ID SRC_AVIS2 Reviewed; 587 AA. AC P15054; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 08-NOV-2023, entry version 144. 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 Avian sarcoma virus (strain PR2257). OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus; OC Y73 avian sarcoma virus. OX NCBI_TaxID=11879; OH NCBI_TaxID=8976; Galliformes. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2463376; DOI=10.1128/jvi.63.2.481-492.1989; RA Geryk J., Dezelee P., Barnier J.V., Svoboda J., Nehyba J., Karakoz I., RA Rynditch A.V., Yatsula B.A., Calothy G.; RT "Transduction of the cellular src gene and 3' adjacent sequences in avian RT sarcoma virus PR2257."; RL J. Virol. 63:481-492(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RA Yatsula B.A., Geryk J., Svoboda J., Rynditch A.V., Calothy G., Dezelee P.; RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; M21526; AAA42583.1; -; Genomic_RNA. DR EMBL; X51863; CAA36156.1; -; Genomic_RNA. DR PIR; A30174; TVFVPR. DR SMR; P15054; -. DR IntAct; P15054; 1. DR MINT; P15054; -. DR BRENDA; 2.7.10.2; 600. 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14203; PTKc_Src_Fyn_like; 1. DR CDD; cd10365; SH2_Src_Src; 1. DR CDD; cd12008; SH3_Src; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. 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; 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 PANTHER; PTHR24418:SF53; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC; 1. DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. 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; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 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..587 FT /note="Tyrosine-protein kinase transforming protein Src" FT /id="PRO_0000088148" 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..520 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..58 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..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" SQ SEQUENCE 587 AA; 65801 MW; 0A6925315EF251D9 CRC64; MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL SFKKGERLQI VNNTEGDWWL AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL KGEMGKYLRL PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERGYR MPCPPECPES LHDLMCQCWR KDPEERPTFE YLQAFLEDYF TSTEPPVPAW REPIGLELLL APEASLWGTG AWLRAEGPRF GEQPQSRMWH GEVSGAPSLI KTVLGHP //