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P17594

- POLG_EMCVD

UniProt

P17594 - POLG_EMCVD

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Protein

Genome polyprotein

Gene
N/A
Organism
Encephalomyocarditis virus (strain emc-d diabetogenic)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Leader protein: promotes host NUP62, NUP153, and NUP214 phosphorylation and induces cessation of active nucleocytoplasmic transport. Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).By similarity
Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function (By similarity).By similarity
Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity). The capsid interacts with host VCAM1 to provide virion attachment on murine vascular endothelial cells.By similarity
Protein VP0: VP0 precursor is a component of immature procapsids.By similarity
Protein 2B: Affects membrane integrity and cause an increase in membrane permeability.By similarity
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).By similarity
Protein 3A, via its hydrophobic domain, serves as membrane anchor.By similarity
Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity).By similarity
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.PROSITE-ProRule annotation

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
NTP + H2O = NDP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei137 – 1382CleavageSequence Analysis
Sitei393 – 3942Cleavage; by protease 3CSequence Analysis
Sitei624 – 6252Cleavage; by protease 3CSequence Analysis
Sitei901 – 9022Cleavage; by protease 3CSequence Analysis
Sitei1044 – 10452Cleavage; by ribosomal skipSequence Analysis
Sitei1194 – 11952Cleavage; by protease 3CSequence Analysis
Sitei1519 – 15202Cleavage; by protease 3CSequence Analysis
Sitei1607 – 16082Cleavage; by protease 3CSequence Analysis
Sitei1627 – 16282Cleavage; by protease 3CSequence Analysis
Active sitei1673 – 16731For protease 3C activitySequence Analysis
Active sitei1705 – 17051For protease 3C activitySequence Analysis
Active sitei1786 – 17861For protease 3C activitySequence Analysis
Sitei1832 – 18332Cleavage; by protease 3CSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri10 – 2213Sequence AnalysisAdd
BLAST
Nucleotide bindingi1313 – 13208ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. ion channel activity Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
  5. RNA binding Source: UniProtKB-KW
  6. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  7. RNA helicase activity Source: InterPro
  8. structural molecule activity Source: InterPro

GO - Biological processi

  1. induction by virus of host autophagy Source: UniProtKB
  2. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  3. protein oligomerization Source: UniProtKB-KW
  4. RNA-protein covalent cross-linking Source: UniProtKB-KW
  5. suppression by virus of host gene expression Source: UniProtKB-KW
  6. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
  7. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  8. transcription, DNA-templated Source: InterPro
  9. viral entry into host cell Source: UniProtKB-KW
  10. viral RNA genome replication Source: InterPro
  11. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Transport, Viral attachment to host cell, Viral immunoevasion, Viral RNA replication, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

Protein family/group databases

MEROPSiC03.009.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Rho
Virion protein 4
Alternative name(s):
Beta
P1B
Virion protein 2
Alternative name(s):
Gamma
P1C
Virion protein 3
Alternative name(s):
Alpha
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Alternative name(s):
G
Protein 2B
Short name:
I
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
C
Short name:
P2C
Protein 3A
Short name:
P3A
Protein 3B
Short name:
P3B
Alternative name(s):
H
VPg
Protease 3C (EC:3.4.22.28)
Short name:
P3C
Alternative name(s):
Picornain 3C
p22
RNA-directed RNA polymerase 3D-POL (EC:2.7.7.48)
Short name:
E
Short name:
P3D-POL
OrganismiEncephalomyocarditis virus (strain emc-d diabetogenic)
Taxonomic identifieri12106 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mus musculus (Mouse) [TaxID: 10090]
Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
Sus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000008662: Genome

Subcellular locationi

Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity
Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity
Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity
Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 15641564CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei1565 – 158319Sequence AnalysisAdd
BLAST
Topological domaini1584 – 2292709CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell cytoplasmic vesicle Source: UniProtKB-KW
  2. host cell nucleus Source: UniProtKB-KW
  3. icosahedral viral capsid Source: InterPro
  4. integral to membrane of host cell Source: UniProtKB-KW
  5. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6767Leader proteinPRO_0000039804Add
BLAST
Chaini68 – 393326Protein VP0Sequence AnalysisPRO_0000310969Add
BLAST
Chaini68 – 13770Protein VP4Sequence AnalysisPRO_0000039805Add
BLAST
Chaini138 – 393256Protein VP2Sequence AnalysisPRO_0000039806Add
BLAST
Chaini394 – 624231Protein VP3Sequence AnalysisPRO_0000039807Add
BLAST
Chaini625 – 901277Protein VP1Sequence AnalysisPRO_0000039808Add
BLAST
Chaini902 – 1044143Protein 2ASequence AnalysisPRO_0000039809Add
BLAST
Chaini1045 – 1194150Protein 2BSequence AnalysisPRO_0000039810Add
BLAST
Chaini1195 – 1519325Protein 2CSequence AnalysisPRO_0000039811Add
BLAST
Chaini1520 – 160788Protein 3ASequence AnalysisPRO_0000039812Add
BLAST
Chaini1608 – 162720Protein 3BSequence AnalysisPRO_0000039813Add
BLAST
Chaini1628 – 1832205Protease 3CSequence AnalysisPRO_0000039814Add
BLAST
Chaini1833 – 2292460RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039815Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi68 – 681N-myristoyl glycine; by hostBy similarity
Modified residuei1610 – 16101O-(5'-phospho-RNA)-tyrosineBy similarity

