SRC_RSVPA
ID SRC_RSVPA Reviewed; 523 AA.
AC P31693;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 120.
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 PA101T).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=31667;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1322589; DOI=10.1016/0042-6822(92)90579-e;
RA Dezelee P., Barnier J.V., Hampe A., Laugier D., Marx M., Galibert F.,
RA Calothy G.;
RT "Small deletion in v-src SH3 domain of a transformation defective mutant of
RT Rous sarcoma virus restores wild type transforming properties.";
RL Virology 189:556-567(1992).
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 -!- 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}.
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DR EMBL; M84475; AAA42581.1; ALT_SEQ; Genomic_DNA.
DR PIR; A42994; TVFVMT.
DR SMR; P31693; -.
DR BRENDA; 2.7.10.2; 5464.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Lipoprotein; Myristate; Nucleotide-binding; Oncogene;
KW Phosphoprotein; SH2 domain; SH3 domain; Transferase;
KW Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..523
FT /note="Tyrosine-protein kinase transforming protein Src"
FT /id="PRO_0000088151"
FT DOMAIN 71..139
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 145..242
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 264..514
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 270..278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 413
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 523 AA; 58778 MW; 853245739F6B90ED CRC64;
MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATELKL
FGDFNTSDTV TSPQRAGALA GSVTTFGTRE SRIETDLSFK KRERLQIVNN TEGTWWLAHS
LTTGQTGYIP SNYVAPSDSI QAEEWYFGKI TRRESGRLLL NPENPRGTFL VRESETTKGA
YCLSVSDFDN AKGLNVKHYK IRKLDSGGFY ITSRTQFSSL QQLVAYYSKH ADGLCHRLTN
VCPTSKPQTQ GLAKDAWEIP RESLRLEVKL GQGYFGEVWM GTWNGTTRVA IKTLKPGTMS
PEAFLQEAQV MKKLRHEKLV QLYAMVSEEP IYIVIEYMSK GSLLDFLKGE MGKYLRLPQL
VEMAAQIASG MAYVERMNYV HRDLRAANIL VGENLVCKVA DFGLARLIED NEYTARPGAR
FPVKWTAPEA ALYGRFTIKS DVWSFGILLT ELTTKGRVPY PGMVNGEVLD RVERGYRMPC
PPECPESLHD LMCQCWRKDP EERPTFEYLQ AQLLPACVLK IAE
