MARCS_BOVIN
ID MARCS_BOVIN Reviewed; 333 AA.
AC P12624; Q1LZI0;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 6.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Myristoylated alanine-rich C-kinase substrate;
DE Short=MARCKS;
DE AltName: Full=ACAMP-81;
GN Name=MARCKS; Synonyms=MACS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2734111; DOI=10.1093/nar/17.10.3987;
RA Stumpo D.J., Graff J.M., Albert K.A., Greengard P., Blackshear P.J.;
RT "Nucleotide sequence of a cDNA for the bovine myristoylated alanine-rich C
RT kinase substrate (MARCKS).";
RL Nucleic Acids Res. 17:3987-3988(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2726763; DOI=10.1073/pnas.86.11.4012;
RA Stumpo D.J., Graff J.M., Albert K.A., Greengard P., Blackshear P.J.;
RT "Molecular cloning, characterization, and expression of a cDNA encoding the
RT '80- to 87-kDa' myristoylated alanine-rich C kinase substrate: a major
RT cellular substrate for protein kinase C.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4012-4016(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-322.
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 [5]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1540183; DOI=10.1016/0006-291x(92)91888-w;
RA Mizutani A., Tokumitsu H., Hidaka H.;
RT "Acidic calmodulin binding protein, ACAMP-81, is MARCKS protein interacting
RT with synapsin I.";
RL Biochem. Biophys. Res. Commun. 182:1395-1401(1992).
RN [6]
RP PROTEIN SEQUENCE OF 3-12, IDENTIFICATION OF A NON-MYRISTOYLATED FORM,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=8463217; DOI=10.1016/s0021-9258(18)53121-5;
RA Manenti S., Sorokine O., van Dorsselaer A., Taniguchi H.;
RT "Isolation of the non-myristoylated form of a major substrate of protein
RT kinase C (MARCKS) from bovine brain.";
RL J. Biol. Chem. 268:6878-6881(1993).
RN [7]
RP PHOSPHORYLATION AT SER-158; SER-162; SER-166 AND SER-169.
RX PubMed=2473066; DOI=10.1016/s0021-9258(18)80153-3;
RA Graff J.M., Stumpo D.J., Blackshear P.J.;
RT "Characterization of the phosphorylation sites in the chicken and bovine
RT myristoylated alanine-rich C kinase substrate protein, a prominent cellular
RT substrate for protein kinase C.";
RL J. Biol. Chem. 264:11912-11919(1989).
RN [8]
RP SEQUENCE REVISION, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-27;
RP SER-46; SER-81; SER-100; SER-117 AND SER-134, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=8034575; DOI=10.1016/s0021-9258(17)32304-9;
RA Taniguchi H., Manenti S., Suzuki M., Titani K.;
RT "Myristoylated alanine-rich C kinase substrate (MARCKS), a major protein
RT kinase C substrate, is an in vivo substrate of proline-directed protein
RT kinase(s). A mass spectroscopic analysis of the post-translational
RT modifications.";
RL J. Biol. Chem. 269:18299-18302(1994).
RN [9]
RP REVERSIBLE ASSOCIATION WITH THE MEMBRANE.
RX PubMed=2034276; DOI=10.1038/351320a0;
RA Thelen M., Rosen A., Nairn A.C., Aderem A.;
RT "Regulation by phosphorylation of reversible association of a myristoylated
RT protein kinase C substrate with the plasma membrane.";
RL Nature 351:320-322(1991).
RN [10]
RP ACTIN-FILAMENT CROSS-LINKING.
RX PubMed=1560845; DOI=10.1038/356618a0;
RA Hartwig J.H., Thelen M., Rosen A., Janmey P.A., Nairn A.C., Aderem A.;
RT "MARCKS is an actin filament crosslinking protein regulated by protein
RT kinase C and calcium-calmodulin.";
RL Nature 356:618-622(1992).
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: Cell membrane {ECO:0000269|PubMed:8463217};
CC Lipid-anchor {ECO:0000269|PubMed:8463217}. Cytoplasm
CC {ECO:0000269|PubMed:8463217}.
