P36551 (HEM6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coproporphyrinogen-III oxidase, mitochondrial
Short name=COX
Short name=Coprogen oxidase
Short name=Coproporphyrinogenase
EC=1.3.3.3

Gene names

Name:	CPOX
Synonyms:	CPO, CPX

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	454 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III.
Catalytic activity	Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.
Subunit structure	Homodimer. Ref.10
Subcellular location	Mitochondrion intermembrane space.
Involvement in disease	Hereditary coproporphyria (HCP) [MIM:121300]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. Hereditary coproporphyria is an acute hepatic porphyria characterized by skin photosensitivity, attacks of abdominal pain, neurological disturbances, and psychiatric symptoms. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors. Hereditary coproporphyria is biochemically characterized by overexcretion of coproporphyrin III in the urine and in the feces. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20
Sequence similarities	Belongs to the aerobic coproporphyrinogen-III oxidase family.
Sequence caution	The sequence BAA04033.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	heme biosynthetic process Traceable author statement. Source: Reactome protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway response to arsenic-containing substance Inferred from electronic annotation. Source: Compara response to insecticide Inferred from electronic annotation. Source: Compara response to iron ion Inferred from electronic annotation. Source: Compara response to lead ion Inferred from electronic annotation. Source: Compara response to methylmercury Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: Compara mitochondrial intermembrane space Traceable author statement. Source: Reactome
Molecular_function	coproporphyrinogen oxidase activity Traceable author statement. Source: Reactome protein homodimerization activity Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 110

110

Mitochondrion By similarity

Chain

111 – 454

344

Coproporphyrinogen-III oxidase, mitochondrial

PRO_0000006029

Regions

Region

193 – 202

10

Important for dimerization

Region

260 – 262

3

Substrate binding

Region

392 – 428

37

Important for dimerization

Region

411 – 416

6

Substrate binding

Sites

Active site

258

1

Proton donor

Binding site

244

1

Substrate

Site

327

1

Important for dimerization

Amino acid modifications

Modified residue

371

1

N6-acetyllysine By similarity

Natural variations

Natural variant

135

1

V → A in HCP. Ref.19

VAR_023444

Natural variant

162 – 168

7

Missing in HCP.

VAR_002151

Natural variant

189

1

G → S in HCP; <5% of activity. Ref.12

VAR_002152

Natural variant

197

1

G → W in HCP. Ref.17

VAR_002153

Natural variant

201

1

E → K in HCP. Ref.16

VAR_002154

Natural variant

208

1

S → F in HCP. Ref.18
Corresponds to variant rs28929486 [ dbSNP | Ensembl ].

VAR_019067

Natural variant

214

1

L → R in HCP. Ref.19

VAR_023445

Natural variant

249

1

P → R in HCP. Ref.19

VAR_023446

Natural variant

249

1

P → S in HCP. Ref.16

VAR_002155

Natural variant

272

1

N → H. Ref.7 Ref.12
Corresponds to variant rs1131857 [ dbSNP | Ensembl ].

VAR_002156

Natural variant

279

1

G → R in HCP; a patient carrying also the L-12 mutation in ALAD. Ref.20

VAR_058005

Natural variant

280

1

G → R in HCP. Ref.14

VAR_002157

Natural variant

294

1

V → I. Ref.3 Ref.5 Ref.12
Corresponds to variant rs2228056 [ dbSNP | Ensembl ].

VAR_002158

Natural variant

295

1

H → D in HCP. Ref.15

VAR_002159

Natural variant

328

1

R → C in HCP. Ref.18
Corresponds to variant rs28929487 [ dbSNP | Ensembl ].

VAR_019068

Natural variant

331

1

R → W in HCP. Ref.11 Ref.18

VAR_002160

Natural variant

352

1

R → C.
Corresponds to variant rs11921054 [ dbSNP | Ensembl ].

VAR_048827

Natural variant

390

1

Missing in HCP. Ref.17

VAR_002161

Natural variant

404

1

K → E in HCP; harderoporphyria form. Ref.13

VAR_002162

Natural variant

427

1

W → R in HCP. Ref.17

VAR_002163

Natural variant

447

1

R → C in HCP. Ref.18
Corresponds to variant rs28931603 [ dbSNP | Ensembl ].

VAR_019069

Experimental info

Mutagenesis

392 – 418

27

Missing: Loss for dimerization. Ref.10

Sequence conflict

247

1

I → T in CAA82250. Ref.7

Secondary structure

1

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454

Helix Strand Turn

Details...

