RAF proto-oncogene serine/threonine-protein kinase - Xenopus laevis (African clawed frog)

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P09560 (RAF1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
RAF proto-oncogene serine/threonine-protein kinase
EC=2.7.11.1

Alternative name(s):
C-RAF

Gene names

Name:	raf1
Synonyms:	raf

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2) By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subcellular location	Cytoplasm By similarity. Cell membrane By similarity.
Post-translational modification	Phosphorylation at Ser-257 inactivates kinase activity. Dephosphorylation of Ser-257 by a complex containing protein phosphatase 1 relieves inactivation, leading to stimulate RAF1 activity By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. RAF subfamily. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 protein kinase domain. Contains 1 RBD (Ras-binding) domain.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Disease	Proto-oncogene
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological_process	intracellular signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW receptor signaling protein activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 638

638

RAF proto-oncogene serine/threonine-protein kinase

PRO_0000086600

Regions

Domain

56 – 130

RBD

Domain

340 – 600

261

Protein kinase

Zinc finger

137 – 183

Phorbol-ester/DAG-type

Nucleotide binding

346 – 354

ATP By similarity

Sites

Active site

459

Proton acceptor By similarity

Metal binding

138

Zinc 1 By similarity

Metal binding

151

Zinc 2 By similarity

Metal binding

154

Zinc 2 By similarity

Metal binding

164

Zinc 1 By similarity

Metal binding

167

Zinc 1 By similarity

Metal binding

172

Zinc 2 By similarity

Metal binding

175

Zinc 2 By similarity

Metal binding

183

Zinc 1 By similarity

Binding site

366

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

257

Phosphoserine By similarity

Modified residue

266

Phosphothreonine; by autocatalysis By similarity

Modified residue

329

Phosphoserine By similarity

Modified residue

490

Phosphoserine By similarity

Experimental info

Sequence conflict

309

K → R in AAB20707. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P09560 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 1FF352BFFBF528DF
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FASTA

638

71,960

        10         20         30         40         50         60 
MEHIQGAWKT LSNGFGFKES VFEGSSCMSP TIVHQFGYQR RASDDGKLSD TSKTSSTMRV 

        70         80         90        100        110        120 
YLPNKQRTVV NVRSGMSLHD CLMKSLKVRG LQPECCAVFR LIQDPKGKLR LDWNTDAMSL 

       130        140        150        160        170        180 
VGAELQVDFL DHVPLTTHNF VRKTFLKLAF CDICQKFLLN AFRCQTCGYK FHEHCSTKVP 

       190        200        210        220        230        240 
TMCVDWSNIR QLLLFPNPNN IEGGSHTLPS LTMRRIGESV RIPVSSQQRY STPHPFSFST 

       250        260        270        280        290        300 
PSPVSECSLS QRQRSTSTPN VHMVSTTMAV DSRVIEDALR SHSESGSPNN LSPTGWSNAK 

       310        320        330        340        350        360 
APAPTHREKA ASSTGQEKNK IRARGQRDSS YYWEIIASEV MLSSRIGSGS FGTVYKGKWH 

       370        380        390        400        410        420 
GDVAVKILKV TDPTPEQLQA FRNEVAVLRK TRHVNILLFM GYMTKDNLAI VTQWCEGSSL 

       430        440        450        460        470        480 
YYHLHVLDTK FQMFQLIDIA RQTAQGMDYL HAKNIIHRDM KSNNIFLHEG LTVKIGDFGL 

       490        500        510        520        530        540 
ATVKTRWSGS QQVEQLTGSI LWMAPEVIRM QDNNPFSFQS DVYSYGIVLY ELMTGELPYS 

       550        560        570        580        590        600 
HIRDRDQIIF LVGRGGVVPD LSKLYKNCPK AMKRLVADSI KKLRDERPLF PQILSSIELL 

       610        620        630 
QHSLPKINRS ALEPSLHRAA HTEDISSCAL TSTRLPVF

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References

[1]	"Nucleotide sequence of Xenopus C-raf coding region." le Guellec R., le Guellec K., Paris J., Philippe M. Nucleic Acids Res. 16:10357-10357(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Oocyte.
[2]	"Xenopus c-raf proto-oncogene: cloning and expression during oogenesis and early development." le Guellec R., Couturier A., le Guellec K., Paris J., le Fur N., Philippe M. Biol. Cell 72:39-45(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X12948 mRNA. Translation: CAA31407.1. S74063 mRNA. Translation: AAB20707.1.
PIR	TVXLRF. S01930.
UniGene	Xl.5697.
3D structure databases
ProteinModelPortal	P09560.
SMR	P09560. Positions 55-131, 135-186, 333-606.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1075N.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Xenbase	XB-GENE-6053397. raf1.
Phylogenomic databases
HOVERGEN	HBG001886.
Enzyme and pathway databases
BRENDA	2.7.10.2. 6726.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR003116. Raf-like_ras-bd. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00130. C1_1. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF02196. RBD. 1 hit. [Graphical view]
SMART	SM00109. C1. 1 hit. SM00455. RBD. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS50898. RBD. 1 hit. PS00479. ZF_DAG_PE_1. 1 hit. PS50081. ZF_DAG_PE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RAF1_XENLA

Accession

Primary (citable) accession number: P09560
Secondary accession number(s): Q91390

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents