3-beta-hydroxy-Delta(5)-steroid dehydrogenase
     (EC 1.1.1.145)
     (3-beta-hydroxy-5-ene steroid dehydrogenase)
     (Progesterone reductase)
Steroid Delta-isomerase
     (EC 5.3.3.1)
     (Delta-5-3-ketosteroid isomerase)

Gene name

	Name:	HSD3B2
	Synonyms:	HSDB3B

From

Homo sapiens (Human)

[TaxID: 9606]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Adrenal gland; PubMed=1944309 [NCBI, ExPASy, EBI, Israel, Japan] Rheaume E., Lachance Y., Zhao H.-F., Breton N., Dumont M., de Launoit Y., Trudel C., Luu-The V., Simard J., Labrie F.; "Structure and expression of a new complementary DNA encoding the almost exclusive 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4-isomerase in human adrenals and gonads."; Mol. Endocrinol. 5:1147-1157(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1741954 [NCBI, ExPASy, EBI, Israel, Japan] Lachance Y., Luu-The V., Verreault H., Dumont M., Rheaume E., Leblanc G., Labrie F.; "Structure of the human type II 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD) gene: adrenal and gonadal specificity."; DNA Cell Biol. 10:701-711(1991).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Small intestine; Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan] Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; "The DNA sequence and biological annotation of human chromosome 1."; Nature 441:315-321(2006).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-205. DOI=10.1038/ng0792-239; PubMed=1363812 [NCBI, ExPASy, EBI, Israel, Japan] Rheaume E., Simard J., Morel Y., Mebarki F., Zachmann M., Forest M.G., New M.I., Labrie F.; "Congenital adrenal hyperplasia due to point mutations in the type II 3 beta-hydroxysteroid dehydrogenase gene."; Nat. Genet. 1:239-245(1992).
[7]	POSSIBLE INVOLVEMENT IN INSULIN-RESISTANT POLYCYSTIC OVARY SYNDROME. DOI=10.1210/jc.2003-030934; PubMed=14764797 [NCBI, ExPASy, EBI, Israel, Japan] Carbunaru G., Prasad P., Scoccia B., Shea P., Hopwood N., Ziai F., Chang Y.T., Myers S.E., Mason J.I., Pang S.; "The hormonal phenotype of nonclassic 3 beta-hydroxysteroid dehydrogenase (HSD3B) deficiency in hyperandrogenic females is associated with insulin-resistant polycystic ovary syndrome and is not a variant of inherited HSD3B2 deficiency."; J. Clin. Endocrinol. Metab. 89:783-794(2004).
[8]	VARIANTS AH2 LYS-142; PRO-245 AND ASN-253. DOI=10.1210/me.7.5.716; PubMed=8316254 [NCBI, ExPASy, EBI, Israel, Japan] Simard J., Rheaume E., Sanchez R., Laflamme N., de Launoit Y., Luu-The V., van Seters A.P., Gordon R.D., Bettendorf M., Heinrich U., Moshang T., New M.I., Labrie F.; "Molecular basis of congenital adrenal hyperplasia due to 3 beta-hydroxysteroid dehydrogenase deficiency."; Mol. Endocrinol. 7:716-728(1993).
