P51636 (CAV2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Caveolin-2

Gene names

Name:

CAV2

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

General annotation (Comments)

Function	May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression By similarity. Ref.10 Ref.11
Subunit structure	Monomer or homodimer. Interacts with CAV1; the interaction forms a stable heterooligomeric complex that is required for targeting to lipid rafts and for caveolae formation. Tyrosine phosphorylated forms do not form heterooligomers with the Tyr-19-phosphorylated form existing as a monomer or dimer, and the Tyr-27-form as a monomer only. Interacts (tyrosine phosphorylated form) with the SH2 domain-containing proteins, RASA1, NCK1 and SRC. Interacts (tyrosine phosphorylated form) with INSR, the interaction (Tyr-27-phosphorylated form) is increased on insulin stimulation. Interacts (Tyr-19 phosphorylated form) with MAPK1 (phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation. Interacts with STAT3; the interaction is increased on insulin-induced tyrosine phosphorylation leading to STAT activation By similarity. Ref.2 Ref.8 Ref.9 Ref.10
Subcellular location	Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane › caveola; Peripheral membrane protein. Note: Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin By similarity. Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11
Tissue specificity	Expressed in endothelial cells, smooth muscle cells, skeletal myoblasts and fibroblasts. Ref.2
Post-translational modification	Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells By similarity. Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin By similarity. Ref.9 Ref.10 Ref.11
Sequence similarities	Belongs to the caveolin family.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Golgi apparatus Membrane Nucleus
Coding sequence diversity	Alternative initiation Alternative splicing Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	caveola assembly Inferred from mutant phenotype PubMed 12633858. Source: BHF-UCL endoplasmic reticulum organization Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion organization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of endothelial cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of dopamine receptor signaling pathway Inferred from mutant phenotype PubMed 15569306. Source: BHF-UCL positive regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Compara protein oligomerization Inferred from electronic annotation. Source: Compara regulation of mitosis Inferred from expression pattern Ref.11. Source: BHF-UCL skeletal muscle fiber development Inferred from sequence or structural similarity. Source: UniProtKB synaptic transmission Inferred from electronic annotation. Source: Compara vesicle docking Inferred from direct assay PubMed 12743374. Source: BHF-UCL vesicle fusion Inferred from direct assay PubMed 12743374. Source: BHF-UCL
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: BHF-UCL Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell acrosomal membrane Inferred from electronic annotation. Source: Compara caveola Inferred from direct assay PubMed 15703204Ref.11. Source: BHF-UCL cell surface Inferred from electronic annotation. Source: Compara cytosol Inferred from electronic annotation. Source: Compara endoplasmic reticulum part Inferred from direct assay PubMed 22792322. Source: MGI extrinsic to internal side of plasma membrane Inferred from direct assay PubMed 15569306. Source: BHF-UCL integral to plasma membrane Inferred from direct assay Ref.1. Source: MGI lipid particle Inferred from electronic annotation. Source: Compara membrane Inferred from direct assay PubMed 15569306PubMed 15569306PubMed 15569306. Source: BHF-UCL nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from direct assay Ref.11. Source: BHF-UCL protein complex Inferred from electronic annotation. Source: Compara transport vesicle Inferred from direct assay. Source: LIFEdb
Molecular_function	protein homodimerization activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative initiation. [Align] [Select]

Isoform Alpha (identifier: P51636-1)

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 Beta (identifier: P51636-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.

Note: Produced by alternative initiation.

Isoform C (identifier: P51636-3)

The sequence of this isoform differs from the canonical sequence as follows:
     51-112: LGFEDVIAEP...LFATLSCLHI → DFNAFCKDLP...WTPGLEIGIL
     113-162: Missing.

