LOCUS       NP_033833                604 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase A-Raf isoform 1 [Mus musculus].
ACCESSION   NP_033833
VERSION     NP_033833.1
DBSOURCE    REFSEQ: accession NM_009703.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Su,D., Zhu,S., Hou,Z., Hao,F., Xu,K., Xu,F., Zhu,Y., Liu,D., Xu,J.
            and Tao,J.
  TITLE     Toxoplasma gondii infection regulates apoptosis of host cells via
            miR-185/ARAF axis
  JOURNAL   Parasit Vectors 16 (1), 371 (2023)
   PUBMED   37858158
  REMARK    GeneRIF: Toxoplasma gondii infection regulates apoptosis of host
            cells via miR-185/ARAF axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Takahashi,K., Itakura,E., Takano,K. and Endo,T.
  TITLE     DA-Raf, a dominant-negative regulator of the Ras-ERK pathway, is
            essential for skeletal myocyte differentiation including myoblast
            fusion and apoptosis
  JOURNAL   Exp Cell Res 376 (2), 168-180 (2019)
   PUBMED   30742807
  REMARK    GeneRIF: DA-Raf1 (DA-Raf) is a splicing variant of A-Raf that
            suppresses the Ras-ERK pathway and is essential for both myocyte
            differentiation including myoblast fusion and apoptosis but
            apoptosis is not a prerequisite for myoblast fusion
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Horiuchi,Y., Nakatsu,D., Kano,F. and Murata,M.
  TITLE     Pyruvate kinase M1 interacts with A-Raf and inhibits endoplasmic
            reticulum stress-induced apoptosis by activating MEK1/ERK pathway
            in mouse insulinoma cells
  JOURNAL   Cell Signal 38, 212-222 (2017)
   PUBMED   28743549
  REMARK    GeneRIF: PKM1 interacts with A-Raf, an upstream regulator of the
            MEK/ERK pathway, and that this interaction contributes to MEK1
            phosphorylation by A-Raf.
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Papaioannou,G., Petit,E.T., Liu,E.S., Baccarini,M., Pritchard,C.
            and Demay,M.B.
  TITLE     Raf Kinases Are Essential for Phosphate Induction of ERK1/2
            Phosphorylation in Hypertrophic Chondrocytes and Normal
            Endochondral Bone Development
  JOURNAL   J Biol Chem 292 (8), 3164-3171 (2017)
   PUBMED   28073913
  REMARK    GeneRIF: A- and B-Raf ablation in chondrocytes does not alter
            skeletal development, whereas ablation of C-Raf decreases
            hypertrophic chondrocyte apoptosis and impairs vascularization of
            the growth plate. However, ablation of C-Raf does not impair
            phosphate-induced ERK1/2 phosphorylation in vitro, but leads to
            rickets by decreasing VEGF protein stability.
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Derry,J.M. and Barnard,P.J.
  TITLE     Physical linkage of the A-raf-1, properdin, synapsin I, and TIMP
            genes on the human and mouse X chromosomes
  JOURNAL   Genomics 12 (4), 632-638 (1992)
   PUBMED   1572636
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Grant,S.G. and Chapman,V.M.
  TITLE     Detailed genetic mapping of the A-raf proto-oncogene on the mouse X
            chromosome
  JOURNAL   Oncogene 6 (3), 397-402 (1991)
   PUBMED   2011396
REFERENCE   8  (residues 1 to 604)
  AUTHORS   Storm,S.M., Cleveland,J.L. and Rapp,U.R.
  TITLE     Expression of raf family proto-oncogenes in normal mouse tissues
  JOURNAL   Oncogene 5 (3), 345-351 (1990)
   PUBMED   1690378
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Avner,P., Bucan,M., Arnaud,D., Lehrach,H. and Rapp,U.
