GRHL3_HUMAN
ID GRHL3_HUMAN Reviewed; 626 AA.
AC Q8TE85; A2A297; B2RCL1; G3XAF0; Q5TH78; Q86Y06; Q8N407;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Grainyhead-like protein 3 homolog {ECO:0000312|HGNC:HGNC:25839};
DE AltName: Full=Sister of mammalian grainyhead;
DE AltName: Full=Transcription factor CP2-like 4;
GN Name=GRHL3 {ECO:0000312|HGNC:HGNC:25839};
GN Synonyms=SOM, TFCP2L4 {ECO:0000312|HGNC:HGNC:25839};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), FUNCTION, TISSUE
RP SPECIFICITY, ALTERNATIVE SPLICING, AND INTERACTION WITH GRHL1 AND GRHL2.
RC TISSUE=Testis;
RX PubMed=12549979; DOI=10.1042/bj20021476;
RA Ting S.B., Wilanowski T., Cerruti L., Zhao L.L., Cunningham J.M.,
RA Jane S.M.;
RT "The identification and characterization of human sister-of-mammalian
RT grainyhead (SOM) expands the grainyhead-like family of developmental
RT transcription factors.";
RL Biochem. J. 370:953-962(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Kidney epithelium, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21081122; DOI=10.1016/j.ydbio.2010.11.011;
RA Boglev Y., Wilanowski T., Caddy J., Parekh V., Auden A., Darido C.,
RA Hislop N.R., Cangkrama M., Ting S.B., Jane S.M.;
RT "The unique and cooperative roles of the Grainy head-like transcription
RT factors in epidermal development reflect unexpected target gene
RT specificity.";
RL Dev. Biol. 349:512-522(2011).
RN [7]
RP FUNCTION.
RX PubMed=25347468; DOI=10.1172/jci77138;
RA Gordon W.M., Zeller M.D., Klein R.H., Swindell W.R., Ho H., Espetia F.,
RA Gudjonsson J.E., Baldi P.F., Andersen B.;
RT "A GRHL3-regulated repair pathway suppresses immune-mediated epidermal
RT hyperplasia.";
RL J. Clin. Invest. 124:5205-5218(2014).
RN [8]
RP VARIANTS VWS2 HIS-298; CYS-391 AND GLN-520, CHARACTERIZATION OF VARIANTS
RP VWS2 HIS-298; CYS-391 AND GLN-520, AND FUNCTION.
RX PubMed=24360809; DOI=10.1016/j.ajhg.2013.11.009;
RA Peyrard-Janvid M., Leslie E.J., Kousa Y.A., Smith T.L., Dunnwald M.,
RA Magnusson M., Lentz B.A., Unneberg P., Fransson I., Koillinen H.K.,
RA Rautio J., Pegelow M., Karsten A., Basel-Vanagaite L., Gordon W.,
RA Andersen B., Svensson T., Murray J.C., Cornell R.A., Kere J., Schutte B.C.;
RT "Dominant mutations in GRHL3 cause Van der Woude Syndrome and disrupt oral
RT periderm development.";
RL Am. J. Hum. Genet. 94:23-32(2014).
CC -!- FUNCTION: Transcription factor playing important roles in primary
CC neurulation and in the differentiation of stratified epithelia of both
CC ectodermal and endodermal origin (By similarity). Binds directly to the
CC consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and
CC repressor on distinct target genes (PubMed:21081122, PubMed:25347468).
CC xhibits functional redundancy with GRHL2 in epidermal morphogenetic
CC events and epidermal wound repair (By similarity). Exhibits functional
CC redundancy with GRHL2 in epidermal morphogenetic events and epidermal
CC wound repair but is essential to form the epidermal barrier with TGM3
CC as critical direct target gene among others. Despite being dispensable
CC during normal epidermal homeostasis in the adulthood, is again required
CC for barrier repair after immune-mediated epidermal damage, regulates
CC distinct gene batteries in embryonic epidermal differentiation and
CC adult epidermal barrier reformation after injury. Plays unique and
CC cooperative roles with GRHL2 in establishing distinct zones of primary
CC neurulation. Essential for spinal closure, functions cooperatively with
CC GRHL2 in closure 2 (forebrain/midbrain boundary) and posterior
CC neuropore closure (By similarity). Also required for proper development
CC of the oral periderm (PubMed:24360809). No genetic interaction with
CC GRHL3, no functional cooperativity due to diverse target gene
CC selectivity (PubMed:21081122). {ECO:0000250|UniProtKB:Q5FWH3,
CC ECO:0000269|PubMed:12549979, ECO:0000269|PubMed:21081122,
CC ECO:0000269|PubMed:24360809, ECO:0000269|PubMed:25347468}.
