LOCUS       NP_150233                480 aa            linear   ROD 25-FEB-2025
DEFINITION  RAC-alpha serine/threonine-protein kinase [Rattus norvegicus].
ACCESSION   NP_150233
VERSION     NP_150233.1
DBSOURCE    REFSEQ: accession NM_033230.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Liu,H., Lin,X., Chilufya,M.M., Qiao,L., Bao,M., Wen,X., Xiang,R.,
            He,H., Li,M. and Han,J.
  TITLE     Synergistic effects of T-2 toxin and selenium deficiency exacerbate
            renal fibrosis through modulation of the ERalpha/PI3K/Akt signaling
            pathway
  JOURNAL   Ecotoxicol Environ Saf 269, 115748 (2024)
   PUBMED   38029582
  REMARK    GeneRIF: Synergistic effects of T-2 toxin and selenium deficiency
            exacerbate renal fibrosis through modulation of the
            ERalpha/PI3K/Akt signaling pathway.
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Hirai,T., Wang,W., Murono,N., Iwasa,K. and Inoue,M.
  TITLE     Potential role of Akt in the regulation of fibroblast growth factor
            21 by berberine
  JOURNAL   J Nat Med 78 (1), 169-179 (2024)
   PUBMED   37951850
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Lin,Y.K., Hsiao,L.C., Wu,M.Y., Chen,Y.F., Lin,Y.N., Chang,C.M.,
            Chung,W.H., Chen,K.W., Lu,C.R., Chen,W.Y., Chang,S.S., Shyu,W.C.,
            Lee,A.S., Chen,C.H., Jeng,L.B. and Chang,K.C.
  TITLE     PD-L1 and AKT Overexpressing Adipose-Derived Mesenchymal Stem Cells
            Enhance Myocardial Protection by Upregulating CD25+ T Cells in
            Acute Myocardial Infarction Rat Model
  JOURNAL   Int J Mol Sci 25 (1), 134 (2023)
   PUBMED   38203304
  REMARK    GeneRIF: PD-L1 and AKT Overexpressing Adipose-Derived Mesenchymal
            Stem Cells Enhance Myocardial Protection by Upregulating CD25[+] T
            Cells in Acute Myocardial Infarction Rat Model.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Yang,R. and Zeng,C.
  TITLE     MiR-182 promotes apoptosis of neural cells in cerebral infarction
            rats by PI3K/AKT signaling pathway
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (12), 139-143 (2023)
   PUBMED   38063104
  REMARK    GeneRIF: MiR-182 promotes apoptosis of neural cells in cerebral
            infarction rats by PI3K/AKT signaling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Li,F. and Liu,H.
  TITLE     MiR- 211 represses apoptosis of nerve cells in rats with cerebral
            infarction through PI3K/AKT signaling pathway
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (12), 150-155 (2023)
   PUBMED   38063101
  REMARK    GeneRIF: MiR- 211 represses apoptosis of nerve cells in rats with
            cerebral infarction through PI3K/AKT signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Cross,D.A., Alessi,D.R., Cohen,P., Andjelkovich,M. and
            Hemmings,B.A.
  TITLE     Inhibition of glycogen synthase kinase-3 by insulin mediated by
            protein kinase B
  JOURNAL   Nature 378 (6559), 785-789 (1995)
   PUBMED   8524413
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Konishi,H., Kuroda,S., Tanaka,M., Matsuzaki,H., Ono,Y.,
            Kameyama,K., Haga,T. and Kikkawa,U.
  TITLE     Molecular cloning and characterization of a new member of the RAC
            protein kinase family: association of the pleckstrin homology
            domain of three types of RAC protein kinase with protein kinase C
            subspecies and beta gamma subunits of G proteins
  JOURNAL   Biochem Biophys Res Commun 216 (2), 526-534 (1995)
   PUBMED   7488143
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Franke,T.F., Yang,S.I., Chan,T.O., Datta,K., Kazlauskas,A.,
            Morrison,D.K., Kaplan,D.R. and Tsichlis,P.N.
