Q10002 (APN1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-(apurinic or apyrimidinic site) lyase
EC=4.2.99.18

Alternative name(s):
Apurinic-apyrimidinic endonuclease
Short name=AP endonuclease

Gene names

Name:	apn-1
ORF Names:	T05H10.2

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Cofactor	Binds 3 zinc ions By similarity.
Subcellular location	Nucleus Potential.
Sequence similarities	Belongs to the AP endonuclease 2 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair Inferred from direct assay PubMed 15907773. Source: WormBase
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-(apurinic or apyrimidinic site) lyase activity Inferred from direct assay PubMed 15907773. Source: WormBase endonuclease activity Inferred from electronic annotation. Source: InterPro phosphoric diester hydrolase activity Inferred from direct assay PubMed 15907773. Source: WormBase zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 396	396	DNA-(apurinic or apyrimidinic site) lyase		PRO_0000190899
Sites
	Metal binding	185	1	Zinc 1 By similarity
	Metal binding	225	1	Zinc 1 By similarity
	Metal binding	261	1	Zinc 1 By similarity
	Metal binding	261	1	Zinc 2 By similarity
	Metal binding	295	1	Zinc 2 By similarity
	Metal binding	298	1	Zinc 3 By similarity
	Metal binding	332	1	Zinc 2 By similarity
	Metal binding	345	1	Zinc 3 By similarity
	Metal binding	347	1	Zinc 3 By similarity
	Metal binding	377	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q10002 [UniParc]. Last modified December 19, 2001. Version 2. Checksum: 0C1D1B26AB35BA15	FASTA	396	44,747
	10 20 30 40 50 60 MANKKVTFRE DVKSPAIRKL KQKLTPLKIK KGRGKIQKHI QKTLQKMKEE EESENQSPGT 70 80 90 100 110 120 TVEETLTEEN ISTDKEETSK LENKPKKTRK TSGETIAQKK SRETVGVEVL KTSEGSSKML 130 140 150 160 170 180 GFHVSAAGGL EQAIYNARAE GCRSFAMFVR NQRTWNHKPM SEEVVENWWK AVRETNFPLD 190 200 210 220 230 240 QIVPHGSYLM NAGSPEAEKL EKSRLAMLDE CQRAEKLGIT MYNFHPGSTV GKCEKEECMT 250 260 270 280 290 300 TIAETIDFVV EKTENIILVL ETMAGQGNSI GGTFEELKFI IDKVKVKSRV GVCIDTCHIF 310 320 330 340 350 360 AGGYDIRTQK AYEEVMKNFG EVVGWNYLKA IHINDSKGDV GSKLDRHEHI GQGKIGKAAF 370 380 390 ELLMNDNRLD GIPMILETPE GKYPEEMMIM YNMDKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	"The Caenorhabditis elegans gene CeAPN1 encodes a homolog of Escherichia coli and yeast apurinic/apyrimidinic endonuclease." Masson J.Y., Tremblay S., Ramotar D. Gene 179:291-293(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 104-396.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z47812 Genomic DNA. Translation: CAA87789.2. U40707 mRNA. Translation: AAB39924.1.
PIR	JC5235.
RefSeq	NP_495687.1. NM_063286.5.
3D structure databases
ProteinModelPortal	Q10002.
SMR	Q10002. Positions 118-378.
ModBase	Search...
Protein-protein interaction databases
STRING	6239.T05H10.2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	T05H10.2.1; T05H10.2.1; T05H10.2. T05H10.2.2; T05H10.2.2; T05H10.2.
GeneID	174291.
KEGG	cel:CELE_T05H10.2.
UCSC	T05H10.2. c. elegans.
Organism-specific databases
CTD	174291.
WormBase	T05H10.2; CE28953; WBGene00000151; apn-1.
Phylogenomic databases
eggNOG	COG0648.
GeneTree	ENSGT00390000013698.
HOGENOM	HOG000224893.
InParanoid	Q10002.
KO	K10771.
OMA	LLGAHEG.
Family and domain databases
Gene3D	3.20.20.150. 1 hit.
InterPro	IPR018246. AP_endonuc_F2_Zn_BS. IPR001719. Endodeoxyribonuclease_IV. IPR013022. Xyl_isomerase-like_TIM-brl. [Graphical view]
PANTHER	PTHR21445. PTHR21445. 1 hit.
Pfam	PF01261. AP_endonuc_2. 1 hit. [Graphical view]
SMART	SM00518. AP2Ec. 1 hit. [Graphical view]
SUPFAM	SSF51658. Xyl_isomerase-like_TIM-brl. 1 hit.
TIGRFAMs	TIGR00587. nfo. 1 hit.
PROSITE	PS00729. AP_NUCLEASE_F2_1. 1 hit. PS00730. AP_NUCLEASE_F2_2. 1 hit. PS00731. AP_NUCLEASE_F2_3. 1 hit. PS51432. AP_NUCLEASE_F2_4. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	883392.

Entry information

Entry name

APN1_CAEEL

Accession

Primary (citable) accession number: Q10002

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	December 19, 2001
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project