Post-translational modificationi

Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle. The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond. This process would release the L-P1-2A peptide from the translational complex (By similarity).By similarity
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Protease 3C interacts with host TRIM22; this interaction leads to the ubiquitination of protease 3C and may restrict the virus replication. Protein 2A interacts with host EIF4E (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP17594.
SMRiP17594. Positions 1-32, 76-898.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1281 – 1447167SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini2061 – 2179119RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 6125AcidicBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 2 peptidase C3 domains.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri10 – 2213Sequence AnalysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProiIPR015031. Capsid_VP4_Picornavir.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR021573. Leader_pept_picornaV.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 2 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
PF11475. VP_N-CPKC. 1 hit.
[Graphical view]
PRINTSiPR00918. CALICVIRUSNS.
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17594-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MATTMEQEIC AHSLTFKGCP KCSALQYRNG FYLLKYDEEW YPEELLTDGE
60 70 80 90 100
DDVFDPELDM EVVFELQGNS TSSDKNNSSS DGNEGVIINN FYSNQYQNSI
110 120 130 140 150
DLSANATGSD PPRTYGQFSN LLSGAVNAFS NMIPLLADQN TEEMENLSDR
160 170 180 190 200
VLQDTAGNTV TNTQSTVGRL VGYGAVHDGE HPASCADTAS EKILAVERYY
210 220 230 240 250
TFKVNDWTST QKPFEYIRIP LPHVLSGEDG GVFGAALRRH YLVKTGWRVQ
260 270 280 290 300
VQCNASQFHA GSLLVFMAPE YPTLDAFAMD NRWSKDNLPN GTKTQTNRKG
310 320 330 340 350
PFAMDHQNFW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT
360 370 380 390 400
LVIAVVAPLT YSTGASTSLD ITASIQPVRP VFNGLRHETL SRQSPIPVTI
410 420 430 440 450
REHAGTWYST LPDSTVPIYG KTPVAPANYM VGEYKDFLEI AQIPTFIGNK
460 470 480 490 500
IPNAVPYIEA SNTAVKTQPL ATYQVTLSCS CLANTFLAAL SRNFAQYRGS
510 520 530 540 550
LVYTFVFTGT AMMKGKFLIA YTPPGAGKPT SRDQAMQATY AIWDLGLNSS
560 570 580 590 600
YSFTVPFISP THFRMVGTDQ VNITNVDGWV TVWQLTPLTY PPGCPTSAKI
610 620 630 640 650
LTMVSAGKDF SLKMPISPAP WSPQGVENAE RGVTEDTDAT ADFVAQPVYL
660 670 680 690 700
PENQTKVAFF YDRSSPIGAF AVKSGSLESG FAPFSNETCP NSVILTPGPQ
710 720 730 740 750
FDPAYDQLRP QRLTEIWGNG NEETSKVFPL KSKQDYSFCL FSPFVYYKCD
760 770 780 790 800
LEVTLSPHTS GNHGLLVRWC PTGTPAKPTT QVLHEVSSLS EGRTPQVYSA
810 820 830 840 850
GPGISNQISF VVPYNSPLSV LPAVWYNGHK RFDNTGSLGI APNSDFGTLF
860 870 880 890 900
FAGTKPDIKF TVYLRYKNMR VFCPRPTVFF PWPSSGDKID MTPRAGVLML
910 920 930 940 950
ESPNALDISR TYPTLHILIQ FNHGGLEIRL FRHGMFWAEA HADVILRSRT
960 970 980 990 1000
KQISFLNNGS FPSMDARAPW NPWKNTYHAV LRAEPYRVTM DVYHKRIRPF
1010 1020 1030 1040 1050
RLPLVQKEWN VREENVFGLY GIFNAHYAGY FADLLIHDIE TNPGPFMAKP
1060 1070 1080 1090 1100
KKQVFQTQGA AVSSMAQTLL PNDLASKVMG SAFTALLDAN EDAQKAMRII
1110 1120 1130 1140 1150
KTLSSLSDAW ENVKETLNNP EFWKQLLSRC VQLIAGMTIA VMHPDPLTLL
1160 1170 1180 1190 1200
CLGTLTAAEI TSQTSLCEEI VAKFKKIFTT PPPRFPTISL FQQQSPLKQV
1210 1220 1230 1240 1250
NDVFSLAKNL DWAVKTVEKV VDWFGTWVVQ EEKEQTLDQL LQRFPEHAKR
