P80365 (DHI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Corticosteroid 11-beta-dehydrogenase isozyme 2
EC=1.1.1.-

Alternative name(s):
11-beta-hydroxysteroid dehydrogenase type 2
Short name=11-DH2
Short name=11-beta-HSD2
11-beta-hydroxysteroid dehydrogenase type II
Short name=-HSD11 type II
NAD-dependent 11-beta-hydroxysteroid dehydrogenase
Short name=11-beta-HSD

Gene names

Name:	HSD11B2
Synonyms:	HSD11K

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

General annotation (Comments)

Function	Catalyzes the conversion of cortisol to the inactive metabolite cortisone. Modulates intracellular glucocorticoid levels, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids.
Catalytic activity	An 11-beta-hydroxysteroid + NAD+ = an 11-oxosteroid + NADH.
Enzyme regulation	Inhibited by glycyrrhetinic acid (derived from liquorice), carbenoloxone and 11-alpha-OH-progesterone By similarity.
Subunit structure	Interacts with ligand-free cytoplasmic NR3C2. Ref.12
Subcellular location	Microsome. Endoplasmic reticulum Ref.24.
Tissue specificity	Found in placenta, kidney, pancreas, prostate, ovary, small intestine and colon.
Involvement in disease	Apparent mineralocorticoid excess (AME) [MIM:218030]: An autosomal recessive form of low-renin hypertension. It is usually diagnosed within the first years of life and is characterized by polyuria and polydipsia, failure to thrive, hypernatremia, severe hypertension with low renin and aldosterone levels, profound hypokalemia with metabolic alkalosis, and most often nephrocalcinosis. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24
Miscellaneous	Consumption of large amounts of liquorice can lead to apparent mineralocorticoid excess and hypertension.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Biophysicochemical properties	Kinetic parameters: X. KM=26.1 nM for cortisol (Ref.23) Ref.23 Ref.24 KM=785 nM for cortisol (Ref.24) KM=77 nM for cortisterone Vmax=64.1 nmol/h/mg enzyme toward cortisterone Vmax=66 nmol/h/mg enzyme toward cortisol