Note: Produced by alternative splicing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 162	162	Caveolin-2		PRO_0000004772
Regions
	Topological domain	1 – 86	86	Cytoplasmic Potential
	Intramembrane	87 – 107	21	Helical; Potential
	Topological domain	108 – 162	55	Cytoplasmic Potential
Amino acid modifications
	Modified residue	19	1	Phosphotyrosine; by SRC Ref.9 Ref.10
	Modified residue	23	1	Phosphoserine Ref.11
	Modified residue	27	1	Phosphotyrosine; by SRC Ref.10
	Modified residue	36	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	1 – 13	13	Missing in isoform Beta.		VSP_018696
	Alternative sequence	51 – 112	62	LGFED…SCLHI → DFNAFCKDLPNGSAFSADNM EECDRCYHCSIVYERRTMLL FCQPATEPGLNTWTPGLEIG IL in isoform C.		VSP_038114
	Alternative sequence	113 – 162	50	Missing in isoform C.		VSP_038115
	Natural variant	130	1	Q → E. Corresponds to variant rs8940 [ dbSNP | Ensembl ].		VAR_012071
Experimental info
	Mutagenesis	19	1	Y → A: Greatly reduced Src-mediated phosphorylation and binding of RASA1, SRC and NCK1. Completely eliminates Src-mediated tyrosine phosphorylation and binding to RASA1, SRC and NCK1; when associated with A-27. Ref.10
	Mutagenesis	23	1	S → A: Abolishes phosphorylation. Ref.11
	Mutagenesis	27	1	Y → A: Greatly reduced Src-mediated phosphorylation and binding of RASA1, SRC and NCK1. Completely eliminates Src-mediated phosphorylation and binding of RASA1, SRC and NCK1; when associated with A-19. Ref.10
	Mutagenesis	36	1	S → A: Abolishes phosphorylation. Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified July 15, 1999. Version 2. Checksum: 89FDEDA861330B87	FASTA	162	18,291
	10 20 30 40 50 60 MGLETEKADV QLFMDDDSYS HHSGLEYADP EKFADSDQDR DPHRLNSHLK LGFEDVIAEP 70 80 90 100 110 120 VTTHSFDKVW ICSHALFEIS KYVMYKFLTV FLAIPLAFIA GILFATLSCL HIWILMPFVK 130 140 150 160 TCLMVLPSVQ TIWKSVTDVI IAPLCTSVGR CFSSVSLQLS QD
	Isoform Beta [UniParc]. Checksum: 0706B574F5E1AAD8	FASTA	149	16,829
	10 20 30 40 50 60 MDDDSYSHHS GLEYADPEKF ADSDQDRDPH RLNSHLKLGF EDVIAEPVTT HSFDKVWICS 70 80 90 100 110 120 HALFEISKYV MYKFLTVFLA IPLAFIAGIL FATLSCLHIW ILMPFVKTCL MVLPSVQTIW 130 140 KSVTDVIIAP LCTSVGRCFS SVSLQLSQD
	Isoform C [UniParc]. Checksum: 7C60DC5ABD6B0105	FASTA	112	12,780
	10 20 30 40 50 60 MGLETEKADV QLFMDDDSYS HHSGLEYADP EKFADSDQDR DPHRLNSHLK DFNAFCKDLP 70 80 90 100 110 NGSAFSADNM EECDRCYHCS IVYERRTMLL FCQPATEPGL NTWTPGLEIG IL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification, sequence, and expression of caveolin-2 defines a caveolin gene family." Scherer P.E., Okamoto T., Chun M., Nishimoto I., Lodish H.F., Lisanti M.P. Proc. Natl. Acad. Sci. U.S.A. 93:131-135(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
[2]	"Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo." Scherer P.E., Lewis R.Y., Volonte D., Engelman J.A., Galbiati F., Couet J., Kohtz D.S., van Donselaar E., Peters P., Lisanti M.P. J. Biol. Chem. 272:29337-29346(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), INTERACTION WITH CAV1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]	"Sequence and detailed organization of the human caveolin-1 and -2 genes located near the D7S522 locus (7q31.1). Methylation of a CpG island in the 5' promoter region of the caveolin-1 gene in human breast cancer cell lines." Engelman J.A., Zhang X.L., Lisanti M.P. FEBS Lett. 448:221-230(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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] (ISOFORM ALPHA).
[5]	"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] (ISOFORM C). Tissue: Hepatoma.
[6]	"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].
[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 ALPHA). Tissue: Kidney.
[8]	"Mutational analysis of caveolin-induced vesicle formation. Expression of caveolin-1 recruits caveolin-2 to caveolae membranes." Li S., Galbiati F., Volonte D., Sargiacomo M., Engelman J.A., Das K., Scherer P.E., Lisanti M.P. FEBS Lett. 434:127-134(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CAV1, ALTERNATIVE PRODUCTS, SUBCELLULAR LOCATION.
[9]	"Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1." Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P. J. Biol. Chem. 277:34556-34567(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-19, SUBCELLULAR LOCATION, INTERACTION WITH CAV1; SRC; RASA1 AND NCK1.
[10]	"Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)." Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., Campos-Gonzalez R., Lisanti M.P. Biochemistry 43:13694-13706(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-19 AND TYR-27, SUBCELLULAR LOCATION, INTERACTION WITH CAV1; NCK1; RASA1 AND SRC, FUNCTION, MUTAGENESIS OF TYR-19 AND TYR-27.
[11]	"Serine 23 and 36 phosphorylation of caveolin-2 is differentially regulated by targeting to lipid raft/caveolae and in mitotic endothelial cells." Sowa G., Xie L., Xu L., Sessa W.C. Biochemistry 47:101-111(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-23 AND SER-36, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-23 AND SER-36.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[13]	"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.

