[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17). PubMed=3029127 [NCBI, ExPASy, EBI, Israel, Japan] Morishita K., Kubota N., Asano S., Kaziro Y., Nagata S.; "Molecular cloning and characterization of cDNA for human myeloperoxidase."; J. Biol. Chem. 262:3844-3851(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2444596 [NCBI, ExPASy, EBI, Israel, Japan] Morishita K., Tsuchiya M., Asano S., Kaziro Y., Nagata S.; "Chromosomal gene structure of human myeloperoxidase and regulation of its expression by granulocyte colony-stimulating factor."; J. Biol. Chem. 262:15208-15213(1987).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17). PubMed=3654979 [NCBI, ExPASy, EBI, Israel, Japan] Seto P., Hirayu H., Magnusson R.P., Gestautas J., Portmann L., Degroot L.J., Rapoport B.; "Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase."; J. Clin. Invest. 80:1205-1208(1987).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17). DOI=10.1093/nar/15.5.2013; PubMed=3031585 [NCBI, ExPASy, EBI, Israel, Japan] Johnson K.R., Nauseef W.M., Care A., Wheelock M.J., Shane S., Hudson S., Koeffler H.P., Selsted M., Miller C., Rovera G.; "Characterization of cDNA clones for human myeloperoxidase: predicted amino acid sequence and evidence for multiple mRNA species."; Nucleic Acids Res. 15:2013-2028(1987).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS H7; H14 AND H17), AND PROTEIN SEQUENCE OF 165-183; 216-222; 295-304; 311-331; 464-479; 662-676 AND 766-776. TISSUE=Leukemia; DOI=10.1021/bi00416a013; PubMed=2903767 [NCBI, ExPASy, EBI, Israel, Japan] Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S., Yamada M.; "Multiple species of myeloperoxidase messenger RNAs produced by alternative splicing and differential polyadenylation."; Biochemistry 27:5906-5914(1988).
[6]	ERRATUM. Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S., Yamada M.; Biochemistry 27:9226-9226(1988).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1093/nar/17.19.7985; PubMed=2552418 [NCBI, ExPASy, EBI, Israel, Japan] Johnson K.R., Gemperlein I., Hudson S., Shane S., Rovera G.; "Complete nucleotide sequence of the human myeloperoxidase gene."; Nucleic Acids Res. 17:7985-7986(1989).
[8]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17). PubMed=8383257 [NCBI, ExPASy, EBI, Israel, Japan] Hosokawa Y., Kawaguchi R., Hikiji K., Yamada M., Suzuki K., Nakagawa T., Yoshihara T., Yamaguchi K.; "Cloning and characterization of four types of cDNA encoding myeloperoxidase from human monocytic leukemia cell line, SKM-1."; Leukemia 7:441-445(1993).
[9]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-53; CYS-604; GLN-683 AND VAL-717. NIEHS SNPs program; Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[10]	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.
[11]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM H17). 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).
[12]	PROTEIN SEQUENCE OF 49-66. DOI=10.1016/0006-291X(90)90888-T; PubMed=2154223 [NCBI, ExPASy, EBI, Israel, Japan] Yamada M., Hur S.-J., Toda H.; "Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures."; Biochem. Biophys. Res. Commun. 166:852-859(1990).
[13]	PROTEIN SEQUENCE OF 279-424. TISSUE=Leukocyte; PubMed=1334087 [NCBI, ExPASy, EBI, Israel, Japan] Taylor K.L., Pohl J., Kinkade J.M. Jr.; "Unique autolytic cleavage of human myeloperoxidase. Implications for the involvement of active site MET409."; J. Biol. Chem. 267:25282-25288(1992).
[14]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-629. PubMed=8390465 [NCBI, ExPASy, EBI, Israel, Japan] Yamada M., Yoshida M., Hashinaka K.; "Identification of transcriptional cis-elements in introns 7 and 9 of the myeloperoxidase gene."; J. Biol. Chem. 268:13479-13485(1993).
