ID   GRHL1_XENLA             Reviewed;         609 AA.
AC   Q5EY87;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Grainyhead-like protein 1 homolog {ECO:0000250|UniProtKB:Q9NZI5};
DE   AltName: Full=Transcription factor CP2-like 2;
GN   Name=grhl1 {ECO:0000250|UniProtKB:Q9NZI5};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=15705857; DOI=10.1242/dev.01641;
RA   Tao J., Kuliyev E., Wang X., Li X., Wilanowski T., Jane S.M., Mead P.E.,
RA   Cunningham J.M.;
RT   "BMP4-dependent expression of Xenopus Grainyhead-like 1 is essential for
RT   epidermal differentiation.";
RL   Development 132:1021-1034(2005).
CC   -!- FUNCTION: Transcription factor involved in epithelial development
CC       (PubMed:15705857). Binds directly to the consensus DNA sequence 5'-
CC       AACCGGTT-3' and modulates expression of epidermal-specific genes,
CC       including XK81A1 (PubMed:15705857). Important regulator of DSG1 in the
CC       context of epidermal differentiation. Regulates the maintenance of skin
CC       barrier. No genetic interaction with GRHL3, no functional cooperativity
CC       due to diverse target gene selectivity during epithelia development (By
CC       similarity). Functions downstream of BMP-signaling cascade modulating
CC       endogenous bmp4-responsive targets (PubMed:15705857).
CC       {ECO:0000250|UniProtKB:Q921D9, ECO:0000269|PubMed:15705857}.
CC   -!- SUBUNIT: Binds DNA as homodimer. {ECO:0000250|UniProtKB:Q9NZI5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q921D9}.
CC   -!- DEVELOPMENTAL STAGE: After fertilization, expressed at the animal pole.
CC       Expression becomes restricted to the non-neuronal ectoderm of the
CC       embryo with progression through gastrulation and neurulation.
CC       Expression is observed only in the most superficial cellular layer of
CC       the embryo, being absent from the neural plate At later stages,
CC       expression is restricted to tissues with an epidermal fate.
CC       {ECO:0000269|PubMed:15705857}.
CC   -!- DISEASE: Note=Defects in grhl1 are the cause of defective epidermal
CC       differentiation.
CC   -!- MISCELLANEOUS: GRHL genes (GRHL1, GRHL2 and GRHL3) show a paradoxal
CC       lack of redundancy despite their extensive sequence identity in the
CC       DNA-binding and protein dimerization domains and the fact that the core
CC       consensus DNA binding sites are identical. They have related but
CC       remarkably different functions during embryogenesis because of their
CC       differential spatiotemporal expression patterns during development.
CC       {ECO:0000250|UniProtKB:Q921D9}.
CC   -!- SIMILARITY: Belongs to the grh/CP2 family. Grainyhead subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY591750; AAT88108.1; -; mRNA.
DR   RefSeq; NP_001089071.1; NM_001095602.1.
DR   AlphaFoldDB; Q5EY87; -.
DR   SMR; Q5EY87; -.
DR   GeneID; 733170; -.
DR   KEGG; xla:733170; -.
DR   CTD; 733170; -.
DR   Xenbase; XB-GENE-486580; grhl1.L.
DR   OrthoDB; 286319at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 733170; Expressed in zone of skin and 9 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR007604; CP2.
DR   Pfam; PF04516; CP2; 1.
DR   PROSITE; PS51968; GRH_CP2_DB; 1.
PE   2: Evidence at transcript level;
KW   Activator; Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..609
FT                   /note="Grainyhead-like protein 1 homolog"
FT                   /id="PRO_0000227993"
FT   DOMAIN          239..465
FT                   /note="Grh/CP2 DB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01313"
FT   REGION          1..91
FT                   /note="Transcription activation"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K5C0"
FT   REGION          183..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..380
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZI5"
FT   REGION          418..421
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZI5"
FT   COMPBIAS        183..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  69732 MW;  5CA9D434915D4C53 CRC64;
     MTQDYDNKRP VLVLQNDGLY QQRRSYTNED EAWKSFLENP LTAATKAMMS INGDEDSAAA
     LGLLYDYYKV PRERRLSAAK QEHDHADHEH SKRNGLPQIN EQALLPDNRV QVLKTVPFNI
     VVPLANQVDK RGHLTTPDTT AAVSIAHPIK TESQSHCFSV GLQSVFHTEP TERIVAFDRA
     VPSDHFTSNN QPPNSQRRTP DSTFSETYKE DVPEVFFPPD LSLRMGSMNS EDYVFDSVAG
     NNFEYTLEAS KSLRPKPGDS TMTYLNKGQF YPITLKEIGS NKGIHHPISK VRSVIMVVFA
     DDKSREDQLR HWKYWHSRQH TAKQRCIDIA DYKESFNTIS NIEEIAYNAI SFTWDLNDEG
     KVFISVNCLS TDFSSQKGVK GLPLNLQIDT YSYNNRSNKP VHRAYCQIKV FCDKGAERKI
     RDEERKQSKR KVQDVKVGLL PTHKRTDITV FKPMMDLDTQ PVLFIPDVHF ANLQRTTHVL
     PISPEDMEGE LNPGMKRLPF SPEEDFNTPP AKLPRVDEPK RVLLYVRRET EEVFDALMLK
     TPTLKGLMEA VSEKYEVPIE KIGKIFKKCK KGILVNMDDN IIKHYSNEDT FHLQIEESGG
     SYKLTLTEI