[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 34-49. DOI=10.1016/0378-1119(89)90335-1; PubMed=2509294 [NCBI, ExPASy, EBI, Israel, Japan] Bragg T.S., Robertson D.L.; "Nucleotide sequence and analysis of the lethal factor gene (lef) from Bacillus anthracis."; Gene 81:45-54(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Lowe J.; "A comparison of Bacillus anthracis sequences."; Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Sterne; PubMed=10515943 [NCBI, ExPASy, EBI, Israel, Japan] Okinaka R.T., Cloud K., Hampton O., Hoffmaster A.R., Hill K.K., Keim P., Koehler T.M., Lamke G., Kumano S., Mahillon J., Manter D., Martinez Y., Ricke D., Svensson R., Jackson P.J.; "Sequence and organization of pXO1, the large Bacillus anthracis plasmid harboring the anthrax toxin genes."; J. Bacteriol. 181:6509-6515(1999).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Ames / isolate Florida / A2012; DOI=10.1126/science.1071837; PubMed=12004073 [NCBI, ExPASy, EBI, Israel, Japan] Read T.D., Salzberg S.L., Pop M., Shumway M.F., Umayam L., Jiang L., Holtzapple E., Busch J.D., Smith K.L., Schupp J.M., Solomon D., Keim P., Fraser C.M.; "Comparative genome sequencing for discovery of novel polymorphisms in Bacillus anthracis."; Science 296:2028-2033(2002).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Ames ancestor; Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.; "Bacillus anthracis comparative genomics."; Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-809. STRAIN=Carbosap, and Ferrara; DOI=10.1046/j.1365-2672.2002.01660.x; PubMed=12067380 [NCBI, ExPASy, EBI, Israel, Japan] Adone R., Pasquali P., La Rosa G., Marianelli C., Muscillo M., Fasanella A., Francia M., Ciuchini F.; "Sequence analysis of the genes encoding for the major virulence factors of Bacillus anthracis vaccine strain 'Carbosap'."; J. Appl. Microbiol. 93:117-121(2002).
[7]	FUNCTION. DOI=10.1126/science.280.5364.734; PubMed=9563949 [NCBI, ExPASy, EBI, Israel, Japan] Duesbery N.S., Webb C.P., Leppla S.H., Gordon V.M., Klimpel K.R., Copeland T.D., Ahn N.G., Oskarsson M.K., Fukasawa K., Paull K.D., Vande Woude G.F.; "Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor."; Science 280:734-737(1998).
[8]	FUNCTION. DOI=10.1006/bbrc.1998.9040; PubMed=9703991 [NCBI, ExPASy, EBI, Israel, Japan] Vitale G., Pellizzari R., Recchi C., Napolitani G., Mock M., Montecucco C.; "Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages."; Biochem. Biophys. Res. Commun. 248:706-711(1998).
[9]	FUNCTION. DOI=10.1046/j.1365-2672.1999.00892.x; PubMed=10475971 [NCBI, ExPASy, EBI, Israel, Japan] Duesbery N.S., Vande Woude G.F.; "Anthrax lethal factor causes proteolytic inactivation of mitogen-activated protein kinase kinase."; J. Appl. Microbiol. 87:289-293(1999).
[10]	FUNCTION. DOI=10.1042/0264-6021:3520739; PubMed=11104681 [NCBI, ExPASy, EBI, Israel, Japan] Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C.; "Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor."; Biochem. J. 352:739-745(2000).
[11]	FUNCTION. PubMed=10338520 [NCBI, ExPASy, EBI, Israel, Japan] Tang G., Leppla S.H.; "Proteasome activity is required for anthrax lethal toxin to kill macrophages."; Infect. Immun. 67:3055-3060(1999).
