PARI_MOUSE
ID PARI_MOUSE Reviewed; 573 AA.
AC Q6IRT3; Q3UAQ9; Q3V278; Q8C0J4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 25-MAY-2022, entry version 96.
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 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=Bone marrow, and Thymus;
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; TISSUE=Head;
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 INTERACTION WITH TASOR, AND TISSUE SPECIFICITY.
RX PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA Prochazka J., Sedlacek R.;
RT "Fam208a orchestrates interaction protein network essential for early
RT embryonic development and cell division.";
RL Exp. Cell Res. 382:111437-111437(2019).
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 (PubMed:31112734).
CC {ECO:0000250|UniProtKB:Q9NWS1, ECO:0000269|PubMed:31112734}.
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 -!- TISSUE SPECIFICITY: Expressed in the ovary, Sertoli cells of the testis
CC and in granular cells within the cerebellum.
CC {ECO:0000269|PubMed:31112734}.
CC -!- SIMILARITY: Belongs to the PARI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27197.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK030970; BAC27197.1; ALT_INIT; mRNA.
DR EMBL; AK131981; BAE20920.1; -; mRNA.
DR EMBL; AK150571; BAE29666.1; -; mRNA.
DR EMBL; AK151268; BAE30255.1; -; mRNA.
DR EMBL; AK152208; BAE31036.1; -; mRNA.
DR EMBL; BC070476; AAH70476.2; -; mRNA.
DR CCDS; CCDS36022.1; -.
DR RefSeq; NP_083525.1; NM_029249.2.
DR AlphaFoldDB; Q6IRT3; -.
DR SMR; Q6IRT3; -.
DR BioGRID; 217389; 1.
DR IntAct; Q6IRT3; 1.
DR STRING; 10090.ENSMUSP00000038375; -.
DR iPTMnet; Q6IRT3; -.
DR PhosphoSitePlus; Q6IRT3; -.
DR PaxDb; Q6IRT3; -.
DR PRIDE; Q6IRT3; -.
DR ProteomicsDB; 287781; -.
DR GeneID; 75317; -.
DR KEGG; mmu:75317; -.
DR UCSC; uc007grd.1; mouse.
DR CTD; 55010; -.
DR MGI; MGI:1922567; Parpbp.
DR eggNOG; ENOG502QR2U; Eukaryota.
DR InParanoid; Q6IRT3; -.
DR OrthoDB; 355941at2759; -.
DR PhylomeDB; Q6IRT3; -.
DR TreeFam; TF332230; -.
DR BioGRID-ORCS; 75317; 1 hit in 109 CRISPR screens.
DR ChiTaRS; Parpbp; mouse.
DR PRO; PR:Q6IRT3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6IRT3; protein.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..573
FT /note="PCNA-interacting partner"
FT /id="PRO_0000280270"
FT REGION 470..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 215
FT /note="Q -> H (in Ref. 1; BAE20920)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="G -> R (in Ref. 1; BAE20920/BAC27197 and 2;
FT AAH70476)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="D -> Y (in Ref. 1; BAE20920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 64105 MW; 66471ECAF8577040 CRC64;
MAVLNQLPVL GMIKEFRRSW RALCSSERTT LCGPDSMLLA LQLSMAENNK QHRGEFTVCL
SDVLLTWKYF LHEKLNLPIE NMKVVEHYED IKKTYDDFLK NSNTLDLIDV YKKCSSLTSN
YENNMISPIQ LRDFLSGTEY AVSDEANPHM PESPVKCSQN DEQVRVLVKK IFFSYLSLLV
NSKNDLALAS ILNIPDRGLG REAFTNLKHA AREKQLSMFL MATSFIRTLE LGGKGYAPSP
SDPLWAHVKG LSEFINFIDK LDEILGKIPN PSLAGSRILS AIKMQLIKGH SSGEPFYKAV
EEVVQDLNLR IKNIINSQEG VAVSANNISP VPPKSFAINH DTAYCGRDAV KILLVLLDED
AASAPTRNKA ELLYNDESTV PHSGPSVLTL FRSPTQEKNT SVKPLRERIH KSLQTEKNKM
WQTLIRSQFA CTYKDDCIMS KNKWHVNSSS KPLSALHLED DVSEGAQSSV GKARIEASSE
NAHVGRWKGD KLPRKSTQRQ ISKGKQLDLD SENLHCDRGN ELYQHKNIKI PKVPSGSHSK
AGGKLAQGTK GNRCPARGKL IPGQTKLTQF FML
