GCM1_MOUSE
ID GCM1_MOUSE Reviewed; 436 AA.
AC P70348; O09103;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Chorion-specific transcription factor GCMa;
DE AltName: Full=GCM motif protein 1;
DE Short=mGCM1;
DE Short=mGCMa;
DE AltName: Full=Glial cells missing homolog 1;
GN Name=Gcm1; Synonyms=Gcma;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=8814290; DOI=10.1016/0014-5793(96)00890-3;
RA Altshuller Y., Copeland N.G., Gilbert D.J., Jenkins N.A., Frohman M.A.;
RT "Gcm1, a mammalian homolog of Drosophila glial cells missing.";
RL FEBS Lett. 393:201-204(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-174 IN COMPLEX WITH DNA AND
RP ZINC IONS, AND MUTAGENESIS OF ASN-63; ASN-65; LYS-74; CYS-76; CYS-82;
RP CYS-113; CYS-125; HIS-152 AND HIS-154.
RX PubMed=12682016; DOI=10.1093/emboj/cdg182;
RA Cohen S.X., Moulin M., Hashemolhosseini S., Kilian K., Wegner M.,
RA Mueller C.W.;
RT "Structure of the GCM domain-DNA complex: a DNA-binding domain with a novel
RT fold and mode of target site recognition.";
RL EMBO J. 22:1835-1845(2003).
CC -!- FUNCTION: Transcription factor that is necessary for placental
CC development (PubMed:8962155). Involved in the control of expression of
CC placental growth factor (PGF) and other placenta-specific genes. Binds
CC to the trophoblast-specific element 2 (TSE2) of the aromatase gene
CC enhancer. Binds to the SYDE1 promoter. Has a central role in mediating
CC the differentiation of trophoblast cells along both the villous and
CC extravillous pathways in placental development (By similarity).
CC {ECO:0000250|UniProtKB:Q9NP62, ECO:0000269|PubMed:8962155}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00245}.
CC -!- TISSUE SPECIFICITY: Placenta specific. {ECO:0000269|PubMed:8814290}.
CC -!- PTM: Polyubiquitinated in the presence of UBE2D2 and FBXW2 (in vitro).
CC {ECO:0000250}.
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DR EMBL; U59876; AAC52822.1; -; mRNA.
DR EMBL; D88612; BAA13650.1; -; mRNA.
DR EMBL; BC066866; AAH66866.1; -; mRNA.
DR CCDS; CCDS23356.1; -.
DR PIR; S74257; S74257.
DR RefSeq; NP_032129.2; NM_008103.3.
DR PDB; 1ODH; X-ray; 2.85 A; A=1-174.
DR PDBsum; 1ODH; -.
DR AlphaFoldDB; P70348; -.
DR SMR; P70348; -.
DR STRING; 10090.ENSMUSP00000024104; -.
DR iPTMnet; P70348; -.
DR PhosphoSitePlus; P70348; -.
DR PaxDb; P70348; -.
DR PRIDE; P70348; -.
DR Antibodypedia; 17251; 318 antibodies from 31 providers.
DR DNASU; 14531; -.
DR Ensembl; ENSMUST00000024104; ENSMUSP00000024104; ENSMUSG00000023333.
DR GeneID; 14531; -.
DR KEGG; mmu:14531; -.
DR UCSC; uc009qto.1; mouse.
DR CTD; 8521; -.
DR MGI; MGI:108045; Gcm1.
DR VEuPathDB; HostDB:ENSMUSG00000023333; -.
DR eggNOG; ENOG502QWH2; Eukaryota.
DR GeneTree; ENSGT00390000006777; -.
DR HOGENOM; CLU_043105_0_0_1; -.
DR InParanoid; P70348; -.
DR OMA; FPLTNWP; -.
DR OrthoDB; 396012at2759; -.
DR PhylomeDB; P70348; -.
DR TreeFam; TF324146; -.
DR BioGRID-ORCS; 14531; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Gcm1; mouse.
DR EvolutionaryTrace; P70348; -.
