PIF1_MOUSE
ID PIF1_MOUSE Reviewed; 650 AA.
AC Q80SX8; Q80W44; Q8BIZ3; Q8BJ72;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH TELOMERASE.
RX PubMed=17130244; DOI=10.1128/mcb.01866-06;
RA Snow B.E., Mateyak M., Paderova J., Wakeham A., Iorio C., Zakian V.,
RA Squire J., Harrington L.;
RT "Murine Pif1 interacts with telomerase and is dispensable for telomere
RT function in vivo.";
RL Mol. Cell. Biol. 27:1017-1026(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129/SvJ;
RA Lo A.W.I., Murnane J.P.;
RT "Assignment of the mouse Pif1 gene to mouse chromosome 9D by FISH and
RT interspecific backcross analyses.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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).
RN [5]
RP ALTERNATIVE INITIATION (ISOFORM 3), AND SUBCELLULAR LOCATION (ISOFORM 3).
RX PubMed=23275553; DOI=10.1093/nar/gks1347;
RA Kazak L., Reyes A., Duncan A.L., Rorbach J., Wood S.R., Brea-Calvo G.,
RA Gammage P.A., Robinson A.J., Minczuk M., Holt I.J.;
RT "Alternative translation initiation augments the human mitochondrial
RT proteome.";
RL Nucleic Acids Res. 41:2354-2369(2013).
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 (By similarity). Interacts with telomerase.
CC {ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:17130244}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03176,
CC ECO:0000269|PubMed:17130244}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion {ECO:0000255|HAMAP-
CC Rule:MF_03176, ECO:0000269|PubMed:23275553}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=1;
CC IsoId=Q80SX8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80SX8-2; Sequence=VSP_026718, VSP_026719;
CC Name=3;
CC IsoId=Q80SX8-3; Sequence=VSP_047458;
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 -!- DISRUPTION PHENOTYPE: Mice do not exhibit any change in telomere length
CC in thymocytes or plenocytes nor significant change in chromosome gain
CC or rearrangements. {ECO:0000269|PubMed:17130244}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation of
CC isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03176}.
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DR EMBL; AY498715; AAS77397.1; -; mRNA.
DR EMBL; AY100322; AAM50051.1; -; mRNA.
DR EMBL; AY100323; AAM50052.1; -; Genomic_DNA.
DR EMBL; AK028460; BAC25963.1; -; mRNA.
DR EMBL; AK049353; BAC33702.1; -; mRNA.
DR EMBL; BC046611; AAH46611.1; -; mRNA.
DR RefSeq; NP_766041.1; NM_172453.3.
DR RefSeq; XP_006510982.1; XM_006510919.2.
DR RefSeq; XP_006510983.1; XM_006510920.2.
DR AlphaFoldDB; Q80SX8; -.
DR SMR; Q80SX8; -.
DR STRING; 10090.ENSMUSP00000049046; -.
DR iPTMnet; Q80SX8; -.
DR PhosphoSitePlus; Q80SX8; -.
DR EPD; Q80SX8; -.
DR PaxDb; Q80SX8; -.
DR PRIDE; Q80SX8; -.
DR Antibodypedia; 4360; 124 antibodies from 23 providers.
DR DNASU; 208084; -.
DR Ensembl; ENSMUST00000239405; ENSMUSP00000159314; ENSMUSG00000041064. [Q80SX8-1]
DR GeneID; 208084; -.
DR KEGG; mmu:208084; -.
DR UCSC; uc009qdp.2; mouse. [Q80SX8-1]
DR CTD; 80119; -.
DR MGI; MGI:2143057; Pif1.
DR VEuPathDB; HostDB:ENSMUSG00000041064; -.
DR eggNOG; KOG0987; Eukaryota.
DR GeneTree; ENSGT00530000063561; -.
DR HOGENOM; CLU_001613_7_1_1; -.
DR InParanoid; Q80SX8; -.
DR OrthoDB; 931726at2759; -.
DR PhylomeDB; Q80SX8; -.
DR TreeFam; TF319207; -.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR BioGRID-ORCS; 208084; 1 hit in 110 CRISPR screens.
DR ChiTaRS; Pif1; mouse.
DR PRO; PR:Q80SX8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q80SX8; protein.
DR Bgee; ENSMUSG00000041064; Expressed in ear vesicle and 134 other tissues.
DR ExpressionAtlas; Q80SX8; baseline and differential.
DR Genevisible; Q80SX8; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
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:MGI.
DR GO; GO:0033678; F:5'-3' DNA/RNA helicase activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
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:MGI.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISO:MGI.
DR GO; GO:0010521; F:telomerase inhibitor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:MGI.
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:MGI.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0032204; P:regulation of telomere maintenance; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_03176; PIF1; 1.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF05970; PIF1; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; ATP-binding; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..650
FT /note="ATP-dependent DNA helicase PIF1"
FT /id="PRO_0000295091"
FT DNA_BIND 586..605
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT REGION 14..192
FT /note="PINT"
FT /evidence="ECO:0000250"
FT REGION 171..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 237..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H611"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H611"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047458"
FT VAR_SEQ 241..272
FT /note="TGKSYLLKHILGSLPPTGTVATASTGVAACHI -> NRAGIRWWAALGGSRQ
FT ATLTLPTTQGQESPTC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026718"
FT VAR_SEQ 273..650
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026719"
FT CONFLICT 79
FT /note="P -> L (in Ref. 1; AAS77397 and 2; AAM50051/
FT AAM50052)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="P -> L (in Ref. 1; AAS77397 and 2; AAM50051/
FT AAM50052)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="P -> S (in Ref. 4; AAH46611)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="K -> R (in Ref. 4; AAH46611)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="Q -> R (in Ref. 4; AAH46611)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="W -> R (in Ref. 4; AAH46611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 70942 MW; 0330ABA54006DDE4 CRC64;
MRSGLCTPAE ALEMPSSTEA ATDECDDAEL RCRVAVEELS PGGQPRKRQA LRAAELSLGR
NERRELMLRL QAPGPTGRPR CFPLRAVRLF TRFAATGRST LRLPTDGVPG AGSVQLLLSD
CPPERLRRFL RTLRLKLAVA PGPGPASARA QLLGPRPRDF VTISPVQPEE LQRAAATKAP
DSALEKRPME SQTSTEAPRW PLPVKKLRMP STKPKLSEEQ AAVLRMVLKG QSIFFTGSAG
TGKSYLLKHI LGSLPPTGTV ATASTGVAAC HIGGTTLHAF AGIGSGQAPL AQCMALANRP
GVRQGWLNCQ RLVIDEISMV EADFFDKLEA VARAVRQQKK PFGGIQLIIC GDFLQLPPVT
KGSQQPQFCF QAKSWRRCVP VILELTEVWR QADQTFISLL QAVRLGRCSD EVTRQLRATA
AHKVGRDGIV ATRLCTHQDD VALTNEKWLK ALPGDVHSFE AIDSDPELSR TLDAQCPVSR
VLQLKLGAQV MLVKNLAVSR GLVNGARGVV VGFESEGRGL PRVRFLCGIT EVIRTDRWTV
QVTGGQYLSR QQLPLQLAWA ISIHKSQGMS LDCVEISLGR VFASGQAYVA LSRARSLQGL
RVLDFDPTVV RCDSRVLHFY ATLRQGRGLS LESQDDEEAN SDLENMDPNL
