ID   TIPIN_XENLA             Reviewed;         360 AA.
AC   Q0IHI4; Q3LGB8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=TIMELESS-interacting protein;
DE   AltName: Full=XTipin;
GN   Name=tipin;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tsujimura T., Hashimoto H., Takisawa H.;
RT   "Xenopus Tim1 and Tipin are required for stable association of Claspin/Mrc1
RT   with replication forks.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) 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 required fin
CC       the replication checkpoint induced by hydroxyurea or ultraviolet light
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with timeless, which impairs timeless self-
CC       association. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q0IHI4; Q9DE46: pola1; NbExp=3; IntAct=EBI-7570880, EBI-3645423;
CC       Q0IHI4; O13046: wdhd1; NbExp=5; IntAct=EBI-7570880, EBI-3510652;
CC       Q0IHI4; Q3LGB9: XTim1; NbExp=2; IntAct=EBI-7570880, EBI-15657607;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CSM3 family. {ECO:0000305}.
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DR   EMBL; AB208777; BAE45345.1; -; mRNA.
DR   EMBL; BC123142; AAI23143.1; -; mRNA.
DR   RefSeq; NP_001081090.1; NM_001087621.1.
DR   AlphaFoldDB; Q0IHI4; -.
DR   SMR; Q0IHI4; -.
DR   DIP; DIP-46439N; -.
DR   IntAct; Q0IHI4; 4.
DR   MINT; Q0IHI4; -.
DR   PRIDE; Q0IHI4; -.
DR   DNASU; 394376; -.
DR   GeneID; 394376; -.
DR   KEGG; xla:394376; -.
DR   CTD; 394376; -.
DR   Xenbase; XB-GENE-17340911; tipin.L.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 394376; Expressed in egg cell and 19 other tissues.
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: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:0048478; P:replication fork protection; IEA:InterPro.
DR   InterPro; IPR012923; Csm3.
DR   InterPro; IPR040038; TIPIN/Csm3/Swi3.
DR   PANTHER; PTHR13220; PTHR13220; 1.
DR   Pfam; PF07962; Swi3; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; DNA damage; Mitosis; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..360
FT                   /note="TIMELESS-interacting protein"
FT                   /id="PRO_0000305258"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..150
FT                   /note="Interaction with TIMELESS"
FT                   /evidence="ECO:0000250"
FT   REGION          178..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        39
FT                   /note="E -> D (in Ref. 2; BAE45345)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="P -> S (in Ref. 2; BAE45345)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        337
FT                   /note="D -> DDS (in Ref. 2; BAE45345)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354
FT                   /note="T -> A (in Ref. 2; BAE45345)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  40337 MW;  7F839CB9B51032D8 CRC64;
     MMDPLDNGLF DLPDYEHTED ENFPPLPPPH SPGADDEAED VANGDDWTEN AGQTQREEAP
     KPARRVVKRP QPKLDGQRLA SQRGLPALRH MFDDVKFKGK GHETEDLKIL LRQMENWAHR
     LFPKLQFEDF LNRLESMGNK KEVQTCLKKI RMDLPIVHDD FLSEEVVVQT EDHAIDMPSE
     DFSFPDELHV PSPSQPVKVD LSEETLQRIE RNRRLALERR MEKMQAQAES QALSQATQSD
     PNEIPDDAFD AEMLDAVESM TGIPTASQSP PHVDKDLSLV LHSHDLPVQD VSQSPAPCPK
     PQGDAPPEKA LSLVHSALPS TSDPTSPRKP LTEQLPDDAD TSSATPYTEA PACTNTKEEY