CC -!- SUBUNIT: Homodimer, also forms heterodimers with GRHL1 and GRHL2
CC (PubMed:12549979). Interacts with LMO4 (By similarity).
CC {ECO:0000250|UniProtKB:Q5FWH3, ECO:0000269|PubMed:12549979}.
CC -!- INTERACTION:
CC Q8TE85; O14744: PRMT5; NbExp=2; IntAct=EBI-8469396, EBI-351098;
CC Q8TE85; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-8469396, EBI-912440;
CC Q8TE85-2; Q96JC9: EAF1; NbExp=3; IntAct=EBI-12827521, EBI-769261;
CC Q8TE85-2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-12827521, EBI-744099;
CC Q8TE85-2; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-12827521, EBI-10226430;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21081122}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8TE85-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TE85-2; Sequence=VSP_017645, VSP_017646;
CC Name=3;
CC IsoId=Q8TE85-3; Sequence=VSP_017644, VSP_017646;
CC Name=4;
CC IsoId=Q8TE85-4; Sequence=VSP_017643, VSP_017646;
CC Name=5;
CC IsoId=Q8TE85-5; Sequence=VSP_017646;
CC -!- TISSUE SPECIFICITY: Expressed in brain, colon, pancreas, placenta and
CC kidney. Isoform 1 is expressed in lung and tonsil. Isoform 2 is
CC prostate-specific. {ECO:0000269|PubMed:12549979}.
CC -!- DISEASE: Van der Woude syndrome 2 (VWS2) [MIM:606713]: An autosomal
CC dominant developmental disorder characterized by lower lip pits, cleft
CC lip and/or cleft palate. {ECO:0000269|PubMed:24360809}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: GRHL genes (GRHL1, GRHL2 and GRHL3) show a paradoxical
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:Q5FWH3}.
CC -!- SIMILARITY: Belongs to the grh/CP2 family. Grainyhead subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36890.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG37608.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY231160; AAO67370.1; -; mRNA.
DR EMBL; AY231161; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK074386; BAB85067.1; -; mRNA.
DR EMBL; AK315164; BAG37608.1; ALT_INIT; mRNA.
DR EMBL; AL031431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471134; EAW95121.1; -; Genomic_DNA.
DR EMBL; BC036890; AAH36890.1; ALT_INIT; mRNA.
DR CCDS; CCDS251.1; -. [Q8TE85-2]
DR CCDS; CCDS252.2; -. [Q8TE85-1]
DR CCDS; CCDS44088.1; -. [Q8TE85-5]
DR CCDS; CCDS53284.1; -. [Q8TE85-3]
DR RefSeq; NP_001181939.1; NM_001195010.1. [Q8TE85-3]
DR RefSeq; NP_067003.2; NM_021180.3. [Q8TE85-2]
DR RefSeq; NP_937816.1; NM_198173.2. [Q8TE85-5]
DR RefSeq; NP_937817.3; NM_198174.2. [Q8TE85-1]
DR RefSeq; XP_011540171.1; XM_011541869.1. [Q8TE85-3]
DR RefSeq; XP_011540172.1; XM_011541870.2. [Q8TE85-4]
DR AlphaFoldDB; Q8TE85; -.
DR SMR; Q8TE85; -.
DR BioGRID; 121781; 10.
DR IntAct; Q8TE85; 8.
DR MINT; Q8TE85; -.
DR STRING; 9606.ENSP00000288955; -.