[15]	NUCLEOTIDE SEQUENCE [MRNA] OF 588-745. DOI=10.1016/0003-9861(87)90304-3; PubMed=2884926 [NCBI, ExPASy, EBI, Israel, Japan] Yamada M., Hur S.-J., Hashinaka K., Tsuneoka K., Saeki T., Nishio C., Sakiyama F., Tsunasawa S.; "Isolation and characterization of a cDNA coding for human myeloperoxidase."; Arch. Biochem. Biophys. 255:147-155(1987).
[16]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139 AND ASN-483, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.; "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."; J. Proteome Res. 4:2070-2080(2005).
[17]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323 AND ASN-483, AND MASS SPECTROMETRY. TISSUE=Saliva; DOI=10.1021/pr050492k; PubMed=16740002 [NCBI, ExPASy, EBI, Israel, Japan] Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.; "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."; J. Proteome Res. 5:1493-1503(2006).
[18]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-355 AND ASN-391, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan] Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."; J. Proteome Res. 8:651-661(2009).
[19]	X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 167-744. DOI=10.1074/jbc.275.16.11964; PubMed=10766826 [NCBI, ExPASy, EBI, Israel, Japan] Fiedler T.J., Davey C.A., Fenna R.E.; "X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8-A resolution."; J. Biol. Chem. 275:11964-11971(2000).
[20]	X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 167-744. DOI=10.1006/abbi.1995.1086; PubMed=7840679 [NCBI, ExPASy, EBI, Israel, Japan] Fenna R.E., Zeng J., Davey C.; "Structure of the green heme in myeloperoxidase."; Arch. Biochem. Biophys. 316:653-656(1995).
[21]	X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-744. DOI=10.1021/bi0111808; PubMed=11705390 [NCBI, ExPASy, EBI, Israel, Japan] Blair-Johnson M., Fiedler T., Fenna R.; "Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution."; Biochemistry 40:13990-13997(2001).
[22]	VARIANT MPD TRP-569. PubMed=8142659 [NCBI, ExPASy, EBI, Israel, Japan] Kizaki M., Miller C.W., Selsted M.E., Koeffler H.P.; "Myeloperoxidase (MPO) gene mutation in hereditary MPO deficiency."; Blood 83:1935-1940(1994).
[23]	VARIANT MPD TRP-569. PubMed=7904599 [NCBI, ExPASy, EBI, Israel, Japan] Nauseef W.M., Brigham S., Cogley M.; "Hereditary myeloperoxidase deficiency due to a missense mutation of arginine 569 to tryptophan."; J. Biol. Chem. 269:1212-1216(1994).
[24]	CHARACTERIZATION OF VARIANT MPD TRP-569. DOI=10.1074/jbc.271.16.9546; PubMed=8621627 [NCBI, ExPASy, EBI, Israel, Japan] Nauseef W., Cogley M., McCormick S.; "Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase."; J. Biol. Chem. 271:9546-9549(1996).
[25]	VARIANT MPD CYS-173, AND CHARACTERIZATION OF VARIANT MPD CYS-173. PubMed=9637725 [NCBI, ExPASy, EBI, Israel, Japan] DeLeo F.R., Goedken M., McCormick S.J., Nauseef W.M.; "A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation."; J. Clin. Invest. 101:2900-2909(1998).
[26]	VARIANT MPD THR-251. PubMed=9354683 [NCBI, ExPASy, EBI, Israel, Japan] Romano M., Dri P., Dadalt L., Patriarca P., Baralle F.E.; "Biochemical and molecular characterization of hereditary myeloperoxidase deficiency."; Blood 90:4126-4134(1997).
[27]	VARIANT [LARGE SCALE ANALYSIS] GLN-447. DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan] Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.; "The consensus coding sequences of human breast and colorectal cancers."; Science 314:268-274(2006).

