Q13057 (COASY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional coenzyme A synthase
Short name=CoA synthase

Alternative name(s):
NBP
POV-2

Including the following 2 domains:

1. Phosphopantetheine adenylyltransferase
   EC=2.7.7.3
   Alternative name(s):
   Dephospho-CoA pyrophosphorylase
   Pantetheine-phosphate adenylyltransferase
   Short name=PPAT
2. Dephospho-CoA kinase
   Short name=DPCK
   EC=2.7.1.24
   Alternative name(s):
   Dephosphocoenzyme A kinase
   Short name=DPCOAK

Gene names

Name:	COASY
ORF Names:	PSEC0106

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	564 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation. Ref.1
Catalytic activity	ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA. ATP + 3'-dephospho-CoA = ADP + CoA.
Pathway	Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subunit structure	Monomer. Ref.2
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Expressed in all tissues examined including brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocyte. Lowest expression in peripheral blood leukocytes and highest in kidney and liver. Isoform 2 is expressed mainly in the brain. Ref.1
Sequence similarities	In the central section; belongs to the eukaryotic CoaD family. Contains 1 DPCK (dephospho-CoA kinase) domain.
Biophysicochemical properties	Kinetic parameters: KM=7.6 mM for 4'-phoshopantetheine KM=145 mM for ATP (in the PPAT reaction) KM=16.7 mM for dephospho-CoA KM=34.4 mM for ATP (in the DPCK reaction)
Sequence caution	The sequence AAA69699.1 differs from that shown. Reason: Frameshift at position 535. The sequence AAF87955.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH06354.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH20985.1 differs from that shown. Reason: Erroneous initiation. The sequence AK075415 differs from that shown. Reason: Frameshift at position 315.

Ontologies

Keywords
Biological process	Coenzyme A biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	coenzyme A biosynthetic process Traceable author statement Ref.2. Source: UniProtKB pantothenate metabolic process Traceable author statement. Source: Reactome
Cellular_component	mitochondrial outer membrane Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW dephospho-CoA kinase activity Inferred from direct assay Ref.2. Source: UniProtKB pantetheine-phosphate adenylyltransferase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13057-1)

Also known as: CoASy alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13057-2)

Also known as: CoASy beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRTPRLRAQPRGAVYQAPSPPPAPVGLGSM