DR iPTMnet; Q8TE85; -.
DR PhosphoSitePlus; Q8TE85; -.
DR BioMuta; GRHL3; -.
DR DMDM; 116242504; -.
DR EPD; Q8TE85; -.
DR jPOST; Q8TE85; -.
DR MassIVE; Q8TE85; -.
DR MaxQB; Q8TE85; -.
DR PaxDb; Q8TE85; -.
DR PeptideAtlas; Q8TE85; -.
DR PRIDE; Q8TE85; -.
DR ProteomicsDB; 182; -.
DR ProteomicsDB; 33731; -.
DR ProteomicsDB; 74420; -. [Q8TE85-1]
DR ProteomicsDB; 74421; -. [Q8TE85-2]
DR ProteomicsDB; 74422; -. [Q8TE85-3]
DR ProteomicsDB; 74423; -. [Q8TE85-4]
DR Antibodypedia; 15710; 184 antibodies from 22 providers.
DR DNASU; 57822; -.
DR Ensembl; ENST00000236255.4; ENSP00000236255.4; ENSG00000158055.17. [Q8TE85-2]
DR Ensembl; ENST00000350501.9; ENSP00000288955.5; ENSG00000158055.17. [Q8TE85-1]
DR Ensembl; ENST00000356046.6; ENSP00000348333.2; ENSG00000158055.17. [Q8TE85-3]
DR Ensembl; ENST00000361548.9; ENSP00000354943.5; ENSG00000158055.17. [Q8TE85-5]
DR Ensembl; ENST00000524724.6; ENSP00000431290.2; ENSG00000158055.17. [Q8TE85-3]
DR Ensembl; ENST00000528064.6; ENSP00000435130.2; ENSG00000158055.17. [Q8TE85-4]
DR Ensembl; ENST00000689444.1; ENSP00000509040.1; ENSG00000158055.17. [Q8TE85-3]
DR Ensembl; ENST00000690803.1; ENSP00000510783.1; ENSG00000158055.17. [Q8TE85-4]
DR Ensembl; ENST00000692334.1; ENSP00000509790.1; ENSG00000158055.17. [Q8TE85-4]
DR GeneID; 57822; -.
DR KEGG; hsa:57822; -.
DR MANE-Select; ENST00000361548.9; ENSP00000354943.5; NM_198173.3; NP_937816.1. [Q8TE85-5]
DR UCSC; uc001bix.3; human. [Q8TE85-1]
DR CTD; 57822; -.
DR DisGeNET; 57822; -.
DR GeneCards; GRHL3; -.
DR HGNC; HGNC:25839; GRHL3.
DR HPA; ENSG00000158055; Tissue enhanced (esophagus, skin, vagina).
DR MalaCards; GRHL3; -.
DR MIM; 606713; phenotype.
DR MIM; 608317; gene.
DR neXtProt; NX_Q8TE85; -.
DR OpenTargets; ENSG00000158055; -.
DR Orphanet; 99771; Bifid uvula.
DR Orphanet; 101023; Cleft hard palate.
DR Orphanet; 99772; Cleft velum.
DR Orphanet; 155878; Submucosal cleft palate.
DR Orphanet; 888; Van der Woude syndrome.
DR PharmGKB; PA134987320; -.
DR VEuPathDB; HostDB:ENSG00000158055; -.
DR eggNOG; KOG4091; Eukaryota.
DR GeneTree; ENSGT00940000157970; -.
DR HOGENOM; CLU_021156_1_1_1; -.
DR InParanoid; Q8TE85; -.
DR OMA; PEENICK; -.
DR OrthoDB; 286319at2759; -.
DR PhylomeDB; Q8TE85; -.
DR TreeFam; TF314132; -.
DR PathwayCommons; Q8TE85; -.
DR SignaLink; Q8TE85; -.
DR BioGRID-ORCS; 57822; 14 hits in 1098 CRISPR screens.
DR ChiTaRS; GRHL3; human.
DR GenomeRNAi; 57822; -.
DR Pharos; Q8TE85; Tbio.
DR PRO; PR:Q8TE85; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8TE85; protein.
