FAN1_CAEEL
ID FAN1_CAEEL Reviewed; 865 AA.
AC P90740;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Fanconi-associated nuclease 1 homolog {ECO:0000305};
DE EC=3.1.4.1 {ECO:0000250|UniProtKB:Q9Y2M0};
GN Name=fan-1; ORFNames=C01G5.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20603015; DOI=10.1016/j.cell.2010.06.021;
RA MacKay C., Declais A.C., Lundin C., Agostinho A., Deans A.J.,
RA MacArtney T.J., Hofmann K., Gartner A., West S.C., Helleday T.,
RA Lilley D.M., Rouse J.;
RT "Identification of KIAA1018/FAN1, a DNA repair nuclease recruited to DNA
RT damage by monoubiquitinated FANCD2.";
RL Cell 142:65-76(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20603016; DOI=10.1016/j.cell.2010.06.022;
RA Kratz K., Schopf B., Kaden S., Sendoel A., Eberhard R., Lademann C.,
RA Cannavo E., Sartori A.A., Hengartner M.O., Jiricny J.;
RT "Deficiency of FANCD2-associated nuclease KIAA1018/FAN1 sensitizes cells to
RT interstrand crosslinking agents.";
RL Cell 142:77-88(2010).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20603073; DOI=10.1016/j.molcel.2010.06.023;
RA Smogorzewska A., Desetty R., Saito T.T., Schlabach M., Lach F.P.,
RA Sowa M.E., Clark A.B., Kunkel T.A., Harper J.W., Colaiacovo M.P.,
RA Elledge S.J.;
RT "A genetic screen identifies FAN1, a Fanconi anemia-associated nuclease
RT necessary for DNA interstrand crosslink repair.";
RL Mol. Cell 39:36-47(2010).
CC -!- FUNCTION: Nuclease required for the repair of DNA interstrand cross-
CC links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of
CC DNA and cleaves DNA successively at every third nucleotide, allowing to
CC excise an ICL from one strand through flanking incisions.
CC {ECO:0000250|UniProtKB:Q9Y2M0, ECO:0000269|PubMed:20603015,
CC ECO:0000269|PubMed:20603016, ECO:0000269|PubMed:20603073}.
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 -!- INTERACTION:
CC P90740; P55853: smo-1; NbExp=3; IntAct=EBI-313626, EBI-313647;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y2M0}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in normal conditions. Strong
CC increase of embryonic lethality following cisplatin, nitrogen mustard
CC or mitomycin-C (MMC) treatment. {ECO:0000269|PubMed:20603015,
CC ECO:0000269|PubMed:20603016, ECO:0000269|PubMed:20603073}.
CC -!- SIMILARITY: Belongs to the FAN1 family. {ECO:0000305}.
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DR EMBL; FO080264; CCD62449.1; -; Genomic_DNA.
DR PIR; T30998; T30998.
DR RefSeq; NP_500997.1; NM_068596.4.
DR AlphaFoldDB; P90740; -.
DR SMR; P90740; -.
DR BioGRID; 42536; 5.
DR DIP; DIP-24423N; -.
DR IntAct; P90740; 3.
DR STRING; 6239.C01G5.8; -.
DR PaxDb; P90740; -.
DR EnsemblMetazoa; C01G5.8a.1; C01G5.8a.1; WBGene00015310.
DR GeneID; 177415; -.
DR KEGG; cel:CELE_C01G5.8; -.
DR UCSC; C01G5.8; c. elegans.
DR CTD; 177415; -.
DR WormBase; C01G5.8a; CE07800; WBGene00015310; fan-1.
DR eggNOG; KOG2143; Eukaryota.
DR HOGENOM; CLU_311526_0_0_1; -.
DR InParanoid; P90740; -.
DR OMA; LEEHYMW; -.
DR OrthoDB; 1003565at2759; -.
DR PhylomeDB; P90740; -.
DR SignaLink; P90740; -.
DR PRO; PR:P90740; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00015310; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; P90740; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR033315; Fan1-like.
DR InterPro; IPR006642; Rad18_UBZ4.
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.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nuclease; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..865
FT /note="Fanconi-associated nuclease 1 homolog"
FT /id="PRO_0000398622"
FT DOMAIN 744..857
FT /note="VRR-NUC"
FT ZN_FING 35..62
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 90..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 682
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 810
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 810
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 825
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 826
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
SQ SEQUENCE 865 AA; 99406 MW; 3F11059CEB769B50 CRC64;
MKKAKKEKKE KIIKPDGPIN FNRSIMAAFE KQSRGKICPL CETKFSLASY KSHMNTCNVA
DDDEEIEVIA TYTRDEAILM RAGPEIILGD ASFSDKSENP TKRRKTDERE VPSEDDIVPE
VPGPSGIVKN HEMPSESLDV TEISENIEKV IKKSPEWINH RRRSSRLLQN SQKDQADNAN
KEDPVKKETA TISEVLQAIE RFEQRVSGPE QTWPYYIKIT IKIMKRVIST EKFDGTFYAD
DFWLPSDIIT FYRFVELLSE GAKCLLVRLF IRKPAWYNLE KLEQKYPEIP NIKEAVSELA
KGHFIDDDSS MKTLDEALQI SDVVALKNVT KKFKLDGTKN RQELIQSLRK FAQSQQSIFG
GTGNVEKSIL KSLKQELGPC VRVRGGFVDL FKCLFTIYCP VTTNSANVID NPSTTNVYQD
LLYLMLSVAN GTVQFPAPNP CPIIASFYKN RNMLQDYMIS KSLEIAIVSQ MSNGNLDAAL
DLAIDAKEFI EQMSDDDKRY YESLEIHERK FTSIWVFTRC CGHASSILER QKKYGMAVEW
QKDLLITNKD IQSYCIDSRG IWWDRMLLNL DSHLKEKKEC AKMIQIALQD PSILEKELLM
IQDRALKLKE MPADFVTPIN IGNPEKKTIT ANVITKSLGD GRINRFMIRD HETDDDVECS
VEEVTRRHYL ENEGFSTGVH DEGSTWHTLF GLFFYDVIFA TDESVESTWL SELQDCPSDL
SNTLYSKRKE KFEDRFVWLE EAEQELIEEN IRKIWDLKHN ETNRECSWKQ FPMGAEDCVS
FFQCIPRPAL ILILRRLAEN YRNSRSGFPD LTLWNPETKR VAVVEVKGPG DRLSTKQRLW
LAIFADSGIR AEVCHVAAQN SRLLV
