PIF1_RAT
ID PIF1_RAT Reviewed; 637 AA.
AC Q1HG60;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=ATP-dependent DNA helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03176};
DE AltName: Full=DNA repair and recombination helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176};
DE AltName: Full=PIF1/RRM3 DNA helicase-like protein;
GN Name=Pif1;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Spleen;
RA Snow B.E., Harrington L.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the
CC maintenance of both mitochondrial and nuclear genome stability.
CC Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA
CC hybrids. Resolves G4 structures, preventing replication pausing and
CC double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance
CC of telomeric DNA. Inhibits telomere elongation, de novo telomere
CC formation and telomere addition to DSBs via catalytic inhibition of
CC telomerase. Reduces the processivity of telomerase by displacing active
CC telomerase from DNA ends. Releases telomerase by unwinding the short
CC telomerase RNA/telomeric DNA hybrid that is the intermediate in the
CC telomerase reaction. Possesses an intrinsic strand annealing activity.
CC {ECO:0000255|HAMAP-Rule:MF_03176}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03176};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03176};
CC -!- SUBUNIT: Monomer. Interacts with telomerase. {ECO:0000255|HAMAP-
CC Rule:MF_03176}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03176}.
CC Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03176}.
CC -!- DOMAIN: The PIF1 N-terminal (PINT) domain enhances the interaction with
CC ssDNA through intrinsic binding activity, it also harbors DNA strand-
CC annealing activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03176}.
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DR EMBL; DQ489562; ABF29535.1; -; mRNA.
DR RefSeq; NP_001037718.1; NM_001044253.1.
DR AlphaFoldDB; Q1HG60; -.
DR SMR; Q1HG60; -.
DR STRING; 10116.ENSRNOP00000021265; -.
DR CarbonylDB; Q1HG60; -.
DR PaxDb; Q1HG60; -.
DR PRIDE; Q1HG60; -.
DR Ensembl; ENSRNOT00000021265; ENSRNOP00000021265; ENSRNOG00000015878.
DR GeneID; 367645; -.
DR KEGG; rno:367645; -.
DR UCSC; RGD:1586053; rat.
DR CTD; 80119; -.
DR RGD; 1586053; Pif1.
DR eggNOG; KOG0987; Eukaryota.
DR GeneTree; ENSGT00530000063561; -.
DR HOGENOM; CLU_001613_7_1_1; -.
DR InParanoid; Q1HG60; -.
DR OMA; ITLHQFA; -.
DR OrthoDB; 931726at2759; -.
DR PhylomeDB; Q1HG60; -.
DR Reactome; R-RNO-171319; Telomere Extension By Telomerase.
DR PRO; PR:Q1HG60; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000015878; Expressed in thymus and 12 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; ISO:RGD.
DR GO; GO:0033678; F:5'-3' DNA/RNA helicase activity; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISO:RGD.
DR GO; GO:0010521; F:telomerase inhibitor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:RGD.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0051974; P:negative regulation of telomerase activity; ISO:RGD.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:0032204; P:regulation of telomere maintenance; ISO:RGD.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_03176; PIF1; 1.
DR InterPro; IPR003840; DNA_helicase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02689; Herpes_Helicase; 1.
DR Pfam; PF05970; PIF1; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Mitochondrion; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..637
FT /note="ATP-dependent DNA helicase PIF1"
FT /id="PRO_0000295092"
FT DNA_BIND 573..592
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT REGION 1..180
FT /note="PINT"
FT /evidence="ECO:0000250"
FT REGION 159..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 224..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H611"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H611"
SQ SEQUENCE 637 AA; 69758 MW; 36CD14D1B5BB5558 CRC64;
MPSSTEVATD ECDDTELRCR VAVEELSPGG QPRKRQALRA AELSLGRNER RELMLRLQAP
GPEGRPRCFP LRAVRLFTRF AAVGRSTLRL PADGVPRAGS VQLLLSDCPP ERLRRFLRTL
RLKLAVAPGP GPASARAQLL GPRPRDFVTI SPVQPEELRR AAATKAPDSA LEKRPMESQP
SMEAPRWPLP VKKLRMPSSK PKLSEEQAAV LRMVLKGQSI FFTGSAGTGK SYLLKHILGS
LPPTGTVATA STGVAACHIG GTTLHAFAGI GSGQAPLAQC VALAHRPGVR QGWLNCQRLV
IDEISMVEAD FFDKLEAVAR AVRQQKKPFG GIQLIICGDF LQLPPVTKGS QHPRFCFQAK
SWRKCVPVTL ELTEVWRQAD QTFISLLKAV RLGRCSDEVT RQLRATAAHK VGRDGIIATR
LCTHQDDVAL TNEKRLKELP GDVHSFEAID SDPELSRTLD AQCPVGRVLQ LKLGAQVMLV
KNLAVSRGLV NGARGVVVGF ESEGRGLPRV RFLCGITEVI RTDRWTVQVT GGQYLSRQQL
PLQLAWAMSI HKSQGMSLDC VEISLGRVFA SGQAYVALSR ARSLQGLRVL DFDPTVVRCD
SRVLQFYATL RQGRGLSLES QDDEEASSDL ENMDPNL
