ID   TIPIN_BOVIN             Reviewed;         290 AA.
AC   Q3ZCC4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=TIMELESS-interacting protein;
GN   Name=TIPIN;
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=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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; BC102519; AAI02520.1; -; mRNA.
DR   RefSeq; NP_001276920.1; NM_001289991.1.
DR   AlphaFoldDB; Q3ZCC4; -.
DR   SMR; Q3ZCC4; -.
DR   STRING; 9913.ENSBTAP00000000482; -.
DR   PaxDb; Q3ZCC4; -.
DR   PRIDE; Q3ZCC4; -.
DR   Ensembl; ENSBTAT00000068089; ENSBTAP00000062695; ENSBTAG00000000372.
DR   GeneID; 506176; -.
DR   KEGG; bta:506176; -.
DR   CTD; 54962; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000372; -.
DR   VGNC; VGNC:35877; TIPIN.
DR   eggNOG; KOG3004; Eukaryota.
DR   GeneTree; ENSGT00390000005764; -.
DR   HOGENOM; CLU_074595_0_0_1; -.
DR   InParanoid; Q3ZCC4; -.
DR   OrthoDB; 1505397at2759; -.
DR   TreeFam; TF313290; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000000372; Expressed in oocyte and 105 other tissues.
DR   ExpressionAtlas; Q3ZCC4; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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   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..290
FT                   /note="TIMELESS-interacting protein"
FT                   /id="PRO_0000305252"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..143
FT                   /note="Interaction with TIMELESS"
FT                   /evidence="ECO:0000250"
FT   REGION          221..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVW5"
FT   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVW5"
FT   MOD_RES         233
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVW5"
FT   MOD_RES         244
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVW5"
SQ   SEQUENCE   290 AA;  32743 MW;  0BF6201F95DAB67B CRC64;
     MLEPQENGLT DLPDYEHIED ETFPPFPPPA SPGREDGEGA EPEEESGRGA PVPVPPKRTV
     KRNIPKLNAE RLISERGLPA LRHVFEKAKF KGKGHEAEDL KTLIRHMEHW AHRLFPKLQF
     EDFIDRVECL GNKKEVQTCL KRIRLDLPIL HEDFVSNNDE VEENNGHDVT ATELDHFLTN
     SYGSVEFASE SSRSLTEEEQ QRIERNKQLA LERRQAKLLS NSQSLGNDLS VNTPSTQTSE
     AGSTGEEQKE EESNGFNKDL LDSPHNAGAA STVNEEEQLK VEETQLDQSF