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Database: UniProt
Entry: A0A3Q2CDM3_CYPVA
LinkDB: A0A3Q2CDM3_CYPVA
Original site: A0A3Q2CDM3_CYPVA 
ID   A0A3Q2CDM3_CYPVA        Unreviewed;       251 AA.
AC   A0A3Q2CDM3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Myristoylated alanine-rich C-kinase substrate {ECO:0000256|ARBA:ARBA00039440};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000003081.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000003081.1}
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   RefSeq; XP_015242291.1; XM_015386805.1.
DR   AlphaFoldDB; A0A3Q2CDM3; -.
DR   STRING; 28743.ENSCVAP00000003081; -.
DR   Ensembl; ENSCVAT00000010633.1; ENSCVAP00000003081.1; ENSCVAG00000004243.1.
DR   GeneID; 107092364; -.
DR   KEGG; cvg:107092364; -.
DR   CTD; 554102; -.
DR   GeneTree; ENSGT00730000111419; -.
DR   OMA; APFKHEK; -.
DR   OrthoDB; 4642898at2759; -.
DR   Proteomes; UP000265020; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020}.
FT   REGION          1..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   251 AA;  25748 MW;  858900E3E6F8B612 CRC64;
     MGAQLSKTSG NAETAAEKPG EAAASPTKTN GQENGHVKAN GDASPAAAEN GKEEVQANGS
     AETPKEEGEK AEAAPAEQEE KVEAASPAPA EGEAKAEDGA TPSTSNETPK KKKKKFSFKK
     SFKLSGFSFK KTKKETGDGA ENQEAAAESA APAEEAKAEA KEEPEAATEE AKPTEGEATP
     AAEQPKEDVE KKPEEEATEV EKPAEEAAAP EEPKAEETPA EAPEEAPKAE EATQEAASAE
     PPAPAAPEAS E
//
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