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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//