FAN1_ARATH
ID FAN1_ARATH Reviewed; 891 AA.
AC Q5XVJ4; Q5XVJ5; Q9SX69;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Fanconi-associated nuclease 1 homolog {ECO:0000305};
DE Short=AtFAN1 {ECO:0000303|PubMed:25779053};
DE EC=3.1.4.1 {ECO:0000250|UniProtKB:Q9Y2M0};
GN Name=FAN1 {ECO:0000303|PubMed:25779053}; OrderedLocusNames=At1g48360;
GN ORFNames=F11A17.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=cv. Columbia;
RX PubMed=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP FUNCTION.
RX PubMed=25779053; DOI=10.1093/nar/gkv208;
RA Herrmann N.J., Knoll A., Puchta H.;
RT "The nuclease FAN1 is involved in DNA crosslink repair in Arabidopsis
RT thaliana independently of the nuclease MUS81.";
RL Nucleic Acids Res. 43:3653-3666(2015).
CC -!- FUNCTION: Nuclease required for the repair of DNA interstrand cross-
CC links (ICLs) (PubMed:25779053). Acts as a 5'-3' exonuclease that
CC anchors at a cut end of DNA and cleaves DNA successively at every third
CC nucleotide, allowing to excise an ICL from one strand through flanking
CC incisions (By similarity). May act upstream of the helicase RECQL4A and
CC the ATPase RAD5A, which is involved in error-free post-replicative
CC repair. Functions independently of MUS81 pathway, but in a similar
CC pathway with RECQ4A, RAD5A and MFH1 in ICL repair (PubMed:25779053).
CC {ECO:0000250|UniProtKB:Q9Y2M0, ECO:0000269|PubMed:25779053}.
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:0000250|UniProtKB:Q9Y2M0}.
CC Note=Localizes to stalled replication forks via its UBZ-type zinc
CC finger. {ECO:0000250|UniProtKB:Q9Y2M0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5XVJ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XVJ4-2; Sequence=VSP_039784, VSP_039785;
CC Name=3;
CC IsoId=Q5XVJ4-3; Sequence=VSP_039786;
CC -!- SIMILARITY: Belongs to the FAN1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD49761.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007932; AAD49761.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32278.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32279.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32280.1; -; Genomic_DNA.
DR EMBL; AY735527; AAU44397.1; -; mRNA.
DR EMBL; AY735528; AAU44398.1; -; mRNA.
DR EMBL; DQ653403; ABK28782.1; -; mRNA.
DR PIR; F96523; F96523.
DR RefSeq; NP_001117447.1; NM_001123975.2. [Q5XVJ4-1]
DR RefSeq; NP_001319172.1; NM_001333325.1. [Q5XVJ4-2]
DR RefSeq; NP_175269.2; NM_103732.3. [Q5XVJ4-3]
DR AlphaFoldDB; Q5XVJ4; -.
DR SMR; Q5XVJ4; -.
DR BioGRID; 26481; 1.
DR STRING; 3702.AT1G48360.2; -.
DR PaxDb; Q5XVJ4; -.
DR PRIDE; Q5XVJ4; -.
DR EnsemblPlants; AT1G48360.1; AT1G48360.1; AT1G48360. [Q5XVJ4-3]
DR EnsemblPlants; AT1G48360.2; AT1G48360.2; AT1G48360. [Q5XVJ4-1]
DR EnsemblPlants; AT1G48360.3; AT1G48360.3; AT1G48360. [Q5XVJ4-2]
DR GeneID; 841256; -.
DR Gramene; AT1G48360.1; AT1G48360.1; AT1G48360. [Q5XVJ4-3]
DR Gramene; AT1G48360.2; AT1G48360.2; AT1G48360. [Q5XVJ4-1]
DR Gramene; AT1G48360.3; AT1G48360.3; AT1G48360. [Q5XVJ4-2]
DR KEGG; ath:AT1G48360; -.
DR Araport; AT1G48360; -.
DR TAIR; locus:2007740; AT1G48360.
