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UniProtKB/Swiss-Prot entry P42330

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AK1C3_HUMAN
Primary accession number P42330
Secondary accession numbers Q5T2L1 Q96DJ1 Q96KI8 Q99530 Q9UCX1 Q9UII3 Q9UKL9
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on May 10, 2002 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 95)
Name and origin of the protein
Protein name Aldo-keto reductase family 1 member C3
Synonyms EC 1.-.-.-
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
EC 1.3.1.20
3-alpha-hydroxysteroid dehydrogenase type 2
3-alpha-HSD type 2
EC 1.1.1.213
3-alpha-HSD type II, brain
Testosterone 17-beta-dehydrogenase 5
EC 1.1.1.63
EC 1.1.1.64
17-beta-hydroxysteroid dehydrogenase type 5
17-beta-HSD 5
Prostaglandin F synthase
PGFS
EC 1.1.1.188
Dihydrodiol dehydrogenase type I
Dihydrodiol dehydrogenase 3
DD-3
DD3
Chlordecone reductase homolog HAKRb
HA1753
Gene name
Name: AKR1C3
Synonyms: DDH1, HSD17B5, KIAA0119, PGFS
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], AND VARIANT ILE-175.
TISSUE=Liver;
DOI=10.1016/0960-0760(93)90308-J; PubMed=8274401 [NCBI, ExPASy, EBI, Israel, Japan]
Qin K.-N., New M.I., Cheng K.-C.;
"Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase.";
J. Steroid Biochem. Mol. Biol. 46:673-679(1993).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, TISSUE SPECIFICITY, AND VARIANT ILE-175.
DOI=10.1074/jbc.270.34.20162; PubMed=7650035 [NCBI, ExPASy, EBI, Israel, Japan]
Khanna M., Qin K.-N., Wang R.W., Cheng K.-C.;
"Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases.";
J. Biol. Chem. 270:20162-20168(1995).
[3]
 NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-5.
TISSUE=Liver;
DOI=10.1016/0960-0760(95)00019-V; PubMed=7626489 [NCBI, ExPASy, EBI, Israel, Japan]
Khanna M., Qin K.-N., Cheng K.-C.;
"Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans.";
J. Steroid Biochem. Mol. Biol. 53:41-46(1995).
[4]
 NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
TISSUE=Prostate;
DOI=10.1210/me.11.13.1971; PubMed=9415401 [NCBI, ExPASy, EBI, Israel, Japan]
Lin H.-K., Jez J.M., Schlegel B.P., Peehl D.M., Pachter J.A., Penning T.M.;
"Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution.";
Mol. Endocrinol. 11:1971-1984(1997).
[5]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
TISSUE=Lung;
DOI=10.1016/S0014-5793(99)01551-3; PubMed=10622721 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki-Yamamoto T., Nishizawa M., Fukui M., Okuda-Ashitaka E., Nakajima T., Ito S., Watanabe K.;
"cDNA cloning, expression and characterization of human prostaglandin F synthase.";
FEBS Lett. 462:335-340(1999).
[6]
 NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
TISSUE=Brain;
DOI=10.1073/pnas.96.23.13512; PubMed=10557352 [NCBI, ExPASy, EBI, Israel, Japan]
Griffin L.D., Mellon S.H.;
"Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 96:13512-13517(1999).
[7]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=10672042 [NCBI, ExPASy, EBI, Israel, Japan]
Nishizawa M., Nakajima T., Yasuda K., Kanzaki H., Sasaguri Y., Watanabe K., Ito S.;
"Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes.";
Genes Cells 5:111-125(2000).
[8]
 NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
TISSUE=Prostate;
DOI=10.1016/S0303-7207(00)00426-3; PubMed=11165022 [NCBI, ExPASy, EBI, Israel, Japan]
Penning T.M., Burczynski M.E., Jez J.M., Lin H.-K., Ma H., Moore M., Ratnam K., Palackal N.;
"Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3).";
Mol. Cell. Endocrinol. 171:137-149(2001).
[9]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
DOI=10.1093/dnares/2.1.37; PubMed=7788527 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[10]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-5.
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[11]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-5.
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[12]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-5.
TISSUE=Colon, and Urinary bladder;
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).
[13]
 CHARACTERIZATION, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT ILE-175, AND MUTAGENESIS OF LYS-75.
DOI=10.1210/en.140.2.568; PubMed=9927279 [NCBI, ExPASy, EBI, Israel, Japan]
Dufort I., Rheault P., Huang X.-F., Soucy P., Luu-The V.;
"Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase.";
Endocrinology 140:568-574(1999).
[14]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH PROSTAGLANDIN H(2); NADPH AND RUTIN.
DOI=10.1021/bi036046x; PubMed=14979715 [NCBI, ExPASy, EBI, Israel, Japan]
Komoto J., Yamada T., Watanabe K., Takusagawa F.;
"Crystal structure of human prostaglandin F synthase (AKR1C3).";
Biochemistry 43:2188-2198(2004).
[15]
 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FLUFENAMIC ACID AND INDOMETHACIN.
