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MAF_XENTR
ID   MAF_XENTR               Reviewed;         352 AA.
AC   Q0V9K1; Q4U1U0;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Transcription factor Maf;
GN   Name=maf;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Fat body;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-346, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=15759153; DOI=10.1007/s00427-005-0476-y;
RA   Coolen M., Sii-Felice K., Bronchain O., Mazabraud A., Bourrat F.,
RA   Retaux S., Felder-Schmittbuhl M.-P., Mazan S., Plouhinec J.-L.;
RT   "Phylogenomic analysis and expression patterns of large Maf genes in
RT   Xenopus tropicalis provide new insights into the functional evolution of
RT   the gene family in osteichthyans.";
RL   Dev. Genes Evol. 215:327-339(2005).
CC   -!- FUNCTION: Acts as a transcriptional activator or repressor.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer or heterodimer. Binds DNA as a homodimer or a
CC       heterodimer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the presumptive lens ectoderm at
CC       stage 24. Expressed in the pronephros from stage 28 onwards. Expressed
CC       in the forming tubules but also in the glomus of the pronephros from
CC       stage 33. Expressed in cells of the optic vesicle in a dorso-temporal
CC       location and in cells showing the expected dorsal location of Rohon-
CC       Beard neurons in the neural tube at stage 35.
CC       {ECO:0000269|PubMed:15759153}.
CC   -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR   EMBL; BC121507; AAI21508.1; -; mRNA.
DR   EMBL; DQ018732; AAY41825.1; -; mRNA.
DR   RefSeq; NP_001027476.1; NM_001032305.1.
DR   AlphaFoldDB; Q0V9K1; -.
DR   SMR; Q0V9K1; -.
DR   STRING; 8364.ENSXETP00000012614; -.
DR   PaxDb; Q0V9K1; -.
DR   DNASU; 613051; -.
DR   GeneID; 613051; -.
DR   KEGG; xtr:613051; -.
DR   CTD; 4094; -.
DR   Xenbase; XB-GENE-6053271; maf.
DR   eggNOG; KOG4196; Eukaryota.
DR   HOGENOM; CLU_063062_0_0_1; -.
DR   InParanoid; Q0V9K1; -.
DR   OMA; SMPGEEM; -.
DR   OrthoDB; 1395389at2759; -.
DR   TreeFam; TF325689; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000000172; Expressed in skeletal muscle tissue and 12 other tissues.
DR   ExpressionAtlas; Q0V9K1; baseline.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR004826; bZIP_Maf.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR028573; Maf/V-MAF.
DR   InterPro; IPR013592; Maf_TF_N.
DR   InterPro; IPR008917; TF_DNA-bd_sf.
DR   InterPro; IPR024874; Transcription_factor_Maf_fam.
DR   PANTHER; PTHR10129; PTHR10129; 1.
DR   PANTHER; PTHR10129:SF9; PTHR10129:SF9; 1.
DR   Pfam; PF03131; bZIP_Maf; 1.
DR   Pfam; PF08383; Maf_N; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF47454; SSF47454; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..352
FT                   /note="Transcription factor Maf"
FT                   /id="PRO_0000364084"
FT   DOMAIN          265..328
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          57..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..290
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          293..314
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          331..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        343..346
FT                   /note="NPSS -> KYFM (in Ref. 2; AAY41825)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   352 AA;  38603 MW;  E8A6BB6C62FFAEE2 CRC64;
     MASELAMSSS DLPTSPLAME YVNDFDLMKF EVKKEPVETD RIISQCGRLI AGGSLSSTPM
     STPCSSVPPS PSFSAPSPGS GSEQKSHLED YYWMSAYPQQ INPEALGFSP EDAVEALISN
     SNQQQQQQQQ QQLQAGYDGF ARGQQYASSG GMPGEDMGSA AAVVSAVIAA AAAQNPHHHH
     HHHHHSVGHQ AGVQPPGGGT GGGGSSGSST SSSVVGALHP PAAHHHHHHH HLHFDDRFSD
     EQLVTMSVRE LNRQLRGVSK EEVIRLKQKR RTLKNRGYAQ SCRFKRVQQR HVLESEKNQL
     LQQVEHLKQE ISRLLRERDA YKEKYEKLLG SGFRENGSSN SDNPSSPEYF MS
 
 
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