P39748 (FEN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Flap endonuclease 1
Short name=FEN-1
EC=3.1.-.-

Alternative name(s):
DNase IV
Flap structure-specific endonuclease 1
Maturation factor 1
Short name=MF1
Short name=hFEN-1

Gene names

Name:	FEN1
Synonyms:	RAD2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA. Ref.6 Ref.7 Ref.9 Ref.11 Ref.13 Ref.15
Cofactor	Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Subunit structure	Interacts with PCNA. Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity. The C-terminal domain binds EP300. Can bind simultaneously to both PCNA and EP300. Interacts with DDX11. Ref.8 Ref.10 Ref.12
Subcellular location	Nucleus › nucleolus. Nucleus › nucleoplasm. Mitochondrion By similarity. Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. Ref.6 Ref.13
Post-translational modification	Acetylated by EP300. Acetylation inhibits both endonuclease and exonuclease activity. Acetylation also reduces DNA-binding activity but does not affect interaction with PCNA or EP300. HAMAP-Rule MF_03140 Phosphorylation upon DNA damage induces relocalization to the nuclear plasma. Phosphorylation at Ser-187 by CDK2 occurs during late S-phase and results in dissociation from PCNA. HAMAP-Rule MF_03140 Methylation at Arg-192 by PRMT5 impedes Ser-187 phosphorylation and increases interaction with PCNA. Ref.15
Sequence similarities	Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication
Cellular component	Mitochondrion Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Endonuclease Exonuclease Hydrolase Nuclease
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication, removal of RNA primer Inferred from direct assay PubMed 18995831. Source: UniProtKB S phase of mitotic cell cycle Traceable author statement. Source: Reactome UV protection Traceable author statement Ref.1. Source: ProtInc base-excision repair Traceable author statement. Source: Reactome double-strand break repair Traceable author statement PubMed 8131753. Source: ProtInc memory Inferred from electronic annotation. Source: Compara phosphatidylinositol-mediated signaling Non-traceable author statement PubMed 15504738. Source: UniProtKB telomere maintenance via recombination Traceable author statement. Source: Reactome telomere maintenance via semi-conservative replication Traceable author statement. Source: Reactome
Cellular_component	mitochondrion Inferred from direct assay PubMed 18995831. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	5'-3' exonuclease activity Inferred from direct assay Ref.6. Source: UniProtKB 5'-flap endonuclease activity Inferred from direct assay PubMed 18995831. Source: UniProtKB damaged DNA binding Traceable author statement Ref.1. Source: ProtInc double-stranded DNA binding Traceable author statement PubMed 8131753. Source: ProtInc double-stranded DNA specific exodeoxyribonuclease activity Traceable author statement PubMed 8131753. Source: ProtInc magnesium ion binding Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: Compara ribonuclease H activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BLM	P54132	4	EBI-707816,EBI-621372
PCNA	P12004	4	EBI-707816,EBI-358311
WRN	Q14191	10	EBI-707816,EBI-368417