DOI=10.1158/0008-5472.CAN-03-2847; PubMed=14996743 [NCBI, ExPASy, EBI, Israel, Japan]
Lovering A.L., Ride J.P., Bunce C.M., Desmond J.C., Cummings S.M., White S.A.;
"Crystal structures of prostaglandin D(2) 11-ketoreductase (AKR1C3) in complex with the nonsteroidal anti-inflammatory drugs flufenamic acid and indomethacin.";
Cancer Res. 64:1802-1810(2004).
[16]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NADP AND DELTA4 -3 ANDROSTENE-3,17-DIONE, AND IMPORTANCE OF TRP-227 AND PHE-306 IN LIGAND RECOGNITION AND PRODUCT RELEASE.
DOI=10.1210/me.2004-0032; PubMed=15087468 [NCBI, ExPASy, EBI, Israel, Japan]
Qiu W., Zhou M., Labrie F., Lin S.-X.;
"Crystal structures of the multispecific 17beta-hydroxysteroid dehydrogenase type 5: critical androgen regulation in human peripheral tissues.";
Mol. Endocrinol. 18:1798-1807(2004).
Comments
  • FUNCTION: Catalyzes the conversion of aldehydes and ketones to alcohols. Catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta-PGF2 to PGD2. Functions as a bi-directional 3-alpha-, 17-beta- and 20-alpha HSD. Can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites. Preferentially transforms androstenedione (4-dione) to testosterone.
  • CATALYTIC ACTIVITY: Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH.
  • CATALYTIC ACTIVITY: Androsterone + NAD(P)+ = 5-alpha-androstane-3,17-dione + NAD(P)H.
  • CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH.
  • CATALYTIC ACTIVITY: Testosterone + NAD+ = androst-4-ene-3,17-dione + NADH.
  • CATALYTIC ACTIVITY: Testosterone + NADP+ = androst-4-ene-3,17-dione + NADPH.
  • ENZYME REGULATION: Strongly inhibited by nonsteroidal anti-inflammatory drugs (NSAID) including flufenamic acid and indomethacin. Also inhibited by the flavinoid, rutin, and by selective serotonin inhibitors (SSRIs).
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=142.1 µM for progesterone;
    KM=2.37 µM for 5-alpha-dihydrotestosterone;
    KM=1.0 µM for androstanediol;
    Vmax=20.1 nmol/min/mg enzyme with progesterone as substrate;
    Vmax=1.8 nmol/min/mg enzyme with 5-alpha-dihydrotestosterone as substrate;
    Vmax=4.4 nmol/min/mg enzyme with androstanediol as substrate;
  • SUBCELLULAR LOCATION: Cytoplasm.
  • TISSUE SPECIFICITY: Expressed in many tissues including adrenal gland, brain, kidney, liver, lung, mammary gland, placenta, small intestine, colon, spleen, prostate and testis. The dominant HSD in prostate and mammary gland. In the prostate, higher levels in epithelial cells than in stromal cells. In the brain, expressed in medulla, spinal cord, frontotemporal lobes, thalamus, subthalamic nuclei and amygdala. Weaker expression in the hippocampus, substantia nigra and caudate.
  • SIMILARITY: Belongs to the aldo/keto reductase family.
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
S68288; AAD14011.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L43839; AAB41916.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L43831; AAB41916.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L43832; AAB41916.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L43833; AAB41916.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L43834; AAB41916.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L43835; AAB41916.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L43836; AAB41916.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L43837; AAB41916.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L43838; AAB41916.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB018580; BAA88488.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB028065; BAA88489.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF149416; AAF07272.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB032157; BAA92892.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D17793; BAA04619.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007286; AAP35950.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391427; CAI14729.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001479; AAH01479.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019230; AAH19230.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B57407; B57407.
I73674; I73674.
RefSeq NP_003730.4; -.
UniGene Hs.78183
3D structure databases
PDB
1RY0; X-ray; 1.69 A; A/B=1-323.[ExPASy / RCSB / EBI]
1RY8; X-ray; 1.69 A; A/B=1-323.[ExPASy / RCSB / EBI]
1S1P; X-ray; 1.20 A; A=1-323.[ExPASy / RCSB / EBI]
1S1R; X-ray; 2.00 A; A=1-323.[ExPASy / RCSB / EBI]
1S2A; X-ray; 1.70 A; A=1-323.[ExPASy / RCSB / EBI]
1S2C; X-ray; 1.80 A; A=1-323.[ExPASy / RCSB / EBI]
1XF0; X-ray; 2.00 A; A=1-323.[ExPASy / RCSB / EBI]
1ZQ5; X-ray; 1.30 A; A=1-323.[ExPASy / RCSB / EBI]
2F38; X-ray; 2.00 A; A=1-323.[ExPASy / RCSB / EBI]
2FGB; X-ray; 1.35 A; A=1-323.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1RY0; -.
1RY8; -.
1S1P; -.
1S1R; -.
1S2A; -.
1S2C; -.
1XF0; -.
1ZQ5; -.
2F38; -.
2FGB; -.
ModBase P42330.
