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UniProtKB/Swiss-Prot entry P22303


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

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Entry information
Entry name ACES_HUMAN
Primary accession number P22303
Secondary accession numbers A4D2E2 Q16169 Q29S23 Q2M324 Q504V3 Q86TM9 Q86YX9 Q9BXP7
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on August 1, 1991 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 107)
Name and origin of the protein
Protein name Acetylcholinesterase [Precursor]
Synonyms AChE
EC 3.1.1.7
Gene name
Name: ACHE
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 T).
DOI=10.1073/pnas.87.24.9688; PubMed=2263619 [NCBI, ExPASy, EBI, Israel, Japan]
Soreq H., Ben-Aziz R., Prody C.A., Seidman S., Gnatt A., Neville L., Lieman-Hurwitz J., Lev-Lehman E., Ginzberg D., Lipidot-Lifson Y., Zakut H.;
"Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure.";
Proc. Natl. Acad. Sci. U.S.A. 87:9688-9692(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS H; R AND T).
DOI=10.1006/excr.1994.1039; PubMed=8299725 [NCBI, ExPASy, EBI, Israel, Japan]
Karpel R., Ben Aziz-Aloya R., Sternfeld M., Ehrlich G., Ginzberg D., Tarroni P., Clementi F., Zakut H., Soreq H.;
"Expression of three alternative acetylcholinesterase messenger RNAs in human tumor cell lines of different tissue origins.";
Exp. Cell Res. 210:268-277(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Yang L., Zhang X.J.;
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T).
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-34; ALA-135 AND ASN-353.
SeattleSNPs variation discovery resource;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS H AND T).
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 521-614.
DOI=10.1093/nar/29.6.1352; PubMed=11239002 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W., Koop B.F.;
"Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5.";
Nucleic Acids Res. 29:1352-1365(2001).
[10]
PROTEIN SEQUENCE OF 256-273; 306-326; 396-422; 465-480 AND 528-551, FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Erythrocyte;
DOI=10.1016/0014-5793(89)81352-3; PubMed=2714437 [NCBI, ExPASy, EBI, Israel, Japan]
Chhajlani V., Derr D., Earles B., Schmell E., August T.;
"Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase.";
FEBS Lett. 247:279-282(1989).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-611.
PubMed=1748670 [NCBI, ExPASy, EBI, Israel, Japan]
Velan B., Grosfeld H., Kronman C., Leitner M., Gozes Y., Lazar A., Flashner Y., Marcus D., Cohen S., Shafferman A.;
"The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580-->Ala mutant.";
J. Biol. Chem. 266:23977-23984(1991).
[12]
FUNCTION, AND MUTAGENESIS OF ASP-206; SER-234; GLU-365; ASP-435 AND HIS-478.
PubMed=1517212 [NCBI, ExPASy, EBI, Israel, Japan]
Shafferman A., Kronman C., Flashner Y., Leitner M., Grosfeld H., Ordentlich A., Gozes Y., Cohen S., Ariel N., Barak D.;
"Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding.";
J. Biol. Chem. 267:17640-17648(1992).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND DISEASE.
DOI=10.1016/S0168-0102(02)00005-6; PubMed=11985878 [NCBI, ExPASy, EBI, Israel, Japan]
Yang L., He H.Y., Zhang X.J.;
"Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells.";
Neurosci. Res. 42:261-268(2002).
[14]
3D-STRUCTURE MODELING OF 35-574.
DOI=10.1016/S1093-3263(98)00005-9; PubMed=9640563 [NCBI, ExPASy, EBI, Israel, Japan]
Felder C.E., Botti S.A., Lifson S., Silman I., Sussman J.L.;
"External and internal electrostatic potentials of cholinesterase models.";
J. Mol. Graph. Model. 15:318-327(1997).
[15]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 32-614 IN COMPLEX WITH FASCICULIN-2, AND GLYCOSYLATION AT ASN-381 AND ASN-495.
DOI=10.1107/S0907444900010659; PubMed=11053835 [NCBI, ExPASy, EBI, Israel, Japan]
Kryger G., Harel M., Giles K., Toker L., Velan B., Lazar A., Kronman C., Barak D., Ariel N., Shafferman A., Silman I., Sussman J.L.;
"Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II.";
Acta Crystallogr. D 56:1385-1394(2000).
[16]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 575-614 IN COMPLEX WITH COLQ.
DOI=10.1038/sj.emboj.7600425; PubMed=15526038 [NCBI, ExPASy, EBI, Israel, Japan]
Dvir H., Harel M., Bon S., Liu W.-Q., Vidal M., Garbay C., Sussman J.L., Massoulie J., Silman I.;
"The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix.";
EMBO J. 23:4394-4405(2004).
[17]
VARIANT BLOOD GROUP YT(B) ASN-353.
PubMed=8488842 [NCBI, ExPASy, EBI, Israel, Japan]
Bartels C.F., Zelinski T., Lockridge O.;
"Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polymorphism.";
Am. J. Hum. Genet. 52:928-936(1993).
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
