LOCUS       NP_035231                672 aa            linear   ROD 27-MAR-2025
DEFINITION  protein kinase C alpha type [Mus musculus].
ACCESSION   NP_035231
VERSION     NP_035231.2
DBSOURCE    REFSEQ: accession NM_011101.3
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 672)
  AUTHORS   Nord,C., Jones,I., Garcia-Maestre,M., Hagglund,A.C. and Carlsson,L.
  TITLE     Reduced mTORC1-signaling in progenitor cells leads to retinal
            lamination deficits
  JOURNAL   Dev Dyn 253 (10), 922-939 (2024)
   PUBMED   38546215
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Xu,Y., Cohen,E., Johnson,C.N., Parent,C.A. and Coulombe,P.A.
  TITLE     Repeated stress to the skin amplifies neutrophil infiltration in a
            keratin 17- and PKCalpha-dependent manner
  JOURNAL   PLoS Biol 22 (8), e3002779 (2024)
   PUBMED   39159283
  REMARK    GeneRIF: Repeated stress to the skin amplifies neutrophil
            infiltration in a keratin 17- and PKCalpha-dependent manner.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Zhu,L., Su,W., Xu,X., Shao,S., Qin,C., Gao,R., Wang,X., Ma,M.,
            Gao,J. and Zhang,Z.
  TITLE     Sphincter of Oddi Dysfunction Induces Gallstone by Inhibiting the
            Expression of ABCB11 via PKC-alpha
  JOURNAL   Appl Biochem Biotechnol 196 (8), 5373-5390 (2024)
   PUBMED   38158489
  REMARK    GeneRIF: Sphincter of Oddi Dysfunction Induces Gallstone by
            Inhibiting the Expression of ABCB11 via PKC-alpha.
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Pang,L., Cui,M., Wu,S. and Kong,J.
  TITLE     Cav-1 regulates the bile salt export pump on the canalicular
            membrane of hepatocytes by PKCalpha-associated signalling under
            cholesterol stimulation
  JOURNAL   J Cell Mol Med 28 (3), e18110 (2024)
   PUBMED   38164042
  REMARK    GeneRIF: Cav-1 regulates the bile salt export pump on the
            canalicular membrane of hepatocytes by PKCalpha-associated
            signalling under cholesterol stimulation.
REFERENCE   5  (residues 1 to 672)
  AUTHORS   Li,Y., Xiao,D., Chen,H., Zheng,X.F.S. and Xiang,M.
  TITLE     Maf1 controls retinal neuron number by both RNA Pol III- and Pol
            II-dependent mechanisms
  JOURNAL   iScience 26 (12), 108544 (2023)
   PUBMED   38089586
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 672)
  AUTHORS   Stetler-Stevenson,W.G., Liotta,L.A. and Seldin,M.F.
  TITLE     Linkage analysis demonstrates that the Timp-2 locus is on mouse
            chromosome 11
  JOURNAL   Genomics 14 (3), 828-829 (1992)
   PUBMED   1427919
REFERENCE   7  (residues 1 to 672)
  AUTHORS   Wilkie,T.M., Gilbert,D.J., Olsen,A.S., Chen,X.N., Amatruda,T.T.,
            Korenberg,J.R., Trask,B.J., de Jong,P., Reed,R.R., Simon,M.I. et
            al.
  TITLE     Evolution of the mammalian G protein alpha subunit multigene family
  JOURNAL   Nat Genet 1 (2), 85-91 (1992)
   PUBMED   1302014
  REMARK    Review article
REFERENCE   8  (residues 1 to 672)
  AUTHORS   Wada,H., Ohno,S., Kubo,K., Taya,C., Tsuji,S., Yonehara,S. and
            Suzuki,K.
  TITLE     Cell type-specific expression of the genes for the protein kinase C
            family: down regulation of mRNAs for PKC alpha and nPKC epsilon
            upon in vitro differentiation of a mouse neuroblastoma cell line
            neuro 2a
  JOURNAL   Biochem Biophys Res Commun 165 (1), 533-538 (1989)
   PUBMED   2590242
REFERENCE   9  (residues 1 to 672)
  AUTHORS   Buchberg,A.M., Brownell,E., Nagata,S., Jenkins,N.A. and
            Copeland,N.G.
  TITLE     A comprehensive genetic map of murine chromosome 11 reveals
            extensive linkage conservation between mouse and human
  JOURNAL   Genetics 122 (1), 153-161 (1989)
   PUBMED   2567264
REFERENCE   10 (residues 1 to 672)
  AUTHORS   Rose-John,S., Dietrich,A. and Marks,F.
