P25311 (ZA2G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc-alpha-2-glycoprotein
Short name=Zn-alpha-2-GP
Short name=Zn-alpha-2-glycoprotein

Gene names

Name:	AZGP1
Synonyms:	ZAG, ZNGP1

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	298 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	Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.
Subunit structure	Interacts with PIP.
Subcellular location	Secreted.
Tissue specificity	Blood plasma, seminal plasma, urine, saliva, sweat, epithelial cells of various human glands, liver.
Post-translational modification	N-glycosylated. N-glycan at Asn-128: Hex5HexNAc4. Ref.19 Ref.20 Ref.21 Ref.22
Sequence similarities	Belongs to the MHC class I family. Contains 1 Ig-like C1-type (immunoglobulin-like) domain.
Caution	It is uncertain whether Met-1 or Met-4 is the initiator.
Sequence caution	The sequence AAA61311.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAA03123.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAA14417.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAA42438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation Inferred from electronic annotation. Source: InterPro cell adhesion Inferred from direct assay PubMed 9813179. Source: UniProtKB immune response Inferred from electronic annotation. Source: InterPro negative regulation of cell proliferation Non-traceable author statement PubMed 10462714. Source: UniProtKB
Cellular_component	MHC class I protein complex Inferred from electronic annotation. Source: InterPro extracellular region Non-traceable author statement PubMed 14718574. Source: UniProtKB
Molecular_function	protein transmembrane transporter activity Non-traceable author statement PubMed 6896906. Source: UniProtKB ribonuclease activity Non-traceable author statement PubMed 10462714. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.9 Ref.10

Chain

21 – 298

278

Zinc-alpha-2-glycoprotein

PRO_0000019012

Regions

Domain

207 – 292

86

Ig-like C1-type

Amino acid modifications

Modified residue

21

1

Pyrrolidone carboxylic acid

Glycosylation

109

1

N-linked (GlcNAc...) Ref.16 Ref.17 Ref.18 Ref.20

Glycosylation

112

1

N-linked (GlcNAc...) Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Glycosylation

128

1

N-linked (GlcNAc...) (complex) Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Glycosylation

259

1

N-linked (GlcNAc...) Ref.20 Ref.21 Ref.22

Disulfide bond

123 ↔ 186

Ref.20 Ref.21 Ref.22

Disulfide bond

225 ↔ 280

Ref.20 Ref.21 Ref.22

Experimental info

Sequence conflict

2

1

V → S in CAA42438. Ref.1

Sequence conflict

5

1

V → L in CAA42438. Ref.1

Sequence conflict

33

1

I → V in AAH05306. Ref.7

Sequence conflict

85

1

Q → E AA sequence Ref.9

Sequence conflict

96 – 97

2

Missing AA sequence Ref.9

Sequence conflict

244

1

E → Q AA sequence Ref.9

Secondary structure

1

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298

Helix Strand Turn

Details...