M55040; AAA68151.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S71129; AAC60618.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF334270; AAO32948.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291321; BAF84010.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY750146; AAU43801.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC011895; AAP22364.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC011895; AAP22365.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH236956; EAL23812.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH236956; EAL23813.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471091; EAW76461.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471091; EAW76463.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036813; AAH36813.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC094752; AAH94752.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105060; AAI05061.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105062; AAI05063.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF312032; AAK21003.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00026103; -.
IPI00220026; -.
IPI00844209; -.
IPI00913969; -.
PIR A39256; A39256.
RefSeq NP_000656.1; -.
NP_056646.1; -.
UniGene Hs.154495
3D structure databases
PDB
1B41; X-ray; 2.76 A; A=36-574.[ExPASy / RCSB / EBI]
1F8U; X-ray; 2.90 A; A=32-614.[ExPASy / RCSB / EBI]
1PUV; Model; -; A=37-574.[ExPASy / RCSB / EBI]
1PUW; Model; -; A=37-574.[ExPASy / RCSB / EBI]
1VZJ; X-ray; 2.35 A; A/B/C/D/E/F/G/H=575-614.[ExPASy / RCSB / EBI]
2CLJ; Model; -; A=32-574.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1B41; -.
1F8U; -.
1PUV; -.
1PUW; -.
1VZJ; -.
2CLJ; -.
ModBase P22303.
Protein-protein interaction databases
DIP DIP:1119N; -.
Protein family/group databases
MEROPS S09.979; -.
Enzyme and pathway databases
BRENDA 3.1.1.7; 247.
2D gel databases
SWISS-2DPAGE P22303; -.
Organism-specific databases
GeneCards GC07M100325; -.
H-InvDB HIX0033555; -.
HGNC HGNC:108; ACHE.
GenAtlas ACHE.
MIM 100740; gene+phenotype. [NCBI / EBI]
112100; phenotype. [NCBI / EBI]
PharmGKB PA20; -.
Gene expression databases
ArrayExpress P22303; -.
Bgee P22303; -.
GermOnline ENSG00000087085; Homo sapiens.
Ontologies
GO
GO:0031225; Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005605; Cellular component: basal lamina (non-traceable author statement from HGNC).
GO:0030054; Cellular component: cell junction (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005794; Cellular component: Golgi apparatus (inferred from direct assay from HGNC).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0048471; Cellular component: perinuclear region of cytoplasm (inferred from direct assay from HGNC).
GO:0045202; Cellular component: synapse (inferred from direct assay from HGNC).
GO:0042166; Molecular function: acetylcholine binding (non-traceable author statement from UniProtKB).
GO:0003990; Molecular function: acetylcholinesterase activity (inferred from mutant phenotype from UniProtKB).
GO:0001540; Molecular function: beta-amyloid binding (traceable author statement from UniProtKB).
GO:0004104; Molecular function: cholinesterase activity (inferred from direct assay from HGNC).
GO:0005518; Molecular function: collagen binding (inferred from direct assay from HGNC).
GO:0043237; Molecular function: laminin-1 binding (inferred from direct assay from HGNC).
GO:0042803; Molecular function: protein homodimerization activity (non-traceable author statement from UniProtKB).
GO:0017171; Molecular function: serine hydrolase activity (inferred from direct assay from HGNC).
GO:0001507; Biological process: acetylcholine catabolic process in synaptic cleft (non-traceable author statement from UniProtKB).
GO:0042982; Biological process: amyloid precursor protein metabolic process (traceable author statement from UniProtKB).
GO:0007155; Biological process: cell adhesion (traceable author statement from UniProtKB).
GO:0008283; Biological process: cell proliferation (traceable author statement from UniProtKB).
GO:0006260; Biological process: DNA replication (traceable author statement from UniProtKB).
GO:0007517; Biological process: muscle organ development (traceable author statement from UniProtKB).
GO:0032223; Biological process: negative regulation of synaptic transmission, cholinergic (inferred by curator from HGNC).
GO:0002076; Biological process: osteoblast development (inferred from expression pattern from HGNC).
GO:0050714; Biological process: positive regulation of protein secretion (traceable author statement from UniProtKB).
GO:0009611; Biological process: response to wounding (traceable author statement from UniProtKB).
GO:0007416; Biological process: synaptogenesis (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR014788; AChE_tetra.
