[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Peripheral blood lymphocyte; DOI=10.1093/nar/17.17.7108; PubMed=2780322 [NCBI, ExPASy, EBI, Israel, Japan] Soeda E., Yokoyama K., Yamazaki M., Akaogi K., Miwa T., Imai T.; "Nucleotide sequence of a full-length cDNA for 90 kDa heat-shock protein from human peripheral blood lymphocytes."; Nucleic Acids Res. 17:7108-7108(1989).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). PubMed=1368637 [NCBI, ExPASy, EBI, Israel, Japan] Yamazaki M., Tashiro H., Yokoyama K., Soeda E.; "Molecular cloning of cDNA encoding a human heat-shock protein whose expression is induced by adenovirus type 12 E1A in HeLa cells."; Agric. Biol. Chem. 54:3163-3170(1990).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Placenta; PubMed=2527334 [NCBI, ExPASy, EBI, Israel, Japan] Hickey E., Brandon S.E., Smale G., Lloyd D., Weber L.A.; "Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein."; Mol. Cell. Biol. 9:2615-2626(1989).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). DOI=10.1016/j.ygeno.2005.08.012; PubMed=16269234 [NCBI, ExPASy, EBI, Israel, Japan] Chen B., Piel W.H., Gui L., Bruford E., Monteiro A.; "The HSP90 family of genes in the human genome: insights into their divergence and evolution."; Genomics 86:627-637(2005).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. NHLBI resequencing and genotyping service (RS&G); Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-312. DOI=10.1016/0378-1119(88)90182-5; PubMed=2469626 [NCBI, ExPASy, EBI, Israel, Japan] Hoffmann T., Hovemann B.; "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens."; Gene 74:491-501(1988).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-312. DOI=10.1016/0378-1119(89)90408-3; PubMed=2591742 [NCBI, ExPASy, EBI, Israel, Japan] Walter T., Drabent B., Krebs H., Tomalak M., Heiss S., Benecke B.J.J.; "Cloning and analysis of a human 86-kDa heat-shock-protein-encoding gene."; Gene 83:105-115(1989).
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-732. TISSUE=Placenta; 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]	PROTEIN SEQUENCE OF 328-338 AND 346-355, AND MASS SPECTROMETRY. TISSUE=Brain, and Cajal-Retzius cell; Lubec G., Vishwanath V.; Submitted (MAR-2007) to UniProtKB.
[10]	NUCLEOTIDE SEQUENCE [MRNA] OF 539-732. TISSUE=Heart; Tanaka M., Tanaka T., Mitsui Y., Yamamoto M., Wood J.N.; "The analysis of the genes reactive to monoclonal antibody, CE5."; Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[11]	PROTEIN SEQUENCE OF 2-21, AND PHOSPHORYLATION. PubMed=2492519 [NCBI, ExPASy, EBI, Israel, Japan] Lees-Miller S.P., Anderson C.W.; "Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II."; J. Biol. Chem. 264:2431-2437(1989).
[12]	PHOSPHORYLATION BY PRKDC. PubMed=2507541 [NCBI, ExPASy, EBI, Israel, Japan] Lees-Miller S.P., Anderson C.W.; "The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues."; J. Biol. Chem. 264:17275-17280(1989).
[13]	SUBUNIT. PubMed=7588731 [NCBI, ExPASy, EBI, Israel, Japan] Nemoto T., Ohara-Nemoto Y., Ota M., Takagi T., Yokoyama K.; "Mechanism of dimer formation of the 90-kDa heat-shock protein."; Eur. J. Biochem. 233:1-8(1995).
[14]	INTERACTION WITH TOM34. DOI=10.1074/jbc.273.29.18007; PubMed=9660753 [NCBI, ExPASy, EBI, Israel, Japan] Young J.C., Obermann W.M., Hartl F.U.; "Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90."; J. Biol. Chem. 273:18007-18010(1998).
[15]	IDENTIFICATION AS A RENAL CANCER ANTIGEN. TISSUE=Renal cell carcinoma; DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; PubMed=10508479 [NCBI, ExPASy, EBI, Israel, Japan] Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.; "Antigens recognized by autologous antibody in patients with renal-cell carcinoma."; Int. J. Cancer 83:456-464(1999).
[16]	INTERACTION WITH AHSA1. DOI=10.1074/jbc.M212761200; PubMed=12604615 [NCBI, ExPASy, EBI, Israel, Japan] Lotz G.P., Lin H., Harst A., Obermann W.M.J.; "Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone."; J. Biol. Chem. 278:17228-17235(2003).
[17]	INTERACTION WITH SMYD3. DOI=10.1038/ncb1151; PubMed=15235609 [NCBI, ExPASy, EBI, Israel, Japan] Hamamoto R., Furukawa Y., Morita M., Iimura Y., Silva F.P., Li M., Yagyu R., Nakamura Y.; "SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells."; Nat. Cell Biol. 6:731-740(2004).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, AND MASS SPECTROMETRY. TISSUE=Brain cortex; DOI=10.1021/pr0498436; PubMed=15822905 [NCBI, ExPASy, EBI, Israel, Japan] DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., Pant H.C., Dosemeci A.; "Phosphoproteomic analysis of synaptosomes from human cerebral cortex."; J. Proteome Res. 4:306-315(2005).
[19]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-252 AND SER-263, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[20]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan] Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."; J. Proteome Res. 5:3135-3144(2006).
[21]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASS SPECTROMETRY. TISSUE=Pituitary; DOI=10.1007/s11102-006-8916-x; PubMed=16807684 [NCBI, ExPASy, EBI, Israel, Japan] Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; "Phosphoproteomic analysis of the human pituitary."; Pituitary 9:109-120(2006).
[22]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[23]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-252 AND SER-263, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan] Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.; "Phosphoproteome of resting human platelets."; J. Proteome Res. 7:526-534(2008).
[24]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan] Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.; "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."; Proteomics 8:1346-1361(2008).
[25]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-223. DOI=10.1016/S0092-8674(00)80203-2; PubMed=9108479 [NCBI, ExPASy, EBI, Israel, Japan] Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., Pavletich N.P.; "Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent."; Cell 89:239-250(1997).
[26]	X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-223. DOI=10.1083/jcb.143.4.901; PubMed=9817749 [NCBI, ExPASy, EBI, Israel, Japan] Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U.; "In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis."; J. Cell Biol. 143:901-910(1998).
[27]	INTERACTION WITH FNIP1, AND IDENTIFICATION BY MASS SPECTROMETRY. DOI=10.1073/pnas.0603781103; PubMed=17028174 [NCBI, ExPASy, EBI, Israel, Japan] Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L., Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III, Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr., Linehan W.M., Schmidt L.S., Zbar B.; "Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling."; Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006).