Comments

FUNCTION: Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.
CATALYTIC ACTIVITY: Donor + H₂O₂ = oxidized donor + 2 H₂O.
CATALYTIC ACTIVITY: Cl^- + H₂O₂ = HOCl + 2 H₂O.
COFACTOR: Binds 1 calcium ion per heterodimer.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer.
SUBUNIT: Tetramer of two light chains and two heavy chains.
SUBCELLULAR LOCATION: Lysosome.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	H17
Synonyms	B
Isoform ID	P05164-1
This is the isoform sequence displayed in this entry.

Name	H14
Isoform ID	P05164-2
Features which should be applied to build the isoform sequence: VSP_007206.

Name	H7
Synonyms	A
Isoform ID	P05164-3
Features which should be applied to build the isoform sequence: VSP_007207.

DISEASE: Defects in MPO are the cause of myeloperoxidase deficiency (MPD) [MIM:254600]. MPD is an autosomal recessive defect that results in disseminated candidiasis.
SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
WEB RESOURCE: Name=MPObase; Note=MPO mutation db; URL="http://bioinf.uta.fi/MPObase/";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mpo/";.
WEB RESOURCE: Name=Wikipedia; Note=Myeloperoxidase entry; URL="http://en.wikipedia.org/wiki/Myeloperoxidase";.

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

J02694; AAA59896.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17176; AAA60346.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17170; AAA60346.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17171; AAA60346.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17172; AAA60346.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17173; AAA60346.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17174; AAA60346.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17175; AAA60346.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04876; CAA28565.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19507; AAA59863.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19508; AAA59864.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19508; AAA59865.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15377; CAA33438.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S56200; AAB25582.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ088846; AAY68218.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471109; EAW94470.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC130476; AAI30477.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D14466; BAA03362.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00007244; -.
IPI00236554; -.
IPI00236556; -.

PIR

A29467; OPHUM.
B28894; B28894.
D28894; D28894.

RefSeq

NP_000241.1; -.

UniGene

Hs.458272

3D structure databases

PDB

1CXP; X-ray; 1.80 A; A/B=167-270, C/D=279-744.	[ExPASy / RCSB / EBI]
1D2V; X-ray; 1.75 A; A/B=167-270, C/D=279-744.	[ExPASy / RCSB / EBI]
1D5L; X-ray; 1.90 A; A/B=167-270, C/D=279-744.	[ExPASy / RCSB / EBI]
1D7W; X-ray; 1.90 A; A/B=167-270, C/D=279-744.	[ExPASy / RCSB / EBI]
1DNU; X-ray; 1.85 A; A/B=167-270, C/D=279-744.	[ExPASy / RCSB / EBI]
1DNW; X-ray; 1.90 A; A/B=167-270, C/D=279-744.	[ExPASy / RCSB / EBI]
1MHL; X-ray; 2.25 A; A/B=165-272, C/D=279-744.	[ExPASy / RCSB / EBI]
1MYP; X-ray; 3.00 A; A/B=165-272, C/D=279-744.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1CXP; -.
1D2V; -.
1D5L; -.
1D7W; -.
1DNU; -.
1DNW; -.
1MHL; -.
1MYP; -.

ModBase

P05164.

Protein family/group databases

PeroxiBase

3315; HsMPO.

PTM databases

GlycoSuiteDB

P05164; -.

PhosphoSite

P05164; -.

Enzyme and pathway databases

BRENDA

1.11.1.7; 247.

Pathway_Interaction_DB

amb2_neutrophils_pathway; amb2 Integrin signaling.
il23pathway; IL23-mediated signaling events.

Organism-specific databases

GC17M053702; -.

HIX0039242; -.

HGNC:7218; MPO.

MPO.

CAB000059; -.

254600; phenotype. [NCBI / EBI]
606989; gene. [NCBI / EBI]

Orphanet

2587; Myeloperoxidase deficiency.

PharmGKB

PA243; -.

Gene expression databases

P05164; -.

P05164; -.

HS_MPO; -.

ENSG00000005381; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0005764;	Cellular component: lysosome (traceable author statement from ProtInc).
GO:0005634;	Cellular component: nucleus (traceable author statement from ProtInc).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003682;	Molecular function: chromatin binding (traceable author statement from ProtInc).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0004601;	Molecular function: peroxidase activity (inferred from direct assay from UniProtKB).
GO:0006916;	Biological process: anti-apoptosis (traceable author statement from ProtInc).
GO:0006952;	Biological process: defense response (traceable author statement from ProtInc).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from direct assay from UniProtKB).
GO:0034374;	Biological process: low-density lipoprotein particle remodeling (inferred from direct assay from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR002007; Haem_peroxidase_animal.
IPR019791; Haem_peroxidase_animal_sg.
IPR019794; Peroxidases_AS.
IPR019793; Peroxidases_heam-ligand_BS.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.640.10; Haem_peroxidase_animal; 1.

Pfam

PF03098; An_peroxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00457; ANPEROXIDASE.

PROSITE

PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; FALSE_NEG.
PS50292; PEROXIDASE_3; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P05164; -.

Genome annotation databases

Ensembl

ENSG00000005381; Homo sapiens. [Contig view]

GeneID

4353; -.

KEGG

hsa:4353; -.