[9]	VARIANTS AH2 TRP-108 AND LEU-186. DOI=10.1093/hmg/3.9.1639; PubMed=7833923 [NCBI, ExPASy, EBI, Israel, Japan] Sanchez R., Mebarki F., Rheaume E., Laflamme N., Forest M.G., Bey-Omar F., David M., Morel Y., Labrie F., Simard J.; "Functional characterization of the novel L108W and P186L mutations detected in the type II 3 beta-hydroxysteroid dehydrogenase gene of a male pseudohermaphrodite with congenital adrenal hyperplasia."; Hum. Mol. Genet. 3:1639-1645(1994).
[10]	VARIANT AH2 ASP-254. DOI=10.1210/jc.78.3.561; PubMed=8126127 [NCBI, ExPASy, EBI, Israel, Japan] Sanchez R., Rheaume E., Laflamme N., Rosenfield R.L., Labrie F., Simard J.; "Detection and functional characterization of the novel missense mutation Y254D in type II 3 beta-hydroxysteroid dehydrogenase (3 beta HSD) gene of a female patient with nonsalt-losing 3 beta HSD deficiency."; J. Clin. Endocrinol. Metab. 78:561-567(1994).
[11]	VARIANT AH2 ARG-129. DOI=10.1210/jc.79.4.1012; PubMed=7962268 [NCBI, ExPASy, EBI, Israel, Japan] Rheaume E., Sanchez R., Simard J., Chang Y.T., Wang J., Pang S., Labrie F.; "Molecular basis of congenital adrenal hyperplasia in two siblings with classical nonsalt-losing 3 beta-hydroxysteroid dehydrogenase deficiency."; J. Clin. Endocrinol. Metab. 79:1012-1018(1994).
[12]	VARIANT AH2 THR-82. PubMed=8185809 [NCBI, ExPASy, EBI, Israel, Japan] Mendonca B.B., Russell A.J., Vasconcelos-Leite M., Arnhold I.J., Bloise W., Wajchenberg B.L., Nicolau W., Sutcliffe R.G., Wallace A.M.; "Mutation in 3 beta-hydroxysteroid dehydrogenase type II associated with pseudohermaphroditism in males and premature pubarche or cryptic expression in females."; J. Mol. Endocrinol. 12:119-122(1994).
[13]	VARIANT AH2 ARG-173. PubMed=8060486 [NCBI, ExPASy, EBI, Israel, Japan] Russell A.J., Wallace A.M., Forest M.G., Donaldson M.D., Edwards C.R., Sutcliffe R.G.; "Mutation in the human gene for 3 beta-hydroxysteroid dehydrogenase type II leading to male pseudohermaphroditism without salt loss."; J. Mol. Endocrinol. 12:225-237(1994).
[14]	VARIANT AH2 ASP-15. DOI=10.1021/bi00009a020; PubMed=7893703 [NCBI, ExPASy, EBI, Israel, Japan] Rheaume E., Sanchez R., Mebarki F., Gagnon E., Carel J.-C., Chaussain J.-L., Morel Y., Labrie F., Simard J.; "Identification and characterization of the G15D mutation found in a male patient with 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD) deficiency: alteration of the putative NAD-binding domain of type II 3 beta-HSD."; Biochemistry 34:2893-2900(1995).
[15]	VARIANT AH2 PRO-205. DOI=10.1093/hmg/4.4.745; PubMed=7633426 [NCBI, ExPASy, EBI, Israel, Japan] Katsumata N., Tanae A., Yasunaga T., Horikawa R., Tanaka T., Hibi I.; "A novel missense mutation in the type II 3 beta-hydroxysteroid dehydrogenase gene in a family with classical salt-wasting congenital adrenal hyperplasia due to 3 beta-hydroxysteroid dehydrogenase deficiency."; Hum. Mol. Genet. 4:745-746(1995).
