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MEOX1_DANRE
ID   MEOX1_DANRE             Reviewed;         253 AA.
AC   F1Q4R9; Q6DHF3;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Homeobox protein MOX-1 {ECO:0000250|UniProtKB:P50221};
DE   AltName: Full=Mesenchyme homeobox 1 {ECO:0000250|UniProtKB:P50221};
DE   AltName: Full=Protein choker {ECO:0000303|PubMed:25119043};
GN   Name=meox1 {ECO:0000312|ZFIN:ZDB-GENE-040718-149};
GN   Synonyms=cho {ECO:0000303|PubMed:25119043};
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|Ensembl:ENSDARP00000096438};
RN   [1]
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=25119043; DOI=10.1038/nature13678;
RA   Nguyen P.D., Hollway G.E., Sonntag C., Miles L.B., Hall T.E., Berger S.,
RA   Fernandez K.J., Gurevich D.B., Cole N.J., Alaei S., Ramialison M.,
RA   Sutherland R.L., Polo J.M., Lieschke G.J., Currie P.D.;
RT   "Haematopoietic stem cell induction by somite-derived endothelial cells
RT   controlled by meox1.";
RL   Nature 512:314-318(2014).
CC   -!- FUNCTION: Mesodermal transcription factor that plays a key role in
CC       somitogenesis and is specifically required for sclerotome development.
CC       Required for maintenance of the sclerotome polarity and formation of
CC       the cranio-cervical joints. Binds specifically to the promoter of
CC       target genes and regulates their expression. Required for hematopoietic
CC       stem cell (HSCs) induction via its role in somitogenesis: specification
CC       of HSCs occurs via the deployment of a specific endothelial precursor
CC       population, which arises within a sub-compartment of the somite named
CC       endotome. Acts by mediating specification of endothelial cells of the
CC       endotome within the nascent somite, notably by repressing expression of
CC       cxcl12b. {ECO:0000269|PubMed:25119043}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P32442}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P32442}. Note=Localizes predominantly in the
CC       nucleus. {ECO:0000250|UniProtKB:P32442}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F1Q4R9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F1Q4R9-2; Sequence=VSP_057099;
CC   -!- DEVELOPMENTAL STAGE: Expressed within the early somite and then becomes
CC       restricted to the external cell layer (ECL) and consequently to
CC       appendicular muscle populations. {ECO:0000269|PubMed:25119043}.
CC   -!- DISRUPTION PHENOTYPE: Defects in somite lineages. Secondary trunk
CC       myogenesis is reduced, as well as appendicular and hypaxial muscles and
CC       their progenitors. These cell types derive from the external cell layer
CC       (ECL) and ECL cell numbers are reduced. The endotome is expanded at the
CC       expense of a second somitic cell type. The resulting increase in
CC       endotome-derived cells that migrate to colonize the dorsal aorta
CC       generates a dramatic increase in chemokine-dependent hematopoietic stem
CC       cell (HSCs) induction. {ECO:0000269|PubMed:25119043}.
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DR   EMBL; CR847827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC076021; AAH76021.1; -; mRNA.
DR   RefSeq; NP_001002450.2; NM_001002450.2. [F1Q4R9-1]
DR   AlphaFoldDB; F1Q4R9; -.
DR   SMR; F1Q4R9; -.
DR   STRING; 7955.ENSDARP00000096438; -.
DR   PaxDb; F1Q4R9; -.
DR   Ensembl; ENSDART00000011252; ENSDARP00000027691; ENSDARG00000115382. [F1Q4R9-1]
DR   Ensembl; ENSDART00000105661; ENSDARP00000096438; ENSDARG00000007891. [F1Q4R9-1]
DR   GeneID; 436723; -.
DR   KEGG; dre:436723; -.
DR   CTD; 4222; -.
DR   ZFIN; ZDB-GENE-040718-149; meox1.
DR   eggNOG; KOG0489; Eukaryota.
DR   GeneTree; ENSGT00940000154018; -.
DR   HOGENOM; CLU_081326_1_0_1; -.
DR   InParanoid; F1Q4R9; -.
DR   OMA; CMRSPQP; -.
DR   OrthoDB; 1522857at2759; -.
DR   PhylomeDB; F1Q4R9; -.
DR   TreeFam; TF351603; -.
DR   PRO; PR:F1Q4R9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 12.
DR   Bgee; ENSDARG00000007891; Expressed in muscle tissue and 8 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR   GO; GO:0003682; F:chromatin binding; IDA:ZFIN.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0048066; P:developmental pigmentation; IMP:ZFIN.
DR   GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:UniProtKB.
DR   GO; GO:0030097; P:hemopoiesis; IMP:ZFIN.
DR   GO; GO:0055001; P:muscle cell development; IMP:ZFIN.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0061056; P:sclerotome development; ISS:UniProtKB.
DR   GO; GO:0001501; P:skeletal system development; IMP:ZFIN.
DR   GO; GO:0061053; P:somite development; IMP:UniProtKB.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR020479; Homeobox_metazoa.
DR   InterPro; IPR042634; MOX-1/MOX-2.
DR   PANTHER; PTHR24328; PTHR24328; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; Cytoplasm; Developmental protein;
KW   DNA-binding; Homeobox; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..253
FT                   /note="Homeobox protein MOX-1"
FT                   /id="PRO_0000430816"
FT   DNA_BIND        170..229
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          136..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         15..27
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_057099"
SQ   SEQUENCE   253 AA;  28150 MW;  36F788BDB2597576 CRC64;
     MEQSASSCMR SPHTGGALWG CVRSPHSGGS GAGIQPYQQA PFALHQKHDF LAYTDFSSSC
     LVPAPHAYPR EDRLYPETHS GYQRTEWQFS PCEPRGRGQE PCQGAAEAVG AEMDSAGGDR
     LAGAVTGCLE GDYSPQSVPA VDTEKKSSKR KREVTDIQDS SFKADSNCKA RKERTAFTKE
     QLRELEAEFT HHNYLTRLRR YEIAVNLDLT ERQVKVWFQN RRMKWKRVKG GQPASPHDLE
     ADELDSAASP SSE
 
 
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