GMFG_MOUSE
ID GMFG_MOUSE Reviewed; 142 AA.
AC Q9ERL7;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glia maturation factor gamma;
DE Short=GMF-gamma;
GN Name=Gmfg;
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 STRAIN=Swiss/IOPS OF1; TISSUE=Liver;
RA Bourgeois F., Guimiot F., Levacher B., Mas C., Simonneau M.J.;
RT "Identification and full-length cloning of GMFB, a putative intracellular
RT kinase regulator, expressed in proliferating telencephalon stem cells.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Inoue Y., Asai K., Yamamoto M., Morikawa M., Iida J., Kishimoto T.,
RA Yamamoto N., Kawai Y.;
RT "Structure of the mouse glia maturation factor-gamma gene and its
RT promoter.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP STRUCTURE BY NMR OF 2-139.
RX PubMed=19768801; DOI=10.1002/pro.248;
RA Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Sato M., Inoue M.,
RA Watanabe S., Hayashizaki Y., Tanaka A., Kigawa T., Yokoyama S.;
RT "NMR solution structures of actin depolymerizing factor homology domains.";
RL Protein Sci. 18:2384-2392(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of glia maturation factor-gamma (GMFG) from Mus musculus
RT at 1.50 A resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. GMF
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF297221; AAG22804.1; -; mRNA.
DR EMBL; AB097120; BAC76941.1; -; Genomic_DNA.
DR EMBL; AK002834; BAB22392.1; -; mRNA.
DR EMBL; AK009967; BAB26617.1; -; mRNA.
DR EMBL; AK014214; BAB29210.1; -; mRNA.
DR EMBL; BC011488; AAH11488.1; -; mRNA.
DR CCDS; CCDS39859.1; -.
DR CCDS; CCDS39860.1; -.
DR RefSeq; NP_001034281.1; NM_001039192.1.
DR RefSeq; NP_071307.1; NM_022024.2.
DR PDB; 1VKK; X-ray; 1.35 A; A=1-142.
DR PDB; 1WFS; NMR; -; A=2-139.
DR PDB; 4JD2; X-ray; 3.08 A; H=1-142.
DR PDBsum; 1VKK; -.
DR PDBsum; 1WFS; -.
DR PDBsum; 4JD2; -.
DR AlphaFoldDB; Q9ERL7; -.
DR BMRB; Q9ERL7; -.
DR SMR; Q9ERL7; -.
DR BioGRID; 211012; 4.
DR DIP; DIP-60543N; -.
DR IntAct; Q9ERL7; 2.
DR STRING; 10090.ENSMUSP00000103927; -.
DR iPTMnet; Q9ERL7; -.
DR PhosphoSitePlus; Q9ERL7; -.
DR EPD; Q9ERL7; -.
DR MaxQB; Q9ERL7; -.
DR PaxDb; Q9ERL7; -.
DR PRIDE; Q9ERL7; -.
DR ProteomicsDB; 267732; -.
DR Antibodypedia; 16749; 223 antibodies from 27 providers.
DR DNASU; 63986; -.
DR Ensembl; ENSMUST00000078845; ENSMUSP00000077889; ENSMUSG00000060791.
DR Ensembl; ENSMUST00000108292; ENSMUSP00000103927; ENSMUSG00000060791.
DR GeneID; 63986; -.
DR KEGG; mmu:63986; -.
DR UCSC; uc009fyx.1; mouse.
DR CTD; 9535; -.
DR MGI; MGI:1927135; Gmfg.
DR VEuPathDB; HostDB:ENSMUSG00000060791; -.
DR eggNOG; KOG1736; Eukaryota.
DR GeneTree; ENSGT00390000008920; -.
DR HOGENOM; CLU_087056_1_0_1; -.
DR InParanoid; Q9ERL7; -.
DR OMA; AIISECH; -.
DR OrthoDB; 1477747at2759; -.
DR PhylomeDB; Q9ERL7; -.
DR TreeFam; TF315147; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 63986; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Gmfg; mouse.
DR EvolutionaryTrace; Q9ERL7; -.
DR PRO; PR:Q9ERL7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9ERL7; protein.
DR Bgee; ENSMUSG00000060791; Expressed in granulocyte and 70 other tissues.
DR ExpressionAtlas; Q9ERL7; baseline and differential.
DR Genevisible; Q9ERL7; MM.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0071933; F:Arp2/3 complex binding; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0071846; P:actin filament debranching; IDA:MGI.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:MGI.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IEA:InterPro.
DR CDD; cd11283; ADF_GMF-beta_like; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR011171; GMF.
DR InterPro; IPR030076; GMFG.
DR PANTHER; PTHR11249; PTHR11249; 1.
DR PANTHER; PTHR11249:SF4; PTHR11249:SF4; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR PIRSF; PIRSF001788; GMF-beta; 1.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Growth factor; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60234"
FT CHAIN 2..142
FT /note="Glia maturation factor gamma"
FT /id="PRO_0000214948"
FT DOMAIN 4..139
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O60234"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:4JD2"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:1VKK"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1VKK"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:1VKK"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:1VKK"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:1VKK"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1VKK"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1VKK"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:4JD2"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1VKK"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4JD2"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:1VKK"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:1VKK"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1VKK"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:1VKK"
SQ SEQUENCE 142 AA; 16748 MW; 25367F2B49378710 CRC64;
MSDSLVVCEV DPELKETLRK FRFRKETNNA AIIMKVDKDR QMVVLEDELQ NISPEELKLE
LPERQPRFVV YSYKYVHDDG RVSYPLCFIF SSPVGCKPEQ QMMYAGSKNR LVQTAELTKV
FEIRTTDDLT ETWLKEKLAF FR