DR PRO; PR:P70348; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P70348; protein.
DR Bgee; ENSMUSG00000023333; Expressed in trophectoderm and 10 other tissues.
DR ExpressionAtlas; P70348; baseline and differential.
DR Genevisible; P70348; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IDA:MGI.
DR GO; GO:0060018; P:astrocyte fate commitment; IDA:MGI.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IMP:MGI.
DR GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IMP:MGI.
DR GO; GO:0042063; P:gliogenesis; IBA:GO_Central.
DR GO; GO:0060143; P:positive regulation of syncytium formation by plasma membrane fusion; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0060800; P:regulation of cell differentiation involved in embryonic placenta development; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0000768; P:syncytium formation by plasma membrane fusion; IGI:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc.
FT CHAIN 1..436
FT /note="Chorion-specific transcription factor GCMa"
FT /id="PRO_0000126648"
FT DNA_BIND 14..169
FT /note="GCM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00245"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT MUTAGEN 63
FT /note="N->A: No effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:12682016"
FT MUTAGEN 63
FT /note="N->Q: Slight decrease of DNA binding."
FT /evidence="ECO:0000269|PubMed:12682016"
FT MUTAGEN 65
FT /note="N->A: Strong decrease of DNA binding."
FT /evidence="ECO:0000269|PubMed:12682016"
FT MUTAGEN 65
FT /note="N->D: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:12682016"
FT MUTAGEN 74
FT /note="K->A,L,M: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:12682016"
FT MUTAGEN 76
FT /note="C->A: Loss of transcription activation."
FT /evidence="ECO:0000269|PubMed:12682016"
FT MUTAGEN 82
FT /note="C->A: Loss of transcription activation."
FT /evidence="ECO:0000269|PubMed:12682016"
FT MUTAGEN 113
FT /note="C->A: Loss of transcription activation."
FT /evidence="ECO:0000269|PubMed:12682016"
FT MUTAGEN 125
FT /note="C->A: Loss of transcription activation."
FT /evidence="ECO:0000269|PubMed:12682016"
FT MUTAGEN 152
FT /note="H->A: Loss of transcription activation."
FT /evidence="ECO:0000269|PubMed:12682016"
FT MUTAGEN 154
FT /note="H->A: Loss of transcription activation."
FT /evidence="ECO:0000269|PubMed:12682016"
FT CONFLICT 211
FT /note="G -> S (in Ref. 2; BAA13650)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="N -> K (in Ref. 2; BAA13650)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="S -> N (in Ref. 2; BAA13650)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="D -> E (in Ref. 2; BAA13650)"
FT /evidence="ECO:0000305"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1ODH"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1ODH"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1ODH"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1ODH"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1ODH"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:1ODH"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1ODH"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1ODH"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1ODH"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:1ODH"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:1ODH"
SQ SEQUENCE 436 AA; 49589 MW; 99F4E441800582DB CRC64;
MELDDFDPED KEILSWDIND VKLPQNVKTT DWFQEWPDSY VKHIYSSDDR NAQRHLSSWA
MRNTNNHNSR ILKKSCLGVV VCSRDCSTEE GRKIYLRPAI CDKARQKQQR KSCPNCNGPL
KLIPCRGHGG FPVTNFWRHD GRFIFFQSKG EHDHPRPETK LEAEARRAMK KVHMASASNS
LRMKGRPAAK ALPAEIPSQG SLPLTWSFQE GVQLPGTYST PLIANAPQQN SLNDCLSFPK
SYDLGGSTEL EDPTSTLDSM KFYERCKFSS SRIYGSEEQF QPPVPGTYGD YEDLQTWNKN
VALGRNPSDD IYYPAYPLPV ASWPYDYFPS QNSLEHLPQQ VPSEPPAAQP GCHPLWSNPG
GEPYEEKVSV DLSSYVPSLT YHPPQQDPFL LTYGSPTQQQ HALPGKSNRW DFDEEMACMG
LDHFNNEMLL NFCSLR