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 564	564	Bifunctional coenzyme A synthase		PRO_0000173039
Regions
	Domain	360 – 563	204	DPCK
	Nucleotide binding	365 – 372	8	ATP Potential
	Region	180 – 358	179	Phosphopantetheine adenylyltransferase
Amino acid modifications
	Modified residue	178	1	Phosphoserine Ref.12 Ref.13 Ref.14
	Modified residue	183	1	Phosphoserine Ref.14
Natural variations
	Alternative sequence	1	1	M → MRTPRLRAQPRGAVYQAPSP PPAPVGLGSM in isoform 2.		VSP_036404
	Natural variant	55	1	S → Y. Ref.1 Ref.4 Ref.6 Ref.7 Corresponds to variant rs615942 [ dbSNP | Ensembl ].		VAR_030299
Experimental info
	Sequence conflict	41	1	L → P in BAG36775. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CoASy alpha) [UniParc]. Last modified June 27, 2003. Version 4. Checksum: 7DC9E93B356C5DB7	FASTA	564	62,329
	10 20 30 40 50 60 MAVFRSGLLV LTTPLASLAP RLASILTSAA RLVNHTLYVH LQPGMSLEGP AQPQSSPVQA 70 80 90 100 110 120 TFEVLDFITH LYAGADVHRH LDVRILLTNI RTKSTFLPPL PTSVQNLAHP PEVVLTDFQT 130 140 150 160 170 180 LDGSQYNPVK QQLVRYATSC YSCCPRLASV LLYSDYGIGE VPVEPLDVPL PSTIRPASPV 190 200 210 220 230 240 AGSPKQPVRG YYRGAVGGTF DRLHNAHKVL LSVACILAQE QLVVGVADKD LLKSKLLPEL 250 260 270 280 290 300 LQPYTERVEH LSEFLVDIKP SLTFDVIPLL DPYGPAGSDP SLEFLVVSEE TYRGGMAINR 310 320 330 340 350 360 FRLENDLEEL ALYQIQLLKD LRHTENEEDK VSSSSFRQRM LGNLLRPPYE RPELPTCLYV 370 380 390 400 410 420 IGLTGISGSG KSSIAQRLKG LGAFVIDSDH LGHRAYAPGG PAYQPVVEAF GTDILHKDGI 430 440 450 460 470 480 INRKVLGSRV FGNKKQLKIL TDIMWPIIAK LAREEMDRAV AEGKRVCVID AAVLLEAGWQ 490 500 510 520 530 540 NLVHEVWTAV IPETEAVRRI VERDGLSEAA AQSRLQSQMS GQQLVEQSHV VLSTLWEPHI 550 560 TQRQVEKAWA LLQKRIPKTH QALD
	Isoform 2 (CoASy beta) [UniParc]. Checksum: BE77FF6197170615	FASTA	593	65,339
	10 20 30 40 50 60 MRTPRLRAQP RGAVYQAPSP PPAPVGLGSM AVFRSGLLVL TTPLASLAPR LASILTSAAR 70 80 90 100 110 120 LVNHTLYVHL QPGMSLEGPA QPQSSPVQAT FEVLDFITHL YAGADVHRHL DVRILLTNIR 130 140 150 160 170 180 TKSTFLPPLP TSVQNLAHPP EVVLTDFQTL DGSQYNPVKQ QLVRYATSCY SCCPRLASVL 190 200 210 220 230 240 LYSDYGIGEV PVEPLDVPLP STIRPASPVA GSPKQPVRGY YRGAVGGTFD RLHNAHKVLL 250 260 270 280 290 300 SVACILAQEQ LVVGVADKDL LKSKLLPELL QPYTERVEHL SEFLVDIKPS LTFDVIPLLD 310 320 330 340 350 360 PYGPAGSDPS LEFLVVSEET YRGGMAINRF RLENDLEELA LYQIQLLKDL RHTENEEDKV 370 380 390 400 410 420 SSSSFRQRML GNLLRPPYER PELPTCLYVI GLTGISGSGK SSIAQRLKGL GAFVIDSDHL 430 440 450 460 470 480 GHRAYAPGGP AYQPVVEAFG TDILHKDGII NRKVLGSRVF GNKKQLKILT DIMWPIIAKL 490 500 510 520 530 540 AREEMDRAVA EGKRVCVIDA AVLLEAGWQN LVHEVWTAVI PETEAVRRIV ERDGLSEAAA 550 560 570 580 590 QSRLQSQMSG QQLVEQSHVV LSTLWEPHIT QRQVEKAWAL LQKRIPKTHQ ALD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics." Daugherty M., Polanuyer B., Farrell M., Scholle M., Lykidis A., de Crecy-Lagard V., Osterman A. J. Biol. Chem. 277:21431-21439(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT TYR-55.
[2]	"Identification and characterization of the gene encoding the human phosphopantetheine adenylyltransferase and dephospho-CoA kinase bifunctional enzyme (CoA synthase)." Aghajanian S., Worrall D.M. Biochem. J. 365:13-18(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT.
[3]	"HRI human cDNA sequencing project." Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S., Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y., Nagahari K., Sugano S., Isogai T. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Teratocarcinoma.
[4]	"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] (ISOFORMS 1 AND 2), VARIANT TYR-55.
[5]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TYR-55.
[7]	"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] (ISOFORM 1), VARIANT TYR-55. Tissue: Colon, Muscle and Uterus.
[8]	"Molecular cloning of a NBP gene cDNA." Zhu Y.-B., Han Y. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 165-564 (ISOFORMS 1/2).