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 380

380

Flap endonuclease 1 HAMAP-Rule MF_03140

PRO_0000154069

Regions

Region

1 – 104

104

N-domain HAMAP-Rule MF_03140

Region

122 – 253

132

I-domain HAMAP-Rule MF_03140

Region

336 – 344

9

Interaction with PCNA HAMAP-Rule MF_03140

Sites

Metal binding

34

1

Magnesium 1

Metal binding

86

1

Magnesium 1

Metal binding

158

1

Magnesium 1

Metal binding

160

1

Magnesium 1

Metal binding

179

1

Magnesium 2

Metal binding

181

1

Magnesium 2

Metal binding

233

1

Magnesium 2

Binding site

47

1

DNA substrate

Binding site

70

1

DNA substrate

Binding site

158

1

DNA substrate

Binding site

231

1

DNA substrate

Binding site

233

1

DNA substrate

Amino acid modifications

Modified residue

19

1

Symmetric dimethylarginine; by PRMT5 HAMAP-Rule MF_03140

Modified residue

80

1

N6-acetyllysine Ref.14

Modified residue

100

1

Symmetric dimethylarginine; by PRMT5 HAMAP-Rule MF_03140

Modified residue

104

1

Symmetric dimethylarginine; by PRMT5 HAMAP-Rule MF_03140

Modified residue

187

1

Phosphoserine; by CDK2 Ref.15

Modified residue

192

1

Symmetric dimethylarginine; by PRMT5 Ref.15

Modified residue

197

1

Phosphoserine Ref.16

Modified residue

354

1

N6-acetyllysine Ref.10

Modified residue

364

1

Phosphothreonine Ref.16

Modified residue

375

1

N6-acetyllysine Ref.10 Ref.14

Modified residue

377

1

N6-acetyllysine Ref.10

Modified residue

380

1

N6-acetyllysine Ref.10

Experimental info

Mutagenesis

29

1

R → A: No significant effect on exonuclease activity or flap endonuclease activity. Ref.11

Mutagenesis

34

1

D → A: Loss of flap endonuclease activity but substrate binding activity is retained. Ref.7

Mutagenesis

47

1

R → A: Significantly reduced exonuclease activity and reduced substrate binding. The positions of the cleavage sites are also shifted. Ref.11

Mutagenesis

70

1

R → A: Loss of exonuclease activity and reduced endonuclease activity. Reduced substrate binding. Ref.11

Mutagenesis

73

1

R → A: No significant effect on exonuclease activity or flap endonuclease activity. Ref.11

Mutagenesis

80

1

K → A: No significant effect on exonuclease activity or flap endonuclease activity. Ref.11

Mutagenesis

86

1

D → A: Loss of flap endonuclease activity but substrate binding activity is retained. Ref.7

Mutagenesis

103

1

R → A: No effect on flap endonuclease activity or substrate binding. Ref.7

Mutagenesis

158

1

E → A: Loss of flap endonuclease activity and substrate binding. Ref.7

Mutagenesis

179

1

D → A: No effect on flap endonuclease activity or substrate binding. Ref.7

Mutagenesis

181

1

D → A: Loss of flap endonuclease activity but substrate binding activity is retained. Ref.7

Mutagenesis

187

1

S → A: Fails to translocate from nucleoli to the nuclear plasma. Ref.13

Mutagenesis

187

1

S → D: Diminishes nucleolar localization. Ref.13

Mutagenesis

192

1

R → K: Impairs ability to localize to sites of DNA replication or repair. Ref.15

Mutagenesis

231

1

G → A: Loss of flap endonuclease activity and substrate binding. Ref.7

Mutagenesis

233

1

D → A: Loss of flap endonuclease activity and substrate binding. Ref.7

Secondary structure

1

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380

Helix Strand Turn

Details...