Phylogenomic databases

HOVERGEN

P05164; -.

OMA

P05164; KSSGCAY.

Other

DB00535; Cefdinir.

17126; -.

P05164; -.

MPO; Homo sapiens.

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

Keywords

3D-structure; Alternative splicing; Calcium; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron; Lysosome; Metal-binding; Oxidation; Oxidoreductase; Peroxidase; Polymorphism; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 48`	`48`
`CHAIN`	`49 745`	`697`	`89 kDa myeloperoxidase.`	`PRO_0000023651`
`PROPEP`	`49 164`	`116`		`PRO_0000023652`
`CHAIN`	`155 745`	`591`	`84 kDa myeloperoxidase.`	`PRO_0000023653`
`CHAIN`	`165 745`	`581`	`Myeloperoxidase.`	`PRO_0000023654`
`CHAIN`	`165 278`	`114`	`Myeloperoxidase light chain.`	`PRO_0000023655`
`CHAIN`	`279 745`	`467`	`Myeloperoxidase heavy chain.`	`PRO_0000023656`
`ACT_SITE`	`261 261`		`Proton acceptor.`
`METAL`	`262 262`		`Calcium.`
`METAL`	`334 334`		`Calcium.`
`METAL`	`336 336`		`Calcium; via carbonyl oxygen.`
`METAL`	`338 338`		`Calcium.`
`METAL`	`340 340`		`Calcium.`
`METAL`	`502 502`		`Iron (heme axial ligand).`
`BINDING`	`260 260`		`Heme (covalent; via 3 links).`
`BINDING`	`408 408`		`Heme (covalent; via 3 links).`
`BINDING`	`409 409`		`Heme (covalent; via 3 links).`
`SITE`	`405 405`	`1`	`Transition state stabilizer.`
`MOD_RES`	`316 316`		`Cysteine sulfenic acid (-SOH).`
`CARBOHYD`	`139 139`		`N-linked (GlcNAc...).`
`CARBOHYD`	`323 323`		`N-linked (GlcNAc...).`
`CARBOHYD`	`355 355`		`N-linked (GlcNAc...).`
`CARBOHYD`	`391 391`		`N-linked (GlcNAc...).`
`CARBOHYD`	`483 483`		`N-linked (GlcNAc...) [GlycoSuiteDB].`	`CAR_000220`
`DISULFID`	`167 180`
`DISULFID`	`281 291`
`DISULFID`	`285 309`
`DISULFID`	`319 319`		`Interchain.`
`DISULFID`	`387 398`
`DISULFID`	`606 663`
`DISULFID`	`704 730`
`VAR_SEQ`	`1 95`		`Missing (in isoform H14).`	`VSP_007206`
`VAR_SEQ`	`182 182`		`N -> NRCGWLGVAAGTGLREASRTPQASRCQRPVLPC (in isoform H7).`	`VSP_007207`
`VARIANT`	`53 53`	`1`	`V -> F (in dbSNP:rs7208693 [NCBI]).`	`VAR_023995`
`VARIANT`	`173 173`	`1`	`Y -> C (in MPD; affects proteolytic processing and secretion).`	`VAR_015377 [3D]`
`VARIANT`	`251 251`	`1`	`M -> T (in MPD).`	`VAR_015378 [3D]`
`VARIANT`	`447 447`	`1`	`R -> Q (in a colorectal cancer sample; somatic mutation).`	`VAR_036517 [3D]`
`VARIANT`	`569 569`	`1`	`R -> W (in MPD; suppress post-translational processing).`	`VAR_015379 [3D]`
`VARIANT`	`604 604`	`1`	`R -> C.`	`VAR_023996 [3D]`
`VARIANT`	`683 683`	`1`	`E -> Q.`	`VAR_023997 [3D]`
`VARIANT`	`717 717`	`1`	`I -> V (in dbSNP:rs2759 [NCBI]).`	`VAR_012066 [3D]`
`CONFLICT`	`36 36`		`L -> V (in Ref. 4; CAA28565 and 7; CAA33438).`
`STRAND`	`181 185`	`5`
`TURN`	`186 189`	`4`
`STRAND`	`191 194`	`4`
`STRAND`	`206 208`	`3`
`HELIX`	`227 234`	`8`
`HELIX`	`239 241`	`3`
`STRAND`	`244 249`	`6`
`HELIX`	`250 263`	`14`
`TURN`	`281 283`	`3`
`STRAND`	`317 319`	`3`
`STRAND`	`323 325`	`3`
`STRAND`	`329 331`	`3`
`HELIX`	`340 343`	`4`
`HELIX`	`347 353`	`7`
`STRAND`	`358 360`	`3`
`HELIX`	`386 389`	`4`
`TURN`	`392 394`	`3`
`TURN`	`404 407`	`4`
`HELIX`	`410 433`	`24`
`HELIX`	`439 460`	`22`
`HELIX`	`463 467`	`5`
`HELIX`	`469 475`	`7`
`HELIX`	`492 497`	`6`
`HELIX`	`498 504`	`7`
`STRAND`	`507 510`	`4`
`STRAND`	`516 518`	`3`
`STRAND`	`523 526`	`4`
`HELIX`	`527 529`	`3`
`TURN`	`530 532`	`3`
`HELIX`	`534 539`	`6`
`HELIX`	`544 552`	`9`
`STRAND`	`553 556`	`4`
`HELIX`	`566 569`	`4`
`HELIX`	`574 576`	`3`
`STRAND`	`577 579`	`3`
`HELIX`	`583 593`	`11`
`HELIX`	`599 605`	`7`
`HELIX`	`614 621`	`8`
`HELIX`	`624 634`	`11`
`HELIX`	`637 639`	`3`
`HELIX`	`642 648`	`7`
`STRAND`	`655 657`	`3`
`HELIX`	`659 674`	`16`
`HELIX`	`688 694`	`7`
`HELIX`	`699 706`	`8`
`STRAND`	`711 713`	`3`
`TURN`	`717 719`	`3`
`TURN`	`723 726`	`4`
`STRAND`	`727 729`	`3`
`HELIX`	`730 732`	`3`
`HELIX`	`738 741`	`4`

