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UniProtKB/Swiss-Prot entry P23141


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

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Entry information
Entry name EST1_HUMAN
Primary accession number P23141
Secondary accession numbers A8K3K8 A8K844 P82127 Q00015 Q13657 Q14062 Q16737 Q16788 Q549X7 Q549X8 Q86UK2 Q96EE8 Q9UC52 Q9UK77 Q9ULY2
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on August 1, 1992 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 105)
Name and origin of the protein
Protein name Liver carboxylesterase 1 [Precursor]
Synonyms EC 3.1.1.1
Acyl coenzyme A:cholesterol acyltransferase
ACAT
Monocyte/macrophage serine esterase
HMSE
Serine esterase 1
Brain carboxylesterase hBr1
Triacylglycerol hydrolase
TGH
Egasyn
Retinyl ester hydrolase
REH
Gene name
Name: CES1
Synonyms: CES2, SES1
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] (ISOFORM 1).
PubMed=1918003 [NCBI, ExPASy, EBI, Israel, Japan]
Munger J.S., Shi G.P., Mark E.A., Chin D.T., Gerard C., Chapman H.A.;
"A serine esterase released by human alveolar macrophages is closely related to liver microsomal carboxylesterases.";
J. Biol. Chem. 266:18832-18838(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Liver;
DOI=10.1021/bi00094a018; PubMed=8218228 [NCBI, ExPASy, EBI, Israel, Japan]
Kroetz D.L., McBride O.W., Gonzalez F.J.;
"Glycosylation-dependent activity of baculovirus-expressed human liver carboxylesterases: cDNA cloning and characterization of two highly similar enzyme forms.";
Biochemistry 32:11606-11617(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Peripheral blood, and Placenta;
DOI=10.1006/geno.1993.1285; PubMed=8406473 [NCBI, ExPASy, EBI, Israel, Japan]
Shibata F., Takagi Y., Kitajima M., Kuroda T., Omura T.;
"Molecular cloning and characterization of a human carboxylesterase gene.";
Genomics 17:76-82(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=8049197 [NCBI, ExPASy, EBI, Israel, Japan]
Becker A., Bottcher A., Lackner K.J., Fehringer P., Notka F., Aslanidis C., Schmitz G.;
"Purification, cloning, and expression of a human enzyme with acyl coenzyme A: cholesterol acyltransferase activity, which is identical to liver carboxylesterase.";
Arterioscler. Thromb. 14:1346-1355(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH BETA-GLUCURONIDASE.
TISSUE=Liver;
DOI=10.1006/abbi.1999.1449; PubMed=10562416 [NCBI, ExPASy, EBI, Israel, Japan]
Islam M.R., Waheed A., Shah G.N., Tomatsu S., Sly W.S.;
"Human egasyn binds beta-glucuronidase but neither the esterase active site of egasyn nor the C-terminus of beta-glucuronidase is involved in their interaction.";
Arch. Biochem. Biophys. 372:53-61(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Macrophage;
PubMed=11015575 [NCBI, ExPASy, EBI, Israel, Japan]
Ghosh S.;
"Cholesteryl ester hydrolase in human monocyte/macrophage: cloning, sequencing, and expression of full-length cDNA.";
Physiol. Genomics 2:1-8(2000).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 19-28.
TISSUE=Liver;
DOI=10.1006/prep.2001.1553; PubMed=11812220 [NCBI, ExPASy, EBI, Israel, Japan]
Alam M., Ho S., Vance D.E., Lehner R.;
"Heterologous expression, purification, and characterization of human triacylglycerol hydrolase.";
Protein Expr. Purif. 24:33-42(2002).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
TISSUE=Liver;
Hosokawa M., Yaginuma Y., Watanabe N., Yamamoto N., Tsukada E., Ohhata Y., Satoh T., Chiba K.;
"Inverted duplication of human carboxylesterase 1(CES1) genes, which are difference in regulation at the transcriptional level.";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT GLN-362 DEL.
TISSUE=Heart, and Oesophagus;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-362 DEL.
TISSUE=Blood, and Lung;
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-429 (ISOFORM 1).
TISSUE=Brain;
DOI=10.1016/S0014-5793(99)01111-4; PubMed=10518925 [NCBI, ExPASy, EBI, Israel, Japan]
Mori M., Hosokawa M., Ogasawara Y., Tsukada E., Chiba K.;
"cDNA cloning, characterization and stable expression of novel human brain carboxylesterase.";
FEBS Lett. 458:17-22(1999).
[12]