  TITLE     The protein kinase encoded by the Akt proto-oncogene is a target of
            the PDGF-activated phosphatidylinositol 3-kinase
  JOURNAL   Cell 81 (5), 727-736 (1995)
   PUBMED   7774014
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Datta,K., Franke,T.F., Chan,T.O., Makris,A., Yang,S.I.,
            Kaplan,D.R., Morrison,D.K., Golemis,E.A. and Tsichlis,P.N.
  TITLE     AH/PH domain-mediated interaction between Akt molecules and its
            potential role in Akt regulation
  JOURNAL   Mol Cell Biol 15 (4), 2304-2310 (1995)
   PUBMED   7891724
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Konishi,H., Shinomura,T., Kuroda,S., Ono,Y. and Kikkawa,U.
  TITLE     Molecular cloning of rat RAC protein kinase alpha and beta and
            their association with protein kinase C zeta
  JOURNAL   Biochem Biophys Res Commun 205 (1), 817-825 (1994)
   PUBMED   7999118
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            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 :: D30040.1, SRR26643285.26018.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..480
                     /product="RAC-alpha serine/threonine-protein kinase"
                     /EC_number="2.7.11.1"
                     /note="murine thymoma viral (v-akt) oncogene homolog 1;
                     RAC-PK-alpha; thymoma viral proto-oncogene 1; AKT1 kinase;
                     RAC protein kinase alpha RAC-PK alpha; PKB alpha; protein
                     kinase B alpha; v-akt murine thymoma viral oncogene
                     homolog 1"
                     /calculated_mol_wt=55605
     Region          4..111
                     /region_name="PH_PKB"
                     /note="Protein Kinase B-like pleckstrin homology (PH)
                     domain; cd01241"
                     /db_xref="CDD:269947"
     Site            order(14,16..19,23,25,52..53,55,86)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269947"
     Site            14
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            20
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Region          124..479
                     /region_name="STKc_PKB_alpha"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Protein Kinase B alpha (also called Akt1); cd05594"
                     /db_xref="CDD:270746"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            126
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            129
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            order(156..157,159..160,164,177,179,191,194,211,227..230,
                     234,236,240,274,276,278..279,281,291..292,295,309..316,
                     341,347,350,438,442)
                     /site_type="active"
                     /db_xref="CDD:270746"
     Site            order(156..157,159,164,177,179,211,227..230,234,274,276,
                     278..279,281,291..292,438)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270746"
     Site            order(160,191,194,234,236,240,274,276,278,295,309..316,
                     341,347,350,442)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270746"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by TNK2.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            291..314
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270746"
     Site            305
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            308
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by IKKE, PDPK1 and TBK1.
                     /evidence=ECO:0000269|PubMed:9228007; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            312
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MTOR.
                     /evidence=ECO:0000250|UniProtKB:P31750; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            450
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270746"
     Region          451..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47196.1)"
     Site            462
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000250|UniProtKB:P31750; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            469..474
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270746"
     Site            473
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P31750; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKE, MTOR and TBK1, alternate.
                     /evidence=ECO:0000305|PubMed:10400692; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P31749; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31750; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     Site            479
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P31750; propagated from
                     UniProtKB/Swiss-Prot (P47196.1)"
     CDS             1..480
                     /gene="Akt1"
                     /gene_synonym="Akt"
                     /coded_by="NM_033230.3:39..1481"
                     /db_xref="GeneID:24185"
                     /db_xref="RGD:2081"
ORIGIN      
        1 mndvaivkeg wlhkrgeyik twrpryfllk ndgtfigyke rpqdveqres plnnfsvaqc
       61 qlmkterprp ntfiirclqw ttviertfhv etpeereewt taiqtvadgl krqeeetmdf
      121 rsgspsdnsg aeemevalak pkhrvtmnef eylkllgkgt fgkvilvkek atgryyamki
      181 lkkevivakd evahtltenr vlqnsrhpfl talkysfqth drlcfvmeya nggelffhls
      241 rervfsedra rfygaeivsa ldylhseknv vyrdlklenl mldkdghiki tdfglckegi
      301 kdgatmktfc gtpeylapev ledndygrav dwwglgvvmy emmcgrlpfy nqdheklfel
      361 ilmeeirfpr tlgpeaksll sgllkkdptq rlgggsedak eimqhrffan ivwqdvyekk
      421 lsppfkpqvt setdtryfde eftaqmitit ppdqddsmec vdserrphfp qfsysasgta
//