Beta strand

27 – 39

13

Beta strand

42 – 44

3

Beta strand

46 – 53

8

Beta strand

56 – 62

7

Turn

63 – 65

3

Helix

72 – 76

5

Beta strand

79 – 81

3

Helix

83 – 107

25

Beta strand

116 – 126

11

Beta strand

129 – 139

11

Beta strand

142 – 148

7

Turn

149 – 152

4

Beta strand

153 – 156

4

Helix

159 – 168

10

Helix

173 – 183

11

Helix

185 – 196

12

Helix

198 – 201

4

Beta strand

208 – 215

8

Beta strand

217 – 219

3

Beta strand

221 – 233

13

Beta strand

235 – 241

7

Beta strand

244 – 246

3

Beta strand

249 – 256

8

Turn

257 – 260

4

Beta strand

261 – 270

10

Beta strand

278 – 284

7

Beta strand

291 – 294

4

Sequences

	Sequence		Length	Mass (Da)
	P25311 [UniParc]. Last modified March 23, 2010. Version 2. Checksum: 006A153A8E32A0B1	FASTA	298	34,259
	10 20 30 40 50 60 MVRMVPVLLS LLLLLGPAVP QENQDGRYSL TYIYTGLSKH VEDVPAFQAL GSLNDLQFFR 70 80 90 100 110 120 YNSKDRKSQP MGLWRQVEGM EDWKQDSQLQ KAREDIFMET LKDIVEYYND SNGSHVLQGR 130 140 150 160 170 180 FGCEIENNRS SGAFWKYYYD GKDYIEFNKE IPAWVPFDPA AQITKQKWEA EPVYVQRAKA 190 200 210 220 230 240 YLEEECPATL RKYLKYSKNI LDRQDPPSVV VTSHQAPGEK KKLKCLAYDF YPGKIDVHWT 250 260 270 280 290 RAGEVQEPEL RGDVLHNGNG TYQSWVVVAV PPQDTAPYSC HVQHSSLAQP LVVPWEAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human Zn-alpha 2-glycoprotein cDNA cloning and expression analysis in benign and malignant breast tissues." Freije J.P., Fueyo A., Uria J., Lopez-Otin C. FEBS Lett. 290:247-249(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary gland.
[2]	"Molecular cloning and chromosomal assignment of the gene for human Zn-alpha 2-glycoprotein." Ueyama H., Deng H.X., Ohkubo I. Biochemistry 32:12968-12976(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Human Zn-alpha 2-glycoprotein: complete genomic sequence, identification of a related pseudogene and relationship to class I major histocompatibility complex genes." Freije J.P., Fueyo A., Uria J.A., Velasco G., Sanchez L.M., Lopez-Boado Y.S., Lopez-Otin C. Genomics 18:575-587(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Leukocyte.
[4]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]. Tissue: Colon and Prostate.
[8]	"Cloning and nucleotide sequence of a human Zn-alpha 2-glycoprotein cDNA and chromosomal assignment of its gene." Ueyama H., Niwa M., Tada T., Sasaki M., Ohkubo I. Biochem. Biophys. Res. Commun. 177:696-703(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-298. Tissue: Liver and Prostate.
[9]	"Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and its homology to histocompatibility antigens." Araki T., Gejyo F., Takagaki K., Haupt H., Schwick H.G., Buergi W., Marti T., Schaller J., Rickli E., Brossmer R., Atkinson P.H., Putnam F.W., Schmid K. Proc. Natl. Acad. Sci. U.S.A. 85:679-683(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-298. Tissue: Plasma.
[10]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-35.
[11]	"Biochemical characterization and crystallization of human Zn-alpha2-glycoprotein, a soluble class I major histocompatibility complex homolog." Sanchez L.M., Lopez-Otin C., Bjorkman P.J. Proc. Natl. Acad. Sci. U.S.A. 94:4626-4630(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, CRYSTALLIZATION.
[12]	"Hydrophobic ligand binding by Zn-alpha 2-glycoprotein, a soluble fat-depleting factor related to major histocompatibility complex proteins." Kennedy M.W., Heikema A.P., Cooper A., Bjorkman P.J., Sanchez L.M. J. Biol. Chem. 276:35008-35013(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IN VITRO BINDING OF FATTY ACID.
[13]	"A proteomic analysis of human bile." Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A. Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128, MASS SPECTROMETRY. Tissue: Bile.
[14]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112 AND ASN-128, MASS SPECTROMETRY. Tissue: Plasma.
[15]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112, MASS SPECTROMETRY. Tissue: Plasma.
[16]	"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry." Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A. J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128, MASS SPECTROMETRY. Tissue: Saliva.
[17]	"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry." Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F. Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128, MASS SPECTROMETRY. Tissue: Milk.
[18]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128, MASS SPECTROMETRY. Tissue: Liver.
[19]	"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD." Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G. Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-128, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
[20]	"Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules." Sanchez L.M., Chirino A.J., Bjorkman P.J. Science 283:1914-1919(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT ASN-109; ASN-128 AND ASN-259.
[21]	"Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein." Delker S.L., West A.P. Jr., McDermott L., Kennedy M.W., Bjorkman P.J. J. Struct. Biol. 148:205-213(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 21-298, DISULFIDE BONDS, GLYCOSYLATION AT ASN-128 AND ASN-259.
[22]	"Crystal structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human seminal plasma." Hassan M.I., Bilgrami S., Kumar V., Singh N., Yadav S., Kaur P., Singh T.P. J. Mol. Biol. 384:663-672(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 32-149 IN COMPLEX WITH PIP, DISULFIDE BONDS, GLYCOSYLATION AT ASN-259.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59766 mRNA. Translation: CAA42438.1. Different initiation.
D14034 Genomic DNA. Translation: BAA03123.1. Different initiation.
X69953 Genomic DNA. Translation: CAA49574.1.
AC004522 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23862.1.
CH471091 Genomic DNA. Translation: EAW76621.1.
CH471091 Genomic DNA. Translation: EAW76622.1.
BC005306 mRNA. Translation: AAH05306.1.
BC033830 mRNA. Translation: AAH33830.1.
D90427 mRNA. Translation: BAA14417.1. Different initiation.
M76707 mRNA. Translation: AAA61311.1. Different initiation.