PROTEIN SEQUENCE OF 18-28; 65-78; 93-107; 243-255; 258-266; 297-313 AND 341-346, CATALYTIC ACTIVITY, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Liver;
DOI=10.1046/j.1432-1327.1998.2510863.x; PubMed=9490062 [NCBI, ExPASy, EBI, Israel, Japan]
Schindler R., Mentlein R., Feldheim W.;
"Purification and characterization of retinyl ester hydrolase as a member of the non-specific carboxylesterase supergene family.";
Eur. J. Biochem. 251:863-873(1998).
[13]
PROTEIN SEQUENCE OF 19-34, NUCLEOTIDE SEQUENCE [MRNA] OF 113-121; 138-149; 216-224; 351-357 AND 466-471, AND SUBUNIT.
TISSUE=Liver;
DOI=10.1016/0378-4274(95)03493-5; PubMed=8597091 [NCBI, ExPASy, EBI, Israel, Japan]
Satoh T., Hosokawa M.;
"Molecular aspects of carboxylesterase isoforms in comparison with other esterases.";
Toxicol. Lett. 82:439-445(1995).
[14]
PROTEIN SEQUENCE OF 19-28, ACTIVE SITES, GLYCOSYLATION AT ASN-79, AND MUTAGENESIS OF ASN-79; SER-221; GLU-354; HIS-468 AND 564-HIS--LEU-567.
DOI=10.1021/bi0255625; PubMed=12022871 [NCBI, ExPASy, EBI, Israel, Japan]
Alam M., Vance D.E., Lehner R.;
"Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: identification of the catalytic triad and a glycosylation site.";
Biochemistry 41:6679-6687(2002).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 61-567.
TISSUE=Liver;
DOI=10.1016/0024-3205(91)90515-D; PubMed=1997784 [NCBI, ExPASy, EBI, Israel, Japan]
Long R.M., Calabrese M.R., Martin B.M., Pohl L.R.;
"Cloning and sequencing of a human liver carboxylesterase isoenzyme.";
Life Sci. 48:PL43-PL49(1991).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 64-567, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2070086 [NCBI, ExPASy, EBI, Israel, Japan]
Zschunke F., Salmassi A., Kreipe H., Buck F., Parwaresch M.R., Radzun H.J.;
"cDNA cloning and characterization of human monocyte/macrophage serine esterase-1.";
Blood 78:506-512(1991).
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 114-567.
TISSUE=Liver;
DOI=10.1016/0378-1119(91)90448-K; PubMed=1748313 [NCBI, ExPASy, EBI, Israel, Japan]
Riddles P.W., Richards L.J., Bowles M.R., Pond S.M.;
"Cloning and analysis of a cDNA encoding a human liver carboxylesterase.";
Gene 108:289-292(1991).
[18]
BIOPHYSICOCHEMICAL PROPERTIES, VARIANT GLU-143, AND CHARACTERIZATION OF VARIANT GLU-143.
DOI=10.1016/j.ajhg.2008.04.015; PubMed=18485328 [NCBI, ExPASy, EBI, Israel, Japan]
Zhu H.-J., Patrick K.S., Yuan H.-J., Wang J.-S., Donovan J.L., DeVane C.L., Malcolm R., Johnson J.A., Youngblood G.L., Sweet D.H., Langaee T.Y., Markowitz J.S.;
"Two CES1 gene mutations lead to dysfunctional carboxylesterase 1 activity in man: clinical significance and molecular basis.";
Am. J. Hum. Genet. 82:1241-1248(2008).
[19]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
DOI=10.1016/S1074-5521(03)00071-1; PubMed=12725862 [NCBI, ExPASy, EBI, Israel, Japan]
Bencharit S., Morton C.L., Hyatt J.L., Kuhn P., Danks M.K., Potter P.M., Redinbo M.R.;
"Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine. From binding promiscuity to selective inhibition.";
Chem. Biol. 10:341-349(2003).
[20]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATES.
DOI=10.1038/nsb919; PubMed=12679808 [NCBI, ExPASy, EBI, Israel, Japan]
Bencharit S., Morton C.L., Xue Y., Potter P.M., Redinbo M.R.;
"Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme.";
Nat. Struct. Biol. 10:349-356(2003).
Comments
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
M73499; AAA35649.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L07764; AAA16036.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L07765; AAA35711.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D21088; BAA04650.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S73751; AAC60631.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF177775; AAD53175.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY268104; AAP20868.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB119995; BAC87748.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB119996; BAC87749.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB119997; BAC87750.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB119998; BAC87751.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK290623; BAF83312.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK292209; BAF84898.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012418; AAH12418.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC110338; AAI10339.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB025026; BAA84995.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55509; AAA35650.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X52973; CAA37147.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M65261; AAA83932.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00010180; -.