Web resources

Wikipedia

Caveolin entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF035752 mRNA. Translation: AAB88492.1. AJ133269 Genomic DNA. Translation: CAB63653.1. BT007051 mRNA. Translation: AAP35700.1. BC005256 mRNA. Translation: AAH05256.1. AJ242718 Genomic DNA. Translation: CAB65090.1. AK310786 mRNA. No translation available. CH236947 Genomic DNA. Translation: EAL24361.1.
IPI	IPI00019870. IPI00386526. IPI00759514.
RefSeq	NP_001193676.1. NM_001206747.1. NP_001193677.1. NM_001206748.1. NP_001224.1. NM_001233.4. NP_937855.1. NM_198212.2.
UniGene	Hs.212332. Hs.603096.
3D structure databases
ProteinModelPortal	P51636.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51636. 3 interactions.
MINT	MINT-1403441.
STRING	9606.ENSP00000222693.
PTM databases
PhosphoSite	P51636.
Polymorphism databases
DMDM	5915890.
Proteomic databases
PaxDb	P51636.
PRIDE	P51636.
Protocols and materials databases
DNASU	858.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000222693; ENSP00000222693; ENSG00000105971. ENST00000343213; ENSP00000345679; ENSG00000105971.
GeneID	858.
KEGG	hsa:858.
UCSC	uc003vid.3. human. uc003vie.3. human. uc022akj.1. human.
Organism-specific databases
CTD	858.
GeneCards	GC07P115926.
HGNC	HGNC:1528. CAV2.
HPA	CAB013488.
MIM	601048. gene.
neXtProt	NX_P51636.
PharmGKB	PA26108.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG74268.
HOGENOM	HOG000036550.
HOVERGEN	HBG003422.
InParanoid	P51636.
KO	K12958.
OMA	STHSFDK.
OrthoDB	EOG4PRSRW.
PhylomeDB	P51636.
Enzyme and pathway databases
Pathway_Interaction_DB	syndecan_2_pathway. Syndecan-2-mediated signaling events.
SignaLink	P51636.
Gene expression databases
ArrayExpress	P51636.
Bgee	P51636.
CleanEx	HS_CAV2.
Genevestigator	P51636.
GermOnline	ENSG00000105971. Homo sapiens.
Family and domain databases
InterPro	IPR001612. Caveolin. IPR018361. Caveolin_CS. [Graphical view]
PANTHER	PTHR10844. PTHR10844. 1 hit.
Pfam	PF01146. Caveolin. 1 hit. [Graphical view]
PROSITE	PS01210. CAVEOLIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CAV2. human.
GenomeRNAi	858.
NextBio	3560.
SOURCE	Search...

Entry information

Entry name

CAV2_HUMAN

Accession

Primary (citable) accession number: P51636
Secondary accession number(s): A4D0U2, Q9UGM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 15, 1999
Last modified:	May 29, 2013
This is version 130 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.