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Non-structural polyprotein (Polyprotein nsP1234) (P1234) [Cleaved into: P123; P123'; mRNA-capping enzyme nsP1 (EC 2.1.1.-) (EC 2.7.7.-) (Non-structural protein 1); Protease nsP2 (EC 3.1.3.33) (EC 3.4.22.-) (EC 3.6.1.15) (EC 3.6.4.13) (Non-structural protein 2) (nsP2); Non-structural protein 3 (nsP3); Non-structural protein 3' (nsP3'); RNA-directed RNA polymerase nsP4 (EC 2.7.7.48) (Non-structural protein 4) (nsP4)]

 POLN_EEEVF              Reviewed;        2493 AA.
Q4QXJ8; Q4QXK0; Q5XZF4;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 2.
25-OCT-2017, entry version 93.
RecName: Full=Non-structural polyprotein;
AltName: Full=Polyprotein nsP1234;
Short=P1234;
Contains:
RecName: Full=P123;
Contains:
RecName: Full=P123';
Contains:
RecName: Full=mRNA-capping enzyme nsP1;
EC=2.1.1.-;
EC=2.7.7.-;
AltName: Full=Non-structural protein 1;
Contains:
RecName: Full=Protease nsP2;
EC=3.1.3.33;
EC=3.4.22.-;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Non-structural protein 2;
Short=nsP2;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsP3;
Contains:
RecName: Full=Non-structural protein 3';
Short=nsP3';
Contains:
RecName: Full=RNA-directed RNA polymerase nsP4;
EC=2.7.7.48;
AltName: Full=Non-structural protein 4;
Short=nsP4;
Eastern equine encephalitis virus (strain Florida 91-469) (EEEV)
(Eastern equine encephalomyelitis virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Alphavirus; EEEV complex.
NCBI_TaxID=374598;
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9126; Passeriformes.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Florida91-469, Georgia 97, and PE6;
PubMed=16147892; DOI=10.1080/10425170500136889;
Platteborze P.L., Kondig J.P., Schoepp R.J., Wasieloski L.P.;
"Comparative sequence analysis of the eastern equine encephalitis
virus pathogenic strains FL91-4679 and GA97 to other North American
strains.";
DNA Seq. 16:308-320(2005).
-!- FUNCTION: P123 and P123' are short-lived polyproteins,
accumulating during early stage of infection. P123 is directly
translated from the genome, whereas P123' is a product of the
cleavage of P1234. They localize the viral replication complex to
the cytoplasmic surface of modified endosomes and lysosomes. By
interacting with nsP4, they start viral genome replication into
antigenome. After these early events, P123 and P123' are cleaved
sequentially into nsP1, nsP2 and nsP3/nsP3'. This sequence of
delayed processing would allow correct assembly and membrane
association of the RNA polymerase complex (By similarity).
{ECO:0000250}.
-!- FUNCTION: nsP1 is a cytoplasmic capping enzyme. This function is
necessary since all viral RNAs are synthesized in the cytoplasm,
and host capping enzymes are restricted to the nucleus. The
enzymatic reaction involves a covalent link between 7-methyl-GMP
and nsP1, whereas eukaryotic capping enzymes form a covalent
complex only with GMP. nsP1 capping would consist in the following
reactions: GTP is first methylated and then forms the m7GMp-nsP1
complex, from which 7-methyl-GMP complex is transferred to the
mRNA to create the cap structure. Palmitoylated nsP1 is remodeling
host cell cytoskeleton, and induces filopodium-like structure
formation at the surface of the host cell (By similarity).
{ECO:0000250}.
-!- FUNCTION: nsP2 has two separate domain with different biological
activities. The N-terminal section is part of the RNA polymerase
complex and has RNA trisphosphatase and RNA helicase activity. The
C-terminal section harbors a protease that specifically cleaves
and releases the four mature proteins. Also inhibits cellular
transcription by inducing rapid degradation of POLR2A, a catalytic
subunit of the RNAPII complex. The resulting inhibition of
cellular protein synthesis serves to ensure maximal viral gene
expression and to evade host immune response (By similarity).
{ECO:0000250}.
-!- FUNCTION: nsP3 and nsP3' are essential for minus strand and
subgenomic 26S mRNA synthesis. {ECO:0000250}.
-!- FUNCTION: nsP4 is an RNA dependent RNA polymerase. It replicates
genomic and antigenomic RNA by recognizing replications specific
signals. Transcribes also a 26S subgenomic mRNA by initiating RNA
synthesis internally on antigenomic RNA. This 26S mRNA codes for
structural proteins. nsP4 is a short-lived protein regulated by
several ways: the opal codon readthrough and degradation by
ubiquitin pathway (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + GTP = m(7)GTP.