Comments

FUNCTION: Molecular chaperone. Has ATPase activity (By similarity).
SUBUNIT: Homodimer. Interacts with AHSA1, SMYD3 and TOM34. Interacts with FNIP1.
INTERACTION:
O15116:LSM1; NbExp=1; IntAct=EBI-296047, EBI-347619;
P08253:MMP2; NbExp=1; IntAct=EBI-296047, EBI-1033518;
Q92597:NDRG1; NbExp=1; IntAct=EBI-296047, EBI-716486;
P61247:RPS3A; NbExp=1; IntAct=EBI-296047, EBI-352378;
SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	HSP90AA1-1, HSP90-alpha 2
Isoform ID	P07900-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	HSP90AA1-2
Isoform ID	P07900-2
Features which should be applied to build the isoform sequence: VSP_026604.

SIMILARITY: Belongs to the heat shock protein 90 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

X15183; CAA33259.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M27024; AAA63194.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ890082; CAI64495.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ890083; CAI64496.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ314871; ABC40730.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X07270; CAA30255.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M30626; AAA36023.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000987; AAH00987.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC121062; AAI21063.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D87666; BAA13430.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D87666; BAA13431.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A32319; HHHU86.

NP_005339.3; -.

3D structure databases

PDB

1BYQ; X-ray; 1.50 A; A=9-236.	[ExPASy / RCSB / EBI]
1OSF; X-ray; 1.75 A; A=9-223.	[ExPASy / RCSB / EBI]
1UY6; X-ray; 1.90 A; A=1-236.	[ExPASy / RCSB / EBI]
1UY7; X-ray; 1.90 A; A=1-236.	[ExPASy / RCSB / EBI]
1UY8; X-ray; 1.98 A; A=1-236.	[ExPASy / RCSB / EBI]
1UY9; X-ray; 2.00 A; A=1-236.	[ExPASy / RCSB / EBI]
1UYC; X-ray; 2.00 A; A=1-236.	[ExPASy / RCSB / EBI]
1UYD; X-ray; 2.20 A; A=1-236.	[ExPASy / RCSB / EBI]
1UYE; X-ray; 2.00 A; A=1-236.	[ExPASy / RCSB / EBI]
1UYF; X-ray; 2.00 A; A=1-236.	[ExPASy / RCSB / EBI]
1UYG; X-ray; 2.00 A; A=1-236.	[ExPASy / RCSB / EBI]
1UYH; X-ray; 2.20 A; A=1-236.	[ExPASy / RCSB / EBI]
