN
ID REPI1_BOVIN Reviewed; 559 AA.
AC Q0VCC5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Replication initiator 1;
GN Name=REPIN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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; BC120236; AAI20237.1; -; mRNA.
DR RefSeq; NP_001068989.1; NM_001075521.1.
DR AlphaFoldDB; Q0VCC5; -.
DR SMR; Q0VCC5; -.
DR STRING; 9913.ENSBTAP00000052175; -.
DR PaxDb; Q0VCC5; -.
DR PRIDE; Q0VCC5; -.
DR Ensembl; ENSBTAT00000056211; ENSBTAP00000052175; ENSBTAG00000038241.
DR GeneID; 511510; -.
DR KEGG; bta:511510; -.
DR CTD; 29803; -.
DR VEuPathDB; HostDB:ENSBTAG00000038241; -.
DR VGNC; VGNC:33868; REPIN1.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162588; -.
DR HOGENOM; CLU_002678_36_0_1; -.
DR InParanoid; Q0VCC5; -.
DR OMA; AYRCARC; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF326846; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000038241; Expressed in laryngeal cartilage and 102 other tissues.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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: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; 14.
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..559
FT /note="Replication initiator 1"
FT /id="PRO_0000274911"
FT ZN_FING 57..81
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 85..107
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 116..138
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 145..168
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 177..199
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 236..258
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 264..286
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 292..314
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 367..389
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 395..417
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 423..445
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 451..473
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 479..501
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 507..529
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 535..557
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 REGION 313..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWE0"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWE0"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWE0"
FT MOD_RES 276
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWE0"
SQ SEQUENCE 559 AA; 62372 MW; 344D698F00742F79 CRC64;
MLERRCRGPV AMGPAQPRLL SGPSQESPQT LEKEPQGLRS RGTAAAQSGG QALGRAHRCA
HCRRHFPGWV ALWLHARRCQ ARLPRPCPEC GRRFRHAPFL ALHCQVHAAA TPDQGFACHL
CGQSFRGWVA LVLHLRAHSA AKRPIACPAC ERRFWRRKQL RAHSRRCHPP APEARPFICG
NCGRSFAQWD QLVTHKRVHV AEALEEAAAK ALGPRPRGRP AVTAPRPGGD AVDRPFQCAC
CGKRFRHKPN LIAHRRVHTG ERPHQCPECG KRFTNKPYLT SHRRIHTGEK PYPCTECGRR
FRHKPNLLSH SKIHKRSEGS AQGGPQPPAS APERTPEPPP EPAPEPAEVP VGPGQPSAAA
EAPPSLHTCA DCGRGFRLER FLRAHQRQHG GERPFACAEC GKHFGKKTHL VAHSRVHSGE
RPFACEECGR RFSQGSHLAA HRRDHAPERP FVCPDCGKAF RHKPYLAAHR RIHTGEKPYV
CPECGKAFSQ KSNLVSHRRI HTGERPYACP DCDRSFSQKS NLITHRKSHI RDGAFCCAIC
GQTFDDEGKL LAHQKKHDV