-!- CATALYTIC ACTIVITY: m7GTP + [nsP1 protein] = m7GMP-[nsP1 protein]
+ diphosphate.
-!- CATALYTIC ACTIVITY: m7GMP-[nsP1 protein] + (5')pp-Pur-mRNA =
m(7)G(5')ppp-Pur-mRNA + [nsP1 protein].
-!- CATALYTIC ACTIVITY: (5')ppp-mRNA + H(2)O = (5')pp-mRNA +
phosphate.
-!- CATALYTIC ACTIVITY: A 5'-phosphopolynucleotide + H(2)O = a
polynucleotide + phosphate.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBUNIT: P123 interacts with nsP4; nsP1, nsP2, nsP3 and nsP4
interact with each other, and with uncharacterized host factors.
-!- SUBCELLULAR LOCATION: Non-structural polyprotein: Host endosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Note=Located on the cytoplasmic
surface of modified endosomes and lysosomes, also called
cytopathic vacuoles type I (CPVI). These vacuoles contain numerous
small circular invaginations (spherules) which may be the sites of
RNA synthesis.
-!- SUBCELLULAR LOCATION: P123: Host endosome membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Host lysosome membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
-!- SUBCELLULAR LOCATION: P123': Host endosome membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Host lysosome membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
-!- SUBCELLULAR LOCATION: mRNA-capping enzyme nsP1: Host endosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host cell membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Host cell projection, host filopodium
{ECO:0000250}. Note=In the late phase of infection, the
polyprotein is quickly cleaved before localization to cellular
membranes. Then a fraction of nsP1 localizes to the inner surface
of the plasma membrane and its filopodial extensions (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protease nsP2: Host endosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host nucleus {ECO:0000250}.
Note=In the late phase of infection, the polyprotein is quickly
cleaved before localization to cellular membranes. Then
approximately half of nsP2 is found in the nucleus (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: Host endosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host cytoplasm {ECO:0000250}.
Note=In the late phase of infection, the polyprotein is quickly
cleaved before localization to cellular membranes. Then nsP3 and
nsP3' seems to aggregate in cytoplasm (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3': Host endosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host lysosome membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Host cytoplasm {ECO:0000250}.
Note=In the late phase of infection, the polyprotein is quickly
cleaved before localization to cellular membranes. Then nsP3 and
nsP3' seems to aggregate in cytoplasm (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase nsP4: Host
endosome membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Host lysosome
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}.
-!- INDUCTION: Viral replication produces dsRNA in the late phase of
infection, resulting in a strong activation of host EIF2AK2/PKR,
leading to almost complete phosphorylation of EIF2A. This
inactivates completely cellular translation initiation, resulting
in a dramatic shutoff of proteins synthesis. Translation of viral
non-structural polyprotein and all cellular proteins are stopped
in infected cell between 2 and 4 hours post infection. Only the
26S mRNA is still translated into viral structural proteins,
presumably through a unique mechanism of enhancer element which
counteract the translation inhibition mediated by EIF2A. By doing
this, the virus uses the cellular defense for its own advantage:
shutoff of cellular translation allows to produce big amounts of
structural proteins needed for the virus to bud out of the doomed
cell.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
The polyprotein is synthesized as P123, or P1234 by stop codon
readthrough. These polyproteins are processed differently
depending on the stage of infection. In early stages, P1234 is
first cleaved in trans, through its nsP2 protease activity,
releasing P123' and nsP4. P123/P123' and nsP4 start to replicate
the viral genome into its antigenome. After these early events,
nsP1 is cleaved in cis by nsP2 protease, releasing the P23/P23'
polyprotein. Cleavage of nsP1 exposes an 'activator' at the N-
terminus of P23/P23' which induces its cleavage into nsP2 and nsP3
by the viral protease. This sequence of delayed processing would
allow correct assembly and membrane association of the RNA-
polymerase complex. In the late stage of infection, the presence
of free nsP2 in the cytoplasm cleaves P1234 quickly into P12 and
P34, then into the four nsP (By similarity). {ECO:0000250}.
-!- PTM: nsP1 is palmitoylated by host. {ECO:0000250}.
-!- PTM: nsP4 is ubiquitinated; targets the protein for rapid
degradation via the ubiquitin system. {ECO:0000250}.