DR Bgee; ENSG00000158055; Expressed in lower esophagus mucosa and 108 other tissues.
DR ExpressionAtlas; Q8TE85; baseline and differential.
DR Genevisible; Q8TE85; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:HGNC.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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; ISS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0007398; P:ectoderm development; IEA:Ensembl.
DR GO; GO:0008544; P:epidermis development; ISS:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
DR GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:HGNC.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR InterPro; IPR007604; CP2.
DR Pfam; PF04516; CP2; 1.
DR PROSITE; PS51968; GRH_CP2_DB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..626
FT /note="Grainyhead-like protein 3 homolog"
FT /id="PRO_0000227997"
FT DOMAIN 226..460
FT /note="Grh/CP2 DB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01313"
FT REGION 30..95
FT /note="Transcription activation"
FT /evidence="ECO:0000269|PubMed:12549979"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12549979"
FT /id="VSP_017643"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017644"
FT VAR_SEQ 1..6
FT /note="MSNELD -> MWMNSILPIFL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12549979"
FT /id="VSP_017645"
FT VAR_SEQ 566..626
FT /note="ETSLLHPRLSRHPPPDCLECSHPVTQVRNMGFGDGFWRQRDLDSNPSPTTVN
FT SLHFTVNSE -> ILVNMDNNIIQHYSNHVAFLLDMGELDGKIQIILKEL (in
FT isoform 2, isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12549979,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_017646"
FT VARIANT 55
FT /note="D -> E (in dbSNP:rs2486668)"
FT /id="VAR_027907"
FT VARIANT 160
FT /note="V -> A (in dbSNP:rs34637004)"
FT /id="VAR_055881"
FT VARIANT 298
FT /note="R -> H (in VWS2; dbSNP:rs752673677)"
FT /evidence="ECO:0000269|PubMed:24360809"
FT /id="VAR_072616"
FT VARIANT 391
FT /note="R -> C (in VWS2; dbSNP:rs879255245)"
FT /evidence="ECO:0000269|PubMed:24360809"
FT /id="VAR_072617"
FT VARIANT 520
FT /note="R -> Q (in VWS2; dbSNP:rs946439477)"
FT /evidence="ECO:0000269|PubMed:24360809"
FT /id="VAR_072618"
FT CONFLICT 20
FT /note="L -> S (in Ref. 2; BAB85067)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="I -> V (in Ref. 2; BAG37608)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="K -> R (in Ref. 2; BAB85067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 70345 MW; 225C0E2049FF0CE6 CRC64;
MSNELDFRSV RLLKNDPVNL QKFSYTSEDE AWKTYLENPL TAATKAMMRV NGDDDSVAAL
SFLYDYYMGP KEKRILSSST GGRNDQGKRY YHGMEYETDL TPLESPTHLM KFLTENVSGT
PEYPDLLKKN NLMSLEGALP TPGKAAPLPA GPSKLEAGSV DSYLLPTTDM YDNGSLNSLF
ESIHGVPPTQ RWQPDSTFKD DPQESMLFPD ILKTSPEPPC PEDYPSLKSD FEYTLGSPKA
IHIKSGESPM AYLNKGQFYP VTLRTPAGGK GLALSSNKVK SVVMVVFDNE KVPVEQLRFW
KHWHSRQPTA KQRVIDVADC KENFNTVEHI EEVAYNALSF VWNVNEEAKV FIGVNCLSTD
FSSQKGVKGV PLNLQIDTYD CGLGTERLVH RAVCQIKIFC DKGAERKMRD DERKQFRRKV
KCPDSSNSGV KGCLLSGFRG NETTYLRPET DLETPPVLFI PNVHFSSLQR SGGAAPSAGP
SSSNRLPLKR TCSPFTEEFE PLPSKQAKEG DLQRVLLYVR RETEEVFDAL MLKTPDLKGL
RNAISEKYGF PEENIYKVYK KCKRGETSLL HPRLSRHPPP DCLECSHPVT QVRNMGFGDG
FWRQRDLDSN PSPTTVNSLH FTVNSE