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Microsome
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	female pregnancy Inferred from electronic annotation. Source: Compara glucocorticoid biosynthetic process Traceable author statement Ref.1. Source: ProtInc regulation of blood volume by renal aldosterone Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to food Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to insulin stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity Inferred from electronic annotation. Source: Compara NAD binding Inferred from electronic annotation. Source: Compara steroid binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 405	405	Corticosteroid 11-beta-dehydrogenase isozyme 2		PRO_0000054627
Regions
	Nucleotide binding	82 – 111	30	NAD By similarity
	Region	335 – 339	5	Essential for protein stability
Sites
	Active site	232	1	Proton acceptor By similarity
	Binding site	219	1	Substrate By similarity
Natural variations
	Natural variant	114 – 115	2	Missing in AME; reduces enzyme activity by at least 95%.		VAR_015634
	Natural variant	147	1	R → H. Corresponds to variant rs13306425 [ dbSNP | Ensembl ].		VAR_052317
	Natural variant	179	1	L → R in AME; abolishes enzyme activity. Ref.21		VAR_015635
	Natural variant	180	1	S → F in AME; reduces enzyme activity. Ref.21		VAR_015636
	Natural variant	186	1	R → C in AME. Ref.10 Ref.17		VAR_015637
	Natural variant	208	1	R → C in AME; reduces enzyme activity by at least 95%. Ref.10 Ref.14 Ref.17		VAR_006958
	Natural variant	208	1	R → H in AME; abolishes enzyme activity. Ref.15 Ref.21		VAR_015638
	Natural variant	213	1	R → C in AME; reduces enzyme activity by ca. 90%. Ref.14 Ref.18 Ref.20		VAR_006959
	Natural variant	223	1	D → N in AME; reduces enzyme activity to about 6% of wild type. Ref.23		VAR_066514
	Natural variant	227	1	P → L in hypertension; decreases affinity for cortisol. Ref.19		VAR_015639
	Natural variant	237	1	A → V in AME; reduces enzyme activity. Ref.21		VAR_015640
	Natural variant	244	1	D → N in AME; associated with R-250. Ref.17		VAR_015641
	Natural variant	250 – 251	2	LL → PS in AME; abolishes enzyme activity.		VAR_015643
	Natural variant	250	1	L → R in AME; associated with N-244. Ref.17		VAR_015642
	Natural variant	279	1	R → C in AME; decreases enzyme activity by ca. 33%. Ref.16		VAR_015644
	Natural variant	328	1	A → V in AME; abolishes enzyme activity. Ref.20 Ref.21		VAR_015645
	Natural variant	337 – 338	2	RY → H in AME; abolishes enzyme activity.		VAR_015647
	Natural variant	337	1	R → C in AME; decreased half-life from 21 to 4 hours compared to wild-type, probably due to degradation via the proteasomal pathway. Ref.13 Ref.17 Ref.24		VAR_066515
	Natural variant	338	1	Y → H in AME; abolishes enzyme activity; decreased half-life from 21 to 3 hours compared to wild-type, probably due to degradation via the proteasomal pathway. Ref.24		VAR_015646
Experimental info
	Mutagenesis	115	1	E → K or Q: Abolishes cofactor specificity. Ref.22
	Mutagenesis	335	1	R → A or Q: Reduced enzyme activity. Ref.24
	Mutagenesis	335	1	R → K: No effect on enzyme activity. Ref.24
	Mutagenesis	336	1	R → A or Q: Almost complete loss of enzyme activity. Ref.24
	Mutagenesis	336	1	R → K: Reduced enzyme activity. Ref.24
	Mutagenesis	337	1	R → A or Q: Almost complete loss of enzyme activity. Ref.24
	Mutagenesis	337	1	R → K: Reduced enzyme activity. Ref.24
	Mutagenesis	338	1	Y → F or A: Complete loss of enzyme activity. Ref.24
	Mutagenesis	339	1	Y → A, F or H: Reduced enzyme activity. Ref.24
	Sequence conflict	148	1	V → F in AAB48544. Ref.2
	Sequence conflict	148	1	V → L in AAA91969. Ref.1
	Sequence conflict	350	1	I → T in AAH64536. Ref.7
	Sequence conflict	392	1	D → G in AAH36780. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P80365 [UniParc]. Last modified April 30, 2003. Version 2. Checksum: 4AB269E269982D24	FASTA	405	44,127
	10 20 30 40 50 60 MERWPWPSGG AWLLVAARAL LQLLRSDLRL GRPLLAALAL LAALDWLCQR LLPPPAALAV 70 80 90 100 110 120 LAAAGWIALS RLARPQRLPV ATRAVLITGC DSGFGKETAK KLDSMGFTVL ATVLELNSPG 130 140 150 160 170 180 AIELRTCCSP RLRLLQMDLT KPGDISRVLE FTKAHTTSTG LWGLVNNAGH NEVVADAELS 190 200 210 220 230 240 PVATFRSCME VNFFGALELT KGLLPLLRSS RGRIVTVGSP AGDMPYPCLG AYGTSKAAVA 250 260 270 280 290 300 LLMDTFSCEL LPWGVKVSII QPGCFKTESV RNVGQWEKRK QLLLANLPQE LLQAYGKDYI 310 320 330 340 350 360 EHLHGQFLHS LRLAMSDLTP VVDAITDALL AARPRRRYYP GQGLGLMYFI HYYLPEGLRR 370 380 390 400 RFLQAFFISH CLPRALQPGQ PGTTPPQDAA QDPNLSPGPS PAVAR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and tissue distribution of the human 11 beta-hydroxysteroid dehydrogenase type 2 enzyme." Albiston A.L., Obeyesekere V.R., Smith R.E., Krozowski Z.S. Mol. Cell. Endocrinol. 105:R11-R17(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"Gene structure and chromosomal localization of the human HSD11K gene encoding the kidney (type 2) isozyme of 11 beta-hydroxysteroid dehydrogenase." Agarwal A.K., Rogerson F.M., Mune T., White P.C. Genomics 29:195-199(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Kidney.