-!- MISCELLANEOUS: The genome codes for P123, but readthrough of a
terminator codon UGA occurs between the codons for Asn-1879 and
Arg-1880. This readthrough produces P1234, cleaved quickly by nsP2
into P123' and nsP4. Further processing of p123' gives nsP1, nsP2
and nsP3' which is 7 amino acids longer than nsP3 since the
cleavage site is after the readthrough. This unusual molecular
mechanism ensures that few nsP4 are produced compared to other
non-structural proteins. Mutant viruses with no alternative
termination site grow significantly slower than wild-type virus
(By similarity). {ECO:0000250}.
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EMBL; AY705241; AAT96379.1; -; Genomic_RNA.
EMBL; AY705240; AAT96377.1; -; Genomic_RNA.
EMBL; AY722102; AAU95734.1; -; Genomic_RNA.
ProteinModelPortal; Q4QXJ8; -.
SMR; Q4QXJ8; -.
MEROPS; C09.002; -.
PRIDE; Q4QXJ8; -.
OrthoDB; VOG09000007; -.
Proteomes; UP000008298; Genome.
Proteomes; UP000110644; Genome.
Proteomes; UP000170335; Genome.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0044176; C:host cell filopodium; IEA:UniProtKB-SubCell.
GO; GO:0044188; C:host cell lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
GO; GO:0039523; P:suppression by virus of host RNA polymerase II activity; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR002588; Alphavirus-like_MT_dom.
InterPro; IPR002620; Alphavirus_nsp2pro.
InterPro; IPR002589; Macro_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
Pfam; PF01661; Macro; 1.
Pfam; PF01707; Peptidase_C9; 1.
Pfam; PF00978; RdRP_2; 1.
Pfam; PF01443; Viral_helicase1; 1.
Pfam; PF01660; Vmethyltransf; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51743; ALPHAVIRUS_MT; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51520; NSP2PRO; 1.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host transcription shutoff by virus; GTP-binding; Helicase;
Host cell membrane; Host cell projection; Host cytoplasm;
Host endosome; Host gene expression shutoff by virus; Host lysosome;
Host membrane; Host nucleus; Host-virus interaction; Hydrolase;
Inhibition of host RNA polymerase II by virus; Lipoprotein; Membrane;
Methyltransferase; mRNA capping; mRNA processing;
Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
Palmitate; Phosphoprotein; Protease; RNA suppression of termination;
RNA-binding; RNA-directed RNA polymerase; S-adenosyl-L-methionine;
Thiol protease; Transferase; Ubl conjugation; Viral RNA replication.
CHAIN 1 2493 Non-structural polyprotein.
/FTId=PRO_0000308386.
CHAIN 1 1886 P123'.
/FTId=PRO_0000228760.
CHAIN 1 1879 P123.
/FTId=PRO_0000228761.
CHAIN 1 533 mRNA-capping enzyme nsP1.
/FTId=PRO_0000228762.
CHAIN 534 1327 Protease nsP2.
/FTId=PRO_0000228763.
CHAIN 1328 1885 Non-structural protein 3'.
/FTId=PRO_0000228764.
CHAIN 1328 1879 Non-structural protein 3.
/FTId=PRO_0000228765.
CHAIN 1886 2493 RNA-directed RNA polymerase nsP4.
/FTId=PRO_0000228766.
DOMAIN 28 257 Alphavirus-like MT. {ECO:0000255|PROSITE-
ProRule:PRU01079}.
DOMAIN 674 839 (+)RNA virus helicase ATP-binding.
DOMAIN 840 988 (+)RNA virus helicase C-terminal.
DOMAIN 1001 1320 Peptidase C9. {ECO:0000255|PROSITE-
ProRule:PRU00853}.
DOMAIN 1328 1486 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 2251 2366 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 719 726 ATP. {ECO:0000255}.
REGION 242 261 nsP1 membrane-binding. {ECO:0000250}.
REGION 1002 1021 Nucleolus localization signal.
{ECO:0000250}.
MOTIF 1177 1181 Nuclear localization signal.
{ECO:0000250}.
ACT_SITE 1010 1010 For cysteine protease nsP2 activity.
{ECO:0000255|PROSITE-ProRule:PRU00853}.
ACT_SITE 1079 1079 For cysteine protease nsP2 activity.
{ECO:0000255|PROSITE-ProRule:PRU00853}.
SITE 533 534 Cleavage; by nsP2. {ECO:0000250}.
SITE 1327 1328 Cleavage; by nsP2. {ECO:0000250}.
SITE 1885 1886 Cleavage; by nsP2. {ECO:0000250}.
