[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

FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.
CATALYTIC ACTIVITY: Acetylcholine + H₂O = choline + acetate.
SUBUNIT: Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers (By similarity). Isoform H generates GPI-anchored dimers; disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, isoform T subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform T tetramers, from monomers and dimers. Isoform R may be monomeric.
SUBCELLULAR LOCATION: Cell junction, synapse. Secreted (By similarity). Cell membrane; Peripheral membrane protein (By similarity).
SUBCELLULAR LOCATION: Isoform T: Nucleus. Note=Only observed in apoptotic nuclei.
SUBCELLULAR LOCATION: Isoform H: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side (By similarity).

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.

Name	T
Synonyms	ACHE-S, synaptic
Isoform ID	P22303-1
This is the isoform sequence displayed in this entry.

Name	H
Synonyms	ACHE-E, erythrocytic, E4-E5
Isoform ID	P22303-2
Note: The displayed full length sequence of this isoform is cleaved at position 589 to the mature form of the protein which is then linked to glycosylphosphatidyl inositol.
Features which should be applied to build the isoform sequence: VSP_001457.

Name	R
Synonyms	ACHE-R, readthrough
Isoform ID	P22303-4
Features which should be applied to build the isoform sequence: VSP_035569, VSP_035570.

Name	4
Isoform ID	P22303-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_035568.

TISSUE SPECIFICITY: Isoform H is highly expressed in erythrocytes.
POLYMORPHISM: ACHE is responsible for the Yt blood group system. The molecular basis of the Yt(a)=Yt1/Yt(b)=Yt2 blood group antigens is a single variation in position 353; His-353 corresponds to Yt(a) and the rare variant with Asn-353 to Yt(b).
DISEASE: Behaves as an amyloid-promoting factor to promote the formation of amyloid plaques in Alzheimer disease.
SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
SEQUENCE CAUTION:
- Sequence=AAA68151.1; Type=Frameshift; Positions=604;
WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation database; URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=yt";.
WEB RESOURCE: Name=Wikipedia; Note=Acetylcholinesterase entry; URL="http://en.wikipedia.org/wiki/Acetylcholinesterase";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/ache/";.

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

GC07M100325; -.

HIX0033555; -.

HGNC:108; ACHE.

100740; gene+phenotype. [NCBI / EBI]
112100; phenotype. [NCBI / EBI]

PharmGKB

PA20; -.

Gene expression databases

ArrayExpress

P22303; -.

Bgee

P22303; -.

GermOnline

ENSG00000087085; Homo sapiens.

Ontologies

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.

173; -.

ACHE; Homo sapiens.

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

Feature table viewer

`Key`	`From 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 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