IPI

IPI00166729.

PIR

A54175.

RefSeq

NP_001176.1. NM_001185.3.

UniGene

Hs.546239.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T7V	X-ray	1.95	A	21-298	[»]
1T7W	X-ray	2.70	A	21-298	[»]
1T7X	X-ray	3.10	A	21-298	[»]
1T7Y	X-ray	2.80	A	21-298	[»]
1T7Z	X-ray	3.00	A	21-298	[»]
1T80	X-ray	2.10	A	21-298	[»]
1ZAG	X-ray	2.80	A/B/C/D	25-298	[»]
3ES6	X-ray	3.23	A	22-298	[»]

ProteinModelPortal

P25311.

SMR

P25311. Positions 25-298.

ModBase

Search...

Protein-protein interaction databases

IntAct

P25311. 5 interactions.

STRING

9606.ENSP00000292401.

PTM databases

PhosphoSite

P25311.

Polymorphism databases

DMDM

292495049.

2D gel databases

REPRODUCTION-2DPAGE

IPI00166729.

SWISS-2DPAGE

P25311.

Proteomic databases

PaxDb

P25311.

PRIDE

P25311.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000292401; ENSP00000292401; ENSG00000160862.

GeneID

563.

KEGG

hsa:563.

UCSC

uc003ush.3. human.

Organism-specific databases

CTD

563.

GeneCards

GC07M099564.

HGNC

HGNC:910. AZGP1.

HPA

CAB016087.
HPA012582.

MIM

194460. gene.

neXtProt

NX_P25311.

PharmGKB

PA25203.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG25830.

HOGENOM

HOG000296917.

HOVERGEN

HBG016709.

InParanoid

P25311.

OMA

NILDRQD.

OrthoDB

EOG45QHDM.

PhylomeDB

P25311.

Gene expression databases

ArrayExpress

P25311.

Bgee

P25311.

CleanEx

HS_AZGP1.

Genevestigator

P25311.

GermOnline

ENSG00000160862. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.
3.30.500.10. 1 hit.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011161. MHC_I-like_Ag-recog.
IPR011162. MHC_I/II-like_Ag-recog.
IPR001039. MHC_I_a_a1/a2.
[Graphical view]

Pfam

PF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
[Graphical view]

PRINTS

PR01638. MHCCLASSI.

SMART

SM00407. IGc1. 1 hit.
[Graphical view]

SUPFAM

SSF54452. MHC_I/II-like_Ag-recog. 1 hit.

PROSITE

PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

AZGP1. human.

EvolutionaryTrace

P25311.

GenomeRNAi

563.

NextBio

2301.

SOURCE

Search...

Entry information

Entry name

ZA2G_HUMAN

Accession

Primary (citable) accession number: P25311
Secondary accession number(s): D6W5T8 , O60386, Q5XKQ4, Q8N4N0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	March 23, 2010
Last modified:	May 1, 2013
This is version 140 of the entry and version 2 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.