Q08493 (PDE4C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase 4C
EC=3.1.4.17

Alternative name(s):
DPDE1
PDE21

Gene names

Name:	PDE4C
Synonyms:	DPDE1

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

General annotation (Comments)

Function	Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. Ref.7
Catalytic activity	Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.
Cofactor	Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. Ref.7
Enzyme regulation	Inhibited by rolipram.
Pathway	Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
Subunit structure	Part of a complex containing AKAP5, ADCY5, ADCY6 and PKD2 By similarity.
Subcellular location	Cell projection › cilium By similarity.
Tissue specificity	Expressed in various tissues but not in cells of the immune system.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily.

Ontologies

Keywords
Cellular component	Cell projection Cilium
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding cAMP
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cAMP catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Traceable author statement. Source: Reactome primary cilium Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	3',5'-cyclic-AMP phosphodiesterase activity Traceable author statement PubMed 9349724. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform PDE4C1 (identifier: Q08493-1)

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 PDE4C2 (identifier: Q08493-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-106: Missing.

Isoform PDE4C3 (identifier: Q08493-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: MENLGVGEGA...LSWPVSSCRR → MQGPPAPAPV...RRFTVAHPLC

Isoform PDE4C4 (identifier: Q08493-4)

The sequence of this isoform is not available.

Isoform PDE4C5 (identifier: Q08493-5)

The sequence of this isoform is not available.

Isoform PDE4C6 (identifier: Q08493-6)

The sequence of this isoform is not available.

Isoform PDE4C7 (identifier: Q08493-7)

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 712

712

cAMP-specific 3',5'-cyclic phosphodiesterase 4C

PRO_0000198811

Regions

Nucleotide binding

388 – 392

5

cAMP By similarity

Sites

Active site

388

1

Proton donor By similarity

Metal binding

392

1

Divalent metal cation 1

Metal binding

428

1

Divalent metal cation 1

Metal binding

429

1

Divalent metal cation 1

Metal binding

429

1

Divalent metal cation 2

Metal binding

546

1

Divalent metal cation 1

Binding site

429

1

cAMP By similarity

Binding site

546

1

cAMP By similarity

Binding site

597

1

cAMP By similarity

Site

549

1

Binds AMP, but not cAMP By similarity

Natural variations

Alternative sequence

1 – 106

106

Missing in isoform PDE4C2.

VSP_004575

Alternative sequence

1 – 81

81

MENLG…SSCRR → MQGPPAPAPVPGPGSPRGSP RGSPGLFRKLLVNQSIRLQR RFTVAHPLC in isoform PDE4C3.

VSP_004574

Natural variant

131

1

S → L.
Corresponds to variant rs10413646 [ dbSNP | Ensembl ].

VAR_050473

Natural variant

289

1

R → Q.
Corresponds to variant rs34503849 [ dbSNP | Ensembl ].

VAR_050474

Natural variant

344

1

R → Q.
Corresponds to variant rs2229228 [ dbSNP | Ensembl ].

VAR_034374

Natural variant

344

1

R → W.
Corresponds to variant rs11879710 [ dbSNP | Ensembl ].

VAR_061497

Experimental info

Sequence conflict

204

1

K → N in AAD47053. Ref.2

Sequence conflict

204

1

K → N in AAD47054. Ref.2

Sequence conflict

211

1

D → Y in AAD47053. Ref.2

Sequence conflict

211

1

D → Y in AAD47054. Ref.2

Sequence conflict

339 – 340

2

EL → DV in CAA86601. Ref.1

Sequence conflict

444 – 446

3

NSE → K in AAC83047. Ref.4

Sequence conflict

446 – 447

2

EL → DV in CAA86601. Ref.1

Secondary structure

1

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712

Helix Strand Turn

Details...