[9]	"A 100-kb physical and transcriptional map around the EDH17B2 gene: identification of three novel genes and a pseudogene of a human homologue of the rat PRL-1 tyrosine phosphatase." Montagna M., Serova O., Sylla B.S., Feunteun J., Lenoir G.M. Hum. Genet. 96:532-538(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 332-564 (ISOFORMS 1/2). Tissue: Ovary.
[10]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-564 (ISOFORMS 1/2).
[11]	"Identification of a novel CoA synthase isoform, which is primarily expressed in the brain." Nemazanyy I., Panasyuk G., Breus O., Zhyvoloup A., Filonenko V., Gout I.T. Biochem. Biophys. Res. Commun. 341:995-1000(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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-178 AND SER-183, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF453478 mRNA. Translation: AAL50813.1. AY094602 mRNA. Translation: AAM19996.1. AK075415 mRNA. No translation available. AK297153 mRNA. Translation: BAG59652.1. AK314076 mRNA. Translation: BAG36775.1. AC067852 Genomic DNA. No translation available. CH471152 Genomic DNA. Translation: EAW60840.1. BC006354 mRNA. Translation: AAH06354.1. Different initiation. BC020985 mRNA. Translation: AAH20985.1. Different initiation. BC067254 mRNA. Translation: AAH67254.1. AF208536 mRNA. Translation: AAF87955.1. Different initiation. U18919 mRNA. Translation: AAA69699.1. Frameshift. BT007168 mRNA. Translation: AAP35832.1.
IPI	IPI00184821. IPI00909064.
RefSeq	NP_001035994.1. NM_001042529.2. NP_001035997.2. NM_001042532.3. NP_079509.5. NM_025233.6.
UniGene	Hs.296422. Hs.742262.
3D structure databases
ProteinModelPortal	Q13057.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13057. 2 interactions.
MINT	MINT-1212728.
STRING	9606.ENSP00000377404.
PTM databases
PhosphoSite	Q13057.
Polymorphism databases
DMDM	32363505.
Proteomic databases
PaxDb	Q13057.
PRIDE	Q13057.
Protocols and materials databases
DNASU	80347.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000393818; ENSP00000377406; ENSG00000068120. ENST00000420359; ENSP00000413338; ENSG00000068120. ENST00000421097; ENSP00000393564; ENSG00000068120. ENST00000449624; ENSP00000407740; ENSG00000068120. ENST00000590958; ENSP00000464814; ENSG00000068120.
GeneID	80347.
KEGG	hsa:80347.
UCSC	uc002hzz.3. human. uc010cyj.3. human.
Organism-specific databases
CTD	80347.
GeneCards	GC17P040714.
HGNC	HGNC:29932. COASY.
HPA	HPA022875. HPA022912. HPA023273.
MIM	609855. gene.
neXtProt	NX_Q13057.
PharmGKB	PA134867942.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0237.
HOVERGEN	HBG051059.
InParanoid	Q13057.
KO	K02318.
OMA	PVQATFE.
OrthoDB	EOG4RXXZW.
PhylomeDB	Q13057.
Enzyme and pathway databases
BRENDA	2.7.1.24. 2681.
Reactome	REACT_111217. Metabolism.
SABIO-RK	Q13057.
UniPathway	UPA00241; UER00355. UPA00241; UER00356.
Gene expression databases
Bgee	Q13057.
CleanEx	HS_COASY.
Genevestigator	Q13057.
GermOnline	ENSG00000068120. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
InterPro	IPR004821. Cyt_trans-like. IPR001977. Depp_CoAkinase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF01121. CoaE. 1 hit. PF01467. CTP_transf_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00152. TIGR00152. 1 hit.
PROSITE	PS51219. DPCK. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	COASY. human.
GenomeRNAi	80347.
NextBio	70944.
SOURCE	Search...

Entry information

Entry name

COASY_HUMAN

Accession

Primary (citable) accession number: Q13057
Secondary accession number(s): B2RA78 , B4DLU0, Q6GS23, Q8NBM7, Q8NEW1, Q8WXD4, Q9NRM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	June 27, 2003
Last modified:	May 1, 2013
This is version 133 of the entry and version 4 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.