1UYI; X-ray; 2.20 A; A=1-236.	[ExPASy / RCSB / EBI]
1UYK; X-ray; 2.20 A; A=1-236.	[ExPASy / RCSB / EBI]
1UYL; X-ray; 1.40 A; A=1-236.	[ExPASy / RCSB / EBI]
1YC1; X-ray; 1.70 A; A=1-236.	[ExPASy / RCSB / EBI]
1YC3; X-ray; 2.12 A; A=1-236.	[ExPASy / RCSB / EBI]
1YC4; X-ray; 1.81 A; A=1-236.	[ExPASy / RCSB / EBI]
1YER; X-ray; 1.65 A; A=9-236.	[ExPASy / RCSB / EBI]
1YES; X-ray; 2.20 A; A=9-236.	[ExPASy / RCSB / EBI]
1YET; X-ray; 1.90 A; A=9-236.	[ExPASy / RCSB / EBI]
2BSM; X-ray; 2.05 A; A=1-236.	[ExPASy / RCSB / EBI]
2BT0; X-ray; 1.90 A; A/B=1-236.	[ExPASy / RCSB / EBI]
2BUG; NMR; -; B=-.	[ExPASy / RCSB / EBI]
2BYH; X-ray; 1.90 A; A=1-236.	[ExPASy / RCSB / EBI]
2BYI; X-ray; 1.60 A; A=1-236.	[ExPASy / RCSB / EBI]
2BZ5; X-ray; 1.90 A; A/B=1-236.	[ExPASy / RCSB / EBI]
2C2L; X-ray; 3.30 A; E/F/G/H=724-732.	[ExPASy / RCSB / EBI]
2CCS; X-ray; 1.79 A; A=1-236.	[ExPASy / RCSB / EBI]
2CCT; X-ray; 2.30 A; A=1-236.	[ExPASy / RCSB / EBI]
2CCU; X-ray; 2.70 A; A=1-236.	[ExPASy / RCSB / EBI]
2CDD; X-ray; 1.90 A; A/B=1-236.	[ExPASy / RCSB / EBI]
2FWY; X-ray; 2.10 A; A=1-236.	[ExPASy / RCSB / EBI]
2FWZ; X-ray; 2.10 A; A=1-236.	[ExPASy / RCSB / EBI]
2H55; X-ray; 2.00 A; A=1-236.	[ExPASy / RCSB / EBI]
2QF6; X-ray; 3.10 A; A/B/C/D=17-223.	[ExPASy / RCSB / EBI]
2QFO; X-ray; 1.68 A; A/B=17-223.	[ExPASy / RCSB / EBI]
2QG0; X-ray; 1.85 A; A/B=17-223.	[ExPASy / RCSB / EBI]
2QG2; X-ray; 1.80 A; A=17-223.	[ExPASy / RCSB / EBI]
2UWD; X-ray; 1.90 A; A=1-236.	[ExPASy / RCSB / EBI]
2VCI; X-ray; 2.00 A; A=1-236.	[ExPASy / RCSB / EBI]
2VCJ; X-ray; 2.50 A; A=1-236.	[ExPASy / RCSB / EBI]
3BM9; X-ray; 1.60 A; A=10-236.	[ExPASy / RCSB / EBI]
3BMY; X-ray; 1.60 A; A=10-236.	[ExPASy / RCSB / EBI]
3D0B; X-ray; 1.74 A; A=1-232.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BYQ; -.
1OSF; -.
1UY6; -.
1UY7; -.
1UY8; -.
1UY9; -.
1UYC; -.
1UYD; -.
1UYE; -.
1UYF; -.
1UYG; -.
1UYH; -.
1UYI; -.
1UYK; -.
1UYL; -.
1YC1; -.
1YC3; -.
1YC4; -.
1YER; -.
1YES; -.
1YET; -.
2BSM; -.
2BT0; -.
2BUG; -.
2BYH; -.
2BYI; -.
2BZ5; -.
2C2L; -.
2CCS; -.
2CCT; -.
2CCU; -.
2CDD; -.
2FWY; -.
2FWZ; -.
2H55; -.
2QF6; -.
2QFO; -.
2QG0; -.
2QG2; -.
2UWD; -.
2VCI; -.
2VCJ; -.
3BM9; -.
3BMY; -.
3D0B; -.

