FPS_FUJSV
ID FPS_FUJSV Reviewed; 873 AA.
AC P00530;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Tyrosine-protein kinase transforming protein Fps;
DE EC=2.7.10.2;
GN Name=V-FPS;
OS Fujinami sarcoma virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=11885;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6291784; DOI=10.1016/0092-8674(82)90283-5;
RA Shibuya M., Hanafusa H.;
RT "Nucleotide sequence of Fujinami sarcoma virus: evolutionary relationship
RT of its transforming gene with transforming genes of other sarcoma
RT viruses.";
RL Cell 30:787-795(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] (CLONE TS).
RX PubMed=2877522; DOI=10.1016/0042-6822(86)90172-8;
RA Chen L.H., Hatada E., Wheatley W., Lee W.H.;
RT "Single amino acid substitution, from Glu1025 to Asp, of the fps oncogenic
RT protein causes temperature sensitivity in transformation and kinase
RT activity.";
RL Virology 155:106-119(1986).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- MISCELLANEOUS: This protein is synthesized as a Gag-Fps polyprotein.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA42402.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J02194; AAA42402.1; ALT_INIT; Genomic_RNA.
DR EMBL; M14930; AAA42403.1; -; Genomic_RNA.
DR PIR; A00636; TVFVF.
DR PIR; A26898; TVFVFS.
DR SMR; P00530; -.
DR BindingDB; P00530; -.
DR ChEMBL; CHEMBL5708; -.
DR BRENDA; 2.7.10.2; 2335.
DR Proteomes; UP000124870; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR035849; Fes/Fps/Fer_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016250; Tyr-prot_kinase_Fes/Fps.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PIRSF; PIRSF000632; TyrPK_fps; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Oncogene;
KW Phosphoprotein; SH2 domain; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..873
FT /note="Tyrosine-protein kinase transforming protein Fps"
FT /id="PRO_0000088096"
FT DOMAIN 50..313
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 511..600
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 612..865
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 734
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 618..626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 764
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT VARIANT 63
FT /note="T -> S (in clone TS)"
FT VARIANT 251
FT /note="H -> R (in clone TS)"
FT VARIANT 300
FT /note="K -> E (in clone TS)"
FT VARIANT 343
FT /note="N -> S (in clone TS)"
FT VARIANT 438
FT /note="A -> T (in clone TS)"
FT VARIANT 447
FT /note="E -> D (in clone TS)"
FT VARIANT 463
FT /note="R -> C (in clone TS)"
FT VARIANT 716
FT /note="E -> D (in clone TS)"
SQ SEQUENCE 873 AA; 99536 MW; 1D774D48B18466B6 CRC64;
ASGQLHRPQP QEHTSTSAAA GTWRLTQASE SRHRLPHCSA APSHQDHSAM GFGPELWCPK
GHTELLRLQD SELRLLELMK KWMSQRAKSD REYAGMLHHM FSQLEKQEGL GHLRATDHSS
QIGESWWVLA SQTETLSQTL RRHAEELAAG PLAKLSILIR DKQQLRKVFS EQWQQLSQEY
AWTTQQEVEK LKAQYRSLVR DSTQAKRKYQ EASKDKEREK AKEKYVRSLS KLYALHNQYV
LAVQAAALHH HHHYQRALPT LHESLYSLQQ EMVLVLKEIL GEYCSITSLV QEDVLAIHQK
VAHAVEMIDP ATEYSSFVQC HRYDSEVPPA VTFDESLLEE AENLEPGELQ LNELTIESVQ
HSLTSIEEEL LASRKAVSSK EQRVWELQVE LRGEELALSP GERVHLLGKR QGLREAQQQL
QGLVCAQAKL QAQRDMLANK LAELGSEEPP PALPLQEDRQ SARSTDQERS GVTALKTIKN
HISGIFSPRF SLPPPVPLIP EVQKPLCQQA WYHGAIPRSE VQELLKYSGD FLVRESQGKQ
EYVLSVLWDG QPRHFIIQAA DNLYRLEDDG LPTIPLLIDH LLQSQRPITR KSGIVLTRAV
LKDKWVLNHE DVLLGERIGR GNFGEVFSGR LRADNTPVAV KSCRETLPPE LKAKFLQEAR
ILKQCNHPNI VRLIGVCTQK QPIYIVMELV QGGDFLSFLR SKGPRLKMKK LIKMMENAAA
GMEYLESKHC IHRDLAARNC LVTEKNTLKI SDFGMSRQEE DGVYASTGGM KQIPVKWTAP
EALNYGWYSS ESDVWSFGIL LWEAFSLGAV PYANLSNQQT REAIEQGVRL EPPEQCPEDV
YRLMQRCWEY DPHRRPSFGA VHQDLIAIRK RHR