Helix

6 – 13

8

Helix

15 – 17

3

Beta strand

18 – 22

5

Helix

23 – 26

4

Beta strand

30 – 34

5

Helix

35 – 45

11

Beta strand

47 – 52

6

Helix

62 – 75

14

Turn

76 – 78

3

Beta strand

80 – 85

6

Helix

91 – 93

3

Helix

94 – 115

22

Helix

120 – 129

10

Helix

135 – 148

14

Beta strand

152 – 154

3

Helix

159 – 168

10

Beta strand

171 – 176

6

Helix

181 – 184

4

Beta strand

188 – 193

6

Beta strand

203 – 208

6

Helix

209 – 216

8

Helix

220 – 230

11

Beta strand

233 – 235

3

Helix

243 – 253

11

Helix

256 – 262

7

Turn

265 – 267

3

Helix

276 – 284

9

Turn

291 – 293

3

Helix

303 – 310

8

Turn

311 – 314

4

Helix

318 – 335

18

Helix

340 – 342

3

Beta strand

344 – 351

8

Sequences

	Sequence		Length	Mass (Da)
	P39748 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 5154F2F6E57592C5	FASTA	380	42,593
	10 20 30 40 50 60 MGIQGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG DVLQNEEGET 70 80 90 100 110 120 TSHLMGMFYR TIRMMENGIK PVYVFDGKPP QLKSGELAKR SERRAEAEKQ LQQAQAAGAE 130 140 150 160 170 180 QEVEKFTKRL VKVTKQHNDE CKHLLSLMGI PYLDAPSEAE ASCAALVKAG KVYAAATEDM 190 200 210 220 230 240 DCLTFGSPVL MRHLTASEAK KLPIQEFHLS RILQELGLNQ EQFVDLCILL GSDYCESIRG 250 260 270 280 290 300 IGPKRAVDLI QKHKSIEEIV RRLDPNKYPV PENWLHKEAH QLFLEPEVLD PESVELKWSE 310 320 330 340 350 360 PNEEELIKFM CGEKQFSEER IRSGVKRLSK SRQGSTQGRL DDFFKVTGSL SSAKRKEPEP 370 380 KGSTKKKAKT GAAGKFKRGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural and functional conservation of the human homolog of the Schizosaccharomyces pombe rad2 gene, which is required for chromosome segregation and recovery from DNA damage." Murray J.M., Tavassoli M., Al-Harithy R., Sheldrick K.S., Lehmann A.R., Carr A.M., Watts F.Z. Mol. Cell. Biol. 14:4878-4888(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence of human FEN-1, a structure-specific endonuclease, and chromosomal localization of the gene (FEN1) in mouse and human." Hiraoka L.R., Harrington J.J., Gerhard D.S., Lieber M.R., Hsieh C.-L. Genomics 25:220-225(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leukemic T-cell.
[3]	NIEHS SNPs program Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[6]	"Structural and functional homology between mammalian DNase IV and the 5'-nuclease domain of Escherichia coli DNA polymerase I." Robins P., Pappin D.J.C., Wood R.D., Lindahl T. J. Biol. Chem. 269:28535-28538(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
[7]	"Essential amino acids for substrate binding and catalysis of human flap endonuclease 1." Shen B., Nolan J.P., Sklar L.A., Park M.S. J. Biol. Chem. 271:9173-9176(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE-BINDING SITES, MUTAGENESIS OF ASP-34; ASP-86; ARG-103; GLU-158; ASP-179; ASP-181; GLY-231 AND ASP-233.
[8]	"The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21." Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., Park M.S. J. Biol. Chem. 272:24522-24529(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PCNA.
[9]	"Mechanism whereby proliferating cell nuclear antigen stimulates flap endonuclease 1." Tom S., Henricksen L.A., Bambara R.A. J. Biol. Chem. 275:10498-10505(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300." Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P., Hubscher U., Hottiger M.O. Mol. Cell 7:1221-1231(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH P300, ACETYLATION AT LYS-354; LYS-375; LYS-377 AND LYS-380.
[11]	"Arginine residues 47 and 70 of human flap endonuclease-1 are involved in DNA substrate interactions and cleavage site determination." Qiu J., Bimston D.N., Partikian A., Shen B. J. Biol. Chem. 277:24659-24666(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBSTRATE-BINDING SITES ARG-47 AND ARG-70, MUTAGENESIS OF ARG-29; ARG-47; ARG-70; ARG-73 AND LYS-80.
[12]	"Studies with the human cohesin establishment factor, ChlR1. Association of ChlR1 with Ctf18-RFC and Fen1." Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S., Hurwitz J. J. Biol. Chem. 283:20925-20936(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDX11.
[13]	"Nucleolar localization and dynamic roles of flap endonuclease 1 in ribosomal DNA replication and damage repair." Guo Z., Qian L., Liu R., Dai H., Zhou M., Zheng L., Shen B. Mol. Cell. Biol. 28:4310-4319(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-187.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80 AND LYS-375, MASS SPECTROMETRY.
[15]	"Methylation of FEN1 suppresses nearby phosphorylation and facilitates PCNA binding." Guo Z., Zheng L., Xu H., Dai H., Zhou M., Pascua M.R., Chen Q.M., Shen B. Nat. Chem. Biol. 6:766-773(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-192, METHYLATION AT ARG-192, PHOSPHORYLATION AT SER-187.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND THR-364, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"Structural and thermodynamic analysis of human PCNA with peptides derived from DNA polymerase-delta p66 subunit and flap endonuclease-1." Bruning J.B., Shamoo Y. Structure 12:2209-2219(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 331-350.
[19]	"Structural basis for recruitment of human flap endonuclease 1 to PCNA." Sakurai S., Kitano K., Yamaguchi H., Hamada K., Okada K., Fukuda K., Uchida M., Ohtsuka E., Morioka H., Hakoshima T. EMBO J. 24:683-693(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 2-380 IN COMPLEX WITH PCNA.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X76771 mRNA. Translation: CAA54166.1.
L37374 mRNA. Translation: AAA91331.1.
AF523117 Genomic DNA. Translation: AAM74238.1.
AC004770 Genomic DNA. Translation: AAC23394.1.
BC000323 mRNA. Translation: AAH00323.1.

