ID   KRAF_HUMAN     STANDARD;      PRT;   648 AA.
AC   P04049;
DT   01-NOV-1986 (Rel. 03, Created)
DT   01-NOV-1986 (Rel. 03, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   RAF PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE (EC 2.7.1.-)
DE   (RAF-1) (C-RAF).
GN   RAF1.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 86120351.
RA   Bonner T.I., Oppermann H., Seeburg P., Kerby S.B., Gunnell M.A.,
RA   Young A.C., Rapp U.R.;
RT   "The complete coding sequence of the human raf oncogene and the
RT   corresponding structure of the c-raf-1 gene.";
RL   Nucleic Acids Res. 14:1009-1015(1986).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 51-131.
RX   MEDLINE; 95312074.
RA   Nassar N., Horn G., Herrmann C., Scherer A., McCormick F.,
RA   Wittinghofer A.;
RT   "The 2.2 A crystal structure of the Ras-binding domain of the
RT   serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP
RT   analogue.";
RL   Nature 375:554-560(1995).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 56-131.
RX   MEDLINE; 96313130.
RA   Nassar N., Horn G., Herrmann C., Block C., Janknecht R.,
RA   Wittinghofer A.;
RT   "Ras/Rap effector specificity determined by charge reversal.";
RL   Nat. Struct. Biol. 3:723-729(1996).
RN   [4]
RP   STRUCTURE BY NMR OF 55-132.
RX   MEDLINE; 95284022.
RA   Emerson S.D., Madison V.S., Palermo R.E., Waugh D.S., Scheffler J.E.,
RA   Tsao K.L., Kiefer S.E., Liu S.P., Fry D.C.;
RT   "Solution structure of the Ras-binding domain of c-Raf-1 and
RT   identification of its Ras interaction surface.";
RL   Biochemistry 34:6911-6918(1995).
RN   [5]
RP   STRUCTURE BY NMR OF 136-187.
RX   MEDLINE; 96323218.
RA   Mott H.R., Carpenter J.W., Zhong S., Ghosh S., Bell R.M.,
RA   Campbell S.L.;
RT   "The solution structure of the Raf-1 cysteine-rich domain: a novel
RT   ras and phospholipid binding site.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:8312-8317(1996).
CC   -!- FUNCTION: INVOLVED IN THE TRANSDUCTION OF MITOGENIC SIGNALS FROM
CC       THE CELL MEMBRANE TO THE NUCLEUS. PART OF THE RAS-DEPENDENT
CC       SIGNALING PATHWAY FROM RECEPTORS TO THE NUCLEUS.
CC   -!- SIMILARITY: WITH THE CONSERVED CATALYTIC DOMAINS OF SER/THR-
CC       PROTEIN KINASES. BELONGS TO THE MIL/RAF SUBFAMILY.
CC   -!- SIMILARITY: CONTAINS 1 ZINC-DEPENDENT PHORBOL-ESTER AND DAG
CC       BINDING DOMAIN.
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DR   EMBL; X03484; CAA27204.1; -.
DR   PIR; A00637; TVHUF6.
DR   PDB; 1FAQ; 27-JAN-97.
DR   PDB; 1FAR; 27-JAN-97.
DR   PDB; 1RFA; 20-JUN-96.
DR   PDB; 1GUA; 11-JAN-97.
DR   MIM; 164760; -.
DR   PFAM; PF00130; DAG_PE-bind; 1.
DR   PFAM; PF00069; pkinase; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00479; DAG_PE_BINDING_DOMAIN; 1.
KW   Transferase; Serine/threonine-protein kinase; Proto-oncogene; Zinc;
KW   ATP-binding; Phorbol-ester binding; 3D-structure.
FT   DOMAIN      139    184       PHORBOL-ESTER AND DAG BINDING.
FT   DOMAIN      349    609       PROTEIN KINASE.
FT   NP_BIND     355    363       ATP (BY SIMILARITY).
FT   BINDING     375    375       ATP (BY SIMILARITY).
FT   ACT_SITE    468    468       BY SIMILARITY.
SQ   SEQUENCE   648 AA;  73051 MW;  EF821B5349711BC3 CRC64;
     MEHIQGAWKT ISNGFGFKDA VFDGSSCISP TIVQQFGYQR RASDDGKLTD PSKTSNTIRV
     FLPNKQRTVV NVRNGMSLHD CLMKALKVRG LQPECCAVFR LLHEHKGKKA RLDWNTDAAS
     LIGEELQVDF LDHVPLTTHN FARKTFLKLA FCDICQKFLL NGFRCQTCGY KFHEHCSTKV
     PTMCVDWSNI RQLLLFPNST IGDSGVPALP SLTMRRMRES VSRMPVSSQH RYSTPHAFTF
     NTSSPSSEGS LSQRQRSTST PNVHMVSTTL PVDSRMIEDA IRSHSESASP SALSSSPNNL
     SPTGWSQPKT PVPAQRERAP VSGTQEKNKI RPRGQRDSSY YWEIEASEVM LSTRIGSGSF
     GTVYKGKWHG DVAVKILKVV DPTPEQFQAF RNEVAVLRKT RHVNILLFMG YMTKDNLAIV
     TQWCEGSSLY KHLHVQETKF QMFQLIDIAR QTAQGMDYLH AKNIIHRDMK SNNIFLHEGL
     TVKIGDFGLA TVKSRWSGSQ QVEQPTGSVL WMAPEVIRMQ DNNPFSFQSD VYSYGIVLYE
     LMTGELPYSH INNRDQIIFM VGRGYASPDL SKLYKNCPKA MKRLVADCVK KVKEERPLFP
     QILSSIELLQ HSLPKINRSA SEPSLHRAAH TEDINACTLT TSPRLPVF
//