P1 proteinase
     (N-terminal protein)
Helper component proteinase
     (HC-pro)
     (EC 3.4.22.45)
Protein P3
6 kDa protein 1
     (6K1)
Cytoplasmic inclusion protein
     (CI)
     (EC 3.6.1.-)
6 kDa protein 2
     (6K2)
Viral genome-linked protein
     (VPg)
Nuclear inclusion protein A
     (NI-a)
     (NIa)
     (EC 3.4.22.44)
     (NIa-pro)
     (49 kDa proteinase)
     (49 kDa-Pro)
Nuclear inclusion protein B
     (NI-b)
     (NIb)
     (EC 2.7.7.48)
     (RNA-directed RNA polymerase)
Coat protein
     (CP)

Gene name

None

From

Tobacco etch virus (TEV)

[TaxID: 12227]

Taxonomy

Viruses; ssRNA positive-strand viruses, no DNA stage; Potyviridae; Potyvirus.

Virus hosts

Capsicum annuum (Bell pepper) [TaxID: 4072]
Cassia [TaxID: 53851]
Datura stramonium (Jimsonweed) (Common thornapple) [TaxID: 4076]
Nicotiana tabacum (Common tobacco) [TaxID: 4097]
Physalis [TaxID: 24663]
Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [TaxID: 4081]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Allison R., Johnston R.E., Dougherty W.G.; "The nucleotide sequence of the coding region of tobacco etch virus genomic RNA: evidence for the synthesis of a single polyprotein."; Virology 154:9-20(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2344-3054. PubMed=16593574 [NCBI, ExPASy, EBI, Israel, Japan] Allison R.F., Sorenson J.C., Kelly M.E., Armstrong F.B., Dougherty W.G.; "Sequence determination of the capsid protein gene and flanking regions of tobacco etch virus: evidence for synthesis and processing of a polyprotein in potyvirus genome expression."; Proc. Natl. Acad. Sci. U.S.A. 82:3969-3972(1985).
[3]	IDENTIFICATION OF PROTEASES. PubMed=2656254 [NCBI, ExPASy, EBI, Israel, Japan] Carrigton J.C., Cary S.M., Parks T.D., Dougherty W.G.; "A second proteinase encoded by a plant potyvirus genome."; EMBO J. 8:365-370(1989).
[4]	ACTIVE SITES OF HELPER COMPONENT PROTEINASE, AND MUTAGENESIS OF SER-610; HIS-619; SER-625; ASP-627; ASP-632; CYS-649; ASP-675; ASP-689; CYS-694; SER-698; ASP-715; HIS-716; HIS-722; ASP-725; SER-726; HIS-735; SER-743 AND SER-755. DOI=10.1016/0042-6822(89)90582-5; PubMed=2688301 [NCBI, ExPASy, EBI, Israel, Japan] Oh C.-S., Carrington J.C.; "Identification of essential residues in potyvirus proteinase HC-Pro by site-directed mutagenesis."; Virology 173:692-699(1989).
[5]	ACTIVE SITES OF NUCLEAR INCLUSION PROTEIN A. DOI=10.1016/0042-6822(89)90132-3; PubMed=2475971 [NCBI, ExPASy, EBI, Israel, Japan] Dougherty W.G., Parks T.D., Cary S.M., Bazan J.F., Fletterick R.J.; "Characterization of the catalytic residues of the tobacco etch virus 49-kDa proteinase."; Virology 172:302-310(1989).
[6]	ACTIVE SITES OF P1 PROTEINASE, AND MUTAGENESIS OF HIS-214 AND SER-256. DOI=10.1016/0042-6822(91)90522-D; PubMed=1962435 [NCBI, ExPASy, EBI, Israel, Japan] Verchot J., Koonin E.V., Carrington J.C.; "The 35-kDa protein from the N-terminus of the potyviral polyprotein functions as a third virus-encoded proteinase."; Virology 185:527-535(1991).
[7]	FUNCTION OF HELPER COMPONENT PROTEINASE, AND MUTAGENESIS OF LYS-358. PubMed=9880030 [NCBI, ExPASy, EBI, Israel, Japan] Blanc S., Ammar E.D., Garcia-Lampasona S., Dolja V.V., Llave C., Baker J., Pirone T.P.; "Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets."; J. Gen. Virol. 79:3119-3122(1998).
[8]	FUNCTION OF HELPER COMPONENT PROTEINASE. DOI=10.1006/viro.2001.0901; PubMed=11414807 [NCBI, ExPASy, EBI, Israel, Japan] Kasschau K.D., Carrington J.C.; "Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro."; Virology 285:71-81(2001).
[9]	REVIEW. DOI=10.1016/S0168-1702(01)00220-9; PubMed=11226583 [NCBI, ExPASy, EBI, Israel, Japan] Urcuqui-Inchima S., Haenni A.L., Bernardi F.; "Potyvirus proteins: a wealth of functions."; Virus Res. 74:157-175(2001).

Comments

FUNCTION: Coat protein is involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
FUNCTION: Nuclear inclusion protein B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication.
FUNCTION: Helper component proteinase is required for aphid transmission and also has proteolytic activity. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.
FUNCTION: Cytoplasmic inclusion protein has helicase activity. It may be involved in replication.
FUNCTION: Both 6K peptides are indispensable for virus replication (By similarity).
FUNCTION: Nuclear inclusion protein A has RNA-binding and proteolytic activities.
CATALYTIC ACTIVITY: Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
CATALYTIC ACTIVITY: Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
SUBCELLULAR LOCATION: Coat protein: Virion (Potential).
DOMAIN: The N-terminus of helper component proteinase is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus.
PTM: VPg is covalently linked to the genomic RNA (By similarity).
PTM: The viral RNA of potyviruses is expressed as a single polyprotein which undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity).
SIMILARITY: Belongs to the potyviruses polyprotein family.
SIMILARITY: Contains 1 helicase ATP-binding domain.
SIMILARITY: Contains 1 helicase C-terminal domain.
SIMILARITY: Contains 1 peptidase C4 domain [view classification].
SIMILARITY: Contains 1 peptidase C6 domain [view classification].
SIMILARITY: Contains 1 peptidase S30 domain [view classification].
SIMILARITY: Contains 1 RdRp catalytic domain.

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

M15239; AAA47910.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11458; AAA47909.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11216; AAA47908.1; ALT_SEQ; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A04207; GNBVEV.

RefSeq

NP_062908.1; -.

3D structure databases

PDB

1LVB; X-ray; 2.20 A; A/B=2038-2273, C/D=2785-2794.	[ExPASy / RCSB / EBI]
1LVM; X-ray; 1.80 A; A/B=2038-2258, C/D=2786-2794, E=2267-2273.	[ExPASy / RCSB / EBI]
1Q31; X-ray; 2.70 A; A/B=2038-2279.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1LVB; -.
1LVM; -.
1Q31; -.

ModBase

P04517.

Protein family/group databases

MEROPS

S30.001; -.

Ontologies

GO:0005198;	Molecular function: structural molecule activity (inferred from electronic annotation from UniProtKB-KW).
GO:0018144;	Biological process: RNA-protein covalent cross-linking (inferred from electronic annotation from UniProtKB-KW).
GO:0006410;	Biological process: transcription, RNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR014001; DEAD-like_N.
IPR001650; DNA/RNA_helicase_C.
IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
IPR014021; Helicase_SF1/SF2_ATP-bd.
IPR002540; Pept_S30_P1_potyvir.
IPR001730; Peptidase_C4.
IPR001456; Peptidase_C6.
IPR001592; Poty_coat.
IPR013648; PP_Potyviridae.
IPR001205; RNA_pol_P3D.
IPR007094; RNA_pol_PSvir.
Graphical view of domain structure.

Pfam

PF00270; DEAD; 1.
PF00271; Helicase_C; 1.
PF00863; Peptidase_C4; 1.
PF00851; Peptidase_C6; 1.
PF01577; Peptidase_S30; 1.
PF00767; Poty_coat; 1.
PF08440; Poty_PP; 1.
PF00680; RdRP_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00966; NIAPOTYPTASE.

SMART

SM00487; DEXDc; 1.
SM00490; HELICc; 1.
SMART graphical view of domain structure.

