ID A0A3P9AXK7_9CICH Unreviewed; 218 AA.
AC A0A3P9AXK7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Myristoylated alanine-rich C-kinase substrate {ECO:0000256|ARBA:ARBA00039440};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005002421.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005002421.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005002421.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_004540386.1; XM_004540329.2.
DR AlphaFoldDB; A0A3P9AXK7; -.
DR STRING; 106582.ENSMZEP00005002421; -.
DR Ensembl; ENSMZET00005002531.1; ENSMZEP00005002421.1; ENSMZEG00005001901.1.
DR GeneID; 101475091; -.
DR KEGG; mze:101475091; -.
DR CTD; 323201; -.
DR GeneTree; ENSGT00730000111419; -.
DR OrthoDB; 4642898at2759; -.
DR Proteomes; UP000265160; LG19.
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:UP000265160}.
FT REGION 1..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 22233 MW; A017E8E14D863F22 CRC64;
MGAQISKTAG KEEAAVEQPA EGAAVAAKTN GQENGHAKTN GDTSPATEEV NKAEVQANGS
TPTEEAPKEE GEKVEGAEAN GEKEPAATNG EASAKPEEGT PSTSEDGKQK KKRFSFKKPS
FKLSGFSFKK TKKESEEATE DGAGAAAEPA EGEKATSEAP TEEAKPDEAG EEAKEAAAEE
PKAEEGKAEE TAGEEKPAEA SPTEPETAAS PEAAAAAE
//