[12]	CHARACTERIZATION. DOI=10.1021/bi961518b; PubMed=8942659 [NCBI, ExPASy, EBI, Israel, Japan] Wang X.-M., Mock M., Ruysschaert J.-M., Cabiaux V.; "Secondary structure of anthrax lethal toxin proteins and their interaction with large unilamellar vesicles: a Fourier-transform infrared spectroscopy approach."; Biochemistry 35:14939-14946(1996).
[13]	ZINC-BINDING. DOI=10.1016/0378-1097(94)00452-8; PubMed=7851740 [NCBI, ExPASy, EBI, Israel, Japan] Kochi S.K., Schiavo G., Mock M., Montecucco C.; "Zinc content of the Bacillus anthracis lethal factor."; FEMS Microbiol. Lett. 124:343-348(1994).
[14]	REGULATION OF TOXIN EXPRESSION. STRAIN=Sterne; PubMed=8051039 [NCBI, ExPASy, EBI, Israel, Japan] Sirard J.-C., Mock M., Fouet A.; "The three Bacillus anthracis toxin genes are coordinately regulated by bicarbonate and temperature."; J. Bacteriol. 176:5188-5192(1994).
[15]	MUTAGENESIS OF HIS-719; GLU-720 AND HIS-723. STRAIN=Sterne; PubMed=9573135 [NCBI, ExPASy, EBI, Israel, Japan] Hammond S.E., Hanna P.C.; "Lethal factor active-site mutations affect catalytic activity in vitro."; Infect. Immun. 66:2374-2378(1998).
[16]	MUTAGENESIS OF VAL-180; TYR-181; TYR-182; GLU-183; ILE-184; GLY-185 AND LYS-186. STRAIN=Sterne; DOI=10.1006/bbrc.2000.4099; PubMed=11162493 [NCBI, ExPASy, EBI, Israel, Japan] Gupta P., Singh A., Chauhan V., Bhatnagar R.; "Involvement of residues 147VYYEIGK153 in binding of lethal factor to protective antigen of Bacillus anthracis."; Biochem. Biophys. Res. Commun. 280:158-163(2001).
[17]	MUTAGENESIS OF ASP-220; LEU-221; LEU-222 AND PHE-223. STRAIN=Sterne; DOI=10.1111/j.1574-6968.2002.tb11264.x; PubMed=12113932 [NCBI, ExPASy, EBI, Israel, Japan] Singh A., Chauhan V., Sodhi A., Bhatnagar R.; "Asp 187 and Phe 190 residues in lethal factor are required for the expression of anthrax lethal toxin activity."; FEMS Microbiol. Lett. 212:183-186(2002).
[18]	REVIEW. DOI=10.1016/S0041-0101(01)00161-1; PubMed=11595637 [NCBI, ExPASy, EBI, Israel, Japan] Brossier F., Mock M.; "Toxins of Bacillus anthracis."; Toxicon 39:1747-1755(2001).
[19]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND MAP2K2. DOI=10.1038/n35101998; PubMed=11700563 [NCBI, ExPASy, EBI, Israel, Japan] Pannifer A.D., Wong T.Y., Schwarzenbacher R., Renatus M., Petosa C., Bienkowska J., Lacy D.B., Collier R.J., Park S., Leppla S.H., Hanna P.C., Liddington R.C.; "Crystal structure of the anthrax lethal factor."; Nature 414:229-233(2001).
[20]	X-RAY CRYSTALLOGRAPHY (3.52 ANGSTROMS) OF 34-809 IN COMPLEX WITH ZINC IONS AND PEPTIDE SUBSTRATE ANALOG. DOI=10.1038/nsmb708; PubMed=14718924 [NCBI, ExPASy, EBI, Israel, Japan] Turk B.E., Wong T.Y., Schwarzenbacher R., Jarrell E.T., Leppla S.H., Collier R.J., Liddington R.C., Cantley L.C.; "The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor."; Nat. Struct. Mol. Biol. 11:60-66(2004).
[21]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 297-809 IN COMPLEX WITH ZINC IONS AND PROTEASE INHIBITOR. DOI=10.1073/pnas.0502159102; PubMed=15911756 [NCBI, ExPASy, EBI, Israel, Japan] Shoop W.L., Xiong Y., Wiltsie J., Woods A., Guo J., Pivnichny J.V., Felcetto T., Michael B.F., Bansal A., Cummings R.T., Cunningham B.R., Friedlander A.M., Douglas C.M., Patel S.B., Wisniewski D., Scapin G., Salowe S.P., Zaller D.M., Chapman K.T., Scolnick E.M., Schmatz D.M., Bartizal K., MacCoss M., Hermes J.D.; "Anthrax lethal factor inhibition."; Proc. Natl. Acad. Sci. U.S.A. 102:7958-7963(2005).