IPI00607801; -.
PIR A41010; A41010.
RefSeq NP_001020365.1; -.
NP_001020366.1; -.
NP_001257.4; -.
UniGene Hs.558865
3D structure databases
PDB
1MX1; X-ray; 2.40 A; A/B/C/D/E/F=19-567.[ExPASy / RCSB / EBI]
1MX5; X-ray; 2.80 A; A/B/C/D/E/F=19-567.[ExPASy / RCSB / EBI]
1MX9; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=19-567.[ExPASy / RCSB / EBI]
1YA4; X-ray; 3.20 A; A/B/C=21-553.[ExPASy / RCSB / EBI]
1YA8; X-ray; 3.00 A; A/B/C=21-553.[ExPASy / RCSB / EBI]
1YAH; X-ray; 3.00 A; A/B/C=21-553.[ExPASy / RCSB / EBI]
1YAJ; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=21-553.[ExPASy / RCSB / EBI]
2DQY; X-ray; 3.00 A; A/B/C=19-561.[ExPASy / RCSB / EBI]
2DQZ; X-ray; 2.80 A; A/B/C=19-561.[ExPASy / RCSB / EBI]
2DR0; X-ray; 3.20 A; A/B/C=19-561.[ExPASy / RCSB / EBI]
2H7C; X-ray; 2.00 A; A/B/C/D/E/F=19-561.[ExPASy / RCSB / EBI]
2HRQ; X-ray; 2.70 A; A/B/C/D/E/F=21-553.[ExPASy / RCSB / EBI]
2HRR; X-ray; 2.70 A; A/B/C=21-553.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1MX1; -.
1MX5; -.
1MX9; -.
1YA4; -.
1YA8; -.
1YAH; -.
1YAJ; -.
2DQY; -.
2DQZ; -.
2DR0; -.
2H7C; -.
2HRQ; -.
2HRR; -.
ModBase P23141.
Protein family/group databases
MEROPS S09.982; -.
Enzyme and pathway databases
BRENDA 3.1.1.1; 247.
Organism-specific databases
GeneCards GC16M054395; -.
GC16M054396; -.
H-InvDB HIX0013044; -.
HGNC HGNC:1863; CES1.
GenAtlas CES1.
HPA HPA012023; -.
MIM 114835; gene+phenotype. [NCBI / EBI]
PharmGKB PA107; -.
Gene expression databases
Bgee P23141; -.
CleanEx HS_CES1; -.
HS_CES2; -.
GermOnline ENSG00000196959; Homo sapiens.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (inferred from electronic annotation from UniProtKB-KW).
GO:0005788; Cellular component: endoplasmic reticulum lumen (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004091; Molecular function: carboxylesterase activity (traceable author statement from ProtInc).
GO:0008152; Biological process: metabolic process (traceable author statement from ProtInc).
GO:0009636; Biological process: response to toxin (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002018; CarbesteraseB.
IPR019826; Carboxylesterase_B_AS.
IPR019819; Carboxylesterase_B_CS.
Graphical view of domain structure.
PANTHER PTHR11559; CarbesteraseB; 1.
Pfam PF00135; COesterase; 1.
Pfam graphical view of domain structure.
PROSITE PS00122; CARBOXYLESTERASE_B_1; 1.
PS00941; CARBOXYLESTERASE_B_2; 1.
Proteomic databases
PRIDE P23141; -.
Genome annotation databases
Ensembl ENSG00000196959; Homo sapiens. [Contig view]
GeneID 1066; -.
KEGG hsa:1066; -.
Phylogenomic databases
HOVERGEN P23141; -.
OMA P23141; ATERYLG.
Other
DrugBank DB00357; Aminoglutethimide.
DB01393; Bezafibrate.
DB01432; Cholestyramine.
DB00691; Moexipril.
NextBio 4450; -.
SOURCE CES1; Homo sapiens.
ProtoNet P23141.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Polymorphism; Serine esterase; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
CHAIN   19   567  549     Liver carboxylesterase 1. PRO_0000008569
ACT_SITE   221   221        Acyl-ester intermediate. 
ACT_SITE   354   354        Charge relay system. 
ACT_SITE   468   468        Charge relay system. 
CARBOHYD   79    79        N-linked (GlcNAc...). 
DISULFID   87   116         
DISULFID   274   285         
VAR_SEQ   17    17        W -> WA (in isoform 2). VSP_021026
VARIANT   18    18  1     G -> GA. VAR_002357
VARIANT   75    75  1     S -> N (in dbSNP:rs2307240 [NCBI]). VAR_014314 [3D]
VARIANT   143   143  1     G -> E (5.4-fold decrease in activity with p-nitrophenyl acetate as substrate; no change in affinity for p-nitrophenyl acetate; loss of activity with L- or D-methylphenidate as substrate). VAR_046954 [3D]
