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P17594

- POLG_EMCVD

UniProt

P17594 - POLG_EMCVD

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
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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

    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

    GO - Cellular componenti

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

    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...

    Topological domain

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

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1565 – 158319Sequence AnalysisAdd
    BLAST

    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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    MATTMEQEIC AHSLTFKGCP KCSALQYRNG FYLLKYDEEW YPEELLTDGE     50
    DDVFDPELDM EVVFELQGNS TSSDKNNSSS DGNEGVIINN FYSNQYQNSI 100
    DLSANATGSD PPRTYGQFSN LLSGAVNAFS NMIPLLADQN TEEMENLSDR 150
    VLQDTAGNTV TNTQSTVGRL VGYGAVHDGE HPASCADTAS EKILAVERYY 200
    TFKVNDWTST QKPFEYIRIP LPHVLSGEDG GVFGAALRRH YLVKTGWRVQ 250
    VQCNASQFHA GSLLVFMAPE YPTLDAFAMD NRWSKDNLPN GTKTQTNRKG 300
    PFAMDHQNFW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT 350
    LVIAVVAPLT YSTGASTSLD ITASIQPVRP VFNGLRHETL SRQSPIPVTI 400
    REHAGTWYST LPDSTVPIYG KTPVAPANYM VGEYKDFLEI AQIPTFIGNK 450
    IPNAVPYIEA SNTAVKTQPL ATYQVTLSCS CLANTFLAAL SRNFAQYRGS 500
    LVYTFVFTGT AMMKGKFLIA YTPPGAGKPT SRDQAMQATY AIWDLGLNSS 550
    YSFTVPFISP THFRMVGTDQ VNITNVDGWV TVWQLTPLTY PPGCPTSAKI 600
    LTMVSAGKDF SLKMPISPAP WSPQGVENAE RGVTEDTDAT ADFVAQPVYL 650
    PENQTKVAFF YDRSSPIGAF AVKSGSLESG FAPFSNETCP NSVILTPGPQ 700
    FDPAYDQLRP QRLTEIWGNG NEETSKVFPL KSKQDYSFCL FSPFVYYKCD 750
    LEVTLSPHTS GNHGLLVRWC PTGTPAKPTT QVLHEVSSLS EGRTPQVYSA 800
    GPGISNQISF VVPYNSPLSV LPAVWYNGHK RFDNTGSLGI APNSDFGTLF 850
    FAGTKPDIKF TVYLRYKNMR VFCPRPTVFF PWPSSGDKID MTPRAGVLML 900
    ESPNALDISR TYPTLHILIQ FNHGGLEIRL FRHGMFWAEA HADVILRSRT 950
    KQISFLNNGS FPSMDARAPW NPWKNTYHAV LRAEPYRVTM DVYHKRIRPF 1000
    RLPLVQKEWN VREENVFGLY GIFNAHYAGY FADLLIHDIE TNPGPFMAKP 1050
    KKQVFQTQGA AVSSMAQTLL PNDLASKVMG SAFTALLDAN EDAQKAMRII 1100
    KTLSSLSDAW ENVKETLNNP EFWKQLLSRC VQLIAGMTIA VMHPDPLTLL 1150
    CLGTLTAAEI TSQTSLCEEI VAKFKKIFTT PPPRFPTISL FQQQSPLKQV 1200
    NDVFSLAKNL DWAVKTVEKV VDWFGTWVVQ EEKEQTLDQL LQRFPEHAKR 1250
    ISDLRNGMSA YVECKESFDF FEKLYNQAVK EKRTGIAAVC EKFRQKHDHA 1300
    TARCEPVVIV LRGDAGQGKS LSSQVIAQAV SKTIFGRQSV YSLPPDSDFF 1350
    DGYENQFAAI MDDLGQNPDG SDFTTFCQMV STTNFLPNMA SLERNGTPFT 1400
    SQIVVATTNL PEFRPVTIAH YPAVERRITF DYSVSAGPVC SKTEAGYKVL 1450
    DVERAFRPTG DAPLPCFQNN CLFLEKAGLQ FRDNRTKEIL SLVDVIERAV 1500
    ARIERKKKVL TTVQTLVAQA PVDEVSFHSV VQQLKARQEA TDEQLEELQE 1550
    AFAKTQERSS VFSDWMKISA MLCAATLALS QVVKMAKTVK QMVRPDLVRV 1600
    QLDEQEQGPY NEAVRAKPKT LQLLDIQGPN PVMDFEKYVA KFVTAPIDFV 1650
    YPTGVSTQTC LLVKGRTLAV NRHMAESDWS SIVVRGVTHA RSTVRILAIA 1700
    KAGKETDVSF IRLSSGPLFR DNTSKFVKAD DVLPATSAPV IGIMNTDIPM 1750
    MFTGTFLKAG VSVPVETGQT FNHCIHYKAN TRKGWCGSAL LADLGGKKKI 1800
    LGMHSAGSMG RTAASIVSQE MICAVVSAFE PQGALERLPD GPRIHVPRKT 1850
    ALRPTVARRV FQPAYAPAVL SKFDPRTEAD VDEVAFSKHT SNQESLPPVF 1900
    RMVAKEYANR VFTLLGRDNG RLTVKQALEG LEGMDPMDKN TSPGLPYTAL 1950
    GMRRTDVVDW ESATLIPYAA DRLKKMNEGD FSDIVYQTFL KDELRPVEKV 2000
    QAAKTRIVDV PPFEHCILGR QLLGRFASKF QTQPGLELGS AIGCDPDVHW 2050
    TAFGVAMQGF ERVYDVDYSN FDSTHSVAMF RLLAEEFFTP ENGFDPLVKE 2100
    YLESLAISTH AFEEKRYLIT GGLPSGCAAT SMLNTIMNNI IIRAGLYLTY 2150
    KNFEFDDVKV LSYGDDLLVA TNYQLNFDKV RASLAKTGYK ITPANKTSTF 2200
    PLDSTLEDVV FLKRKFKKEG PLYRPVMNRE ALEAMLSYYR PGTLSEKLTS 2250
    ITMLAVHSGK PEYDRLFAPF REVGVVVPSF ESVEYRWRSL FW 2292
    Length:2,292
    Mass (Da):255,428
    Last modified:February 1, 1996 - v2
    Checksum:iF2B0627B0F444107
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22458 Genomic RNA. Translation: AAA43034.1.
    PIRiA31473. GNNYED.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 1, 2014
    This is version 124 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