Helix

122 – 128

7

Beta strand

130 – 132

3

Helix

138 – 143

6

Helix

148 – 170

23

Beta strand

177 – 183

7

Turn

184 – 186

3

Beta strand

187 – 196

10

Beta strand

198 – 213

16

Helix

216 – 224

9

Beta strand

237 – 251

15

Beta strand

256 – 267

12

Beta strand

273 – 284

12

Helix

290 – 305

16

Helix

311 – 322

12

Helix

326 – 328

3

Beta strand

330 – 342

13

Helix

347 – 359

13

Helix

361 – 372

12

Helix

379 – 399

21

Helix

406 – 408

3

Beta strand

409 – 411

3

Helix

414 – 420

7

Helix

438 – 447

10

Sequences

	Sequence		Length	Mass (Da)
	P36551 [UniParc]. Last modified June 7, 2005. Version 3. Checksum: 6EC3D15FD8FD86B5	FASTA	454	50,152
	10 20 30 40 50 60 MALQLGRLSS GPCWLVARGG CGGPRAWSQC GGGGLRAWSQ RSAAGRVCRP PGPAGTEQSR 70 80 90 100 110 120 GLGHGSTSRG GPWVGTGLAA ALAGLVGLAT AAFGHVQRAE MLPKTSGTRA TSLGRPEEEE 130 140 150 160 170 180 DELAHRCSSF MAPPVTDLGE LRRRPGDMKT KMELLILETQ AQVCQALAQV DGGANFSVDR 190 200 210 220 230 240 WERKEGGGGI SCVLQDGCVF EKAGVSISVV HGNLSEEAAK QMRSRGKVLK TKDGKLPFCA 250 260 270 280 290 300 MGVSSVIHPK NPHAPTIHFN YRYFEVEEAD GNKQWWFGGG CDLTPTYLNQ EDAVHFHRTL 310 320 330 340 350 360 KEACDQHGPD LYPKFKKWCD DYFFIAHRGE RRGIGGIFFD DLDSPSKEEV FRFVQSCARA 370 380 390 400 410 420 VVPSYIPLVK KHCDDSFTPQ EKLWQQLRRG RYVEFNLLYD RGTKFGLFTP GSRIESILMS 430 440 450 LPLTARWEYM HSPSENSKEA EILEVLRHPR DWVR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Coproporphyrinogen oxidase: gene organization and description of a mutation leading to exon 6 skipping." Delfau-Larue M.H., Martasek P., Grandchamp B. Hum. Mol. Genet. 3:1325-1330(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thalamus.
[3]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-294.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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], VARIANT ILE-294. Tissue: Brain, Placenta and Uterus.
[6]	"Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase." Taketani S., Kohno H., Furukawa T., Yoshinaga T., Tokunaga R. Biochim. Biophys. Acta 1183:547-549(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 73-454. Tissue: Placenta.
[7]	"Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase." Martasek P., Camadro J.-M., Delfau-Larue M.H., Dumas J.B., Montagne J.J., de Verneuil H., Labbe P., Grandchamp B. Proc. Natl. Acad. Sci. U.S.A. 91:3024-3028(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-454, VARIANT HIS-272. Tissue: Foreskin.
[8]	"The long, but not the short, presequence of human coproporphyrinogen oxidase is essential for its import and sorting to mitochondria." Susa S., Daimon M., Ono H., Li S., Yoshida T., Kato T. Tohoku J. Exp. Med. 200:39-45(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[9]	"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].
[10]	"Structural basis of hereditary coproporphyria." Lee D.-S., Flachsova E., Bodnarova M., Demeler B., Martasek P., Raman C.S. Proc. Natl. Acad. Sci. U.S.A. 102:14232-14237(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 111-453 IN COMPLEX WITH CITRATE, MUTAGENESIS OF 392-TYR--LEU-418, SUBUNIT.
[11]	"Homozygous hereditary coproporphyria caused by an arginine to tryptophane substitution in coproporphyrinogen oxidase and common intragenic polymorphisms." Martasek P., Nordmann Y., Grandchamp B. Hum. Mol. Genet. 3:477-480(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HCP TRP-331.
[12]	"Characterization and expression of cDNA encoding coproporphyrinogen oxidase from a patient with hereditary coproporphyria." Fujita H., Kondo M., Taketani S., Nomura N., Furuyama K., Akagi R., Nagai T., Terajima M., Galbraith R.A., Sassa S. Hum. Mol. Genet. 3:1807-1810(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HCP SER-189, VARIANTS HIS-272 AND ILE-294.
[13]	"A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria." Lamoril J., Martasek P., Deybach J.-C., da Silva V., Grandchamp B., Nordmann Y. Hum. Mol. Genet. 4:275-278(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HCP GLU-404.
[14]	"A novel missense mutation in exon 4 of the human coproporphyrinogen oxidase gene in two patients with hereditary coproporphyria." Daimon M., Gojyou E., Sugawara M., Yamatani K., Tominaga M., Sasaki H. Hum. Genet. 99:199-201(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HCP ARG-280.
[15]	"Three novel mutations in the coproporphyrinogen oxidase gene." Lamoril J., Deybach J.-C., Puy H., Grandchamp B., Nordmann Y. Hum. Mutat. 9:78-80(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HCP 162-GLN--ALA-168 DEL AND ASP-295.
[16]	"Hereditary coproporphyria: exon screening by heteroduplex analysis detects three novel mutations in the coproporphyrinogen oxidase gene." Schreiber W.E., Zhang X., Senz J., Jamani A. Hum. Mutat. 10:196-200(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HCP LYS-201 AND SER-249.
[17]	"Systematic analysis of coproporphyrinogen oxidase gene defects in hereditary coproporphyria and mutation update." Rosipal R., Lamoril J., Puy H., da Silva V., Gouya L., de Rooij F.W.M., Te Velde K., Nordmann Y., Martasek P., Deybach J.-C. Hum. Mutat. 13:44-53(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HCP TRP-197; GLY-390 DEL AND ARG-427.
[18]	"Two novel mutations and coexistence of the 991C>T and the 1339C>T mutation on a single allele in the coproporphyrinogen oxidase gene in Swedish patients with hereditary coproporphyria." Wiman A., Floderus Y., Harper P. J. Hum. Genet. 47:407-412(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HCP PHE-208; CYS-328; TRP-331 AND CYS-447.
[19]	"Biochemical and genetic characterization of four cases of hereditary coproporphyria in Spain." To-Figueras J., Badenas C., Enriquez M.T., Segura S., Alvarez C., Mila M., Lecha M., Herrero C. Mol. Genet. Metab. 85:160-163(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HCP ALA-135; ARG-214 AND ARG-249.
[20]	"Dual gene defects involving delta-aminolaevulinate dehydratase and coproporphyrinogen oxidase in a porphyria patient." Akagi R., Inoue R., Muranaka S., Tahara T., Taketani S., Anderson K.E., Phillips J.D., Sassa S. Br. J. Haematol. 132:237-243(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HCP ARG-279.
[21]	Erratum Akagi R., Inoue R., Muranaka S., Tahara T., Taketani S., Anderson K.E., Phillips J.D., Sassa S. Br. J. Haematol. 132:662-662(2006)
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z34531 , Z34803, Z34804, Z34805, Z34806, Z34807, Z34808 Genomic DNA. Translation: CAA84292.1.
AK290140 mRNA. Translation: BAF82829.1.
AK223481 mRNA. Translation: BAD97201.1.
CH471052 Genomic DNA. Translation: EAW79854.1.
BC017210 mRNA. Translation: AAH17210.1.
BC023551 mRNA. Translation: AAH23551.1.
BC023554 mRNA. Translation: AAH23554.1.
D16611 mRNA. Translation: BAA04033.1. Different initiation.
Z28409 mRNA. Translation: CAA82250.1.