Comments

FUNCTION: One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. LF is the lethal factor that, when associated with PA, causes death. LF is not toxic by itself. It is a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5). Cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. There may be other cytosolic targets of LF involved in cytotoxicity. The proteasome may mediate a toxic process initiated by LF in the cell cytosol involving degradation of unidentified molecules that are essential for macrophage homeostasis. This is an early step in LeTx intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates.
CATALYTIC ACTIVITY: Preferred amino acids around the cleavage site can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases.
COFACTOR: Binds 1 zinc ion per subunit.
SUBUNIT: Anthrax toxins are composed of three distinct proteins, a protective antigen (PA), a lethal factor (LF) and an edema factor (EF). None of these is toxic by itself. PA+LF forms the lethal toxin (LeTx); PA+EF forms the edema toxin (EdTx).
SUBCELLULAR LOCATION: Secreted.
INDUCTION: Positively transcriptionally regulated by AtxA, which, in turn, is induced by bicarbonate and high temperatures (37 degrees Celsius).
DOMAIN: It comprises four domains: domain I binds the membrane-translocating component (PA); domains II, III and IV together create a long deep groove that holds the 16-residue N-terminal tail of MAPKK before cleavage. Domain IV contains the catalytic center.
DOMAIN: The PA-binding region is found in both B.anthracis EF and LF.
MISCELLANEOUS: LF binds to the heptamer formed by cleaved PA on the host cell membrane. This step is followed by internalization of the hetero-oligomeric complex by receptor-mediated endocytosis. LeTx requires passage through an acidic vesicle for activity; at acidic pH, as the pore is inserted into the membrane, LF is translocated and reaches its cytosolic targets. LF is probably directly involved in its routing, by interacting with the lipid membrane. This interaction could involve a conformational change of LF and/or an oligomerization of the protein. LF may have the capability of partially unfolding in order to cross the membrane.
SIMILARITY: Belongs to the peptidase M34 family [view classification].

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

M29081; AAA79216.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M30210; AAA22569.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF065404; AAD32411.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE011190; AAM26117.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017336; AAT28913.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ413934; CAC93932.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ413935; CAC93933.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JQ0032; JQ0032.

RefSeq

NP_052803.1; -.
NP_652928.1; -.
YP_016503.2; -.

3D structure databases

PDB

1J7N; X-ray; 2.30 A; A/B=34-809.	[ExPASy / RCSB / EBI]
1JKY; X-ray; 3.90 A; A=34-809.	[ExPASy / RCSB / EBI]
1PWP; X-ray; 2.90 A; A/B=34-809.	[ExPASy / RCSB / EBI]
1PWQ; X-ray; 3.52 A; A/B=34-809.	[ExPASy / RCSB / EBI]
1PWU; X-ray; 2.70 A; A/B=34-809.	[ExPASy / RCSB / EBI]
1PWV; X-ray; 2.85 A; A/B=34-809.	[ExPASy / RCSB / EBI]
1PWW; X-ray; 2.80 A; A/B=34-809.	[ExPASy / RCSB / EBI]
1YQY; X-ray; 2.30 A; A=297-809.	[ExPASy / RCSB / EBI]
1ZXV; X-ray; 2.67 A; A/B=34-809.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1J7N; -.
1JKY; -.
1PWP; -.
1PWQ; -.
1PWU; -.
1PWV; -.
1PWW; -.
1YQY; -.
1ZXV; -.

ModBase

P15917.

Protein family/group databases

MEROPS

M34.001; -.

Enzyme and pathway databases

BioCyc

BANT261594:GBAA_PXO1_0162-MON; -.

BRENDA

3.4.24.83; 267517.

Pathway_Interaction_DB

anthraxpathway; Cellular roles of Anthrax toxin.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-SubCell).
GO:0008237;	Molecular function: metallopeptidase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR015239; Anthrax_tox_lethal-fac_cen.
IPR003541; Anthrax_toxin_lethal/edema_N.
IPR014781; Anthrax_toxin_lethal/edema_N/C.
IPR006025; Pept_M_Zn_BS.
Graphical view of domain structure.

Pfam

PF09156; Anthrax-tox_M; 1.
PF07737; ATLF; 2.
Pfam graphical view of domain structure.

PRINTS

PR01392; ANTHRAXTOXNA.

PROSITE

PS00142; ZINC_PROTEASE; 1.