PROSITE

PS51192; HELICASE_ATP_BIND_1; 1.
PS51194; HELICASE_CTER; 1.
PS50507; RDRP_SSRNA_POS; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

3D-structure; ATP-binding; Capsid protein; Complete proteome; Covalent protein-RNA linkage; Helicase; Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease; RNA replication; RNA-directed RNA polymerase; Suppressor of RNA silencing; Thiol protease; Transferase; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 304`	`304`	`P1 proteinase (Potential).`	`PRO_0000040450`
`CHAIN`	`305 763`	`459`	`Helper component proteinase (Potential).`	`PRO_0000040451`
`CHAIN`	`764 1110`	`347`	`Protein P3 (By similarity).`	`PRO_0000040452`
`CHAIN`	`1111 1163`	`53`	`6 kDa protein 1 (By similarity).`	`PRO_0000040453`
`CHAIN`	`1164 1796`	`633`	`Cytoplasmic inclusion protein.`	`PRO_0000040454`
`CHAIN`	`1797 1849`	`53`	`6 kDa protein 2.`	`PRO_0000040455`
`CHAIN`	`1850 2037`	`188`	`Viral genome-linked protein (By similarity).`	`PRO_0000040456`
`CHAIN`	`2038 2279`	`242`	`Nuclear inclusion protein A (By similarity).`	`PRO_0000040457`
`CHAIN`	`2280 2791`	`512`	`Nuclear inclusion protein B.`	`PRO_0000040458`
`CHAIN`	`2792 3054`	`263`	`Coat protein.`	`PRO_0000040459`
`DOMAIN`	`1234 1386`	`153`	`Helicase ATP-binding.`
`DOMAIN`	`1401 1564`	`164`	`Helicase C-terminal.`
`DOMAIN`	`2521 2641`	`121`	`RdRp catalytic.`
`NP_BIND`	`1247 1254`	`8`	`ATP (Potential).`
`MOTIF`	`358 361`	`4`	`Involved in interaction with stylet and aphid transmission.`
`MOTIF`	`615 617`	`3`	`Involved in virions binding and aphid transmission (By similarity).`
`MOTIF`	`1336 1339`	`4`	`DECH box.`
`MOTIF`	`1889 1896`	`8`	`Nuclear localization signal (Potential).`
`ACT_SITE`	`214 214`		`For P1 proteinase activity.`
`ACT_SITE`	`223 223`		`For P1 proteinase activity (Potential).`
`ACT_SITE`	`256 256`		`For P1 proteinase activity.`
`ACT_SITE`	`649 649`		`For helper component proteinase activity.`
`ACT_SITE`	`722 722`		`For helper component proteinase activity.`
`ACT_SITE`	`2083 2083`		`For nuclear inclusion protein A activity (Probable).`
`ACT_SITE`	`2118 2118`		`For nuclear inclusion protein A activity (Probable).`
`ACT_SITE`	`2188 2188`		`For nuclear inclusion protein A activity (Probable).`
`SITE`	`304 305`	`2`	`Cleavage; by P1 proteinase (Potential).`
`SITE`	`763 764`	`2`	`Cleavage; by HC-pro.`
`SITE`	`1110 1111`	`2`	`Cleavage; by NIa-pro (By similarity).`
`SITE`	`1163 1164`	`2`	`Cleavage; by NIa-pro (By similarity).`
`SITE`	`1796 1797`	`2`	`Cleavage; by NIa-pro (By similarity).`
`SITE`	`1849 1850`	`2`	`Cleavage; by NIa-pro (By similarity).`
`SITE`	`2037 2038`	`2`	`Cleavage; by NIa-pro (By similarity).`
`SITE`	`2279 2280`	`2`	`Cleavage; by NIa-pro (By similarity).`
`SITE`	`2791 2792`	`2`	`Cleavage; by NIa-pro (By similarity).`
`MOD_RES`	`1911 1911`		`O-(5'-phospho-RNA)-tyrosine (By similarity).`
`MUTAGEN`	`214 214`		`H->A: Complete loss of proteolytic activity of P1 proteinase.`
`MUTAGEN`	`256 256`		`S->A: Complete loss of proteolytic activity of P1 proteinase.`
`MUTAGEN`	`314 314`		`F->L: Complete loss of aphid transmission.`
`MUTAGEN`	`358 358`		`K->E: Complete loss of interaction with stylet and aphid transmission; no effect on virion binding.`
`MUTAGEN`	`610 610`		`S->T: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`619 619`		`H->S: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`625 625`		`S->T: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`627 627`		`D->E: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`632 632`		`D->E: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`649 649`		`C->S: Complete loss of proteolytic activity of HC-pro.`
`MUTAGEN`	`675 675`		`D->E: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`689 689`		`D->E: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`694 694`		`C->S: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`698 698`		`S->T: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`715 715`		`D->E: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`716 716`		`H->S: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`722 722`		`H->S: Complete loss of proteolytic activity of HC-pro.`
`MUTAGEN`	`725 725`		`D->E: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`726 726`		`S->T: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`729 729`		`S->T: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`735 735`		`H->S: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`743 743`		`S->T: No effect on proteolytic activity of HC-pro.`
`MUTAGEN`	`755 755`		`S->T: No effect on proteolytic activity of HC-pro.`
`HELIX`	`2049 2052`	`4`
`STRAND`	`2055 2062`	`8`
`STRAND`	`2065 2074`	`10`
`STRAND`	`2077 2080`	`4`
`HELIX`	`2082 2085`	`4`
`STRAND`	`2089 2096`	`8`
`STRAND`	`2099 2104`	`6`
`HELIX`	`2106 2108`	`3`
`STRAND`	`2110 2113`	`4`
`STRAND`	`2120 2123`	`4`
`STRAND`	`2146 2153`	`8`
`STRAND`	`2155 2162`	`8`
`STRAND`	`2169 2171`	`3`
`TURN`	`2172 2175`	`4`
`STRAND`	`2176 2179`	`4`
`STRAND`	`2191 2194`	`4`
`TURN`	`2195 2197`	`3`
`STRAND`	`2200 2208`	`9`
`STRAND`	`2211 2218`	`8`
`HELIX`	`2223 2228`	`6`
`HELIX`	`2230 2232`	`3`
`STRAND`	`2244 2248`	`5`
`STRAND`	`2251 2256`	`6`
`STRAND`	`2276 2278`	`3`
`STRAND`	`2788 2790`	`3`

