ID H3BB37_LATCH Unreviewed; 240 AA.
AC H3BB37;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=MARCKS like 1 {ECO:0000313|Ensembl:ENSLACP00000019108.1};
GN Name=MARCKSL1 {ECO:0000313|Ensembl:ENSLACP00000019108.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000019108.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000019108.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the MARCKS family.
CC {ECO:0000256|ARBA:ARBA00006456}.
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DR EMBL; AFYH01066727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005995649.1; XM_005995587.2.
DR AlphaFoldDB; H3BB37; -.
DR STRING; 7897.ENSLACP00000019108; -.
DR Ensembl; ENSLACT00000019241.1; ENSLACP00000019108.1; ENSLACG00000016811.1.
DR GeneID; 102357518; -.
DR KEGG; lcm:102357518; -.
DR CTD; 65108; -.
DR eggNOG; ENOG502RYXK; Eukaryota.
DR GeneTree; ENSGT00730000111349; -.
DR HOGENOM; CLU_073091_2_0_1; -.
DR InParanoid; H3BB37; -.
DR OMA; CSTNETE; -.
DR OrthoDB; 5362620at2759; -.
DR TreeFam; TF332815; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000016811; Expressed in pectoral fin and 6 other cell types or tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR InterPro; IPR002101; MARCKS.
DR PANTHER; PTHR14353:SF8; MARCKS-RELATED PROTEIN; 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:UP000008672}.
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 240 AA; 25210 MW; D249EEF27EBB629C CRC64;
MGSQGSKAAK EVIAEKSTDG VGDPSPTKPN GQENGHVKTN GDLSPKADGD AAPVNGNGSA
EPVKENKVES GAGDAIELAP AVEGEGAKAD VETTKETKKK KKMISFKKPA FFKKRISFRK
AKKETGEKVE ETAVAASGED QAEAKENPGA TEAKTEENPG TTTSKTKDQS NEKEEESSVA
GKETKPSTEE EKAEEAPAKE EKPAENQDDQ SKPDATEAST KAAETEVSSS TADSIERKEE
//