[3]	"Cloning and production of antisera to human placental 11 beta-hydroxysteroid dehydrogenase type 2." Brown R.W., Chapman K.E., Kotelevtsev Y., Yau J.L., Lindsay R.S., Brett L., Leckie C., Murad P., Lyons V., Mullins J.J., Edwards C.R.W., Seckl J.R. Biochem. J. 313:1007-1017(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[4]	SeattleSNPs variation discovery resource Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [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].
[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: Ovary.
[8]	"Purification of 11 beta-hydroxysteroid dehydrogenase type 2 from human placenta utilizing a novel affinity labelling technique." Brown R.W., Chapman K.E., Murad P., Edwards C.R., Seckl J.R. Biochem. J. 313:997-1005(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-24; 77-84; 102-112; 134-154; 191-198; 214-227; 229-235; 256-266; 272-278 AND 375-401. Tissue: Placenta.
[9]	"Human hydroxysteroid dehydrogenase type 2 HSD11B2." Amin H.K., Hoeppner W. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-221.
[10]	"Several homozygous mutations in the gene for 11 beta-hydroxysteroid dehydrogenase type 2 in patients with apparent mineralocorticoid excess." Wilson R.C., Harbison M.D., Krozowski Z.S., Funder J.W., Shackleton C.H.L., Hanauske-Abel H.M., Wei J.-Q., Hertecant J., Moran A., Neiberger R.E., Balfe J.W., Fattah A., Daneman D., Licholai T., New M.I. J. Clin. Endocrinol. Metab. 80:3145-3150(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-211; 235-264 AND 325-354, VARIANTS AME CYS-186; CYS-208; 250-PRO-SER-251 AND 337-ARG-TYR-338 DELINS HIS.
[11]	"Mineralocorticoid activity of liquorice: 11-beta-hydroxysteroid dehydrogenase deficiency comes of age." Stewart P.M., Wallace A.M., Valentino R., Burt D., Shackleton C.H.L., Edwards C.R.W. Lancet 2:821-824(1987) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[12]	"The intracellular localization of the mineralocorticoid receptor is regulated by 11beta-hydroxysteroid dehydrogenase type 2." Odermatt A., Arnold P., Frey F.J. J. Biol. Chem. 276:28484-28492(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NR3C2.
[13]	"A mutation in the HSD11B2 gene in a family with apparent mineralocorticoid excess." Wilson R.C., Krozowski Z.S., Li K., Obeyesekere V.R., Razzaghy-Azar M., Harbison M.D., Wei J.-Q., Shackleton C.H.L., Funder J.W., New M.I. J. Clin. Endocrinol. Metab. 80:2263-2266(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AME CYS-337.
[14]	"Human hypertension caused by mutations in the kidney isozyme of 11 beta-hydroxysteroid dehydrogenase." Mune T., Rogerson F.M., Nikkilae H., Agarwal A.K., White P.C. Nat. Genet. 10:394-399(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS AME CYS-208; CYS-213; 250-PRO-SER-251 AND 337-ARG-TYR-338 DELINS HIS.
[15]	"A new compound heterozygous mutation in the 11 beta-hydroxysteroid dehydrogenase type 2 gene in a case of apparent mineralocorticoid excess." Kitanaka S., Katsumata N., Tanae A., Hibi I., Takeyama K., Fuse H., Kato S., Tanaka T. J. Clin. Endocrinol. Metab. 82:4054-4058(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS AME HIS-208 AND 337-ARG-TYR-338 DELINS HIS.
[16]	"Molecular basis for hypertension in the 'type II variant' of apparent mineralocorticoid excess." Li A., Tedde R., Krozowski Z.S., Pala A., Li K.X.Z., Shackleton C.H.L., Mantero F., Palermo M., Stewart P.M. Am. J. Hum. Genet. 63:370-379(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT AME CYS-279.
[17]	"Examination of genotype and phenotype relationships in 14 patients with apparent mineralocorticoid excess." Dave-Sharma S., Wilson R.C., Harbison M.D., Newfield R., Azar M.R., Krozowski Z.S., Funder J.W., Shackleton C.H.L., Bradlow H.L., Wei J.-Q., Hertecant J., Moran A., Neiberger R.E., Balfe J.W., Fattah A., Daneman D., Akkurt H.I., De Santis C., New M.I. J. Clin. Endocrinol. Metab. 83:2244-2254(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AME CYS-186; CYS-208; ASN-244; ARG-250; 250-PRO-SER-251; CYS-337 AND 337-ARG-TYR-338 DELINS HIS.