Helix

317 – 323

7

Helix

324 – 326

3

Helix

334 – 340

7

Helix

345 – 356

12

Helix

359 – 362

4

Helix

367 – 379

13

Beta strand

385 – 389

5

Helix

390 – 404

15

Helix

407 – 409

3

Turn

410 – 412

3

Helix

415 – 427

13

Turn

428 – 431

4

Helix

435 – 437

3

Helix

456 – 467

12

Helix

468 – 470

3

Turn

476 – 479

4

Helix

482 – 497

16

Helix

501 – 503

3

Helix

504 – 516

13

Helix

531 – 546

16

Helix

549 – 551

3

Helix

554 – 569

16

Helix

600 – 603

4

Helix

605 – 616

12

Turn

617 – 620

4

Helix

621 – 630

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform PDE4C1 [UniParc]. Last modified March 27, 2002. Version 2. Checksum: 1932116C9CE0322C	FASTA	712	79,902
	10 20 30 40 50 60 MENLGVGEGA EACSRLSRSR GRHSMTRAPK HLWRQPRRPI RIQQRFYSDP DKSAGCRERD 70 80 90 100 110 120 LSPRPELRKS RLSWPVSSCR RFDLENGLSC GRRALDPQSS PGLGRIMQAP VPHSQRRESF 130 140 150 160 170 180 LYRSDSDYEL SPKAMSRNSS VASDLHGEDM IVTPFAQVLA SLRTVRSNVA ALARQQCLGA 190 200 210 220 230 240 AKQGPVGNPS SSNQLPPAED TGQKLALETL DELDWCLDQL ETLQTRHSVG EMASNKFKRI 250 260 270 280 290 300 LNRELTHLSE TSRSGNQVSE YISRTFLDQQ TEVELPKVTA EEAPQPMSRI SGLHGLCHSA 310 320 330 340 350 360 SLSSATVPRF GVQTDQEEQL AKELEDTNKW GLDVFKVAEL SGNRPLTAII FSIFQERDLL 370 380 390 400 410 420 KTFQIPADTL ATYLLMLEGH YHANVAYHNS LHAADVAQST HVLLATPALE AVFTDLEILA 430 440 450 460 470 480 ALFASAIHDV DHPGVSNQFL INTNSELALM YNDASVLENH HLAVGFKLLQ AENCDIFQNL 490 500 510 520 530 540 SAKQRLSLRR MVIDMVLATD MSKHMNLLAD LKTMVETKKV TSLGVLLLDN YSDRIQVLQN 550 560 570 580 590 600 LVHCADLSNP TKPLPLYRQW TDRIMAEFFQ QGDRERESGL DISPMCDKHT ASVEKSQVGF 610 620 630 640 650 660 IDYIAHPLWE TWADLVHPDA QDLLDTLEDN REWYQSKIPR SPSDLTNPER DGPDRFQFEL 670 680 690 700 710 TLEEAEEEDE EEEEEGEETA LAKEALELPD TELLSPEAGP DPGDLPLDNQ RT
	Isoform PDE4C2 [UniParc]. Checksum: 3C42FC9F237333E1	FASTA	606	67,791
	10 20 30 40 50 60 MQAPVPHSQR RESFLYRSDS DYELSPKAMS RNSSVASDLH GEDMIVTPFA QVLASLRTVR 70 80 90 100 110 120 SNVAALARQQ CLGAAKQGPV GNPSSSNQLP PAEDTGQKLA LETLDELDWC LDQLETLQTR 130 140 150 160 170 180 HSVGEMASNK FKRILNRELT HLSETSRSGN QVSEYISRTF LDQQTEVELP KVTAEEAPQP 190 200 210 220 230 240 MSRISGLHGL CHSASLSSAT VPRFGVQTDQ EEQLAKELED TNKWGLDVFK VAELSGNRPL 250 260 270 280 290 300 TAIIFSIFQE RDLLKTFQIP ADTLATYLLM LEGHYHANVA YHNSLHAADV AQSTHVLLAT 310 320 330 340 350 360 PALEAVFTDL EILAALFASA IHDVDHPGVS NQFLINTNSE LALMYNDASV LENHHLAVGF 370 380 390 400 410 420 KLLQAENCDI FQNLSAKQRL SLRRMVIDMV LATDMSKHMN LLADLKTMVE TKKVTSLGVL 430 440 450 460 470 480 LLDNYSDRIQ VLQNLVHCAD LSNPTKPLPL YRQWTDRIMA EFFQQGDRER ESGLDISPMC 490 500 510 520 530 540 DKHTASVEKS QVGFIDYIAH PLWETWADLV HPDAQDLLDT LEDNREWYQS KIPRSPSDLT 550 560 570 580 590 600 NPERDGPDRF QFELTLEEAE EEDEEEEEEG EETALAKEAL ELPDTELLSP EAGPDPGDLP LDNQRT
	Isoform PDE4C3 [UniParc]. Checksum: E555883F32D17B64	FASTA	680	75,614
	10 20 30 40 50 60 MQGPPAPAPV PGPGSPRGSP RGSPGLFRKL LVNQSIRLQR RFTVAHPLCF DLENGLSCGR 70 80 90 100 110 120 RALDPQSSPG LGRIMQAPVP HSQRRESFLY RSDSDYELSP KAMSRNSSVA SDLHGEDMIV 130 140 150 160 170 180 TPFAQVLASL RTVRSNVAAL ARQQCLGAAK QGPVGNPSSS NQLPPAEDTG QKLALETLDE 190 200 210 220 230 240 LDWCLDQLET LQTRHSVGEM ASNKFKRILN RELTHLSETS RSGNQVSEYI SRTFLDQQTE 250 260 270 280 290 300 VELPKVTAEE APQPMSRISG LHGLCHSASL SSATVPRFGV QTDQEEQLAK ELEDTNKWGL 310 320 330 340 350 360 DVFKVAELSG NRPLTAIIFS IFQERDLLKT FQIPADTLAT YLLMLEGHYH ANVAYHNSLH 370 380 390 400 410 420 AADVAQSTHV LLATPALEAV FTDLEILAAL FASAIHDVDH PGVSNQFLIN TNSELALMYN 430 440 450 460 470 480 DASVLENHHL AVGFKLLQAE NCDIFQNLSA KQRLSLRRMV IDMVLATDMS KHMNLLADLK 490 500 510 520 530 540 TMVETKKVTS LGVLLLDNYS DRIQVLQNLV HCADLSNPTK PLPLYRQWTD RIMAEFFQQG 550 560 570 580 590 600 DRERESGLDI SPMCDKHTAS VEKSQVGFID YIAHPLWETW ADLVHPDAQD LLDTLEDNRE 610 620 630 640 650 660 WYQSKIPRSP SDLTNPERDG PDRFQFELTL EEAEEEDEEE EEEGEETALA KEALELPDTE 670 680 LLSPEAGPDP GDLPLDNQRT
	Isoform PDE4C4 (Sequence not available).		–	–
	Isoform PDE4C5 (Sequence not available).		–	–
	Isoform PDE4C6 (Sequence not available).		–	–
	Isoform PDE4C7 (Sequence not available).		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and functional expression in yeast of a human cAMP-specific phosphodiesterase subtype (PDE IV-C)." Engels P., Sullivan M., Mueller T., Luebbert H. FEBS Lett. 358:305-310(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE4C1). Tissue: Substantia nigra.
[2]	"Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND." Sullivan M., Olsen A.S., Houslay M.D. Cell. Signal. 11:735-742(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS PDE4C1; PDE4C2 AND PDE4C3).
[3]	"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 PDE4C1). Tissue: Tongue.
[4]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs." Bolger G., Michaeli T., Martins T., St John T., Steiner B., Rodgers L., Riggs M., Wigler M., Ferguson K. Mol. Cell. Biol. 13:6558-6571(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 462-712.
[7]	"Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors." Wang H., Peng M.-S., Chen Y., Geng J., Robinson H., Houslay M.D., Cai J., Ke H. Biochem. J. 408:193-201(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 306-663 IN COMPLEX WITH METAL IONS, FUNCTION, COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z46632 mRNA. Translation: CAA86601.1.
AF157816 , AF157811, AF157814, AF157815 Genomic DNA. Translation: AAD47053.1.
AF157816 , AF157812, AF157814, AF157815 Genomic DNA. Translation: AAD47054.1.
AF157816, AF157814, AF157815 Genomic DNA. Translation: AAD47055.1.
AK095384 mRNA. Translation: BAG53036.1.
AC005759 Genomic DNA. Translation: AAC83047.1.
CH471106 Genomic DNA. Translation: EAW84677.1.
L20968 mRNA. Translation: AAA03591.1.