ModBase

P07900.

Protein-protein interaction databases

DIP

DIP:27595N; -.
DIP:414N; -.

IntAct

P07900; -.

PTM databases

PhosphoSite

P07900; -.

2D gel databases

OGP

P07900; -.

REPRODUCTION-2DPAGE

IPI00784295; -.

Organism-specific databases

H-InvDB

HIX0011983; -.
HIX0057370; -.

HGNC:5253; HSP90AA1.

CAB002058; -.

140571; gene. [NCBI / EBI]

GeneCards

P07900.

Gene expression databases

CleanEx

HS_HSP90AA1; -.

GermOnline

ENSG00000080824; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (non-traceable author statement from UniProtKB).
GO:0005524;	Molecular function: ATP binding (traceable author statement from UniProtKB).
GO:0030235;	Molecular function: nitric-oxide synthase regulator activity (inferred from sequence or structural similarity from UniProtKB).
GO:0042803;	Molecular function: protein homodimerization activity (traceable author statement from UniProtKB).
GO:0030911;	Molecular function: TPR domain binding (inferred from direct assay from UniProtKB).
GO:0006839;	Biological process: mitochondrial transport (traceable author statement from UniProtKB).
GO:0045429;	Biological process: positive regulation of nitric oxide biosynthetic process (inferred from sequence or structural similarity from UniProtKB).
GO:0042026;	Biological process: protein refolding (traceable author statement from UniProtKB).
GO:0006986;	Biological process: response to unfolded protein (non-traceable author statement from UniProtKB).
GO:0007165;	Biological process: signal transduction (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR003594; ATP_bd_ATPase.
IPR001404; Hsp90.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.565.10; ATP_bd_ATPase; 1.

PANTHER

PTHR11528; Hsp90; 1.

Pfam

PF02518; HATPase_c; 1.
PF00183; HSP90; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF002583; Hsp90; 1.

PRINTS

PR00775; HEATSHOCK90.

SMART

SM00387; HATPase_c; 1.
SMART graphical view of domain structure.

PS00298; HSP90; 1.

Genome annotation databases

Ensembl

ENSG00000080824; Homo sapiens. [Contig view]

GeneID

3320; -.

Phylogenomic databases

HOVERGEN

P07900; -.

Other

DB00615; Rifabutin.

P07900; -.

13162; -.

HSP90AA1; Homo sapiens.

