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P03079 (MT_POVHA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Middle T antigen

Short name=MT
Short name=MT-AG
OrganismHamster polyomavirus (HaPyV) [Complete proteome]
Taxonomic identifier10626 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stagePolyomaviridaePolyomavirus
Virus hostMesocricetus auratus (Golden hamster) [TaxID: 10036]

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in transformation by modulating the activities of cellular proteins involved in control of cell proliferation and by acting as a functional homolog of an activated tyrosine kinase-associated growth-factor receptor. Recruits upon association with Ppp2/PP2A the Src tyrosine kinase component Fyn, thereby activating its kinase activity. In turn, MT becomes phosphorylated and mediates signal transduction pathways leading to cell cycle progression and cell division. MT plays also a role in regulation of early and late gene expression as well as viral DNA replication By similarity.

Subunit structure

Interacts with host Ppp2/PP2A A and C subunits; this interaction alters PP2A substrate specificity and localization By similarity. Interacts with host Fyn. Ref.2

Subcellular location

Host membrane; Single-pass membrane protein Potential.

Sequence similarities

Contains 1 J domain.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentHost membrane
Membrane
   Coding sequence diversityAlternative splicing
   Developmental stageEarly protein
   DiseaseOncogene
   DomainTransmembrane
Transmembrane helix
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processviral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Middle T antigen (identifier: P03079-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Small t antigen (identifier: P03080-1)

The sequence of this isoform can be found in the external entry P03080.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform Large T antigen (identifier: P03075-1)

The sequence of this isoform can be found in the external entry P03075.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Middle T antigen
PRO_0000115047

Regions

Topological domain1 – 374374Cytoplasmic Potential
Transmembrane375 – 39521Helical; Potential
Topological domain396 – 4016Extracellular Potential
Domain12 – 7564J

Experimental info

Mutagenesis3241Y → F: 70% loss of interaction with host Fyn. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Middle T antigen [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 91B6172F4293F448

FASTA40146,562
        10         20         30         40         50         60 
MDRILTKEEK QALISLLDLE PQYWGDYGRM QKCYKKKCLQ LHPDKGGNEE LMQQLNTLWT 

        70         80         90        100        110        120 
KLKDGLYRVR LLLGPSQVRR LGKDQWNLSL QQTFSGTYFR RLCRLPITCL RNKGISTCNC 

       130        140        150        160        170        180 
ILCLLRKQHF LLKKSWRVPC LVLGECYCID CFALWFGLPV TNMLVPLYAQ FLAPIPVDWL 

       190        200        210        220        230        240 
DLNVHEVYNP ASGMTLMLPP PPADPESSTI LTQEDTGPTL MGQQDTLTSR RNTGKSFSLS 

       250        260        270        280        290        300 
GMLMRTSPAK KSYHHQKMNS PPGIPIPPPP LFLFPVTAPV PPVTRNTQET QAERENEYMP 

       310        320        330        340        350        360 
MAPQIHLYSQ IREPTHQEEE EPQYEEIPIY LELLPENPNQ HLALTSTARR SLRRKYHKHN 

       370        380        390        400 
SHIITQRQRN RLRRLVLMIF LLSLGGFFLT LFFLIKRKMH L 

« Hide

Isoform Small t antigen [UniParc].

See P03080.

Isoform Large T antigen [UniParc].

See P03075.

References

[1]"A new member of the polyomavirus family: the hamster papovavirus. Complete nucleotide sequence and transformation properties."
Delmas V., Bastien C., Scherneck S., Feunteun J.
EMBO J. 4:1279-1286(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Functional interaction between the SH2 domain of Fyn and tyrosine 324 of hamster polyomavirus middle-T antigen."
Dunant N.M., Messerschmitt A.S., Ballmer-Hofer K.
J. Virol. 71:199-206(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-324, INTERACTION WITH HOST FYN.
[3]"The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity."
Mulhern T.D., Shaw G.L., Morton C.J., Day A.J., Campbell I.D.
Structure 5:1313-1323(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 321-331.
[4]"Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck."
Eck M.J., Shoelson S.E., Harrison S.C.
Nature 362:87-91(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 321-331.
[5]"Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms."
Waksman G., Shoelson S.E., Pant N., Cowburn D., Kuriyan J.
Cell 72:779-790(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 321-331.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26281 Genomic DNA. Translation: AAA67117.1.
X02449 Genomic DNA. Translation: CAB59362.1.
PIRTVVPMH. A03615.
RefSeqNP_056731.1. NC_001663.1. [P03079-1]

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOTNMR-P321-331[»]
1AOUNMR-P321-331[»]
1LCJX-ray1.80B321-331[»]
1SPSX-ray2.70D/E/F321-331[»]
ProteinModelPortalP03079.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP03079. 1 interaction.
MINTMINT-8019810.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1489030.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
InterProIPR001623. DnaJ_domain.
IPR003354. Papo_T_antigen.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
PF02380. Papo_T_antigen. 1 hit.
[Graphical view]
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
PROSITEPS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03079.

Entry information

Entry nameMT_POVHA
AccessionPrimary (citable) accession number: P03079
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references