ID   TIPIN_RAT               Reviewed;         276 AA.
AC   Q4QR88;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=TIMELESS-interacting protein;
GN   Name=Tipin;
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 [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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).
CC   -!- FUNCTION: Plays an important role in the control of DNA replication and
CC       the maintenance of replication fork stability. Important for cell
CC       survival after DNA damage or replication stress. May be specifically
CC       required for the ATR-CHEK1 pathway in the replication checkpoint
CC       induced by hydroxyurea or ultraviolet light. Forms a complex with
CC       TIMELESS and this complex regulates DNA replication processes under
CC       both normal and stress conditions, stabilizes replication forks and
CC       influences both CHEK1 phosphorylation and the intra-S phase checkpoint
CC       in response to genotoxic stress.
CC   -!- SUBUNIT: Interacts with TIMELESS, which impairs TIMELESS self-
CC       association. Interacts with RPA2, PRDX2, MCM6 and MCM7 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CSM3 family. {ECO:0000305}.
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DR   EMBL; BC097351; AAH97351.1; -; mRNA.
DR   RefSeq; NP_001020458.1; NM_001025287.1.
DR   AlphaFoldDB; Q4QR88; -.
DR   SMR; Q4QR88; -.
DR   STRING; 10116.ENSRNOP00000053083; -.
DR   PaxDb; Q4QR88; -.
DR   Ensembl; ENSRNOT00000066973; ENSRNOP00000059833; ENSRNOG00000043068.
DR   GeneID; 363076; -.
DR   KEGG; rno:363076; -.
DR   CTD; 54962; -.
DR   RGD; 1564084; Tipin.
DR   eggNOG; KOG3004; Eukaryota.
DR   GeneTree; ENSGT00390000005764; -.
DR   InParanoid; Q4QR88; -.
DR   OrthoDB; 1505397at2759; -.
DR   PhylomeDB; Q4QR88; -.
DR   PRO; PR:Q4QR88; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0031298; C:replication fork protection complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0044770; P:cell cycle phase transition; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:RGD.
DR   GO; GO:0000076; P:DNA replication checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0043111; P:replication fork arrest; IBA:GO_Central.
DR   GO; GO:0048478; P:replication fork protection; IBA:GO_Central.
DR   GO; GO:0009411; P:response to UV; ISO:RGD.
DR   InterPro; IPR012923; Csm3.
DR   InterPro; IPR040038; TIPIN/Csm3/Swi3.
DR   PANTHER; PTHR13220; PTHR13220; 1.
DR   Pfam; PF07962; Swi3; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; DNA damage; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..276
FT                   /note="TIMELESS-interacting protein"
FT                   /id="PRO_0000305255"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..140
FT                   /note="Interaction with TIMELESS"
FT                   /evidence="ECO:0000250"
FT   REGION          217..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVW5"
FT   MOD_RES         233
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVW5"
SQ   SEQUENCE   276 AA;  31137 MW;  38CCA8E93476B280 CRC64;
     MLEQEENGLF EIPDYEHVED ETFPPFPPPG SPERDPAEAE PDEGSGAPVP VPPKRIVKRN
     IPKLDATRLT SERGLPALRH VFDKTKFKGK GHEAEDLKTL IRHMEHWAHR LFPKLQFEDF
     IDRVENLGNK KEVQTCLKRI RLDLPIVHED FVNNNDEVEE TNSLDAAATG FDAFVTSSSD
     SKRFASEASR NLTEEQQQRI EKNKQLALER RQAKLLSNSQ SLENDVTVEE SSTGENQEES
     NGLISADGPH DVPSASTQEE GQLEAEETQL DHPNLD