Sequence information

Length: 3054 AA [This is the length of the unprocessed precursor]

Molecular weight: 346164 Da [This is the MW of the unprocessed precursor]

CRC64: 0AF9A3626960B5CE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALIFGTVNA NILKEVFGGA RMACVTSAHM AGANGSILKK AEETSRAIMH KPVIFGEDYI 

        70         80         90        100        110        120 
TEADLPYTPL HLEVDAEMER MYYLGRRALT HGKRRKVSVN NKRNRRRKVA KTYVGRDSIV 

       130        140        150        160        170        180 
EKIVVPHTER KVDTTAAVED ICNEATTQLV HNSMPKRKKQ KNFLPATSLS NVYAQTWSIV 

       190        200        210        220        230        240 
RKRHMQVEII SKKSVRARVK RFEGSVQLFA SVRHMYGERK RVDLRIDNWQ QETLLDLAKR 

       250        260        270        280        290        300 
FKNERVDQSK LTFGSSGLVL RQGSYGPAHW YRHGMFIVRG RSDGMLVDAR AKVTFAVCHS 

       310        320        330        340        350        360 
MTHYSDKSIS EAFFIPYSKK FLELRPDGIS HECTRGVSVE RCGEVAAILT QALSPCGKIT 

       370        380        390        400        410        420 
CKRCMVETPD IVEGESGESV TNQGKLLAML KEQYPDFPMA EKLLTRFLQQ KSLVNTNLTA 

       430        440        450        460        470        480 
CVSVKQLIGD RKQAPFTHVL AVSEILFKGN KLTGADLEEA STHMLEIARF LNNRTENMRI 

       490        500        510        520        530        540 
GHLGSFRNKI SSKAHVNNAL MCDNQLDQNG NFIWGLRGAH AKRFLKGFFT EIDPNEGYDK 

