ID   MRNIP_BOVIN             Reviewed;         369 AA.
AC   Q3ZBG8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=MRN complex-interacting protein {ECO:0000250|UniProtKB:Q6NTE8};
DE   AltName: Full=MRN-interacting protein {ECO:0000250|UniProtKB:Q6NTE8};
GN   Name=MRNIP {ECO:0000250|UniProtKB:Q6NTE8};
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=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in the cellular response to DNA damage and the
CC       maintenance of genome stability through its association with the MRN
CC       damage-sensing complex. Promotes chromatin loading and activity of the
CC       MRN complex to facilitate subsequent ATM-mediated DNA damage response
CC       signaling and DNA repair. {ECO:0000250|UniProtKB:Q6NTE8}.
CC   -!- SUBUNIT: Associates with the MRE11-RAD50-NBN (MRN) damage-sensing
CC       complex; this association is constitutive. Interacts with MRE11.
CC       Interacts with NBN. Interacts with RAD50.
CC       {ECO:0000250|UniProtKB:Q6NTE8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6NTE8}. Nucleus,
CC       nucleoplasm {ECO:0000250|UniProtKB:Q6NTE8}. Note=Recruited to sites of
CC       DNA damage. Phosphorylation on Ser-115 induces its nuclear localization
CC       and promotes genome stability. {ECO:0000250|UniProtKB:Q6NTE8}.
CC   -!- PTM: Phosphorylated; phosphorylation is constitutive and occurs in the
CC       absence of any DNA-damaging stimulus. Phosphorylation on Ser-115 is
CC       necessary for its nuclear retention. {ECO:0000250|UniProtKB:Q6NTE8}.
CC   -!- SIMILARITY: Belongs to the MRNIP family. {ECO:0000305}.
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DR   EMBL; BC103300; AAI03301.1; -; mRNA.
DR   RefSeq; NP_001161415.1; NM_001167943.1.
DR   AlphaFoldDB; Q3ZBG8; -.
DR   STRING; 9913.ENSBTAP00000020727; -.
DR   PaxDb; Q3ZBG8; -.
DR   PRIDE; Q3ZBG8; -.
DR   GeneID; 614757; -.
DR   KEGG; bta:614757; -.
DR   CTD; 51149; -.
DR   eggNOG; ENOG502S8YD; Eukaryota.
DR   OrthoDB; 1146272at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR   GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR   GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR   InterPro; IPR032739; MRNIP.
DR   PANTHER; PTHR15863; PTHR15863; 1.
DR   Pfam; PF15749; MRNIP; 1.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..369
FT                   /note="MRN complex-interacting protein"
FT                   /id="PRO_0000326118"
FT   REGION          122..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..259
FT                   /note="Necessary for the association with the MRN complex"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NTE8"
FT   REGION          282..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           148..151
FT                   /note="Nuclear localization signal (NLS)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NTE8"
FT   COMPBIAS        220..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NTE8"
SQ   SEQUENCE   369 AA;  40704 MW;  8201287FC5AF38B7 CRC64;
     MAPPQQARVL RCCCCSLFQA HQVKKSLKWT CKACGKKQSF LQAYGEGSGA DCRRHVQKLN
     LLQGQISEMS LRSLGESISA NEEENVGPWQ AARASPQETL QPSKNRWLKY LERDSKELGL
     KGGGVCFNSQ PSSETEKPDP PFSTGLPRKR KWNQSTVQPL CGPHVQDSRN CEVTLKSLKA
     RPLHPTWGAR SSPDCSTWDL PCISEELPPS FTQDRAGLAG KGRESSREDL DTMELVPRGE
     PPCPAQQVRT MSKWEQCLGN SSHLDTEPLT PLQRGLRPIQ AAQAEQGAPR AQTPREGGLC
     RLPGARQSPQ TTHTPMPGPK WLCGRIPEQS QGTGPWAEGV PLVKGMQARS SLMRLCDLFK
     TGEDFDDDL