LIPID 417 417 S-palmitoyl cysteine; by host.
{ECO:0000250}.
VARIANT 81 81 I -> V (in strain: PE6).
VARIANT 101 101 R -> G (in strain: PE6).
VARIANT 135 135 T -> A (in strain: PE6).
VARIANT 613 613 L -> P (in strain: Georgia 97 and PE6).
VARIANT 641 641 V -> A (in strain: PE6).
VARIANT 730 730 K -> Q (in strain: PE6).
VARIANT 1174 1174 M -> T (in strain: PE6).
VARIANT 1358 1358 S -> G (in strain: Georgia 97 and PE6).
VARIANT 1391 1391 V -> I (in strain: Georgia 97).
VARIANT 1618 1618 Q -> H (in strain: Georgia 97).
VARIANT 1774 1774 A -> V (in strain: PE6).
VARIANT 1791 1791 G -> A (in strain: PE6).
VARIANT 1864 1864 V -> A (in strain: Georgia 97 and PE6).
SEQUENCE 2493 AA; 277200 MW; 9CB21F44305D1CFE CRC64;
MEKVHVDLDA DSPFVKSLQR CFPHFEIEAT QVTDNDHANA RAFSHLATKL IEGEVDTDQV
ILDIGSAPVR HTHSKHKYHC ICPMKSAEDP DRLYRYADKL RKSDVTDKCI ASKAADLLTV
MSTPDAETPS LCMHTDSTCR YHGSVAVYQD VYAVHAPTSI YYQALKGVRT IYWIGFDTTP
FMYKNMAGAY PTYNTNWADE SVLEARNIGL GSSDLHEKSF GKVSIMRKKK LQPTNKVIFS
VGSTIYTEER ILLRSWHLPN VFHLKGKTSF TGRCNTIVSC EGYVVKKITL SPGIYGKVDN
LASTMHREGF LSCKVTDTLR GERVSFPVCT YVPATLCDQM TGILATDVSV DDAQKLLVGL
NQRIVVNGRT QRNTNTMQNY LLPVVAQAFS RWAREHRADL EDEKGLGVRE RSLVMGCCWA
FKTHKITSIY KRPGTQTIKK VPAVFNSFVI PQPTSYGLDI GLRRRIKMLF DAKKAPAPII
TEADVAHLKG LQDEAEAVAE AEAVRAALPP LLPEVDKETV EADIDLIMQE AGAGSVETPR
RHIKVTTYPG EEMIGSYAVL SPQAVLNSEK LACIHPLAEQ VLVMTHKGRA GRYKVEPYHG
RVIVPSGTAI PILDFQALSE SATIVFNERE FVNRYLHHIA VNGGALNTDE EYYKVVKSTE
TDSEYVFDID AKKCVKKGDA GPMCLVGELV DPPFHEFAYE SLKTRPAAPH KVPTIGVYGV
PGSGKSGIIK SAVTKRDLVV SAKKENCMEI IKDVKRMRGM DIAARTVDSV LLNGVKHSVD
TLYIDEAFAC HAGTLLALIA IVKPKKVVLC GDPKQCGFFN MMCLKVHFNH EICTEVYHKS
ISRRCTKTVT SIVSTLFYDK RMRTVNPCND KIIIDTTSTT KPLKDDIILT CFRGWVKQLQ
IDYKNHEIMT AAASQGLTRK GVYAVRYKVN ENPLYAQTSE HVNVLLTRTE KRIVWKTLAG
DPWIKTLTAS YPGNFTATLE EWQAEHDAIM AKILETPASS DVFQNKVNVC WAKALEPVLA
TANITLTRSQ WETIPAFKDD KAYSPEMALN FFCTRFFGVD IDSGLFSAPT VPLTYTNEHW
DNSPGPNMYG LCMRTAKELA RRYPCILKAV DTGRVADVRT DTIKDYNPLI NVVPLNRRLP
HSLVVTHRYT GNGDYSQLVT KMTGKTVLVV GTPMNIPGKR VETLGPSPQC TYKAELDLGI
PAALGKYDII FINVRTPYRH HHYQQCEDHA IHHSMLTRKA VDHLNKGGTC IALGYGTADR
ATENIISAVA RSFRFSRVCQ PKCAWENTEV AFVFFGKDNG NHLQDQDRLS VVLNNIYQGS
TQHEAGRAPA YRVVRGDITK SNDEVIVNAA NNKGQPGSGV CGALYRKWPG AFDKQPVATG
KAHLVKHSPN VIHAVGPNFS RLSENEGDQK LSEVYMDIAR IINNERFTKV SIPLLSTGIY
AGGKDRVMQS LNHLFTAMDT TDADITIYCL DKQWESRIKE AITRKESVEE LTEDDRPVDI
ELVRVHPLSS LAGRPGYSTT EGKVYSYLEG TRFHQTAKDI AEIYAMWPNK QEANEQICLY
VLGESMNSIR SKCPVEESEA SSPPHTIPCL CNYAMTAERV YRLRMAKNEQ FAVCSSFQLP
KYRITGVQKI QCSKPVIFSG TVPPAIHPRK FASVTVEDTP VVQPERLVPR RPAPPVPVPA
RIPSPPCTST NGSTTSIQSL GEDQSASASS GAEISVDQVS LWSIPSATGF DVRTSSSLSL