Genome annotation databases

GeneID

1158731; -.
2820148; -.
3361711; -.

GenomeReviews

AE017336_GR; GBAA_pXO1_0172.

KEGG

bar:GBAA_pXO1_0172; -.

TIGR

GBAA_pXO1_0172; -.

Phylogenomic databases

HOGENOM

P15917; -.

Other

ProtoNet

P15917.

UniRef

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

Keywords

3D-structure; Complete proteome; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Plasmid; Protease; Repeat; Secreted; Signal; Toxin; Virulence; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 33`	`33`
`CHAIN`	`34 809`	`776`	`Lethal factor.`	`PRO_0000029233`
`REPEAT`	`315 333`	`19`	`1.`
`REPEAT`	`342 357`	`16`	`2.`
`REPEAT`	`360 378`	`19`	`3.`
`REPEAT`	`380 397`	`18`	`4.`
`REPEAT`	`399 416`	`18`	`5.`
`REGION`	`34 293`	`260`	`PA-binding region (Potential).`
`REGION`	`60 295`	`236`	`I; PA-binding region (Potential).`
`REGION`	`296 330`	`35`	`IIA.`
`REGION`	`315 416`	`102`	`5 X approximate repeats.`
`REGION`	`336 416`	`81`	`III.`
`REGION`	`420 583`	`164`	`IIB.`
`REGION`	`585 809`	`225`	`IV.`
`ACT_SITE`	`720 720`
`METAL`	`719 719`		`Zinc; catalytic.`
`METAL`	`723 723`		`Zinc; catalytic.`
`METAL`	`768 768`		`Zinc; catalytic.`
`VARIANT`	`299 299`	`1`	`A -> S (in strain: Sterne).`
`MUTAGEN`	`180 180`		`V->A: No effect on PA-binding ability.`
`MUTAGEN`	`181 181`		`Y->A: Loss of ability to bind to PA.`
`MUTAGEN`	`182 182`		`Y->A: Loss of ability to bind to PA.`
`MUTAGEN`	`183 183`		`E->A: No effect on PA-binding ability.`
`MUTAGEN`	`184 184`		`I->A: Loss of ability to bind to PA.`
`MUTAGEN`	`185 185`		`G->A: No effect on PA-binding ability.`
`MUTAGEN`	`186 186`		`K->A: Loss of ability to bind to PA.`
`MUTAGEN`	`220 220`		`D->A: Loss of ability to bind to PA and loss of toxicity.`
`MUTAGEN`	`221 221`		`L->A: No effect on PA-binding ability and fully toxic.`
`MUTAGEN`	`222 222`		`L->A: No effect on PA-binding ability and fully toxic.`
`MUTAGEN`	`223 223`		`F->A: Loss of ability to bind to PA and non-toxic.`
`MUTAGEN`	`719 719`		`H->A: Loss of activity and zinc binding.`
`MUTAGEN`	`720 720`		`E->C,D: Loss of activity. No effect on zinc binding.`
`MUTAGEN`	`723 723`		`H->A: Loss of activity and zinc binding.`
`TURN`	`62 65`	`4`
`HELIX`	`66 76`	`11`
`STRAND`	`77 80`	`4`
`HELIX`	`87 97`	`11`
`HELIX`	`101 109`	`9`
`STRAND`	`113 119`	`7`
`HELIX`	`121 123`	`3`
`HELIX`	`125 127`	`3`
`HELIX`	`132 135`	`4`
`STRAND`	`136 138`	`3`
`STRAND`	`144 146`	`3`
`HELIX`	`147 149`	`3`
`STRAND`	`151 155`	`5`
`STRAND`	`157 159`	`3`
`STRAND`	`161 165`	`5`
`TURN`	`170 172`	`3`
`HELIX`	`174 190`	`17`
`HELIX`	`193 196`	`4`
`HELIX`	`201 211`	`11`
`STRAND`	`213 216`	`4`
`HELIX`	`217 222`	`6`
`HELIX`	`225 228`	`4`
`HELIX`	`236 240`	`5`
`HELIX`	`243 258`	`16`
`HELIX`	`260 269`	`10`
`HELIX`	`271 282`	`12`
`HELIX`	`284 293`	`10`
`HELIX`	`297 310`	`14`
`HELIX`	`312 316`	`5`
`HELIX`	`320 330`	`11`
`HELIX`	`337 341`	`5`
`TURN`	`342 346`	`5`
`HELIX`	`347 353`	`7`
`HELIX`	`357 359`	`3`
`STRAND`	`361 363`	`3`
`HELIX`	`365 375`	`11`
`HELIX`	`406 415`	`10`
`HELIX`	`421 428`	`8`
`HELIX`	`439 455`	`17`
`STRAND`	`469 474`	`6`
`HELIX`	`476 478`	`3`
`HELIX`	`481 484`	`4`
`HELIX`	`498 505`	`8`
`STRAND`	`510 513`	`4`
`STRAND`	`518 522`	`5`
`STRAND`	`532 537`	`6`
`STRAND`	`543 547`	`5`
`TURN`	`548 550`	`3`
`STRAND`	`551 554`	`4`
`STRAND`	`556 570`	`15`
`STRAND`	`573 583`	`11`
`HELIX`	`585 606`	`22`
`STRAND`	`616 619`	`4`
`HELIX`	`625 642`	`18`
`HELIX`	`645 657`	`13`
`STRAND`	`662 667`	`6`
`HELIX`	`669 671`	`3`
`HELIX`	`676 678`	`3`
`HELIX`	`682 684`	`3`
`STRAND`	`688 693`	`6`
`TURN`	`694 697`	`4`
`STRAND`	`698 705`	`8`
`HELIX`	`713 731`	`19`
`HELIX`	`745 753`	`9`
`HELIX`	`762 764`	`3`
`HELIX`	`766 777`	`12`
`HELIX`	`782 791`	`10`
`HELIX`	`793 802`	`10`