       550        560        570        580        590        600 
YVIRKHIRGS RKLAIGNLIM STDFQTLRQQ IQGETIERKE IGNHCISMRN GNYVYPCCCV 

       610        620        630        640        650        660 
TLEDGKAQYS DLKHPTKRHL VIGNSGDSKY LDLPVLNEEK MYIANEGYCY MNIFFALLVN 

       670        680        690        700        710        720 
VKEEDAKDFT KFIRDTIVPK LGAWPTMQDV ATACYLLSIL YPDVLRAELP RILVDHDNKT 

       730        740        750        760        770        780 
MHVLDSYGSR TTGYHMLKMN TTSQLIEFVH SGLESEMKTY NVGGMNRDVV TQGAIEMLIK 

       790        800        810        820        830        840 
SIYKPHLMKQ LLEEEPYIIV LAIVSPSILI AMYNSGTFEQ ALQMWLPNTM RLANLAAILS 

       850        860        870        880        890        900 
ALAQKLTLAD LFVQQRNLIN EYAQVILDNL IDGVRVNHSL SLAMEIVTIK LATQEMDMAL 

       910        920        930        940        950        960 
REGGYAVTSE KVHEMLEKNY VKALKDAWDE LTWLEKFSAI RHSRKLLKFG RKPLIMKNTV 

       970        980        990       1000       1010       1020 
DCGGHIDLSV KSLFKFHLEL LKGTISRAVN GGARKVRVAK NAMTKGVFLK IYSMLPDVYK 

      1030       1040       1050       1060       1070       1080 
FITVSSVLSL LLTFLFQIDC MIRAHREAKV AAQLQKESEW DNIINRTFQY SKLENPIGYR 

      1090       1100       1110       1120       1130       1140 
STAEERLQSE HPEAFEYYKF CIGKEDLVEQ AKQPEIAYFE KIIAFITLVL MAFDAERSDG 

      1150       1160       1170       1180       1190       1200 
VFKILNKFKG ILSSTEREII YTQSLDDYVT TFDDNMTINL ELNMDELHKT SLPGVTFKQW 

      1210       1220       1230       1240       1250       1260 
WNNQISRGNV KPHYRTEGHF MEFTRDTAAS VASEISHSPA RDFLVRGAVG SGKSTGLPYH 

      1270       1280       1290       1300       1310       1320 
LSKRGRVLML EPTRPLTDNM HKQLRSEPFN CFPTLRMRGK STFGSSPITV MTSGFALHHF 

      1330       1340       1350       1360       1370       1380 
ARNIAEVKTY DFVIIDECHV NDASAIAFRN LLFEHEFEGK VLKVSATPPG REVEFTTQFP 

      1390       1400       1410       1420       1430       1440 
VKLKIEEALS FQEFVSLQGT GANADVISCG DNILVYVASY NDVDSLGKLL VQKGYKVSKI 

      1450       1460       1470       1480       1490       1500 
DGRTMKSGGT EIITEGTSVK KHFIVATNII ENGVTIDIDV VVDFGTKVVP VLDVDNRAVQ 

      1510       1520       1530       1540       1550       1560 
YNKTVVSYGE RIQKLGRVGR HKEGVALRIG QTNKTLVEIP EMVATEAAFL CFMYNLPVTT 

      1570       1580       1590       1600       1610       1620 
QSVSTTLLEN ATLLQARTMA QFELSYFYTI NFVRFDGSMH PVIHDKLKRF KLHTCETFLN 

      1630       1640       1650       1660       1670       1680 
KLAIPNKGLS SWLTSGEYKR LGYIAEDAGI RIPFVCKEIP DSLHEEIWHI VVAHKGDSGI 

      1690       1700       1710       1720       1730       1740 
GRLTSVQAAK VVYTLQTDVH SIARTLACIN RRIADEQMKQ SHFEAATGRA FSFTNYSIQS 

      1750       1760       1770       1780       1790       1800 
IFDTLKANYA TKHTKENIAV LQQAKDQLLE FSNLAKDQDV TGIIQDFNHL ETIYLQSDSE 