Protein-protein interaction databases
IntAct P42330; -.
PTM databases
PhosphoSite P42330; -.
2D gel databases
DOSAC-COBS-2DPAGE P42330; -.
Organism-specific databases
HGNC HGNC:386; AKR1C3.
GenAtlas AKR1C3.
HPA CAB010874; -.
MIM 603966; gene. [NCBI / EBI]
PharmGKB PA24679; -.
GeneCards P42330.
HUGE KIAA0119.
Gene expression databases
ArrayExpress P42330; -.
CleanEx HS_AKR1C3; -.
GermOnline ENSG00000196139; Homo sapiens.
Ontologies
GO
GO:0005622; Cellular component: intracellular (inferred from direct assay from LIFEdb).
GO:0004033; Molecular function: aldo-keto reductase activity (traceable author statement from UniProtKB).
GO:0055114; Biological process: oxidation reduction (traceable author statement from UniProtKB).
GO:0006693; Biological process: prostaglandin metabolic process (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001395; Aldo/ket_red.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.100; Aldo/ket_red; 1.
PANTHER PTHR11732; Aldo/ket_red; 1.
Pfam PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.
PRINTS PR00069; ALDKETRDTASE.
ProDom PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00798; ALDOKETO_REDUCTASE_1; 1.
PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.
BLOCKS P42330.
Genome annotation databases
Ensembl ENSG00000196139; Homo sapiens. [Contig view]
GeneID 8644; -.
KEGG hsa:8644; -.
Phylogenomic databases
HOVERGEN P42330; -.
Other
BindingDB P42330; -.
DrugBank DB01093; Dimethyl sulfoxide.
DB00157; NADH.
LinkHub P42330; -.
SOURCE AKR1C3; Homo sapiens.
ProtoNet P42330.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; NAD; NADP; Oxidoreductase; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   323  323     Aldo-keto reductase family 1 member C3. PRO_0000124638
NP_BIND   13    22  10     NADP (Potential). 
NP_BIND   217   280  64     NADP (By similarity). 
ACT_SITE   55    55        Proton donor (By similarity). 
BINDING   117   117        Substrate (By similarity). 
SITE   54    54  1     Important for substrate specificity (By similarity). 
SITE   84    84  1     Lowers pKa of active site Tyr (By similarity). 
SITE   227   227  1     Involved in ligand recognition and product release. 
SITE   306   306  1     Involved in ligand recognition and product release. 
VARIANT   5     5  1     Q -> H (in dbSNP:rs12529 [NCBI]). VAR_013288 [3D]
VARIANT   66    66  1     R -> Q (in dbSNP:rs35961894 [NCBI]). VAR_032767 [3D]
VARIANT   170   170  1     R -> C (in dbSNP:rs35575889 [NCBI]). VAR_032768 [3D]
VARIANT   175   175  1     M -> I (no effect on 17beta-HSD activity; dbSNP:rs1131132 [NCBI]). VAR_013289 [3D]
VARIANT   180   180  1     P -> S (in dbSNP:rs34186955 [NCBI]). VAR_032769 [3D]
MUTAGEN   75    75        K->E: No effect on 17beta-HSD activity. 
CONFLICT   3     3        S -> P (in Ref. 3). 
CONFLICT   6     6        Q -> K (in Ref. 3). 
CONFLICT   38    38        T -> S (in Ref. 6; AAF07272). 
CONFLICT   75    75        K -> E (in Ref. 1; AAD14011 and 3). 
CONFLICT   75    75        K -> M (in Ref. 2; AAB41916). 
CONFLICT   89    89        F -> S (in Ref. 6; AAF07272). 
CONFLICT   270   270        K -> R (in Ref. 6; AAF07272). 
STRAND   7     9  3      
STRAND   15    22  8      
HELIX   33    44  12      
STRAND   48    50  3      
HELIX   53    55  3      
HELIX   58    70  13      
HELIX   76    78  3      
STRAND   80    85  6      
HELIX   87    89  3      
HELIX   92    94  3      
HELIX   95   106  12      
STRAND   111   116  6      
HELIX   144   156  13      
STRAND   159   167  9      
HELIX   170   177  8      
STRAND   187   192  6      
HELIX   200   208  9      
STRAND   212   217  6      
TURN   225   227  3      
HELIX   235   237  3      
HELIX   239   248  10      
HELIX   252   262  11      
STRAND   266   270  5      
HELIX   274   280  7      
HELIX   281   285  5      
HELIX   290   297  8      
HELIX   309   312  4      
Sequence information
Length: 323 AA [This is the length of the unprocessed precursor] Molecular weight: 36844 Da [This is the MW of the unprocessed precursor] CRC64: A152E37F6990C5CB [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDSKQQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ 

        70         80         90        100        110        120 
VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM 

       130        140        150        160        170        180 
SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKP 

       190        200        210        220        230        240 
GLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV 

       250        260        270        280        290        300 
LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD 

       310        320 
RNLHYFNSDS FASHPNYPYS DEY
P42330 in FASTA format

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View entry in raw text format (no links)
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