  TITLE     Molecular cloning of mouse protein kinase C (PKC) cDNA from Swiss
            3T3 fibroblasts
  JOURNAL   Gene 74 (2), 465-471 (1988)
   PUBMED   2469625
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK147084.1, AL645535.16 and BF455952.1.
            
            On Jan 12, 2008 this sequence version replaced NP_035231.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            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 :: AK147084.1, SRR14777535.887346.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 70.8 cM"
     Protein         1..672
                     /product="protein kinase C alpha type"
                     /EC_number="2.7.11.13"
                     /note="protein kinase c-alpha; PKC-A; PKC-alpha"
                     /calculated_mol_wt=76693
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P17252; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17252; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Region          35..92
                     /region_name="C1_cPKC_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in the classical (or conventional) protein
                     kinase C (cPKC) family; cd20833"
                     /db_xref="CDD:410383"
     Site            order(42..48,56..60,63)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410383"
     Region          102..155
                     /region_name="C1_cPKC_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in the classical (or conventional) protein
                     kinase C (cPKC) family; cd20836"
                     /db_xref="CDD:410386"
     Site            order(107..113,121..125,128)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410386"
     Region          159..289
                     /region_name="C2_PKC_alpha_gamma"
                     /note="C2 domain in Protein Kinase C (PKC) alpha and
                     gamma; cd04026"
                     /db_xref="CDD:175992"
     Site            order(187,193,246,248,254)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175992"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17252; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05696; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Region          328..668
                     /region_name="STKc_cPKC_alpha"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Classical Protein Kinase C alpha; cd05615"
                     /db_xref="CDD:270766"
     Site            order(345..349,353,366,368,401,417..418,420,424,426,463,
                     465,467..468,470,480..481,484,498..503,530,536,539)
                     /site_type="active"
                     /db_xref="CDD:270766"
     Site            order(345..349,353,366,368,401,418..420,424,463,465,
                     467..468,470,480..481)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270766"
     Site            order(349,424,426,463,465,467,484,498..503,530,536,539)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270766"
     Site            480..503
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270766"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04409; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04409; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PDPK1.
                     /evidence=ECO:0000250|UniProtKB:P04409; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P05771; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Site            628
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17252; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MTOR.
                     /evidence=ECO:0000269|PubMed:33850054; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18566587; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Site            638
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270766"
     Site            651
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17252; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Site            653..658
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270766"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:18566587; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SYK.
                     /evidence=ECO:0000269|PubMed:12881490; propagated from
                     UniProtKB/Swiss-Prot (P20444.3)"
     CDS             1..672
                     /gene="Prkca"
                     /gene_synonym="Pkca"
                     /coded_by="NM_011101.3:222..2240"
                     /db_xref="CCDS:CCDS25573.1"
                     /db_xref="GeneID:18750"
                     /db_xref="MGI:MGI:97595"
ORIGIN      
        1 madvypands tasqdvanrf arkgalrqkn vhevkdhkfi arffkqptfc shctdfiwgf
       61 gkqgfqcqvc cfvvhkrche fvtfscpgad kgpdtddprs khkfkihtyg sptfcdhcgs
      121 llyglihqgm kcdtcdmnvh kqcvinvpsl cgmdhtekrg riylkaevtd eklhvtvrda
      181 knlipmdpng lsdpyvklkl ipdpkneskq ktktirstln pqwnesftfk lkpsdkdrrl
      241 sveiwdwdrt trndfmgsls fgvselmkmp asgwykllnq eegeyynvpi pegdeegnme
      301 lrqkfekakl gpagnkvisp sedrkqpsnn ldrvkltdfn flmvlgkgsf gkvmladrkg
      361 teelyaikil kkdvviqddd vectmvekrv lalldkppfl tqlhscfqtv drlyfvmeyv
      421 nggdlmyhiq qvgkfkepqa vfyaaeisig lfflhkrgii yrdlkldnvm ldseghikia
      481 dfgmckehmm dgvttrtfcg tpdyiapeii ayqpygksvd wwaygvllye mlagqppfdg
      541 ededelfqsi mehnvsypks lskeavsick glmtkhpakr lgcgpegerd vrehaffrri
      601 dweklenrei qppfkpkvcg kgaenfdkff trgqpvltpp dqlvianidq sdfegfsyvn
      661 pqfvhpilqs av
//
