SRC_RSVH1
ID SRC_RSVH1 Reviewed; 526 AA.
AC P25020;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
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 H-19).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=11887;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2587228; DOI=10.1093/nar/17.21.8869;
RA Bodor J., Poliak E., Pichrtova J., Geryk J., Svoboda J.;
RT "Complete nucleotide sequence of LTR, v-src, LTR provirus H-19.";
RL Nucleic Acids Res. 17:8869-8869(1989).
RN [2]
RP PROTEIN SEQUENCE OF 2-9, AND MYRISTOYLATION AT GLY-2.
RC STRAIN=Isolate tsNY68;
RX PubMed=2547372; DOI=10.1016/0006-291x(89)92370-x;
RA Shoji S., Tashiro A., Furuishi K., Takenaka O., Kida Y., Horiuchi S.,
RA Funakoshi T., Kubota Y.;
RT "Antibodies to an NH2-terminal myristoyl glycine moiety can detect NH2-
RT terminal myristoylated proteins in the retrovirus-infected cells.";
RL Biochem. Biophys. Res. Commun. 162:724-732(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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC P25020; P09619: PDGFRB; Xeno; NbExp=4; IntAct=EBI-8636140, EBI-641237;
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; X15345; CAA33404.1; -; mRNA.
DR PIR; S09609; OKFVYR.
DR SMR; P25020; -.
DR IntAct; P25020; 1.
DR MINT; P25020; -.
DR iPTMnet; P25020; -.
DR BRENDA; 2.7.10.2; 5464.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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 ATP-binding; Direct protein sequencing; Kinase; Lipoprotein; Manganese;
KW Metal-binding; Myristate; Nucleotide-binding; Phosphoprotein; 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_0000088155"
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..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:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:2547372"
SQ SEQUENCE 526 AA; 59075 MW; 33B212BCC943C6AF CRC64;
MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPDETAA PDAHRNPSRS FGTVATEPKL
FWGFNTSDTV TSPQRAGALA GGVTTFVALY DYESWTETDL SFKKGERLQI VNNTEGDWWL
AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRKSETA
KGAYCLSVSD FDNAKGPNVK HYKICKLYSG GFYITSRTQF GSLQQLVAYY SKHADGLCHR
LTNVCPTSKP QTQGLAKDAW EIPRESLRLE AKLGQGCFGE VWMGTWNGTT RVAIKTLKPG
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVIEY MSKGSLLDFL KGEMGKYLRL
PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ
GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERAYR
MPCPPECPES LHDLMCQCWR KDPEERPTFK YLQAQLLPAC VLEVAE
