ID MIL_AVIMH Reviewed; 380 AA.
AC P00531;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Serine/threonine-protein kinase-transforming protein mil;
DE EC=2.7.11.1;
GN Name=V-MIL; Synonyms=V-MHT;
OS Avian retrovirus MH2.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=11870;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6325930; DOI=10.1038/309085a0;
RA Sutrave P., Bonner T.I., Rapp U.R., Jansen H.W., Patschinsky T., Bister K.;
RT "Nucleotide sequence of avian retroviral oncogene v-mil: homologue of
RT murine retroviral oncogene v-raf.";
RL Nature 309:85-88(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6328485; DOI=10.1073/pnas.81.10.3000;
RA Kan N.C., Flordellis C.S., Mark G.E., Duesberg P.H., Papas T.S.;
RT "Nucleotide sequence of avian carcinoma virus MH2: two potential onc genes,
RT one related to avian virus MC29 and the other related to murine sarcoma
RT virus 3611.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:3000-3004(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6320371; DOI=10.1126/science.6320371;
RA Kan N.C., Flordellis C.S., Mark G.E., Duesberg P.H., Papas T.S.;
RT "A common onc gene sequence transduced by avian carcinoma virus MH2 and by
RT murine sarcoma virus 3611.";
RL Science 223:813-816(1984).
CC -!- FUNCTION: By itself the v-Mil oncogene has only weak transforming
CC capacity but it abolishes the growth factor requirements of avian
CC macrophages transformed by other oncogenes.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- MISCELLANEOUS: This protein is synthesized as a Gag-Mht or Gag-Mil
CC polyprotein.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. RAF subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA25211.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X00534; CAA25211.1; ALT_INIT; Genomic_RNA.
DR PIR; A00639; TVFVMM.
DR SMR; P00531; -.
DR BRENDA; 2.7.11.1; 597.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF763; RAF PROTO-ONCOGENE SERINE_THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Oncogene;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..380
FT /note="Serine/threonine-protein kinase-transforming protein
FT mil"
FT /id="PRO_0000086328"
FT DOMAIN 82..341
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 88..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 211
FT /note="G -> E (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 42853 MW; 6498695FB7EBEE5D CRC64;
PTMPVDSRII EDAIRNHSES ASPSASSGSP NNMSPTGWSQ PKTPVPAQRE RAPGTNTQEK
NKIRPRGQRD SSYYWEIEAS EVLLSTRIGS GSFGTVYKGK WHGDVAVKIL KVVDPTPEQF
QAFRNEVAVL RKTRHVNILL FMGYMTKDNL AIVTQWCEGS SLYKHLHVQE TKFQMFQLID
IARQTAQGMD YLHAKNIIHR DMKSNNIFLH GGLTVKIGDF GLATVKSRWS GSQQVEQPTG
SILWMAPEVI RMQDSNPFSF QSDVYSYGIV LYELMTGELP YSHINNRDQI IFMVGRGYAS
PDLSKLYKNC PKAMKRLVAD CLKKVREERP LFPQILSSIA LLQHSLPKIN RSASEPSLHR
ASHTEDINSC TLTSTRLPVF
//