DR eggNOG; KOG2143; Eukaryota.
DR HOGENOM; CLU_005116_2_0_1; -.
DR InParanoid; Q5XVJ4; -.
DR OrthoDB; 1003565at2759; -.
DR PhylomeDB; Q5XVJ4; -.
DR PRO; PR:Q5XVJ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5XVJ4; baseline and differential.
DR Genevisible; Q5XVJ4; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IGI:TAIR.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:TAIR.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR033315; Fan1-like.
DR InterPro; IPR014905; HIRAN.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR014883; VRR_NUC.
DR PANTHER; PTHR15749; PTHR15749; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF08774; VRR_NUC; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00990; VRR_NUC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA damage; DNA repair; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..891
FT /note="Fanconi-associated nuclease 1 homolog"
FT /id="PRO_0000398623"
FT DOMAIN 770..884
FT /note="VRR-NUC"
FT BINDING 712
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 833
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 833
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 852
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 853
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT VAR_SEQ 504..513
FT /note="AIEVAQLMDE -> LHGLTQRWFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16244158"
FT /id="VSP_039784"
FT VAR_SEQ 514..891
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16244158"
FT /id="VSP_039785"
FT VAR_SEQ 742..891
FT /note="TAPLDLETESFYLTRKETIESQLEKVANGMAEEILIISYETQRGTACRGVAW
FT ERFSLEELRAAVACVGGMCIASLCRHLAQDYRSWCSGMPDLLVWRFKENGYEGEAKLVE
FT VKSEKDRLSEQQRAWLLLLMDSGFNVEICKVRPASLIKT -> VNETQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16244158,
FT ECO:0000303|PubMed:17147637"
FT /id="VSP_039786"
SQ SEQUENCE 891 AA; 101408 MW; 7F57BB6E3D82D8FA CRC64;
MLTGRESLLR LIGKRRRFLP NRHLLLSAHT PNSLNLEFND YGNLVSLAGD DCRLSEDPTS
SDDPSKFSDD LSLSTRKKRR LTQTTLLQSS FLSVPKQLED GLVICTQQKS ILDSETFEFS
LVQRSEPSES ICCKVEDGSC SPSREESLKT VTLDEDNGEA IETFIVGRKF SDVQDLEIGG
DIFLLRHPEN VKDRNAIKVI SGDSEMLGYL PKDISQCLSP LIDDYDLKFE GTITSVPKKS
SEAVLIKVVC HKMRSDGWKE CELYGDFKPL WEKVLQVVEH QMQFPPKTTR YQLNFNVLLQ
EVLRSCSHLF TADEKAFLES FPTLSEDSQR LFIRLYTRKG PWFRLSNISY PEVTDSLQAL
KDLTVRGFMS SVKDANELDN QKMKEITELL NVTELRDILS MNKVFSRTSR KRDLINSLCS
CYNDGTRINL ATVILERTGL CAKVSSTAES LIWRVERLFF LNGEQDLSSF VLLDLGIIKY
PTYKCIDSEQ IFSNRTKLLA YEEAIEVAQL MDESLDNEDP QTVLKCIIIA ETRISSSSLD
SAHAAAFNRF TAPWVNSKVV LLGVSFFENQ KRYNRAVYLL RRLLSCFNCD GRRGYWTVRL
STDLEHMGRP NESLTVAEQG LLDPWVRAGS RVALQRRILR LAKPPRRWKT PTFSNLVDNK
IPEVTIQGRS LNCEVGIKNR FYGEDGEQCG VEQLALQYYS GEGGGWQGIH TESSIWLTIF
GLLMWDILFS DVPGVFQTRF QTAPLDLETE SFYLTRKETI ESQLEKVANG MAEEILIISY
ETQRGTACRG VAWERFSLEE LRAAVACVGG MCIASLCRHL AQDYRSWCSG MPDLLVWRFK
ENGYEGEAKL VEVKSEKDRL SEQQRAWLLL LMDSGFNVEI CKVRPASLIK T