VARIANT   199   199  1     R -> H (in dbSNP:rs2307243 [NCBI]). VAR_014594 [3D]
VARIANT   203   203  1     D -> E (in dbSNP:rs2307227 [NCBI]). VAR_014595 [3D]
VARIANT   362   362  1     Missing. VAR_002358
MUTAGEN   79    79        N->A: Abolishes glycosylation. 
MUTAGEN   221   221        S->A: Loss of activity. 
MUTAGEN   354   354        E->A: Loss of activity. 
MUTAGEN   468   468        H->A: Loss of activity. 
MUTAGEN   564   567        Missing: Does not result in secretion. 
CONFLICT   2     2        W -> L (in Ref. 5; AAD53175). 
CONFLICT   4     7        RAFI -> PALV (in Ref. 3; BAA04650, 8; BAC87749/BAC87751, 9; BAF83312/BAF84898 and 10; AAH12418). 
CONFLICT   12    12        S -> A (in Ref. 3; BAA04650, 8; BAC87749/BAC87751, 9; BAF83312/BAF84898 and 10; AAH12418). 
CONFLICT   19    21        HPS -> GPP (in Ref. 13; AA sequence). 
CONFLICT   19    19        H -> N (in Ref. 12; AA sequence). 
CONFLICT   21    24        SSPP -> EAVV (in Ref. 12; AA sequence). 
CONFLICT   27    28        DT -> AK (in Ref. 12; AA sequence). 
CONFLICT   28    29        TV -> DT (in Ref. 13; AA sequence). 
CONFLICT   56    56        A -> G (in Ref. 2; AAA16036/AAA35711). 
CONFLICT   64    64        R -> G (in Ref. 16; CAA37147). 
CONFLICT   65    65        F -> S (in Ref. 6; AAP20868). 
CONFLICT   75    75        S -> A (in Ref. 12; AA sequence). 
CONFLICT   78    78        K -> I (in Ref. 12; AA sequence). 
CONFLICT   89    89        Q -> R (in Ref. 6; AAP20868). 
CONFLICT   98    98        S -> F (in Ref. 12; AA sequence). 
CONFLICT   105   107        KEN -> PAD (in Ref. 12; AA sequence). 
CONFLICT   115   115        D -> H (in Ref. 17; AAA83932). 
CONFLICT   186   186        R -> G (in Ref. 16; CAA37147). 
CONFLICT   247   247        S -> I (in Ref. 12; AA sequence). 
CONFLICT   251   251        L -> K (in Ref. 12; AA sequence). 
CONFLICT   253   253        S -> G (in Ref. 12; AA sequence). 
CONFLICT   255   255        L -> P (in Ref. 9; BAF83312). 
CONFLICT   258   258        K -> Q (in Ref. 12; AA sequence). 
CONFLICT   281   281        V -> A (in Ref. 17; AAA83932). 
CONFLICT   298   298        T -> I (in Ref. 12; AA sequence). 
CONFLICT   302   302        K -> A (in Ref. 12; AA sequence). 
CONFLICT   305   305        S -> M (in Ref. 12; AA sequence). 
CONFLICT   337   337        A -> R (in Ref. 17; AAA83932). 
CONFLICT   417   417        F -> I (in Ref. 17; AAA83932). 
CONFLICT   512   512        E -> K (in Ref. 17; AAA83932). 
CONFLICT   536   536        A -> G (in Ref. 2; AAA16036/AAA35711). 
CONFLICT   563   563        E -> D (in Ref. 17; AAA83932). 
STRAND   25    28  4      
STRAND   31    34  4      
STRAND   36    38  3      
STRAND   47    54  8      
HELIX   61    63  3      
STRAND   75    79  5      
STRAND   86    88  3      
HELIX   91   101  11      
STRAND   104   106  3      
STRAND   112   114  3      
STRAND   118   123  6      
STRAND   133   139  7      
TURN   143   145  3      
HELIX   155   161  7      
STRAND   164   168  5      
HELIX   173   177  5      
HELIX   189   204  16      
HELIX   205   208  4      
STRAND   210   220  11      
HELIX   222   231  10      
HELIX   234   236  3      
STRAND   241   247  7      
HELIX   253   255  3      
HELIX   262   271  10      
HELIX   279   288  10      
HELIX   291   301  11      
HELIX   312   314  3      
STRAND   325   327  3      
HELIX   332   337  6      
STRAND   346   351  6      
HELIX   358   363  6      
HELIX   375   384  10      
HELIX   386   389  4      
TURN   393   395  3      
HELIX   396   404  9      
HELIX   410   425  16      
HELIX   427   438  12      
TURN   439   441  3      
STRAND   444   450  7      
TURN   468   471  4      
HELIX   472   475  4      
HELIX   478   480  3      
HELIX   487   506  20      
STRAND   525   532  8      
STRAND   534   537  4      
HELIX   541   550  10      
Sequence information
Length: 567 AA [This is the length of the unprocessed precursor] Molecular weight: 62521 Da [This is the MW of the unprocessed precursor] CRC64: D3A00BDCDC7E5DFF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWLRAFILAT LSASAAWGHP SSPPVVDTVH GKVLGKFVSL EGFAQPVAIF LGIPFAKPPL 

