GCM2_MOUSE
ID GCM2_MOUSE Reviewed; 504 AA.
AC O09102; Q2TB03; Q9QWX7; Q9Z289;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Chorion-specific transcription factor GCMb;
DE Short=mGCMb {ECO:0000303|PubMed:8962155};
DE AltName: Full=GCM motif protein 2;
DE AltName: Full=Glial cells missing homolog 2;
GN Name=Gcm2 {ECO:0000312|MGI:MGI:1861438}; Synonyms=Gcmb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8962155; DOI=10.1073/pnas.93.25.14912;
RA Akiyama Y., Hosoya T., Poole A.M., Hotta Y.;
RT "The gcm-motif: a novel DNA binding motif conserved in Drosophila and
RT mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14912-14916(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvEv, and C57BL/6J;
RX PubMed=9770492; DOI=10.1073/pnas.95.21.12364;
RA Kim J., Jones B.W., Zock C., Chen Z., Wang H., Goodman C.S., Anderson D.J.;
RT "Isolation and characterization of mammalian homologs of the Drosophila
RT gene glial cells missing.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12364-12369(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Transcription factor that binds specific sequences on gene
CC promoters and activate their transcription. Through the regulation of
CC gene transcription, may play a role in parathyroid gland development.
CC {ECO:0000250|UniProtKB:O75603}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75603}.
CC -!- DOMAIN: The C-terminal conserved inhibitory domain (CCID) negatively
CC regulates the transcriptional activity of the protein.
CC {ECO:0000250|UniProtKB:O75603}.
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DR EMBL; D88611; BAA13649.1; -; mRNA.
DR EMBL; AF081556; AAC64782.1; -; mRNA.
DR EMBL; AF081558; AAC64784.1; -; Genomic_DNA.
DR EMBL; BC110631; AAI10632.1; -; mRNA.
DR EMBL; BC110632; AAI10633.1; -; mRNA.
DR CCDS; CCDS26472.1; -.
DR RefSeq; NP_032130.2; NM_008104.2.
DR AlphaFoldDB; O09102; -.
DR SMR; O09102; -.
DR STRING; 10090.ENSMUSP00000021791; -.
DR PhosphoSitePlus; O09102; -.
DR PaxDb; O09102; -.
DR PRIDE; O09102; -.
DR DNASU; 107889; -.
DR GeneID; 107889; -.
DR KEGG; mmu:107889; -.
DR UCSC; uc007qey.1; mouse.
DR CTD; 9247; -.
DR MGI; MGI:1861438; Gcm2.
DR eggNOG; ENOG502QU2X; Eukaryota.
DR InParanoid; O09102; -.
DR OrthoDB; 396012at2759; -.
DR PhylomeDB; O09102; -.
DR TreeFam; TF324146; -.
DR BioGRID-ORCS; 107889; 4 hits in 72 CRISPR screens.
DR PRO; PR:O09102; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O09102; protein.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; ISS:UniProtKB.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0002067; P:glandular epithelial cell differentiation; IMP:MGI.
DR GO; GO:0042063; P:gliogenesis; IBA:GO_Central.
DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:0060017; P:parathyroid gland development; IMP: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; ISS:UniProtKB.
DR Gene3D; 2.20.25.670; -; 1.
DR Gene3D; 3.30.70.3530; -; 1.
DR InterPro; IPR039791; GCM.
DR InterPro; IPR036115; GCM_dom_sf.
DR InterPro; IPR043020; GCM_large.
DR InterPro; IPR043021; GCM_small.
DR InterPro; IPR003902; Tscrpt_reg_GCM.
DR PANTHER; PTHR12414; PTHR12414; 1.
DR Pfam; PF03615; GCM; 1.
DR SUPFAM; SSF90073; SSF90073; 1.
DR PROSITE; PS50807; GCM; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..504
FT /note="Chorion-specific transcription factor GCMb"
FT /id="PRO_0000126651"
FT DNA_BIND 19..174
FT /note="GCM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00245"
FT REGION 155..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..393
FT /note="C-terminal conserved inhibitory domain (CCID)"
FT /evidence="ECO:0000250|UniProtKB:O75603"
FT REGION 438..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00245"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00245"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00245"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00245"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00245"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00245"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00245"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00245"
FT CONFLICT 159
FT /note="H -> R (in Ref. 1; BAA13649)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="E -> G (in Ref. 2; AAC64782)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="H -> Y (in Ref. 2; AAC64782)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="V -> E (in Ref. 2; AAC64782)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="S -> L (in Ref. 2; AAC64782)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="T -> S (in Ref. 2; AAC64782)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="S -> G (in Ref. 2; AAC64782)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="Q -> R (in Ref. 1; BAA13649)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="A -> V (in Ref. 2; AAC64782)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="N -> D (in Ref. 1; BAA13649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 56039 MW; 2EBC3CFD8A120425 CRC64;
MPADSTQDED AVLSYGMKLT WDINDPQMPQ EPTHFDHFRE WPDGYVRFIY SSQEKKAQRH
LSGWAMRNTN NHNGHILKKS CLGVVVCARA CALKDGSHLQ LRPAICDKAR LKQQKKACPN
CHSPLELVPC RGHSGYPVTN FWRLDGNAIF FQAKGVHDHP RPESKSETEG RRSALKRQMA
SFYQPQKRRS EEPEARSTQD IRGHLNSTAA LEPTELFDMT ADTSFPIPGQ PSPSFPNSDV
HRVTCDLPTF QGDIILPFQK YPNPSIYFPG PPWGYELASS GVTGSSPYST LYKDSSVVPD
DPDWIPLNSL QYNVSSYGSY ERTLDFTARY HSWKPTHGKP SLEEKVDCEQ CQAVPTSPYY
NLELPCRYLP VPAAGTQALQ TVITTTVAYQ AYQHPALKHS DSMQEVSSLA SCTYASENLP
MPIYPPALDP QEGVIQAASP SGRAPLKVPG DCQAPRPTLD FPQEADPSGT DGADVWDVCL
SGVGSVMGYL DRTGQPFSFD NEDF
