ID   SRC_AVIST      STANDARD;      PRT;   557 AA.
AC   P14085;
DT   01-JAN-1990 (Rel. 13, Created)
DT   01-JAN-1990 (Rel. 13, Last sequence update)
DT   01-NOV-1995 (Rel. 32, Last annotation update)
DE   TYROSINE-PROTEIN KINASE TRANSFORMING PROTEIN SRC (EC 2.7.1.112) (P60-
DE   SRC).
GN   V-SRC.
OS   Avian sarcoma virus (strain S2).
OC   Viruses; Retroid viruses; Retroviridae; Avian type C retroviruses.
OX   NCBI_TaxID=11882;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=87064539; PubMed=3097513;
RA   Ikawa S., Hagino-Yamagishi K., Kawai S., Yamamoto T., Toyoshima K.;
RT   "Activation of the cellular src gene by transducing retrovirus.";
RL   Mol. Cell. Biol. 6:2420-2428(1986).
CC   -!- FUNCTION: THIS PHOSPHOPROTEIN, REQUIRED FOR BOTH THE INITIATION
CC       AND THE MAINTENANCE OF NEOPLASTIC TRANSFORMATION, IS A PROTEIN
CC       KINASE THAT CATALYZES THE PHOSPHORYLATION OF TYROSINE RESIDUES
CC       IN VITRO.
CC   -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP +
CC       PROTEIN TYROSINE PHOSPHATE.
CC   -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN.
CC   -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN.
CC   -!- SIMILARITY: TO OTHER PROTEIN-TYROSINE KINASES IN THE CATALYTIC
CC       DOMAIN. BELONGS TO THE SRC SUBFAMILY.
DR   PIR; B25375; TVFVS2.
DR   HSSP; P00523; 2PTK.
DR   INTERPRO; IPR000719; -.
DR   INTERPRO; IPR000980; -.
DR   INTERPRO; IPR001245; -.
DR   INTERPRO; IPR001452; -.
DR   PFAM; PF00017; SH2; 1.
DR   PFAM; PF00018; SH3; 1.
DR   PFAM; PF00069; pkinase; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
KW   Tyrosine-protein kinase; Transforming protein; Oncogene;
KW   Transferase; Phosphorylation; ATP-binding; Myristate;
KW   SH3 domain; SH2 domain.
FT   LIPID         2      2       MYRISTATE.
FT   DOMAIN       81    142       SH3.
FT   DOMAIN      148    245       SH2.
FT   DOMAIN      267    520       PROTEIN KINASE.
FT   NP_BIND     273    281       ATP (BY SIMILARITY).
FT   BINDING     295    295       ATP (BY SIMILARITY).
FT   ACT_SITE    386    386       BY SIMILARITY.
FT   MOD_RES     416    416       PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
SQ   SEQUENCE   557 AA;  62582 MW;  BBC2A04CB99CEAFE 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 YLQAFLEDYL GILAWTPWED KQEGPRGETA
     SNKQERPGED TLAADES
//