        70         80         90        100        110        120 
GPLRFTPPQP AEPWSFVKNA TSYPPMCTQD PKAGQLLSEL FTNRKENIPL KLSEDCLYLN 

       130        140        150        160        170        180 
IYTPADLTKK NRLPVMVWIH GGGLMVGAAS TYDGLALAAH ENVVVVTIQY RLGIWGFFST 

       190        200        210        220        230        240 
GDEHSRGNWG HLDQVAALRW VQDNIASFGG NPGSVTIFGE SAGGESVSVL VLSPLAKNLF 

       250        260        270        280        290        300 
HRAISESGVA LTSVLVKKGD VKPLAEQIAI TAGCKTTTSA VMVHCLRQKT EEELLETTLK 

       310        320        330        340        350        360 
MKFLSLDLQG DPRESQPLLG TVIDGMLLLK TPEELQAERN FHTVPYMVGI NKQEFGWLIP 

       370        380        390        400        410        420 
MQLMSYPLSE GQLDQKTAMS LLWKSYPLVC IAKELIPEAT EKYLGGTDDT VKKKDLFLDL 

       430        440        450        460        470        480 
IADVMFGVPS VIVARNHRDA GAPTYMYEFQ YRPSFSSDMK PKTVIGDHGD ELFSVFGAPF 

       490        500        510        520        530        540 
LKEGASEEEI RLSKMVMKFW ANFARNGNPN GEGLPHWPEY NQKEGYLQIG ANTQAAQKLK 

       550        560 
DKEVAFWTNL FAKKAVEKPP QTEHIEL 

P23141 in FASTA format

View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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