IPI

IPI00026215.

PIR

A56531.

RefSeq

NP_004102.1. NM_004111.5.

UniGene

Hs.409065.
Hs.741166.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U7B	X-ray	1.88	B	331-350	[»]
1UL1	X-ray	2.90	X/Y/Z	2-380	[»]
3Q8K	X-ray	2.20	A	2-336	[»]
3Q8L	X-ray	2.32	A	2-336	[»]
3Q8M	X-ray	2.60	A/B	2-336	[»]
3UVU	X-ray	2.38	B	352-370	[»]

ProteinModelPortal

P39748.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24216N.

IntAct

P39748. 6 interactions.

MINT

MINT-5004212.

STRING

9606.ENSP00000305480.

PTM databases

PhosphoSite

P39748.

Polymorphism databases

DMDM

729475.

Proteomic databases

PaxDb

P39748.

PeptideAtlas

P39748.

PRIDE

P39748.

Protocols and materials databases

DNASU

2237.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000305885; ENSP00000305480; ENSG00000168496.

GeneID

2237.

KEGG

hsa:2237.

UCSC

uc001nsg.3. human.

Organism-specific databases

CTD

2237.

GeneCards

GC11P061560.

HGNC

HGNC:3650. FEN1.

HPA

CAB002262.
HPA006748.

MIM

600393. gene.

neXtProt

NX_P39748.

PharmGKB

PA28090.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0258.

HOGENOM

HOG000193853.

HOVERGEN

HBG000844.

InParanoid

P39748.

KO

K04799.

OMA

DYDSLLF.

OrthoDB

EOG415GDQ.

PhylomeDB

P39748.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

P39748.

Bgee

P39748.

CleanEx

HS_FEN1.

Genevestigator

P39748.

GermOnline

ENSG00000168496. Homo sapiens.

Family and domain databases

HAMAP

MF_00614. Fen.

InterPro

IPR020045. 5-3_exonuclease_C.
IPR023426. Flap_endonuc.
IPR008918. HhH2.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]

PANTHER

PTHR11081. PTHR11081. 1 hit.

Pfam

PF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]

PRINTS

PR00853. XPGRADSUPER.

SMART

SM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]

SUPFAM

SSF47807. 5_3_exo_C. 1 hit.

PROSITE

PS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P39748.

ChEMBL

CHEMBL5027.

ChiTaRS

FEN1. human.

EvolutionaryTrace

P39748.

GenomeRNAi

2237.

NextBio

9055.

SOURCE

Search...

Entry information

Entry name

FEN1_HUMAN

Accession

Primary (citable) accession number: P39748

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.