CC -!- PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also
CC inhibits the F-actin cross-linking activity.
CC {ECO:0000269|PubMed:2473066, ECO:0000269|PubMed:8034575}.
CC -!- PTM: Myristoylation is found on 70-80% of the protein chains.
CC {ECO:0000269|PubMed:8034575}.
CC -!- SIMILARITY: Belongs to the MARCKS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA30635.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M24638; AAA30635.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BC115989; AAI15990.1; -; mRNA.
DR PIR; S08341; S08341.
DR RefSeq; NP_001069744.1; NM_001076276.1.
DR AlphaFoldDB; P12624; -.
DR STRING; 9913.ENSBTAP00000002691; -.
DR iPTMnet; P12624; -.
DR PaxDb; P12624; -.
DR PeptideAtlas; P12624; -.
DR PRIDE; P12624; -.
DR Ensembl; ENSBTAT00000002691; ENSBTAP00000002691; ENSBTAG00000002082.
DR Ensembl; ENSBTAT00000052599; ENSBTAP00000052045; ENSBTAG00000002082.
DR GeneID; 613548; -.
DR KEGG; bta:613548; -.
DR CTD; 4082; -.
DR VEuPathDB; HostDB:ENSBTAG00000002082; -.
DR VGNC; VGNC:31244; MARCKS.
DR eggNOG; ENOG502RB4V; Eukaryota.
DR GeneTree; ENSGT00730000111419; -.
DR InParanoid; P12624; -.
DR OMA; HAHQPAK; -.
DR OrthoDB; 1636177at2759; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000002082; Expressed in floor plate of diencephalon and 104 other tissues.
DR GO; GO:0032432; C:actin filament bundle; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042585; C:germinal vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0051764; P:actin crosslink formation; IEA:Ensembl.
DR GO; GO:0051017; P:actin filament bundle assembly; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
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; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8034575"
FT CHAIN 2..333
FT /note="Myristoylated alanine-rich C-kinase substrate"
FT /id="PRO_0000157147"
FT REGION 1..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..175
FT /note="Calmodulin-binding (PSD)"
FT COMPBIAS 124..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26645"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8034575"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8034575"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8034575"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8034575"
FT MOD_RES 117
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000305|PubMed:8034575"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30009"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8034575"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT MOD_RES 158
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:2473066"
FT MOD_RES 162
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:2473066"
FT MOD_RES 166
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:2473066"
FT MOD_RES 169
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:2473066"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26645"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29966"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:8034575"
FT CONFLICT 99..100
FT /note="AS -> H (in Ref. 2; AAA30635)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="E -> G (in Ref. 1 and 2; AAA30635)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="T -> S (in Ref. 1 and 2; AAA30635)"
FT /evidence="ECO:0000305"
FT CONFLICT 254..256
FT /note="SEE -> RRG (in Ref. 2; AAA30635)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="G -> GAAG (in Ref. 2; AAA30635)"
FT /evidence="ECO:0000305"
FT CONFLICT 290..299
FT /note="VPPEQEAAPA -> CPRAGGAPR (in Ref. 1 and 2; AAA30635)"
FT /evidence="ECO:0000305"
FT CONFLICT 304..306
FT /note="AAP -> PPR (in Ref. 1, 2; AAA30635 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="A -> S (in Ref. 1 and 2; AAA30635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 31665 MW; 2F9E895274058062 CRC64;
MGAQFSKTAA KGEATAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA EPGAKEELQA
NGSAPAADKE EPAAAGSGAA SPAAAEKDEP AAAAPDAGAS PVEKEAPVEG EAAEPGSPTA
AEGEAASAAS STSSPKAEDG ATPSPSNETP KKKKKRFSFK KSFKLSGFSF KKNKKEAGEG
GEAEGAAGAS AEGGKDEASG GAAAAAGEAG AAPGEPTAAP GEEAAAGEEG AAGGDPQEAK
PEEAAVAPEK PPASEEAKAV EEPSKAEEKA EEAGVSAAGC EAPSAAGPGV PPEQEAAPAE
EAAAAPASSA CAAPSQEAQP ECSPEAPPAE AAE
