TIPIN_CHICK
ID TIPIN_CHICK Reviewed; 283 AA.
AC Q5F416;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=TIMELESS-interacting protein;
GN Name=TIPIN; ORFNames=RCJMB04_3n6;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CSM3 family. {ECO:0000305}.
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DR EMBL; AJ851484; CAH65118.1; -; mRNA.
DR RefSeq; NP_001012708.1; NM_001012690.1.
DR AlphaFoldDB; Q5F416; -.
DR SMR; Q5F416; -.
DR STRING; 9031.ENSGALP00000012365; -.
DR PaxDb; Q5F416; -.
DR GeneID; 415548; -.
DR KEGG; gga:415548; -.
DR CTD; 54962; -.
DR VEuPathDB; HostDB:geneid_415548; -.
DR eggNOG; KOG3004; Eukaryota.
DR InParanoid; Q5F416; -.
DR OrthoDB; 1505397at2759; -.
DR PhylomeDB; Q5F416; -.
DR PRO; PR:Q5F416; -.
DR Proteomes; UP000000539; Unplaced.
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 Reference proteome.
FT CHAIN 1..283
FT /note="TIMELESS-interacting protein"
FT /id="PRO_0000305256"
FT REGION 1..68
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 186..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 283 AA; 31827 MW; 15211F47221D77EF CRC64;
MAMIDPLENN LFDLPDYENT EDETFPPLPP PTSPGRGDAE WAQANGDPDG NQQSETKDSS
SAARKAVKRS IPKLDANRLV SERGLPALRH MFDNVKFKGK GHEAEDLKTL LRHMEHWAHR
LFPKLQFDDF IDRVESLGNK KEVQTCLKRI RLDLPILHED FTANEGGGGE SNGLDMATEE
VHSFSGNVGE LDSLPGTTLT EEQQQRIKRN RQLALERRQA KMQCNSQSQH DELSPSYPEE
ELNIPVARDL TGALEDTQVT ATNVAVTETE DRERELQCAS EKQ