ID   GRHL1_PONAB             Reviewed;         618 AA.
AC   Q5RAR8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Grainyhead-like protein 1 homolog;
DE   AltName: Full=Transcription factor CP2-like 2;
GN   Name=GRHL1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor involved in epithelial development.
CC       Binds directly to the consensus DNA sequence 5'-AACCGGTT-3'. Important
CC       regulator of DSG1 in the context of hair anchorage and epidermal
CC       differentiation, participates in the maintenance of the skin barrier.
CC       There is no genetic interaction with GRHL3, no functional cooperativity
CC       due to diverse target gene selectivity during epithelia development.
CC       {ECO:0000250|UniProtKB:Q5EY87, ECO:0000250|UniProtKB:Q921D9,
CC       ECO:0000250|UniProtKB:Q9NZI5}.
CC   -!- SUBUNIT: Binds DNA as homodimer. Homodimer, also forms heterodimers
CC       with GRHL2 or GRHL3. {ECO:0000250|UniProtKB:Q9NZI5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q921D9}.
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; CR858944; CAH91142.1; -; mRNA.
DR   RefSeq; NP_001125668.1; NM_001132196.2.
DR   AlphaFoldDB; Q5RAR8; -.
DR   SMR; Q5RAR8; -.
DR   STRING; 9601.ENSPPYP00000014134; -.
DR   GeneID; 100172588; -.
DR   KEGG; pon:100172588; -.
DR   CTD; 29841; -.
DR   eggNOG; KOG4091; Eukaryota.
DR   InParanoid; Q5RAR8; -.
DR   OrthoDB; 286319at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0008544; P:epidermis development; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..618
FT                   /note="Grainyhead-like protein 1 homolog"
FT                   /id="PRO_0000227992"
FT   DOMAIN          248..474
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          74..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..389
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZI5"
FT   REGION          427..430
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZI5"
FT   MOD_RES         208
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZI5"
SQ   SEQUENCE   618 AA;  70158 MW;  DE8DE7743F72BFD0 CRC64;
     MTQEYDNKRP VLVLQNEALY PQRRSYTSED EAWKSFLENP LTAATKAMMS INGDEDSAAA
     LGLLYDYYKV PRERRSSTAK PEVEHPEPDH SKRNSIPIVT EQPLISAGEN RVQVLKNVPF
     NIVLPHGNQL GIDKRGHLTV PDTTVTVSIA TMPTHSIKTE TQPHGFTVGI PPAVYHPEPT
     ERVVVFDRNL STDQFSSGAQ APNAQRRTPD STFSETFKEG VQEVFFPSDL SLRMPGMNSE
     DYVFDSVSGN NFEYTLEASK SLRQKPGDST MTYLNKGQFY PITLKEVSSN EGIHHPISKV
     RSVTMVVFAE DKSREDQLRH WKYWHSRQHT AKQRCIDIAD YKESFNTISN IEEIAYNAIS
     FTWDINDEAK VFISVNCLST DFSSQKGVKG LPLNIQIDTY SYNNRSNKPV HRAYCQIKVF
     CDKGAERKIR DEERKQSKRK VSDVKVPLLP SHKRMDITVF KPFIDLDTQP VLFIPDVHFA
     SLQRGTHVLP IASEELEGEG SVLKRGPYST EDDFAVPPSA KLARIEEPKR VLLYVRKESE
     EVFDALMLKT PSLKGLMEAI SDKYDVPHDK IGKIFKKCKK GILVNMDDNI VKHYSNEDTF
     QLQIEEAGGS YKLTLIEI