IPR002018; CarbesteraseB.
IPR019826; Carboxylesterase_B_AS.
IPR019819; Carboxylesterase_B_CS.
IPR000997; Cholinesterase.
Graphical view of domain structure.
PANTHER PTHR11559; CarbesteraseB; 1.
Pfam PF08674; AChE_tetra; 1.
PF00135; COesterase; 1.
Pfam graphical view of domain structure.
PRINTS PR00878; CHOLNESTRASE.
PROSITE PS00122; CARBOXYLESTERASE_B_1; 1.
PS00941; CARBOXYLESTERASE_B_2; 1.
Proteomic databases
PRIDE P22303; -.
Genome annotation databases
Ensembl ENSG00000087085; Homo sapiens. [Contig view]
GeneID 43; -.
KEGG hsa:43; -.
Phylogenomic databases
HOVERGEN P22303; -.
Other
DrugBank DB01122; Ambenonium.
DB00572; Atropine.
DB00122; Choline.
DB01245; Decamethonium.
DB00944; Demecarium bromide.
DB00843; Donepezil.
DB01010; Edrophonium.
DB01364; Ephedrine.
DB00674; Galantamine.
DB00483; Gallamine Triethiodide.
DB00677; Isoflurophate.
DB01400; Neostigmine.
DB00981; Physostigmine.
DB00545; Pyridostigmine.
DB00989; Rivastigmine.
DB00382; Tacrine.
DB01199; Tubocurarine.
NextBio 173; -.
SOURCE ACHE; Homo sapiens.
ProtoNet P22303.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Blood group antigen; Cell junction; Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Neurotransmitter degradation; Nucleus; Polymorphism; Secreted; Serine esterase; Signal; Synapse.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    31  31     Potential. 
CHAIN   32   614  583     Acetylcholinesterase. PRO_0000008587
ACT_SITE   234   234        Acyl-ester intermediate. 
ACT_SITE   365   365        Charge relay system. 
ACT_SITE   478   478        Charge relay system. 
CARBOHYD   296   296        N-linked (GlcNAc...) (Potential). 
CARBOHYD   381   381        N-linked (GlcNAc...). 
CARBOHYD   495   495        N-linked (GlcNAc...). 
DISULFID   100   127         
DISULFID   288   303         
DISULFID   440   560         
DISULFID   611   611        Interchain. 
VAR_SEQ   357   444        Missing (in isoform 4). VSP_035568
VAR_SEQ   575   614        DTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL -> ASEAPSTCPGFTHGEAAPRPGLPLPLLLLHQLLLLFLS HLRRL (in isoform H). VSP_001457
VAR_SEQ   575   603        DTLDEAERQWKAEFHRWSSYMVHWKNQFD -> GMQGPAGSAGRRGVGARQCNPSLLPLASE (in isoform R). VSP_035569
VAR_SEQ   604   614        Missing (in isoform R). VSP_035570
VARIANT   34    34  1     R -> Q (in dbSNP:rs17881553 [NCBI]). VAR_021325 
VARIANT   135   135  1     P -> A (in dbSNP:rs17885778 [NCBI]). VAR_021326 
VARIANT   333   333  1     V -> E (in dbSNP:rs8286 [NCBI]). VAR_011934 
VARIANT   353   353  1     H -> N (in Yt(b) antigen; dbSNP:rs1799805 [NCBI]). VAR_002359 
MUTAGEN   206   206        D->N: Misfolding, absence of secretion. 
MUTAGEN   234   234        S->A: Loss of activity. 
MUTAGEN   365   365        E->A: Loss of activity. 
MUTAGEN   435   435        D->N: Misfolding, absence of secretion. 
MUTAGEN   478   478        H->A: Loss of activity. 
MUTAGEN   611   611        C->A: Impairment of interchain disulfide bridge formation. 
CONFLICT   22    22        L -> V (in Ref. 8; AAH94752). 
CONFLICT   146   146        L -> I (in Ref. 8; AAH94752). 
STRAND   40    43  4      
STRAND   46    49  4      
STRAND   51    53  3      
STRAND   60    67  8      
HELIX   74    76  3      
STRAND   88    92  5      
STRAND   99   101  3      
HELIX   112   115  4      
STRAND   123   125  3      
STRAND   129   134  6      
STRAND   143   149  7      
TURN   153   155  3      
HELIX   162   164  3      
HELIX   167   173  7      
STRAND   176   180  5      
HELIX   185   189  5      
STRAND   196   198  3      
HELIX   202   217  16      
HELIX   218   221  4      
STRAND   223   233  11      
HELIX   235   244  10      
HELIX   247   252  6      
STRAND   254   260  7      
TURN   266   268  3      
HELIX   272   285  14      
HELIX   297   304  8      
HELIX   309   315  7      
TURN   316   319  4      
STRAND   336   341  6      
HELIX   343   349  7      
STRAND   356   362  7      
STRAND   364   366  3      
HELIX   367   370  4      
TURN   371   373  3      
STRAND   379   381  3      
HELIX   387   397  11      
HELIX   403   412  10      
HELIX   422   437  16      
HELIX   439   451  13      
STRAND   455   461  7      
HELIX   472   474  3      
HELIX   482   485  4      
HELIX   488   490  3      
HELIX   498   517  20      
TURN   536   538  3      
STRAND   540   547  8      
STRAND   550   553  4      
HELIX   557   564  8      
HELIX   566   572  7      
HELIX   576   605  30      
Sequence information
Length: 614 AA [This is the length of the unprocessed precursor] Molecular weight: 67796 Da [This is the MW of the unprocessed precursor] CRC64: B9AA84C77831C302 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRPPQCLLHT PSLASPLLLL LLWLLGGGVG AEGREDAELL VTVRGGRLRG IRLKTPGGPV 

