ID A0A3B5KU12_TAKRU Unreviewed; 200 AA.
AC A0A3B5KU12;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Myristoylated alanine-rich C-kinase substrate {ECO:0000256|ARBA:ARBA00039440};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000056767.2, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000056767.2, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000056767.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00037738}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the MARCKS family.
CC {ECO:0000256|ARBA:ARBA00006456}.
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DR AlphaFoldDB; A0A3B5KU12; -.
DR STRING; 31033.ENSTRUP00000056767; -.
DR Ensembl; ENSTRUT00000056169.2; ENSTRUP00000056767.2; ENSTRUG00000025041.2.
DR GeneTree; ENSGT00730000111419; -.
DR InParanoid; A0A3B5KU12; -.
DR OMA; RENGHAK; -.
DR Proteomes; UP000005226; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IEA:Ensembl.
DR GO; GO:0003381; P:epithelial cell morphogenesis involved in gastrulation; IEA:Ensembl.
DR GO; GO:1900144; P:positive regulation of BMP secretion; IEA:Ensembl.
DR GO; GO:0060541; P:respiratory system development; IEA:Ensembl.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR InterPro; IPR002101; MARCKS.
DR PANTHER; PTHR14353:SF9; MYRISTOYLATED ALANINE-RICH C-KINASE SUBSTRATE; 1.
DR PANTHER; PTHR14353; MYRISTOYLATED ALANINE-RICH C-KINASE SUBSTRATE MARCKS; 1.
DR Pfam; PF02063; MARCKS; 1.
DR PRINTS; PR00963; MARCKS.
PE 3: Inferred from homology;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT REGION 1..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 200 AA; 20321 MW; FE3A5520A4C21047 CRC64;
MGGNVSKTAG KEEAAVEKPG EAAAVAAKAN GQENGHAKTN GDASPAAEDA NKAEVQVNGS
TPTEEAPKEG GENVEGAEAN GEKDEDGKQK KKRFSFKKPS FKLSGFSFKK TKKESEEGAA
VGEEETAEGE KAPASEEAPA EEKQADEGAE KAVAEAPKPE EGAKAQEDAA APEAGEEKPA
EASATEPETA AVSPEAPAAE
//