      1810       1820       1830       1840       1850       1860 
VAKHLKLKSH WNKSQITRDI IIALSVLIGG GWMLATYFKD KFNEPVYFQG KKNQKHKLKM 

      1870       1880       1890       1900       1910       1920 
REARGARGQY EVAAEPEALE HYFGSAYNNK GKRKGTTRGM GAKSRKFINM YGFDPTDFSY 

      1930       1940       1950       1960       1970       1980 
IRFVDPLTGH TIDESTNAPI DLVQHEFGKV RTRMLIDDEI EPQSLSTHTT IHAYLVNSGT 

      1990       2000       2010       2020       2030       2040 
KKVLKVDLTP HSSLRASEKS TAIMGFPERE NELRQTGMAV PVAYDQLPPK NEDLTFEGES 

      2050       2060       2070       2080       2090       2100 
LFKGPRDYNP ISSTICHLTN ESDGHTTSLY GIGFGPFIIT NKHLFRRNNG TLLVQSLHGV 

      2110       2120       2130       2140       2150       2160 
FKVKNTTTLQ QHLIDGRDMI IIRMPKDFPP FPQKLKFREP QREERICLVT TNFQTKSMSS 

      2170       2180       2190       2200       2210       2220 
MVSDTSCTFP SSDGIFWKHW IQTKDGQCGS PLVSTRDGFI VGIHSASNFT NTNNYFTSVP 

      2230       2240       2250       2260       2270       2280 
KNFMELLTNQ EAQQWVSGWR LNADSVLWGG HKVFMSKPEE PFQPVKEATQ LMNELVYSQG 

      2290       2300       2310       2320       2330       2340 
EKRKWVVEAL SGNLRPVAEC PSQLVTKHVV KGKCPLFELY LQLNPEKEAY FKPMMGAYKP 

      2350       2360       2370       2380       2390       2400 
SRLNREAFLK DILKYASEIE IGNVDCDLLE LAISMLVTKL KALGFPTVNY ITDPEEIFSA 

      2410       2420       2430       2440       2450       2460 
LNMKAAMGAL YKGKKKEALS ELTLDEQEAM LKASCLRLYT GKLGIWNGSL KAELRPIEKV 

      2470       2480       2490       2500       2510       2520 
ENNKTRTFTA APIDTLLAGK VCVDDFNNQF YDLNIKAPWT VGMTKFYQGW NELMEALPSG 

      2530       2540       2550       2560       2570       2580 
WVYCDADGSQ FDSSLTPFLI NAVLKVRLAF MEEWDIGEQM LRNLYTEIVY TPILTPDGTI 

      2590       2600       2610       2620       2630       2640 
IKKHKGNNSG QPSTVVDNTL MVIIAMLYTC EKCGINKEEI VYYVNGDDLL IAIHPDKAER 

      2650       2660       2670       2680       2690       2700 
LSRFKESFGE LGLKYEFDCT TRDKTQLWFM SHRALERDGM YIPKLEEERI VSILEWDRSK 

      2710       2720       2730       2740       2750       2760 
EPSHRLEAIC ASMIEAWGYD KLVEEIRNFY AWVLEQAPYS QLAEEGKAPY LAETALKFLY 

      2770       2780       2790       2800       2810       2820 
TSQHGTNSEI EEYLKVLYDY DIPTTENLYF QSGTVDAGAD AGKKKDQKDD KVAEQASKDR 

      2830       2840       2850       2860       2870       2880 
DVNAGTSGTF SVPRINAMAT KLQYPRMRGE VVVNLNHLLG YKPQQIDLSN ARATHEQFAA 

      2890       2900       2910       2920       2930       2940 
WHQAVMTAYG VNEEQMKILL NGFMVWCIEN GTSPNLNGTW VMMDGEDQVS YPLKPMVENA 

      2950       2960       2970       2980       2990       3000 
QPTLRQIMTH FSDLAEAYIE MRNRERPYMP RYGLQRNITD MSLSRYAFDF YELTSKTPVR 

      3010       3020       3030       3040       3050 
AREAHMQMKA AAVRNSGTRL FGLDGNVGTA EEDTERHTAH DVNRNMHTLL GVRQ

P04517 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