MARCS_RAT
ID MARCS_RAT Reviewed; 309 AA.
AC P30009; P20468;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Myristoylated alanine-rich C-kinase substrate;
DE Short=MARCKS;
DE AltName: Full=Protein kinase C substrate 80 kDa protein;
GN Name=Marcks; Synonyms=Macs;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1707878; DOI=10.1016/s0021-9258(20)89611-2;
RA Erusalimsky J.D., Brooks S.F., Herget T., Morris C., Rozengurt E.;
RT "Molecular cloning and characterization of the acidic 80-kDa protein kinase
RT C substrate from rat brain. Identification as a glycoprotein.";
RL J. Biol. Chem. 266:7073-7080(1991).
RN [2]
RP PROTEIN SEQUENCE OF 12-31; 189-217; 252-275 AND 300-309.
RC TISSUE=Brain;
RX PubMed=2676596; DOI=10.1016/0014-5793(89)81079-8;
RA Erusalimsky J.D., Morris C., Perks K., Brown R., Brooks S., Rozengurt E.;
RT "Internal amino acid sequence analysis of the 80 kDa protein kinase C
RT substrate from rat brain: relationship to the 87 kDa substrate from bovine
RT brain.";
RL FEBS Lett. 255:149-153(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 182-301, AND TISSUE SPECIFICITY.
RX PubMed=1396720; DOI=10.1111/j.1432-1033.1992.tb17255.x;
RA Herget T., Brooks S.F., Broad S., Rozengurt E.;
RT "Relationship between the major protein kinase C substrates acidic 80-kDa
RT protein-kinase-C substrate (80K) and myristoylated alanine-rich C-kinase
RT substrate (MARCKS). Members of a gene family or equivalent genes in
RT different species.";
RL Eur. J. Biochem. 209:7-14(1992).
RN [4]
RP PHOSPHORYLATION AT SER-152; SER-156 AND SER-163.
RC TISSUE=Brain;
RX PubMed=8422248; DOI=10.1006/bbrc.1993.1036;
RA Heemskerk F.M., Chen H.C., Huang F.L.;
RT "Protein kinase C phosphorylates Ser-152, Ser-156 and Ser-163 but not Ser-
RT 160 of MARCKS in rat brain.";
RL Biochem. Biophys. Res. Commun. 190:236-241(1993).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-27; SER-29; SER-46;
RP SER-63; SER-74; THR-79; SER-113; SER-122; SER-138; THR-143; SER-156;
RP SER-160; SER-163 AND SER-218, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: MARCKS is the most prominent cellular substrate for protein
CC kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is
CC a filamentous (F) actin cross-linking protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Membrane
CC {ECO:0000250|UniProtKB:P29966}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P29966}.
CC -!- TISSUE SPECIFICITY: Highest levels found in spleen and brain.
CC Intermediate levels seen in thymus, ovary, lung and heart. Very low
CC levels seen in kidney, skeletal muscle and liver.
CC {ECO:0000269|PubMed:1396720}.
CC -!- PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also
CC inhibits the F-actin cross-linking activity.
CC {ECO:0000269|PubMed:8422248}.
CC -!- SIMILARITY: Belongs to the MARCKS family. {ECO:0000305}.
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DR EMBL; M59859; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A39773; A39773.
DR AlphaFoldDB; P30009; -.
DR IntAct; P30009; 3.
DR STRING; 10116.ENSRNOP00000000707; -.
DR iPTMnet; P30009; -.
DR PhosphoSitePlus; P30009; -.
DR jPOST; P30009; -.
DR PaxDb; P30009; -.
DR PRIDE; P30009; -.
DR UCSC; RGD:3028; rat.
DR RGD; 3028; Marcks.
DR eggNOG; ENOG502RB4V; Eukaryota.
DR InParanoid; P30009; -.
DR Reactome; R-RNO-399997; Acetylcholine regulates insulin secretion.
DR PRO; PR:P30009; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0032432; C:actin filament bundle; ISO:RGD.
DR GO; GO:0099025; C:anchored component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0032059; C:bleb; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0033391; C:chromatoid body; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0044307; C:dendritic branch; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0042585; C:germinal vesicle; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043226; C:organelle; ISO:RGD.
DR GO; GO:0001520; C:outer dense fiber; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0099571; C:postsynaptic cytoskeleton; IDA:SynGO.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:RGD.
DR GO; GO:0005543; F:phospholipid binding; IDA:RGD.
DR GO; GO:0005080; F:protein kinase C binding; ISO:RGD.
DR GO; GO:0051764; P:actin crosslink formation; ISO:RGD.
DR GO; GO:0051017; P:actin filament bundle assembly; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IMP:RGD.
DR GO; GO:0031584; P:activation of phospholipase D activity; IDA:RGD.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0031589; P:cell-substrate adhesion; IDA:RGD.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IMP:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0021915; P:neural tube development; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; IDA:RGD.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0003229; P:ventricular cardiac muscle tissue development; IEP:RGD.
DR InterPro; IPR002101; MARCKS.
DR PANTHER; PTHR14353; PTHR14353; 1.
DR Pfam; PF02063; MARCKS; 1.
DR PRINTS; PR00963; MARCKS.
DR PROSITE; PS00826; MARCKS_1; 1.
DR PROSITE; PS00827; MARCKS_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P12624"
FT CHAIN 2..309
FT /note="Myristoylated alanine-rich C-kinase substrate"
FT /id="PRO_0000157150"
FT REGION 1..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..169
FT /note="Calmodulin-binding (PSD)"
FT COMPBIAS 117..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12624"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26645"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 152
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8422248"
FT MOD_RES 156
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8422248,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 163
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8422248,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26645"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT CONFLICT 29
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="D -> E (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="G -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 29795 MW; 9957F2037F203316 CRC64;
MGAQFSKTAA KGEAAAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA EPGAKEELQA
NGSAPAADKE EPASGGAATP AAADKDEAAA APEPGAATAD KEAAEAEPAE PGSPSAETEG
ASASSTSSPK AEDGAAPSPS SETPKKKKKR FSFKKSFKLS GFSFKKSKKE AGEGAEAEGA
TADGAKDEAA AAAGGDAAAA PGEQAGGAGA EGAEGGESRE AEAAEPEQPE QPEQPAAEEP
RAEEPSEAVG EKAEEPAPGA TADDAPSAAG PEQEAPAATD EPAASAAPSA SPEPQPECSP
EAPPAPVAE