1260 1270 1280 1290 1300
ISDLRNGMSA YVECKESFDF FEKLYNQAVK EKRTGIAAVC EKFRQKHDHA
1310 1320 1330 1340 1350
TARCEPVVIV LRGDAGQGKS LSSQVIAQAV SKTIFGRQSV YSLPPDSDFF
1360 1370 1380 1390 1400
DGYENQFAAI MDDLGQNPDG SDFTTFCQMV STTNFLPNMA SLERNGTPFT
1410 1420 1430 1440 1450
SQIVVATTNL PEFRPVTIAH YPAVERRITF DYSVSAGPVC SKTEAGYKVL
1460 1470 1480 1490 1500
DVERAFRPTG DAPLPCFQNN CLFLEKAGLQ FRDNRTKEIL SLVDVIERAV
1510 1520 1530 1540 1550
ARIERKKKVL TTVQTLVAQA PVDEVSFHSV VQQLKARQEA TDEQLEELQE
1560 1570 1580 1590 1600
AFAKTQERSS VFSDWMKISA MLCAATLALS QVVKMAKTVK QMVRPDLVRV
1610 1620 1630 1640 1650
QLDEQEQGPY NEAVRAKPKT LQLLDIQGPN PVMDFEKYVA KFVTAPIDFV
1660 1670 1680 1690 1700
YPTGVSTQTC LLVKGRTLAV NRHMAESDWS SIVVRGVTHA RSTVRILAIA
1710 1720 1730 1740 1750
KAGKETDVSF IRLSSGPLFR DNTSKFVKAD DVLPATSAPV IGIMNTDIPM
1760 1770 1780 1790 1800
MFTGTFLKAG VSVPVETGQT FNHCIHYKAN TRKGWCGSAL LADLGGKKKI
1810 1820 1830 1840 1850
LGMHSAGSMG RTAASIVSQE MICAVVSAFE PQGALERLPD GPRIHVPRKT
1860 1870 1880 1890 1900
ALRPTVARRV FQPAYAPAVL SKFDPRTEAD VDEVAFSKHT SNQESLPPVF
1910 1920 1930 1940 1950
RMVAKEYANR VFTLLGRDNG RLTVKQALEG LEGMDPMDKN TSPGLPYTAL
1960 1970 1980 1990 2000
GMRRTDVVDW ESATLIPYAA DRLKKMNEGD FSDIVYQTFL KDELRPVEKV
2010 2020 2030 2040 2050
QAAKTRIVDV PPFEHCILGR QLLGRFASKF QTQPGLELGS AIGCDPDVHW
2060 2070 2080 2090 2100
TAFGVAMQGF ERVYDVDYSN FDSTHSVAMF RLLAEEFFTP ENGFDPLVKE
2110 2120 2130 2140 2150
YLESLAISTH AFEEKRYLIT GGLPSGCAAT SMLNTIMNNI IIRAGLYLTY
2160 2170 2180 2190 2200
KNFEFDDVKV LSYGDDLLVA TNYQLNFDKV RASLAKTGYK ITPANKTSTF
2210 2220 2230 2240 2250
PLDSTLEDVV FLKRKFKKEG PLYRPVMNRE ALEAMLSYYR PGTLSEKLTS
2260 2270 2280 2290
ITMLAVHSGK PEYDRLFAPF REVGVVVPSF ESVEYRWRSL FW
Length:2,292
Mass (Da):255,428
Last modified:February 1, 1996 - v2
Checksum:iF2B0627B0F444107
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22458 Genomic RNA. Translation: AAA43034.1.
PIRiA31473. GNNYED.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22458 Genomic RNA. Translation: AAA43034.1 .
PIRi A31473. GNNYED.

3D structure databases

ProteinModelPortali P17594.
SMRi P17594. Positions 1-32, 76-898.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProi IPR015031. Capsid_VP4_Picornavir.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR021573. Leader_pept_picornaV.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view ]
Pfami PF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 2 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
PF11475. VP_N-CPKC. 1 hit.
[Graphical view ]
PRINTSi PR00918. CALICVIRUSNS.
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genomic differences between the diabetogenic and nondiabetogenic variants of encephalomyocarditis virus."
    Bae Y.S., Eun H.M., Yoon J.W.
    Virology 170:282-287(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Molecular identification of diabetogenic viral gene."
    Bae Y.S., Eun H.M., Yoon J.W.
    Diabetes 38:316-320(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "VCAM-1 is a receptor for encephalomyocarditis virus on murine vascular endothelial cells."
    Huber S.A.
    J. Virol. 68:3453-3458(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST VCAM1.

Entry informationi

Entry nameiPOLG_EMCVD
AccessioniPrimary (citable) accession number: P17594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3