[16]	VARIANT AH2 ARG-259. DOI=10.1093/hmg/4.5.969; PubMed=7633460 [NCBI, ExPASy, EBI, Israel, Japan] Tajima T., Fujieda K., Nakae J., Shinohara N., Yoshimoto M., Baba T., Kinoshita E., Igarashi Y., Oomura T.; "Molecular analysis of type II 3 beta-hydroxysteroid dehydrogenase gene in Japanese patients with classical 3 beta-hydroxysteroid dehydrogenase deficiency."; Hum. Mol. Genet. 4:969-971(1995).
[17]	VARIANT AH2 SER-100. DOI=10.1210/jc.80.7.2127; PubMed=7608265 [NCBI, ExPASy, EBI, Israel, Japan] Mebarki F., Sanchez R., Rheaume E., Laflamme N., Simard J., Forest M.G., Bey-Omar F., David M., Labrie F., Morel Y.; "Nonsalt-losing male pseudohermaphroditism due to the novel homozygous N100S mutation in the type II 3 beta-hydroxysteroid dehydrogenase gene."; J. Clin. Endocrinol. Metab. 80:2127-2134(1995).
[18]	VARIANT AH2 SER-236. DOI=10.1006/mgme.1998.2715; PubMed=9719627 [NCBI, ExPASy, EBI, Israel, Japan] Nayak S., Lee P.A., Witchel S.F.; "Variants of the type II 3beta-hydroxysteroid dehydrogenase gene in children with premature pubic hair and hyperandrogenic adolescents."; Mol. Genet. Metab. 64:184-192(1998).
[19]	VARIANTS AH2. DOI=10.1210/jc.84.12.4410; PubMed=10599696 [NCBI, ExPASy, EBI, Israel, Japan] Moisan A.M., Ricketts M.L., Tardy V., Desrochers M., Mebarki F., Chaussain J.-L., Cabrol S., Raux-Demay M.C., Forest M.G., Sippell W.G., Peter M., Morel Y., Simard J.; "New insight into the molecular basis of 3beta-hydroxysteroid dehydrogenase deficiency: identification of eight mutations in the HSD3B2 gene in eleven patients from seven new families and comparison of the functional properties of twenty-five mutant enzymes."; J. Clin. Endocrinol. Metab. 84:4410-4425(1999).
[20]	VARIANTS AH2 ARG-129; GLN-222 AND MET-259. PubMed=10651755 [NCBI, ExPASy, EBI, Israel, Japan] Marui S., Castro M., Latronico A.C., Elias L.L., Arnhold I.J., Moreira A.C., Mendonca B.B.; "Mutations in the type II 3beta-hydroxysteroid dehydrogenase (HSD3B2) gene can cause premature pubarche in girls."; Clin. Endocrinol. (Oxf.) 52:67-75(2000).
[21]	VARIANT AH2 GLU-10. DOI=10.1210/jc.85.5.1968; PubMed=10843183 [NCBI, ExPASy, EBI, Israel, Japan] Alos N., Moisan A.M., Ward L., Desrochers M., Legault L., Leboeuf G., van Vliet G., Simard J.; "A novel A10E homozygous mutation in the HSD3B2 gene causing severe salt-wasting 3beta-hydroxysteroid dehydrogenase deficiency in 46,XX and 46,XY French-Canadians: evaluation of gonadal function after puberty."; J. Clin. Endocrinol. Metab. 85:1968-1974(2000).
[22]	VARIANTS AH2 LYS-142 AND THR-222. DOI=10.1210/jc.87.6.2556; PubMed=12050213 [NCBI, ExPASy, EBI, Israel, Japan] Pang S., Wang W., Rich B., David R., Chang Y.T., Carbunaru G., Myers S.E., Howie A.F., Smillie K.J., Mason J.I.; "A novel nonstop mutation in the stop codon and a novel missense mutation in the type II 3-beta-hydroxysteroid dehydrogenase (3-beta-HSD) gene causing, respectively, nonclassic and classic 3-beta-HSD deficiency congenital adrenal hyperplasia."; J. Clin. Endocrinol. Metab. 87:2556-2563(2002).

