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   22-FEB-2023, entry version 109.
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;
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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   OrthoDB; 14669at10239; -.
DR   EvolutionaryTrace; P03079; -.
DR   Proteomes; UP000008477; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.20.120.1860; Small t-antigen, unique domain; 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; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF161240; T-antigen specific domain-like; 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
//