SRC_RSVSE
ID SRC_RSVSE Reviewed; 526 AA.
AC P63185;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Tyrosine-protein kinase transforming protein Src;
DE EC=2.7.10.2;
DE AltName: Full=pp60v-src;
DE Short=p60-Src;
DE Short=v-Src;
GN Name=V-SRC;
OS Rous sarcoma virus (strain Schmidt-Ruppin E) (RSV-SR-E).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=270623;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2537953; DOI=10.1093/nar/17.3.1252;
RA Barnier J.V., Dezelee P., Marx M., Calothy G.;
RT "Nucleotide sequence of the src gene of the Schmidt-Ruppin strain of Rous
RT sarcoma virus type E.";
RL Nucleic Acids Res. 17:1252-1252(1989).
CC -!- FUNCTION: This phosphoprotein, required for both the initiation and the
CC maintenance of neoplastic transformation, is a protein kinase that
CC catalyzes the phosphorylation of tyrosine residues in vitro.
CC {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- PTM: The phosphorylated form is termed pp60v-src.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; X13745; CAA32012.1; -; Genomic_DNA.
DR PDB; 2JYQ; NMR; -; A=144-249.
DR PDBsum; 2JYQ; -.
DR SMR; P63185; -.
DR DrugBank; DB01773; 4-[3-carboxymethyl-3-(4-phosphonooxy-benzyl)-ureido]-4-[(3-cyclohexyl-propyl)-methyl-carbamoyl]butyric acid.
DR EvolutionaryTrace; P63185; -.
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 Gene3D; 3.30.505.10; -; 1.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Lipoprotein; Myristate;
KW Nucleotide-binding; Oncogene; Phosphoprotein; SH2 domain; SH3 domain;
KW Transferase; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..526
FT /note="Tyrosine-protein kinase transforming protein Src"
FT /id="PRO_0000088154"
FT DOMAIN 81..142
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 148..245
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 267..517
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 273..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 416
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:2JYQ"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:2JYQ"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:2JYQ"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2JYQ"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:2JYQ"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:2JYQ"
FT STRAND 196..206
FT /evidence="ECO:0007829|PDB:2JYQ"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:2JYQ"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2JYQ"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:2JYQ"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:2JYQ"
SQ SEQUENCE 526 AA; 58953 MW; 85D356B6B8ECB14D CRC64;
MGSSKSKPKG PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL
FGDFNTSDTV TSPQRAGALA GGVTTFVALY DYESWIETDL SFKKGERLQI VNNTEGNWWL
AHSVTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT
KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR
LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG
TMSPEAFLQE AQVMKKLRHK KLVQLYAVVS EEPIYIVIEY MSKGSLLDFL KGEMGKYLRL
PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ
GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMGNGE VLDRVERGYR
MPCPPECPES LHDLMSQCWR RDPEERPTFE YLQAQLLPAC VLEVAE
