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Database: UniProt
Entry: A0A7J8KC46_ROUAE
LinkDB: A0A7J8KC46_ROUAE
Original site: A0A7J8KC46_ROUAE 
ID   A0A7J8KC46_ROUAE        Unreviewed;       334 AA.
AC   A0A7J8KC46;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   18-JUN-2025, entry version 15.
DE   RecName: Full=Myristoylated alanine-rich C-kinase substrate {ECO:0000256|ARBA:ARBA00039440};
GN   ORFNames=HJG63_013021 {ECO:0000313|EMBL:KAF6506447.1};
OS   Rousettus aegyptiacus (Egyptian fruit bat) (Pteropus aegyptiacus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC   Pteropodidae; Rousettinae; Rousettus.
OX   NCBI_TaxID=9407 {ECO:0000313|EMBL:KAF6506447.1, ECO:0000313|Proteomes:UP000593571};
RN   [1] {ECO:0000313|EMBL:KAF6506447.1, ECO:0000313|Proteomes:UP000593571}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRouAeg1 {ECO:0000313|EMBL:KAF6506447.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAF6506447.1};
RX   PubMed=32699395;
RA   Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA   Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA   Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA   Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA   Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA   Vernes S.C., Myers E.W., Teeling E.C.;
RT   "Six reference-quality genomes reveal evolution of bat adaptations.";
RL   Nature 583:578-584(2020).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}.
CC   -!- SIMILARITY: Belongs to the MARCKS family.
CC       {ECO:0000256|ARBA:ARBA00006456}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAF6506447.1}.
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DR   EMBL; JACASE010000001; KAF6506447.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7J8KC46; -.
DR   OrthoDB; 9950867at2759; -.
DR   Proteomes; UP000593571; Unassembled WGS sequence.
DR   GO; GO:0032432; C:actin filament bundle; IEA:TreeGrafter.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0051015; F:actin filament binding; IEA:TreeGrafter.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007015; P:actin filament organization; IEA:TreeGrafter.
DR   GO; GO:0007417; P:central nervous system development; IEA:TreeGrafter.
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.
DR   PROSITE; PS00827; MARCKS_2; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kinase {ECO:0000313|EMBL:KAF6506447.1};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Reference proteome {ECO:0000313|Proteomes:UP000593571};
KW   Transferase {ECO:0000313|EMBL:KAF6506447.1}.
FT   REGION          1..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..84
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..102
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..136
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..164
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..237
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..334
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  31804 MW;  EEC6629A59C50811 CRC64;
     MGAQFSKTAA KGEAAAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA EPGSKEELQA
     NGSAPAADKE EPAATGSGTA SPAAAEKDEP AAAAAPEPAA SGAEKEAPAE GEAAEPGSPT
     AAEGEAASAA SSTSSPKAED GATPSPSNET PKKKKKRFSF KKSFKLSGFS FKKNKKEAGE
     GGEAEGAAGA SAEGGKDEAA GGAGSAAAEA GAAPGEQAAA PSDEAAAGEE GAAAGDPQEV
     KPEEAAVAPE KPPASEEAKA AEEPNKAEEK TEEAGASAAA CEAPSAAGPG APPEQEAAPA
     EEAAAVSASS ACAAPSQEAQ PECSPEAPPA EAAE
//
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