ID   A0A3B4E4P9_PYGNA        Unreviewed;       269 AA.
AC   A0A3B4E4P9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Myristoylated alanine-rich C-kinase substrate {ECO:0000256|ARBA:ARBA00039440};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000031587.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000031587.1}
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_017544677.1; XM_017689188.1.
DR   AlphaFoldDB; A0A3B4E4P9; -.
DR   STRING; 42514.ENSPNAP00000031587; -.
DR   Ensembl; ENSPNAT00000020680.1; ENSPNAP00000031587.1; ENSPNAG00000019053.1.
DR   GeneID; 108416156; -.
DR   CTD; 554102; -.
DR   GeneTree; ENSGT00730000111419; -.
DR   OMA; APFKHEK; -.
DR   OrthoDB; 4642898at2759; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
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.
DR   PROSITE; PS00826; MARCKS_1; 1.
PE   3: Inferred from homology;
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707}.
FT   REGION          1..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   269 AA;  27487 MW;  C294A4762AFA9E9F CRC64;
     MGAQFSKGAA KGETAAADTP GEAAASCKPN GQENGHVKVN GDASPAAAEG KEEVQANGSA
     AAEEQPKEEE GEKAEAVVAP AEKETGEGEQ EKEAEKEKEE GESATAAPAE GEAATPSTSN
     ETPKKKKKRF SFKKSFKLSG FSFKKTKKET GEGTEEAAGA SDEAKAEGGE ASGEEAKPAS
     EETKPEADEG AAATSLEKPE AKEAEKPAEE PKAASPAEEA PKPEEKPAEP VDEPAPTAVQ
     EEAPKQEEAA PAAQEAESSP VTTAEPVAE
//