UniRef

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

Keywords

3D-structure; Alternative splicing; ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Stress response.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 732`	`731`	`Heat shock protein HSP 90-alpha.`	`PRO_0000062911`
`MOD_RES`	`5 5`		`Phosphothreonine; by PRKDC.`
`MOD_RES`	`7 7`		`Phosphothreonine; by PRKDC.`
`MOD_RES`	`231 231`		`Phosphoserine.`
`MOD_RES`	`252 252`		`Phosphoserine.`
`MOD_RES`	`263 263`		`Phosphoserine.`
`MOD_RES`	`313 313`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`492 492`		`Phosphotyrosine (By similarity).`
`VAR_SEQ`	`1 1`		`M -> MPPCSGGDGSTPPGPSLRDRDCPAQSAEYPRDRLDPRPGS` `PSEASSPPFLRSRAPVNWYQEKAQVFLWHLLVSGSTTLLC` `LWKQPFHVSAFPVTASLAFRQSQGAGQHLYKDLQPFI` `LLRLL (in isoform 2).`	`VSP_026604`
`CONFLICT`	`63 63`		`S -> T (in Ref. 1; CAA33259).`
`CONFLICT`	`74 74`		`K -> R (in Ref. 4; CAI64495).`
`CONFLICT`	`86 86`		`D -> G (in Ref. 4; CAI64495).`
`STRAND`	`18 21`	`4`
`HELIX`	`24 35`	`12`
`HELIX`	`43 65`	`23`
`HELIX`	`67 70`	`4`
`STRAND`	`78 83`	`6`
`TURN`	`84 87`	`4`
`STRAND`	`88 93`	`6`
`HELIX`	`100 104`	`5`
`HELIX`	`106 108`	`3`
`HELIX`	`111 123`	`13`
`HELIX`	`128 134`	`7`
`HELIX`	`137 143`	`7`
`STRAND`	`145 153`	`9`
`STRAND`	`160 164`	`5`
`STRAND`	`169 174`	`6`
`STRAND`	`181 190`	`10`
`HELIX`	`192 198`	`7`
`HELIX`	`200 210`	`11`
`STRAND`	`218 220`	`3`
`STRAND`	`728 730`	`3`

Sequence information

Length: 732 AA [This is the length of the unprocessed precursor]

Molecular weight: 84660 Da [This is the MW of the unprocessed precursor]

CRC64: 969F65FCC0BC86FD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR 

        70         80         90        100        110        120 
YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME 

       130        140        150        160        170        180 
ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM 

       190        200        210        220        230        240 
GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED 

       250        260        270        280        290        300 
KEEEKEKEEK ESEDKPEIED VGSDEEEEKK DGDKKKKKKI KEKYIDQEEL NKTKPIWTRN 

       310        320        330        340        350        360 
PDDITNEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFVPRRAPFD LFENRKKKNN 

       370        380        390        400        410        420 
IKLYVRRVFI MDNCEELIPE YLNFIRGVVD SEDLPLNISR EMLQQSKILK VIRKNLVKKC 

       430        440        450        460        470        480 
LELFTELAED KENYKKFYEQ FSKNIKLGIH EDSQNRKKLS ELLRYYTSAS GDEMVSLKDY 

       490        500        510        520        530        540 
CTRMKENQKH IYYITGETKD QVANSAFVER LRKHGLEVIY MIEPIDEYCV QQLKEFEGKT 

       550        560        570        580        590        600 
LVSVTKEGLE LPEDEEEKKK QEEKKTKFEN LCKIMKDILE KKVEKVVVSN RLVTSPCCIV 

       610        620        630        640        650        660 
TSTYGWTANM ERIMKAQALR DNSTMGYMAA KKHLEINPDH SIIETLRQKA EADKNDKSVK 

       670        680        690        700        710        720 
DLVILLYETA LLSSGFSLED PQTHANRIYR MIKLGLGIDE DDPTADDTSA AVTEEMPPLE 

       730 
GDDDTSRMEE VD

P07900 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