MRPB_DANRE
ID MRPB_DANRE Reviewed; 207 AA.
AC Q6NWH2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=MARCKS-related protein 1-B {ECO:0000305};
DE AltName: Full=MARCKS-like protein 1-A {ECO:0000303|PubMed:27554589};
DE AltName: Full=MARCKS-like protein 1-B {ECO:0000312|ZFIN:ZDB-GENE-040426-2315};
GN Name=marcksl1b {ECO:0000312|ZFIN:ZDB-GENE-040426-2315};
GN Synonyms=marcksl1a {ECO:0000303|PubMed:27554589},
GN marcksl2 {ECO:0000312|EMBL:AEQ28196.1};
GN ORFNames=zgc:85717 {ECO:0000312|EMBL:AAI54303.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|EMBL:AEQ28196.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wei C., Wang Y., Sun Y.;
RT "Zebrafish marcks involved in dorso-ventral patterning of early
RT development.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000312|EMBL:AAH67590.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH67590.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=27554589; DOI=10.1002/jez.b.22691;
RA Prieto D., Zolessi F.R.;
RT "Functional diversification of the four MARCKS family members in zebrafish
RT neural development.";
RL J. Exp. Zool. B Mol. Dev. Evol. 328:119-138(2017).
CC -!- FUNCTION: Involved in the control of cell movement by regulating actin
CC cytoskeleton homeostasis and filopodium and lamellipodium formation.
CC {ECO:0000250|UniProtKB:P28667}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P28667}. Cell membrane
CC {ECO:0000250|UniProtKB:P28667}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P28667}. Note=Associates with the membrane via
CC the insertion of the N-terminal N-myristoyl chain and the partial
CC insertion of the effector domain. {ECO:0000250|UniProtKB:P28667}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in brain and eye. Also detected
CC at lower levels in muscle. {ECO:0000269|PubMed:27554589}.
CC -!- DEVELOPMENTAL STAGE: Detected from 24 to 72 hours post-fertilization
CC (hpf). {ECO:0000269|PubMed:27554589}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein results in
CC reduced head and eye size, a ventrally curved body, and enlarged brain
CC vesicles. In the craniofacial cartilage, the ceratobranchial arches are
CC reduced. Formation of ceratohyal cartilage is disrupted with an
CC abnormal angle relative to wild-type. Morphogenesis of the developing
CC neural tube is abnormal, with a smaller angle between the walls of the
CC hindbrain neuroepithelium at 24 hours post-fertilization (hpf) and in
CC some cases a partial opening in the dorsal region. Some deformation of
CC the midbrain walls is also found. Retinal development is significantly
CC delayed; no retinal ganglion cells (RGCs) are detected at 30 hpf and
CC reduced numbers are found at 60 hpf. RGCs also appear to be
CC mislocalized. In about a third of embryos, three instead of two
CC otoliths are detected in the inner ear. Cilium length in Kupffer's
CC vesicle is significantly reduced. Cilia in the olfactory placode also
CC appear to be fewer in number and have reduced length. Double morpholino
CC knockdown of marcksl1a and marckls1b results in a more pronounced
CC developmental delay in the retina. Double morpholino knockdown of
CC marcksb and marcksl1b results in retinal morphogenesis defects of
CC increased severity. The optic cup structure is not apparent, and very
CC few atoh7-positive retinal ganglion cell precursors are detected.
CC Double morpholino knockdown of marcksb and marcksl1b also results in
CC more severe defects in neural tube morphology, with partial
CC duplications of the neural tube in the hindbrain region.
CC {ECO:0000269|PubMed:27554589}.
CC -!- SIMILARITY: Belongs to the MARCKS family. {ECO:0000305}.
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DR EMBL; JF894246; AEQ28196.1; -; mRNA.
DR EMBL; CU861666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067590; AAH67590.1; -; mRNA.
DR EMBL; BC154302; AAI54303.1; -; mRNA.
DR RefSeq; NP_998388.1; NM_213223.1.
DR AlphaFoldDB; Q6NWH2; -.
DR STRING; 7955.ENSDARP00000051803; -.
DR PaxDb; Q6NWH2; -.
DR PRIDE; Q6NWH2; -.
DR Ensembl; ENSDART00000051804; ENSDARP00000051803; ENSDARG00000035715.
DR Ensembl; ENSDART00000167803; ENSDARP00000130507; ENSDARG00000035715.
DR GeneID; 406504; -.
DR KEGG; dre:406504; -.
DR CTD; 406504; -.
DR ZFIN; ZDB-GENE-040426-2315; marcksl1b.
DR eggNOG; ENOG502RYXK; Eukaryota.
DR GeneTree; ENSGT00940000165880; -.
DR InParanoid; Q6NWH2; -.
DR OMA; ANCQENG; -.
DR TreeFam; TF332815; -.
DR PRO; PR:Q6NWH2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000035715; Expressed in brain and 25 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0051216; P:cartilage development; IMP:ZFIN.
DR GO; GO:0007417; P:central nervous system development; IMP:ZFIN.
DR GO; GO:0003407; P:neural retina development; IMP:ZFIN.
DR InterPro; IPR002101; MARCKS.
DR PANTHER; PTHR14353; PTHR14353; 1.
DR Pfam; PF02063; MARCKS; 1.
DR PRINTS; PR00963; MARCKS.
DR PROSITE; PS00826; MARCKS_1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Lipoprotein; Membrane; Myristate;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P28667"
FT CHAIN 2..207
FT /note="MARCKS-related protein 1-B"
FT /id="PRO_0000445478"
FT REGION 1..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..116
FT /note="Effector domain involved in lipid-binding"
FT /evidence="ECO:0000250|UniProtKB:P28667"
FT COMPBIAS 112..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P28667"
SQ SEQUENCE 207 AA; 20979 MW; 218AC5C17DCF7E2D CRC64;
MGSQASKGGV AVEGKAAAAD PAAVKTNGQE NGHVKTNGDV SAKAEGDAAT TNGSAEAAKE
SEAGAGDAIE PAPAAEGEAA KPEGEATKET PKKKKKKFSL KNSFKFKGIS LKKSKKNAEV
KEEAAAAAPA TEEKPEENGA ATEEKKEEEA KAEETPAAPV ETPKAEEPAA KAEEPAAAKE
EAAAPAVEAT KQTEETNSTP APSEQKE
