SRC_RSVP
ID SRC_RSVP Reviewed; 526 AA.
AC P00526;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
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 Prague C) (RSV-PrC).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=11888;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6299578; DOI=10.1016/0092-8674(83)90071-5;
RA Schwartz D., Tizard R., Gilbert W.;
RT "Nucleotide sequence of Rous sarcoma virus.";
RL Cell 32:853-869(1983).
RN [2]
RP PHOSPHORYLATION AT TYR-416.
RX PubMed=6264320; DOI=10.1038/291675a0;
RA Neil J.C., Ghysdael J., Vogt P.K., Smart J.E.;
RT "Homologous tyrosine phosphorylation sites in transformation-specific gene
RT products of distinct avian sarcoma viruses.";
RL Nature 291:675-677(1981).
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 {ECO:0000269|PubMed:6264320}.
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; J02342; AAB59935.1; -; Genomic_RNA.
DR PIR; A00632; TVFVR.
DR PDB; 5YMW; X-ray; 2.00 A; C/F/I/L=517-524.
DR PDBsum; 5YMW; -.
DR BMRB; P00526; -.
DR SMR; P00526; -.
DR iPTMnet; P00526; -.
DR BRENDA; 2.7.10.2; 5464.
DR Proteomes; UP000007183; 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 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; Repeat; SH2 domain;
KW SH3 domain; 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_0000088152"
FT DOMAIN 71..139
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 81..142
FT /note="SH3 2"
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..52
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 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:0000269|PubMed:6264320"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT VARIANT 242
FT /note="A -> T"
FT VARIANT 288
FT /note="D -> G"
SQ SEQUENCE 526 AA; 59130 MW; 12C12DE33FFFAB11 CRC64;
MGSSKSKPKD PSQRRHSLEP PDSTHHGGFP ASQTPDETAA PDAHRNPSRS FGTVATEPKL
FWGFNTSDTV TSPQRAGALA GGVTTFVALY DYESWTETDL SFKKGERLQI VNNTEGDWWL
AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRKSETA
KGAYCLSVSD FDNAKGPNVK HYKIYKLYSG GFYITSRTQF GSLQQLVAYY SKHADGLCHR
LANVCPTSKP QTQGLAKDAW EIPRESLRLE AKLGQGCFGE VWMGTWNDTT RVAIKTLKPG
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVIEY MSKGSLLDFL KGEMGKYLRL
PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ
GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERGYR
MPCPPECPES LHDLMCQCWR KDPEERPTFK YLQAQLLPAC VLEVAE
