END4_DICDI
ID END4_DICDI Reviewed; 542 AA.
AC Q966U0; Q54W14;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Endonuclease 4 homolog;
DE EC=3.1.21.2;
DE AltName: Full=Apurinic/apyrimidinic endonuclease;
DE Short=AP endonuclease;
DE AltName: Full=DdAPN;
DE AltName: Full=Endodeoxyribonuclease IV homolog;
DE AltName: Full=Endonuclease IV homolog;
GN Name=apnA; ORFNames=DDB_G0279923;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS AN ENDONUCLEASE, AND DOMAIN.
RX PubMed=11356336; DOI=10.1016/s0921-8777(01)00074-x;
RA Tsuji A., Kodaira K., Inoue M., Yasukawa H.;
RT "Endonuclease IV homolog from Dictyostelium discoideum: sequencing and
RT functional expression in AP endonuclease-deficient Escherichia coli.";
RL Mutat. Res. 486:53-57(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Plays a role in DNA repair. It cleaves phosphodiester bonds
CC at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends
CC that are base-free deoxyribose 5-phosphate residues.
CC {ECO:0000269|PubMed:11356336}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-
CC products.; EC=3.1.21.2;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 3 Zn(2+) ions. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: The C-terminal part is sufficient to function as an AP
CC endonuclease. {ECO:0000269|PubMed:11356336}.
CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family. {ECO:0000305}.
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DR EMBL; AB055424; BAB59036.1; -; mRNA.
DR EMBL; AAFI02000035; EAL67433.1; -; Genomic_DNA.
DR RefSeq; XP_641436.1; XM_636344.1.
DR AlphaFoldDB; Q966U0; -.
DR SMR; Q966U0; -.
DR STRING; 44689.DDB0206584; -.
DR PaxDb; Q966U0; -.
DR EnsemblProtists; EAL67433; EAL67433; DDB_G0279923.
DR GeneID; 8622321; -.
DR KEGG; ddi:DDB_G0279923; -.
DR dictyBase; DDB_G0279923; apnA.
DR eggNOG; KOG3997; Eukaryota.
DR HOGENOM; CLU_502926_0_0_1; -.
DR InParanoid; Q966U0; -.
DR OMA; DTFKYIM; -.
DR PhylomeDB; Q966U0; -.
DR PRO; PR:Q966U0; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR CDD; cd00019; AP2Ec; 1.
DR HAMAP; MF_00152; Nfo; 1.
DR InterPro; IPR001719; AP_endonuc_2.
DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR PANTHER; PTHR21445; PTHR21445; 1.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SMART; SM00518; AP2Ec; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR00587; nfo; 1.
DR PROSITE; PS00729; AP_NUCLEASE_F2_1; 1.
DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 1.
DR PROSITE; PS00731; AP_NUCLEASE_F2_3; 1.
DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA damage; DNA repair; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..542
FT /note="Endonuclease 4 homolog"
FT /id="PRO_0000328566"
FT REGION 89..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 171..206
FT /evidence="ECO:0000255"
FT MOTIF 222..227
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 98..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 542 AA; 61952 MW; 28CFAFBA699CEBE3 CRC64;
MNPFVNLFIQ HSKKQIFLNN NKNNILLNFN SKLYSTITYK NNNNNNNNQI INNKTIMKRK
NNEIIQTEED DDNDNGGIHD CDSCDEVDNE EIIPESPPSK KLQQQQQQQQ QQQSKLKPKQ
TSITDFFSPT VKTSKADKIS PFFSNVNNAS TTNTTTNNKN VNKKTTTTTT TKKRNNKDEE
NEDDNEEEEE EEEEEEDKKS KKKTTTTTTT TTTTAYKKKS SPKKKKVNPT ENKFSTINYK
DDQYVQKEEY SSSKKEKLEN VKIGGHVSIK NGYPTLIQSV VAQGFKAVAF FTNPPRTWKH
HTVKLDDSIK FKQSCKSLNF DVNCILPHGS YFLNLGSPNK ENLQKSRDLM IHEMKNCEIL
GVKHFNFHPG SHLNEISESE SIKIVAESLD YILERTKDVV AVIECTAGQG TNLGYTFEHL
RDMIALVKDK TRVGVCLDTC HMFAAGYNIS TKSNCDVIFQ EFDKVVGFKY LKGVHLNDSK
STCGSKLDRH ENIGKGHIGT PCFKYLVNDK RFQNIPMILE TVGPYDQEVK LLYSFIEDDD
KK