IPI

IPI00093057.

PIR

I52444.

RefSeq

NP_000088.3. NM_000097.5.

UniGene

Hs.476982.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AEX	X-ray	1.58	A	111-453	[»]

ProteinModelPortal

P36551.

ModBase

Search...

Protein-protein interaction databases

IntAct

P36551. 1 interaction.

STRING

9606.ENSP00000264193.

PTM databases

PhosphoSite

P36551.

Polymorphism databases

DMDM

67476671.

Proteomic databases

PaxDb

P36551.

PeptideAtlas

P36551.

PRIDE

P36551.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264193; ENSP00000264193; ENSG00000080819.

GeneID

1371.

KEGG

hsa:1371.

UCSC

uc003dsx.3. human.

Organism-specific databases

CTD

1371.

GeneCards

GC03M098239.

HGNC

HGNC:2321. CPOX.

HPA

HPA015736.

MIM

121300. phenotype.
612732. gene.

neXtProt

NX_P36551.

Orphanet

79273. Hereditary coproporphyria.

PharmGKB

PA134979958.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0408.

HOGENOM

HOG000262768.

HOVERGEN

HBG051897.

InParanoid

P36551.

KO

K00228.

OMA

WFATGTS.

PhylomeDB

P36551.

Enzyme and pathway databases

BRENDA

1.3.3.3. 2681.

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00251; UER00322.

Gene expression databases

ArrayExpress

P36551.

Bgee

P36551.

CleanEx

HS_CPO.
HS_CPOX.

Genevestigator

P36551.

GermOnline

ENSG00000080819. Homo sapiens.

Family and domain databases

Gene3D

3.40.1500.10. 1 hit.

InterPro

IPR001260. Coprogen_oxidase_aer.
IPR018375. Coprogen_oxidase_CS.
[Graphical view]

PANTHER

PTHR10755. PTHR10755. 1 hit.

Pfam

PF01218. Coprogen_oxidas. 1 hit.
[Graphical view]

PRINTS

PR00073. COPRGNOXDASE.

SUPFAM

SSF102886. Coprogen_oxidas. 1 hit.

PROSITE

PS01021. COPROGEN_OXIDASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1681618.

EvolutionaryTrace

P36551.

GenomeRNAi

1371.

NextBio

5561.

SOURCE

Search...

Entry information

Entry name

HEM6_HUMAN

Accession

Primary (citable) accession number: P36551
Secondary accession number(s): A8K275 , Q14060, Q53F08, Q8IZ45, Q96AF3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 141 of the entry and version 3 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.