        70         80         90        100        110        120 
SAFLGIPFAE PPMGPRRFLP PEPKQPWSGV VDATTFQSVC YQYVDTLYPG FEGTEMWNPN 

       130        140        150        160        170        180 
RELSEDCLYL NVWTPYPRPT SPTPVLVWIY GGGFYSGASS LDVYDGRFLV QAERTVLVSM 

       190        200        210        220        230        240 
NYRVGAFGFL ALPGSREAPG NVGLLDQRLA LQWVQENVAA FGGDPTSVTL FGESAGAASV 

       250        260        270        280        290        300 
GMHLLSPPSR GLFHRAVLQS GAPNGPWATV GMGEARRRAT QLAHLVGCPP GGTGGNDTEL 

       310        320        330        340        350        360 
VACLRTRPAQ VLVNHEWHVL PQESVFRFSF VPVVDGDFLS DTPEALINAG DFHGLQVLVG 

       370        380        390        400        410        420 
VVKDEGSYFL VYGAPGFSKD NESLISRAEF LAGVRVGVPQ VSDLAAEAVV LHYTDWLHPE 

       430        440        450        460        470        480 
DPARLREALS DVVGDHNVVC PVAQLAGRLA AQGARVYAYV FEHRASTLSW PLWMGVPHGY 

       490        500        510        520        530        540 
EIEFIFGIPL DPSRNYTAEE KIFAQRLMRY WANFARTGDP NEPRDPKAPQ WPPYTAGAQQ 

       550        560        570        580        590        600 
YVSLDLRPLE VRRGLRAQAC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN 

       610 
QFDHYSKQDR CSDL 

P22303 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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