EQPTFPTMVV EAEIHASQGS LWSIPSITGS ETRAPSPPSQ DSRPSTPSAS GSHTSVDLIT
FDSVAEILED FSRSPFQFLS EIKPIPAPRT RVNNMSRSAD TIKPIPKPRK CQVKYTQPPG
VARVISAAEF DEFVRRHSNR YEAGAYIFSS ETGQGHLQQK STRQCKLQYP ILERSVHEKF
YAPRLDLERE KLLQKKLQLC ASEGNRSRYQ SRKVENMKAI TVERLLQGIG SYLSAEPQPV
ECYKVTYPAP MYSSTASNSF SSAEVAVKVC NLVLQENFPT VASYNITDEY DAYLDMVDGA
SCCLDTATFC PAKLRSFPKK HSYLRPEIRS AVPSPIQNTL QNVLAAATKR NCNVTQMREL
PVLDSAAFNV ECFKKYACND EYWDFYKTNP IRLTAENVTQ YVTKLKGPKA AALFAKTHNL
QPLHEIPMDR FVMDLKRDVK VTPGTKHTEE RPKVQVIQAA DPLATAYLCG IHRELVRRLN
AVLLPNIHTL FDMSAEDFDA IIAEHFQFGD AVLETDIASF DKSEDDAIAM SALMILEDLG
VDQALLNLIE AAFGNITSVH LPTGTRFKFG AMMKSGMFLT LFINTVVNIM IASRVLRERL
TTSPCAAFIG DDNIVKGVTS DALMAERCAT WLNMEVKIID AVVGVKAPYF CGGFIVVDQI
TGTACRVADP LKRLFKLGKP LPLDDDQDVD RRRALHDEAA RWNRIGITEE LVKAVESRYE
VNYVSLIITA LTTLASSVSN FKHIRGHPIT LYG


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OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 0.1 mg.
OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 0.1 mg.
20-272-190412 Filensin - Mouse monoclonal [FIL - 7B10] to Filensin; Beaded filament structural protein 1; Lens fiber cell beaded-filament structural protein CP 115; CP115; Lens intermediate filament-like heavy; LIF 0.1 ml
26-812 LPP may play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation 0.05 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 0.5 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 0.1 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 1 mg
EIAAB38762 Cape,Chromosome-associated protein E,FGF-inducible protein 16,Fin16,Mouse,Mus musculus,SMC protein 2,Smc2,SMC-2,Smc2l1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
EIAAB38761 CAPE,Chromosome-associated protein E,hCAP-E,Homo sapiens,Human,PRO0324,SMC protein 2,SMC2,SMC-2,SMC2L1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
EIAAB38770 Kiaa0594,MLZ-453,Mouse,mSMC5,Mus musculus,Protein expressed in male leptotene and zygotene spermatocytes 453,SMC protein 5,Smc5,SMC-5,Smc5l1,Structural maintenance of chromosomes protein 5
EIAAB38758 Mouse,Mus musculus,SMC protein 1B,Smc1b,SMC-1B,SMC-1-beta,Smc1l2,Structural maintenance of chromosomes protein 1B
EIAAB38757 Rat,Rattus norvegicus,SMC protein 1A,Smc1,Smc1a,SMC-1A,Smc1l1,Structural maintenance of chromosomes protein 1A
EIAAB38754 Bos taurus,Bovine,SMC protein 1A,SMC1,SMC1A,SMC-1A,SMC1L1,Structural maintenance of chromosomes protein 1A
orb81767 Measles Virus Non-Structural C-Protein (1-51) protein Proteins 100
EIAAB38773 Kiaa4103,Mouse,mSMC6,Mus musculus,SMC protein 6,Smc6,SMC-6,Smc6l1,Structural maintenance of chromosomes protein 6


 

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