PARI_BOVIN
ID PARI_BOVIN Reviewed; 582 AA.
AC F1MF21;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=PCNA-interacting partner;
DE Short=PARI;
DE AltName: Full=PARP-1 binding protein;
DE AltName: Full=PARP1-binding protein;
DE Short=PARPBP;
GN Name=PARPBP; Synonyms=PARI;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Required to suppress inappropriate homologous recombination,
CC thereby playing a central role DNA repair and in the maintenance of
CC genomic stability. Antagonizes homologous recombination by interfering
CC with the formation of the RAD51-DNA homologous recombination structure.
CC Binds single-strand DNA and poly(A) homopolymers. Positively regulate
CC the poly(ADP-ribosyl)ation activity of PARP1; however such function may
CC be indirect (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RAD51 and PCNA. Interacts with PARP1 (By
CC similarity). Interacts with TASOR (By similarity).
CC {ECO:0000250|UniProtKB:Q6IRT3, ECO:0000250|UniProtKB:Q9NWS1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Localizes to chromatin in response to S phase arrest but not in
CC mitosis. Targeted to chromatin via its interaction with PCNA (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PARI family. {ECO:0000305}.
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DR EMBL; DAAA02013696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1MF21; -.
DR SMR; F1MF21; -.
DR STRING; 9913.ENSBTAP00000053842; -.
DR PaxDb; F1MF21; -.
DR PRIDE; F1MF21; -.
DR eggNOG; ENOG502QR2U; Eukaryota.
DR HOGENOM; CLU_034470_1_0_1; -.
DR InParanoid; F1MF21; -.
DR TreeFam; TF332230; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038932; PARPBP.
DR PANTHER; PTHR32121; PTHR32121; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..582
FT /note="PCNA-interacting partner"
FT /id="PRO_0000415568"
FT REGION 471..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 65429 MW; 486F9D7190082C85 CRC64;
MAGLNQKSIL DMIKEFRRNW HTLCNSERTT VCGADSMLLA LQLSMAENNK QHSGEFTVSL
SDIILTWKYF LHEKLNLPVE NIKVIDHYED IRKIYDDFLK NSNMLDLIDV YKKCSDLTSN
CENYANISPS RLLDFLSGRE YAVDDETDFS EPVSPMSKHN QENEKVQLLA KKIIYSYLNL
LVNSKNDLAL AHILNIPDRG LGREAFTDLK HAAREKQMSI FLVATSFIRT IELGGKGYAP
SPSDPLRAHI KGLSNFINFI DKLDEILGEV SNPSIAGGRI LSVIKMQLIK GQNSRDPFYK
AVEEVAQDLD LRIKNIINSQ QGDVALSTTD ISPARPKSHT INHGTAYCGR DTVKALLVLL
DEEAASAPTK NKAELLYDNE NTIHPNGTSV LTLFRCRSPT QVDNSPMKPL RERIYKSMEE
KKIKMKQTSI RSQFACTYKD DCMISKDKWN NVNSASEPLC VLHMENDLSE GVNSSVGRPT
IGTSSGNVHL GRSEKEKVAR KSSSLTGNTS SKRKQVDLDD ENILCDNGNE PLQHKIVKIP
KTSKDLQNKL DGKLLRVAKS NRCTTKDKLI TGQTKLTQFF RL