  TITLE     A-raf oncogene localizes on mouse X chromosome to region some 10-17
            centimorgans proximal to hypoxanthine phosphoribosyltransferase
            gene
  JOURNAL   Somat Cell Mol Genet 13 (3), 267-272 (1987)
   PUBMED   3299748
REFERENCE   10 (residues 1 to 604)
  AUTHORS   Huleihel,M., Goldsborough,M., Cleveland,J., Gunnell,M., Bonner,T.
            and Rapp,U.R.
  TITLE     Characterization of murine A-raf, a new oncogene related to the
            v-raf oncogene
  JOURNAL   Mol Cell Biol 6 (7), 2655-2662 (1986)
   PUBMED   3491291
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BB857915.1, AK085823.1 and AA960102.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK085823.1, BC004757.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="X"
                     /map="X 16.3 cM"
     Protein         1..604
                     /product="serine/threonine-protein kinase A-Raf isoform 1"
                     /EC_number="2.7.11.1"
                     /note="raf-related oncogene; v-raf murine sarcoma 3611
                     viral oncogene homolog 1; A-Raf proto-oncogene
                     serine/threonine-protein kinase; serine/threonine-protein
                     kinase A-Raf; proto-oncogene A-Raf"
                     /calculated_mol_wt=67451
     Region          19..91
                     /region_name="RBD_ARAF"
                     /note="Ras-binding domain (RBD) found in
                     serine/threonine-protein kinase ARAF; cd17133"
                     /db_xref="CDD:340653"
     Site            order(20,22,27..32,34,47,51..53)
                     /site_type="other"
                     /note="putative RBD_Raf-Ras interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340653"
     Site            order(20,27,29..32,47,50..53)
                     /site_type="other"
                     /note="RBD_Raf-KRas interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340653"
     Site            85
                     /site_type="other"
                     /note="putative Ca binding site [ion binding]"
                     /db_xref="CDD:340653"
     Region          96..147
                     /region_name="C1_A_C-Raf"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma)
                     kinases, and similar proteins; cd20870"
                     /db_xref="CDD:410420"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P04627.2)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P04627.2)"
     Region          177..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04627.2)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P04627.2)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P04627.2)"
     Region          241..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04627.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P04627.2)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P04627.2)"
     Region          307..571
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(314..317,320,322,332,334,365,380..383,427,431..432,
                     434,444..445)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P04627.2)"
     CDS             1..604
                     /gene="Araf"
                     /gene_synonym="1200013E08Rik; A-Raf; Araf1"
                     /coded_by="NM_009703.2:138..1952"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS40886.1"
                     /db_xref="GeneID:11836"
                     /db_xref="MGI:MGI:88065"
ORIGIN      
        1 mepprgppvs gaepsravgt vkvylpnkqr tvvtvregms vydsldkalk vrglnqdccv
       61 vyrlikgrkt vtawdtaiap ldgeelivev ledvpltmhn fvrktffsla fcdfclkflf
      121 hgfrcqtcgy kfhqhcsskv ptvcvdmstn rrqfyhsiqd lsggsrqqea psnlsvnell
      181 tpqgpspftq qrdqehfsfp apanpplqri rststpnvhm vsttapmdss lmqftaqsfs
      241 tdaagrggdg aprgspspas vssgrksphs klpseqrerk sladekkkvk nlgyrdsgyy
      301 wevppsevql lkrigtgsfg tvfrgrwhgd vavkvlkvaq ptaeqaqafk nemqvlrktr
      361 hvnillfmgf mtrpgfaiit qwcegsslyh hlhvadtrfd mvqlidvarq taqgmdylha
      421 kniihrdlks nniflheglt vkigdfglat vktrwsgaqp leqpsgsvlw maaevirmqd
      481 pnpysfqsdv yaygvvlyel mtgslpyshi gsrdqiifmv grgylspdls kifsncpkam
      541 rrlltdclkf qreerplfpq ilatiellqr slpkiersas epslhrtqad elpacllsaa
      601 rlvp
//