Comments

FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids.
CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta⁵-steroid + NAD⁺ = a 3-oxo-Delta⁵-steroid + NADH.
CATALYTIC ACTIVITY: A 3-oxo-Delta⁵-steroid = a 3-oxo-Delta⁴-steroid.
PATHWAY: Lipid metabolism; steroid biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
TISSUE SPECIFICITY: Adrenal glands, testes and ovaries.
DISEASE: Defects in HSD3B2 are the cause of adrenal hyperplasia type 2 (AH2) [MIM:201810]. AH2 is a form of congenital adrenal hyperplasia, a common recessive disease due to defective synthesis of cortisol. Congenital adrenal hyperplasia is characterized by androgen excess leading to ambiguous genitalia in affected females, rapid somatic growth during childhood in both sexes with premature closure of the epiphyses and short adult stature. Four clinical types: 'salt wasting' (SW, the most severe type), 'simple virilizing' (SV, less severely affected patients), with normal aldosterone biosynthesis, 'non-classic form' or late onset (NC or LOAH), and 'cryptic' (asymptomatic). In AH2, virilization is much less marked or does not occur. AH2 is frequently lethal in early life.
DISEASE: Mild HSD3B2 deficiency in hyperandrogenic females is associated with characteristic traits of polycystic ovary syndrome, such as insulin resistance and luteinizing hormon hypersecretion.
SIMILARITY: Belongs to the 3-beta-HSD family.
SEQUENCE CAUTION:
- Sequence=AAC60600.1; Type=Frameshift; Positions=186; Note=The frameshift is caused by a single nucleotide insertion which is found in AH2
WEB RESOURCE: Name=GeneDis; Note=Congenital adrenal hyperplasia website; URL="http://life2.tau.ac.il/GeneDis/Tables/CAH/cah.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=HSD3B2";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M67466; AAA36016.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M77144; AAA36014.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222997; BAD96717.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL359553; CAC19799.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC038419; AAH38419.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S60309; AAC60599.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S60310; AAC60600.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A39488; DEHUH2.

NP_000189.1; -.

3D structure databases

ModBase

P26439.

Enzyme and pathway databases

Reactome

REACT_602; Lipid and lipoprotein metabolism.

Organism-specific databases

H-InvDB

HIX0023638; -.

HGNC

HGNC:5218; HSD3B2.

GeneLynx

HSD3B2; Homo sapiens.

GenAtlas

HSD3B2.

MIM

201810; gene+phenotype. [NCBI / EBI]

Orphanet

418; Adrenal hyperplasia, congenital.
3185; Stein-Leventhal syndrome.

PharmGKB

PA29487; -.

GeneCards

P26439.

Gene expression databases

ArrayExpress

P26439; -.

CleanEx

HS_HSD3B2; -.

GermOnline

ENSG00000203859; Homo sapiens.

Ontologies

GO:0016021;	Cellular component: integral to membrane (non-traceable author statement from UniProtKB).
GO:0005792;	Cellular component: microsome (inferred from sequence or structural similarity from UniProtKB).
GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0005758;	Cellular component: mitochondrial intermembrane space (inferred from sequence or structural similarity from UniProtKB).
GO:0030868;	Cellular component: smooth endoplasmic reticulum membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0003854;	Molecular function: 3-beta-hydroxy-delta5-steroid dehydrogenase activity (inferred from direct assay from UniProtKB).
GO:0004769;	Molecular function: steroid delta-isomerase activity (inferred from direct assay from UniProtKB).
GO:0006694;	Biological process: steroid biosynthetic process (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR002225; 3Beta_OHSteriod_DHase/Estase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01073; 3Beta_HSD; 1.
Pfam graphical view of domain structure.

BLOCKS

P26439.

Genome annotation databases

Ensembl

ENSG00000203859; Homo sapiens. [Contig view]

GeneID

3284; -.

KEGG

hsa:3284; -.

Other

DrugBank

DB00157; NADH.
DB01108; Trilostane.

SOURCE

HSD3B2; Homo sapiens.

ProtoNet

P26439.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Congenital adrenal hyperplasia; Disease mutation; Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; Polymorphism; Steroidogenesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 372`	`371`	`3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2.`	`PRO_0000087775`
`TRANSMEM`	`287 307`	`21`	`Potential.`
`VARIANT`	`10 10`	`1`	`A -> E (in AH2; activity abolished).`	`VAR_010517`
`VARIANT`	`10 10`	`1`	`A -> V (in AH2; nonsalt-wasting form).`	`VAR_010518`
`VARIANT`	`15 15`	`1`	`G -> D (in AH2; activity abolished).`	`VAR_010519`
`VARIANT`	`82 82`	`1`	`A -> T (in AH2).`	`VAR_010520`
`VARIANT`	`94 94`	`1`	`E -> Q (in dbSNP:rs6211 [NCBI]).`	`VAR_014818`
`VARIANT`	`100 100`	`1`	`N -> S (in AH2; nonsalt-wasting form).`	`VAR_010521`
`VARIANT`	`108 108`	`1`	`L -> W (in AH2; activity abolished).`	`VAR_010522`
`VARIANT`	`129 129`	`1`	`G -> R (in AH2; nonsalt-wasting form).`	`VAR_010523`
`VARIANT`	`142 142`	`1`	`E -> K (in AH2; activity abolished).`	`VAR_000006`
`VARIANT`	`155 155`	`1`	`P -> L (in AH2; nonsalt-wasting form).`	`VAR_010524`
`VARIANT`	`167 167`	`1`	`A -> V (in AH2; late onset; almost normal activity).`	`VAR_010525`
`VARIANT`	`173 173`	`1`	`L -> R (in AH2; nonsalt-wasting form).`	`VAR_010526`
`VARIANT`	`186 186`	`1`	`P -> L (in AH2; activity abolished).`	`VAR_010527`
`VARIANT`	`205 205`	`1`	`L -> P (in AH2).`	`VAR_000007`
`VARIANT`	`213 213`	`1`	`S -> G (in AH2; late onset; partial loss of activity).`	`VAR_010528`
`VARIANT`	`216 216`	`1`	`K -> E (in AH2; late onset; partial loss of activity).`	`VAR_010529`
`VARIANT`	`222 222`	`1`	`P -> H (in AH2; nonsalt-wasting form; activity abolished).`	`VAR_010530`
`VARIANT`	`222 222`	`1`	`P -> Q (in AH2; activity abolished).`	`VAR_010531`
`VARIANT`	`222 222`	`1`	`P -> T (in AH2).`	`VAR_015411`
`VARIANT`	`231 238`	`8`	`Missing (in AH2; activity abolished).`	`VAR_010532`
`VARIANT`	`236 236`	`1`	`L -> S (in AH2; mild; 100% of activity).`	`VAR_010533`
`VARIANT`	`245 245`	`1`	`A -> P (in AH2; loss of 88% of activity).`	`VAR_000008`
`VARIANT`	`253 253`	`1`	`Y -> N (in AH2; activity abolished).`	`VAR_000009`
`VARIANT`	`254 254`	`1`	`Y -> D (in AH2; activity abolished).`	`VAR_000010`
`VARIANT`	`259 259`	`1`	`T -> M (in AH2; activity abolished).`	`VAR_010534`
`VARIANT`	`259 259`	`1`	`T -> R (in AH2; activity abolished).`	`VAR_000011`
`VARIANT`	`294 294`	`1`	`G -> V (in AH2; nonsalt-wasting form; activity abolished).`	`VAR_010535`
`CONFLICT`	`232 232`		`H -> L (in Ref. 3; BAD96717).`

Sequence information

Length: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 42052 Da [This is the MW of the unprocessed precursor]

CRC64: 8E0D933488988451 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGWSCLVTGA GGLLGQRIVR LLVEEKELKE IRALDKAFRP ELREEFSKLQ NRTKLTVLEG 

        70         80         90        100        110        120 
DILDEPFLKR ACQDVSVVIH TACIIDVFGV THRESIMNVN VKGTQLLLEA CVQASVPVFI 

       130        140        150        160        170        180 
YTSSIEVAGP NSYKEIIQNG HEEEPLENTW PTPYPYSKKL AEKAVLAANG WNLKNGDTLY 

       190        200        210        220        230        240 
TCALRPTYIY GEGGPFLSAS INEALNNNGI LSSVGKFSTV NPVYVGNVAW AHILALRALR 

       250        260        270        280        290        300 
DPKKAPSVRG QFYYISDDTP HQSYDNLNYI LSKEFGLRLD SRWSLPLTLM YWIGFLLEVV 

       310        320        330        340        350        360 
SFLLSPIYSY QPPFNRHTVT LSNSVFTFSY KKAQRDLAYK PLYSWEEAKQ KTVEWVGSLV 

       370 
DRHKETLKSK TQ

P26439 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools