MT_POVHA
ID MT_POVHA Reviewed; 401 AA.
AC P03079;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Middle T antigen;
DE Short=MT;
DE Short=MT-AG;
OS Hamster polyomavirus (HaPyV) (Mesocricetus auratus polyomavirus 1).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Alphapolyomavirus.
OX NCBI_TaxID=1891729;
OH NCBI_TaxID=10036; Mesocricetus auratus (Golden hamster).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2988942; DOI=10.1002/j.1460-2075.1985.tb03773.x;
RA Delmas V., Bastien C., Scherneck S., Feunteun J.;
RT "A new member of the polyomavirus family: the hamster papovavirus. Complete
RT nucleotide sequence and transformation properties.";
RL EMBO J. 4:1279-1286(1985).
RN [2]
RP MUTAGENESIS OF TYR-324, AND INTERACTION WITH HOST FYN.
RX PubMed=8985339; DOI=10.1128/jvi.71.1.199-206.1997;
RA Dunant N.M., Messerschmitt A.S., Ballmer-Hofer K.;
RT "Functional interaction between the SH2 domain of Fyn and tyrosine 324 of
RT hamster polyomavirus middle-T antigen.";
RL J. Virol. 71:199-206(1997).
RN [3]
RP STRUCTURE BY NMR OF 321-331.
RX PubMed=9351806; DOI=10.1016/s0969-2126(97)00283-9;
RA Mulhern T.D., Shaw G.L., Morton C.J., Day A.J., Campbell I.D.;
RT "The SH2 domain from the tyrosine kinase Fyn in complex with a
RT phosphotyrosyl peptide reveals insights into domain stability and binding
RT specificity.";
RL Structure 5:1313-1323(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 321-331.
RX PubMed=7680435; DOI=10.1038/362087a0;
RA Eck M.J., Shoelson S.E., Harrison S.C.;
RT "Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-
RT 2 domain of p56lck.";
RL Nature 362:87-91(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 321-331.
RX PubMed=7680960; DOI=10.1016/0092-8674(93)90405-f;
RA Waksman G., Shoelson S.E., Pant N., Cowburn D., Kuriyan J.;
RT "Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain:
RT crystal structures of the complexed and peptide-free forms.";
RL Cell 72:779-790(1993).
CC -!- FUNCTION: Plays a role in transformation by modulating the activities
CC of cellular proteins involved in control of cell proliferation and by
CC acting as a functional homolog of an activated tyrosine kinase-
CC associated growth-factor receptor. Recruits upon association with
CC Ppp2/PP2A the Src tyrosine kinase component Fyn, thereby activating its
CC kinase activity. In turn, MT becomes phosphorylated and mediates signal
CC transduction pathways leading to cell cycle progression and cell
CC division. MT also plays a role in regulation of early and late gene
CC expression as well as viral DNA replication (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with host Ppp2/PP2A A and C subunits; this
CC interaction alters PP2A substrate specificity and localization (By
CC similarity). Interacts with host Fyn. {ECO:0000250,
CC ECO:0000269|PubMed:8985339}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Middle T antigen;
CC IsoId=P03079-1; Sequence=Displayed;
CC Name=Small t antigen;
CC IsoId=P03080-1; Sequence=External;
CC Name=Large T antigen;
CC IsoId=P03075-1; Sequence=External;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M26281; AAA67117.1; -; Genomic_DNA.
DR EMBL; X02449; CAB59362.1; -; Genomic_DNA.
DR PIR; A03615; TVVPMH.
DR RefSeq; YP_009111408.1; NC_001663.2. [P03079-1]
DR PDB; 1AOT; NMR; -; P=321-331.
DR PDB; 1AOU; NMR; -; P=321-331.
DR PDB; 1LCJ; X-ray; 1.80 A; B=321-331.
DR PDB; 1SPS; X-ray; 2.70 A; D/E/F=321-331.
DR PDB; 4U1P; X-ray; 1.40 A; B=321-331.
DR PDBsum; 1AOT; -.
DR PDBsum; 1AOU; -.
DR PDBsum; 1LCJ; -.
DR PDBsum; 1SPS; -.
DR PDBsum; 4U1P; -.
DR SMR; P03079; -.
DR ELM; P03079; -.
DR IntAct; P03079; 2.
DR MINT; P03079; -.
DR iPTMnet; P03079; -.
DR GeneID; 29030998; -.
DR KEGG; vg:29030998; -.
DR EvolutionaryTrace; P03079; -.
DR Proteomes; UP000008477; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.20.120.1860; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR003354; Papo_T_antigen.
DR InterPro; IPR036092; Papo_T_antigensf.
DR Pfam; PF02380; Papo_T_antigen; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF161240; SSF161240; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Early protein; Host membrane;
KW Host-virus interaction; Membrane; Oncogene; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..401
FT /note="Middle T antigen"
FT /id="PRO_0000115047"
FT TOPO_DOM 1..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 12..75
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 213..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 324
FT /note="Y->F: 70% loss of interaction with host Fyn."
FT /evidence="ECO:0000269|PubMed:8985339"
SQ SEQUENCE 401 AA; 46562 MW; 91B6172F4293F448 CRC64;
MDRILTKEEK QALISLLDLE PQYWGDYGRM QKCYKKKCLQ LHPDKGGNEE LMQQLNTLWT
KLKDGLYRVR LLLGPSQVRR LGKDQWNLSL QQTFSGTYFR RLCRLPITCL RNKGISTCNC
ILCLLRKQHF LLKKSWRVPC LVLGECYCID CFALWFGLPV TNMLVPLYAQ FLAPIPVDWL
DLNVHEVYNP ASGMTLMLPP PPADPESSTI LTQEDTGPTL MGQQDTLTSR RNTGKSFSLS
GMLMRTSPAK KSYHHQKMNS PPGIPIPPPP LFLFPVTAPV PPVTRNTQET QAERENEYMP
MAPQIHLYSQ IREPTHQEEE EPQYEEIPIY LELLPENPNQ HLALTSTARR SLRRKYHKHN
SHIITQRQRN RLRRLVLMIF LLSLGGFFLT LFFLIKRKMH L