Sequence information

Length: 809 AA [This is the length of the unprocessed precursor]

Molecular weight: 93770 Da [This is the MW of the unprocessed precursor]

CRC64: 2076B4D7277317EE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNIKKEFIKV ISMSCLVTAI TLSGPVFIPL VQGAGGHGDV GMHVKEKEKN KDENKRKDEE 

        70         80         90        100        110        120 
RNKTQEEHLK EIMKHIVKIE VKGEEAVKKE AAEKLLEKVP SDVLEMYKAI GGKIYIVDGD 

       130        140        150        160        170        180 
ITKHISLEAL SEDKKKIKDI YGKDALLHEH YVYAKEGYEP VLVIQSSEDY VENTEKALNV 

       190        200        210        220        230        240 
YYEIGKILSR DILSKINQPY QKFLDVLNTI KNASDSDGQD LLFTNQLKEH PTDFSVEFLE 

       250        260        270        280        290        300 
QNSNEVQEVF AKAFAYYIEP QHRDVLQLYA PEAFNYMDKF NEQEINLSLE ELKDQRMLAR 

       310        320        330        340        350        360 
YEKWEKIKQH YQHWSDSLSE EGRGLLKKLQ IPIEPKKDDI IHSLSQEEKE LLKRIQIDSS 

       370        380        390        400        410        420 
DFLSTEEKEF LKKLQIDIRD SLSEEEKELL NRIQVDSSNP LSEKEKEFLK KLKLDIQPYD 

       430        440        450        460        470        480 
INQRLQDTGG LIDSPSINLD VRKQYKRDIQ NIDALLHQSI GSTLYNKIYL YENMNINNLT 

       490        500        510        520        530        540 
ATLGADLVDS TDNTKINRGI FNEFKKNFKY SISSNYMIVD INERPALDNE RLKWRIQLSP 

       550        560        570        580        590        600 
DTRAGYLENG KLILQRNIGL EIKDVQIIKQ SEKEYIRIDA KVVPKSKIDT KIQEAQLNIN 

       610        620        630        640        650        660 
QEWNKALGLP KYTKLITFNV HNRYASNIVE SAYLILNEWK NNIQSDLIKK VTNYLVDGNG 

       670        680        690        700        710        720 
RFVFTDITLP NIAEQYTHQD EIYEQVHSKG LYVPESRSIL LHGPSKGVEL RNDSEGFIHE 

       730        740        750        760        770        780 
FGHAVDDYAG YLLDKNQSDL VTNSKKFIDI FKEEGSNLTS YGRTNEAEFF AEAFRLMHST 

       790        800 
DHAERLKVQK NAPKTFQFIN DQIKFIINS

P15917 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