Sequence information

Length: 745 AA [This is the length of the unprocessed precursor]

Molecular weight: 83869 Da [This is the MW of the unprocessed precursor]

CRC64: 348B1CE0A11038B4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGVPFFSSLR CMVDLGPCWA GGLTAEMKLL LALAGLLAIL ATPQPSEGAA PAVLGEVDTS 

        70         80         90        100        110        120 
LVLSSMEEAK QLVDKAYKER RESIKQRLRS GSASPMELLS YFKQPVAATR TAVRAADYLH 

       130        140        150        160        170        180 
VALDLLERKL RSLWRRPFNV TDVLTPAQLN VLSKSSGCAY QDVGVTCPEQ DKYRTITGMC 

       190        200        210        220        230        240 
NNRRSPTLGA SNRAFVRWLP AEYEDGFSLP YGWTPGVKRN GFPVALARAV SNEIVRFPTD 

       250        260        270        280        290        300 
QLTPDQERSL MFMQWGQLLD HDLDFTPEPA ARASFVTGVN CETSCVQQPP CFPLKIPPND 

       310        320        330        340        350        360 
PRIKNQADCI PFFRSCPACP GSNITIRNQI NALTSFVDAS MVYGSEEPLA RNLRNMSNQL 

       370        380        390        400        410        420 
GLLAVNQRFQ DNGRALLPFD NLHDDPCLLT NRSARIPCFL AGDTRSSEMP ELTSMHTLLL 

       430        440        450        460        470        480 
REHNRLATEL KSLNPRWDGE RLYQEARKIV GAMVQIITYR DYLPLVLGPT AMRKYLPTYR 

       490        500        510        520        530        540 
SYNDSVDPRI ANVFTNAFRY GHTLIQPFMF RLDNRYQPME PNPRVPLSRV FFASWRVVLE 

       550        560        570        580        590        600 
GGIDPILRGL MATPAKLNRQ NQIAVDEIRE RLFEQVMRIG LDLPALNMQR SRDHGLPGYN 

       610        620        630        640        650        660 
AWRRFCGLPQ PETVGQLGTV LRNLKLARKL MEQYGTPNNI DIWMGGVSEP LKRKGRVGPL 

       670        680        690        700        710        720 
LACIIGTQFR KLRDGDRFWW ENEGVFSMQQ RQALAQISLP RIICDNTGIT TVSKNNIFMS 

       730        740 
NSYPRDFVNC STLPALNLAS WREAS

P05164 in FASTA format

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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