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MRPA_DANRE
ID   MRPA_DANRE              Reviewed;         213 AA.
AC   Q6PD99;
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-A {ECO:0000305};
DE   AltName: Full=MARCKS-like protein 1-A {ECO:0000312|ZFIN:ZDB-GENE-040426-2146};
DE   AltName: Full=MARCKS-like protein 1-B {ECO:0000303|PubMed:27554589};
GN   Name=marcksl1a {ECO:0000312|ZFIN:ZDB-GENE-040426-2146};
GN   Synonyms=marcksl1 {ECO:0000312|EMBL:AEQ28195.1},
GN   marcksl1b {ECO:0000303|PubMed:27554589};
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:AEQ28195.1}
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 {ECO:0000312|Proteomes:UP000000437};
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:AAH58848.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH58848.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2003) 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:P49006}. Cell membrane
CC       {ECO:0000250|UniProtKB:P49006}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P49006}. 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:P49006}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in brain, eye and muscle.
CC       {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 and a ventrally curved body. No significant
CC       effect on formation of craniofacial cartilage. Formation of ceratohyal
CC       cartilage is disrupted with an abnormal angle relative to wild-type.
CC       Morphogenesis of the developing neural tube is abnormal, with a smaller
CC       angle between the walls of the hindbrain neuroepithelium at 24 hours
CC       post-fertilization (hpf). Retinal development is significantly delayed;
CC       no retinal ganglion cells (RGCs) are detected at 30 hours hpf and
CC       reduced numbers are found at 60 hpf. Cilium length in Kupffer's vesicle
CC       is significantly reduced. Double morpholino knockdown of marcksl1a and
CC       marckls1b results in a more pronounced developmental delay in the
CC       retina. {ECO:0000269|PubMed:27554589}.
CC   -!- SIMILARITY: Belongs to the MARCKS family. {ECO:0000305}.
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DR   EMBL; JF894245; AEQ28195.1; -; mRNA.
DR   EMBL; CU571066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC058848; AAH58848.1; -; mRNA.
DR   RefSeq; NP_998298.1; NM_213133.1.
DR   AlphaFoldDB; Q6PD99; -.
DR   STRING; 7955.ENSDARP00000056986; -.
DR   PaxDb; Q6PD99; -.
DR   PRIDE; Q6PD99; -.
DR   Ensembl; ENSDART00000056987; ENSDARP00000056986; ENSDARG00000039034.
DR   GeneID; 406407; -.
DR   KEGG; dre:406407; -.
DR   CTD; 406407; -.
DR   ZFIN; ZDB-GENE-040426-2146; marcksl1a.
DR   eggNOG; ENOG502RYXK; Eukaryota.
DR   GeneTree; ENSGT00940000165880; -.
DR   HOGENOM; CLU_073091_2_0_1; -.
DR   InParanoid; Q6PD99; -.
DR   OMA; EVENEQC; -.
DR   OrthoDB; 1511774at2759; -.
DR   TreeFam; TF332815; -.
DR   PRO; PR:Q6PD99; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 13.
DR   Bgee; ENSDARG00000039034; Expressed in swim bladder and 34 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..213
FT                   /note="MARCKS-related protein 1-A"
FT                   /id="PRO_0000445477"
FT   REGION          1..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..113
FT                   /note="Effector domain involved in lipid-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P28667"
FT   COMPBIAS        134..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P28667"
SQ   SEQUENCE   213 AA;  22094 MW;  4BB431C782BF75CB CRC64;
     MGAQLTKGEA TVEGKAVADK ANGQENGHVK TNGDVSTKPD GEAVAADGNG TAEVAKDEAP
     KTEEGDGIEA APATEAEASK SDGEAAKETK KKKKFSLKNS FKFKGISLKK NKKASEEAAE
     AVATPTTAED KPEENGQAAT ETKEEEPAAE TNETPAPEAE AEPKVEEAEP KAEEPAQQTE
     TAPTEETTKS EESPAPVEET TPTESSDPEP AAE
 
 
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