[18]	"The codon 213 of the 11beta-hydroxysteroid dehydrogenase type 2 gene is a hot spot for mutations in apparent mineralocorticoid excess." Rogoff D., Smolenicka Z., Bergada I., Vallejo G., Barontini M., Heinrich J.J., Ferrari P. J. Clin. Endocrinol. Metab. 83:4391-4393(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT AME CYS-213.
[19]	"A genetic defect resulting in mild low-renin hypertension." Wilson R.C., Dave-Sharma S., Wei J.-Q., Obeyesekere V.R., Li K., Ferrari P., Krozowski Z.S., Shackleton C.H.L., Bradlow L., Wiens T., New M.I. Proc. Natl. Acad. Sci. U.S.A. 95:10200-10205(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT HYPERTENSION LEU-227.
[20]	"Genetic, biochemical, and clinical studies of patients with A328V or R213C mutations in 11betaHSD2 causing apparent mineralocorticoid excess." Morineau G., Marc J.-M., Boudi A., Galons H., Gourmelen M., Corvol P., Pascoe L., Fiet J. Hypertension 34:435-441(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS AME CYS-213 AND VAL-328.
[21]	"Mutants of 11beta-hydroxysteroid dehydrogenase (11-HSD2) with partial activity: improved correlations between genotype and biochemical phenotype in apparent mineralocorticoid excess." Nunez B.S., Rogerson F.M., Mune T., Igarashi Y., Nakagawa Y., Phillipov G., Moudgil A., Travis L.B., Palermo M., Shackleton C.H.L., White P.C. Hypertension 34:638-642(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS AME ARG-179; PHE-180; HIS-208; VAL-237 AND VAL-328.
[22]	"A mutation in the cofactor-binding domain of 11beta-hydroxysteroid dehydrogenase type 2 associated with mineralocorticoid hypertension." Odermatt A., Dick B., Arnold P., Zaehner T., Plueschke V., Deregibus M.N., Repetto H., Frey B.M., Frey F.J., Ferrari P. J. Clin. Endocrinol. Metab. 86:1247-1252(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT AME 114-LEU-GLU-115 DEL, MUTAGENESIS OF GLU-115.
[23]	"Two homozygous mutations in the 11 beta-hydroxysteroid dehydrogenase type 2 gene in a case of apparent mineralocorticoid excess." Carvajal C.A., Gonzalez A.A., Romero D.G., Gonzalez A., Mosso L.M., Lagos E.T., Hevia Mdel P., Rosati M.P., Perez-Acle T.O., Gomez-Sanchez C.E., Montero J.A., Fardella C.E. J. Clin. Endocrinol. Metab. 88:2501-2507(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AME ASN-223, BIOPHYSICOCHEMICAL PROPERTIES.
[24]	"Impaired protein stability of 11beta-hydroxysteroid dehydrogenase type 2: a novel mechanism of apparent mineralocorticoid excess." Atanasov A.G., Ignatova I.D., Nashev L.G., Dick B., Ferrari P., Frey F.J., Odermatt A. J. Am. Soc. Nephrol. 18:1262-1270(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AME CYS-337 AND HIS-338, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-335; ARG-336; ARG-337; TYR-338 AND TYR-339.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14631 mRNA. Translation: AAA91969.1. U27317 Genomic DNA. Translation: AAB48544.1. U26726 mRNA. Translation: AAC50356.1. EF694683 Genomic DNA. Translation: ABS29267.1. FJ515828 Genomic DNA. Translation: ACS13714.1. CH471092 Genomic DNA. Translation: EAW83134.1. BC036780 mRNA. Translation: AAH36780.1. BC064536 mRNA. Translation: AAH64536.1. AY046280 Genomic DNA. Translation: AAK91586.1.
IPI	IPI00300050.
PIR	S62789.
RefSeq	NP_000187.3. NM_000196.3.
UniGene	Hs.1376.
3D structure databases
ProteinModelPortal	P80365.
ModBase	Search...
PTM databases
PhosphoSite	P80365.
Polymorphism databases
DMDM	30316367.
Proteomic databases
PaxDb	P80365.
PRIDE	P80365.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000326152; ENSP00000316786; ENSG00000176387.
GeneID	3291.
KEGG	hsa:3291.
UCSC	uc002etd.3. human.
Organism-specific databases
CTD	3291.
GeneCards	GC16P067465.
HGNC	HGNC:5209. HSD11B2.
HPA	CAB032443.
MIM	218030. phenotype. 614232. gene.
neXtProt	NX_P80365.
Orphanet	320. Apparent mineralocorticoid excess.
PharmGKB	PA29477.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1028.
HOVERGEN	HBG005482.
InParanoid	P80365.
KO	K00071.
OMA	CFKTESV.
OrthoDB	EOG49CQ89.
PhylomeDB	P80365.
Enzyme and pathway databases
BRENDA	1.1.1.146. 2681.
Gene expression databases
Bgee	P80365.
CleanEx	HS_HSD11B2.
Genevestigator	P80365.
GermOnline	ENSG00000176387. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P80365.
ChEMBL	CHEMBL3746.
ChiTaRS	HSD11B2. human.
DrugBank	DB00157. NADH.
GenomeRNAi	3291.
NextBio	13055.
SOURCE	Search...

Entry information

Entry name

DHI2_HUMAN

Accession

Primary (citable) accession number: P80365
Secondary accession number(s): A7LB28 , C5HTY7, Q13194, Q6P2G9, Q8N439, Q96QN8, Q9UC50, Q9UC51, Q9UCW5, Q9UCW6, Q9UCW7, Q9UCW8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	April 30, 2003
Last modified:	May 1, 2013
This is version 126 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.