FAN1_SCHPO
ID FAN1_SCHPO Reviewed; 703 AA.
AC Q9Y804;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Fanconi-associated nuclease 1 homolog {ECO:0000305};
DE EC=3.1.4.1 {ECO:0000250|UniProtKB:Q9Y2M0};
GN ORFNames=SPBC146.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24192486; DOI=10.1016/j.dnarep.2013.10.003;
RA Fontebasso Y., Etheridge T.J., Oliver A.W., Murray J.M., Carr A.M.;
RT "The conserved Fanconi anemia nuclease Fan1 and the SUMO E3 ligase Pli1 act
RT in two novel Pso2-independent pathways of DNA interstrand crosslink repair
RT in yeast.";
RL DNA Repair 12:1011-1023(2013).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF ARG-103; ARG-107; 257-ILE-LEU-258; ALA-360;
RP LEU-564; ASP-651; GLU-666 AND LYS-668.
RX PubMed=25319828; DOI=10.1101/gad.248492.114;
RA Gwon G.H., Kim Y., Liu Y., Watson A.T., Jo A., Etheridge T.J., Yuan F.,
RA Zhang Y., Kim Y., Carr A.M., Cho Y.;
RT "Crystal structure of a Fanconi anemia-associated nuclease homolog bound to
RT 5' flap DNA: basis of interstrand cross-link repair by FAN1.";
RL Genes Dev. 28:2276-2290(2014).
CC -!- FUNCTION: Nuclease required for the repair of DNA interstrand cross-
CC links (ICL) (PubMed:24192486, PubMed:25319828). Acts as a 5'-3'
CC exonuclease that anchors at a cut end of DNA and cleaves DNA
CC successively at every third nucleotide, allowing to excise an ICL from
CC one strand through flanking incisions (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y2M0, ECO:0000269|PubMed:24192486,
CC ECO:0000269|PubMed:25319828}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolytically removes 5'-nucleotides successively from the
CC 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.;
CC EC=3.1.4.1; Evidence={ECO:0000250|UniProtKB:Q9Y2M0};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9I2N0};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9I2N0};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q9I2N0};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to a cross-linking agent.
CC {ECO:0000269|PubMed:24192486}.
CC -!- SIMILARITY: Belongs to the FAN1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB46759.1; -; Genomic_DNA.
DR PIR; T39420; T39420.
DR RefSeq; NP_595395.1; NM_001021302.2.
DR AlphaFoldDB; Q9Y804; -.
DR SMR; Q9Y804; -.
DR BioGRID; 276243; 65.
DR STRING; 4896.SPBC146.06c.1; -.
DR PaxDb; Q9Y804; -.
DR PRIDE; Q9Y804; -.
DR EnsemblFungi; SPBC146.06c.1; SPBC146.06c.1:pep; SPBC146.06c.
DR GeneID; 2539688; -.
DR KEGG; spo:SPBC146.06c; -.
DR PomBase; SPBC146.06c; -.
DR VEuPathDB; FungiDB:SPBC146.06c; -.
DR eggNOG; KOG2143; Eukaryota.
DR HOGENOM; CLU_005116_1_0_1; -.
DR InParanoid; Q9Y804; -.
DR OMA; LEEHYMW; -.
DR PhylomeDB; Q9Y804; -.
DR PRO; PR:Q9Y804; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISO:PomBase.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0070336; F:flap-structured DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:PomBase.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR033315; Fan1-like.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR014883; VRR_NUC.
DR PANTHER; PTHR15749; PTHR15749; 1.
DR Pfam; PF08774; VRR_NUC; 1.
DR SMART; SM00990; VRR_NUC; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease; Nucleus;
KW Reference proteome.
FT CHAIN 1..703
FT /note="Fanconi-associated nuclease 1 homolog"
FT /id="PRO_0000374000"
FT DOMAIN 597..698
FT /note="VRR-NUC"
FT BINDING 529
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 651
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 651
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 666
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 667
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT MUTAGEN 103
FT /note="R->A: Hypersensitivity to a cross-linking agent;
FT when associated with A-107."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 107
FT /note="R->A: Hypersensitivity to a cross-linking agent;
FT when associated with A-103."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 257..258
FT /note="IL->RR: No effect."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 360
FT /note="A->P: Hypersensitivity to a cross-linking agent."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 564
FT /note="L->R: Hypersensitivity to a cross-linking agent."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 651
FT /note="D->A: Hypersensitivity to a cross-linking agent."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 666
FT /note="E->Q: Hypersensitivity to a cross-linking agent."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 668
FT /note="K->A: Hypersensitivity to a cross-linking agent."
FT /evidence="ECO:0000269|PubMed:25319828"
SQ SEQUENCE 703 AA; 82226 MW; 6E629E26CEB1539D CRC64;
MKRFFNEACD INTPDKSGVN ENKLCFPPLK VVCQAPETTV KGQVANTNKH NVYSTKNSMY
LLGFEEILNT VLDCEPHIFT DDELRVIENF KALDSDERYL FVRLFMRKRN KWFRVGHLTY
PDCKDVIACC KQLVLKNFFE DESLMSTEEI IEILSLDELR SLARQTKVCG KSRSEISKEI
IFLSKRQSVL HCNGQQFLSF DAFGVMHKQE SFLRKQLLYQ CKSCVKPKKI LVDLFHRINI
VYFRSSIYDE QSLTSLILAR LNKFSYPNYV LSRTSNVFNC RAQCLEYVEV LELSKNLVPI
FENTAASDKE ALEQALNSFF EIYPIWSTYL NEDIREFWVE ENRKVDTRLV RFSFSFRPGA
VYTYLIHKSL NILAKSRLVE VEHEILDTLL SQNIYLVGKR GHWYNRKALL EYNFKTEDTN
VLRYWKTLAL STCENGIEDK YTHLRYYFSL QRRLVRLRKC LKVSNTTELK SMKLINNNPS
RLFLHGERIH NGDLSNRTVW RSKTNNAITV EELALQHYQS IGWEGIHAES SILLTLFALT
FWDILFEDVP GVFQSPFQSA PLDLHTDSFY ISRESTIMKR LEEIRNGKAG LIIKDNYIRE
HQRKTFCVGL NWSYTCEMLL EIVDCINDNG LAQIFLALTQ DYKNSSSGIP DLCLWNPSKK
KFMFSEVKSD NDRLSEAQKF WISLLISSEV DVEVCHVSMH KKK