IPI

IPI00328206.
IPI00472785.
IPI01009877.

PIR

S71626.

RefSeq

NP_000914.2. NM_000923.4.
NP_001092288.1. NM_001098818.2.
NP_001092289.1. NM_001098819.2.

UniGene

Hs.132584.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LXU	model	-	A	306-649	[»]
2QYM	X-ray	1.90	A	306-663	[»]

ProteinModelPortal

Q08493.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000347689.

PTM databases

PhosphoSite

Q08493.

Polymorphism databases

DMDM

20141263.

Proteomic databases

PaxDb

Q08493.

PRIDE

Q08493.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262805; ENSP00000262805; ENSG00000105650.
ENST00000355502; ENSP00000347689; ENSG00000105650.
ENST00000447275; ENSP00000402091; ENSG00000105650.
ENST00000594465; ENSP00000470210; ENSG00000105650.
ENST00000594617; ENSP00000469696; ENSG00000105650.

GeneID

5143.

KEGG

hsa:5143.

UCSC

uc002nif.4. human.
uc002nii.4. human.

Organism-specific databases

CTD

5143.

GeneCards

GC19M018318.

HGNC

HGNC:8782. PDE4C.

MIM

600128. gene.

neXtProt

NX_Q08493.

PharmGKB

PA264.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG122287.

HOVERGEN

HBG108239.

InParanoid

Q08493.

KO

K01120.

OrthoDB

EOG4ZGPBT.

PhylomeDB

Q08493.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

UniPathway

UPA00762; UER00747.

Gene expression databases

ArrayExpress

Q08493.

Bgee

Q08493.

CleanEx

HS_PDE4C.

Genevestigator

Q08493.

GermOnline

ENSG00000105650. Homo sapiens.

Family and domain databases

Gene3D

1.10.1300.10. 1 hit.

InterPro

IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]

Pfam

PF00233. PDEase_I. 1 hit.
[Graphical view]

PRINTS

PR00387. PDIESTERASE1.

SMART

SM00471. HDc. 1 hit.
[Graphical view]

PROSITE

PS00126. PDEASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q08493.

ChEMBL

CHEMBL291.

DrugBank

DB00651. Dyphylline.

EvolutionaryTrace

Q08493.

GenomeRNAi

5143.

NextBio

19838.

SOURCE

Search...

Entry information

Entry name

PDE4C_HUMAN

Accession

Primary (citable) accession number: Q08493
Secondary accession number(s): B3KTC4 , Q9UN44, Q9UN45, Q9UN46, Q9UPJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	March 27, 2002
Last modified:	May 1, 2013
This is version 116 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.