GMFB_MOUSE
ID GMFB_MOUSE Reviewed; 142 AA.
AC Q9CQI3; Q3UQX5; Q9ERL8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Glia maturation factor beta;
DE Short=GMF-beta;
GN Name=Gmfb;
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=Telencephalon;
RX PubMed=11435704; DOI=10.1159/000056919;
RA Bourgeois F., Guimiot F., Mas C., Bulfone A., Levacher B., Moalic J.M.,
RA Simonneau M.;
RT "Identification and isolation of a full-length clone of mouse GMFB (Gmfb),
RT a putative intracellular kinase regulator, differentially expressed in
RT telencephalon.";
RL Cytogenet. Cell Genet. 92:304-309(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12697657; DOI=10.1093/intimm/dxg056;
RA Utsuyama M., Shiraishi J., Takahashi H., Kasai M., Hirokawa K.;
RT "Glia maturation factor produced by thymic epithelial cells plays a role in
RT T cell differentiation in the thymic microenvironment.";
RL Int. Immunol. 15:557-564(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Eye;
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].
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 1-139.
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).
CC -!- FUNCTION: This protein causes differentiation of brain cells,
CC stimulation of neural regeneration, and inhibition of proliferation of
CC tumor cells. {ECO:0000250}.
CC -!- PTM: Phosphorylated; stimulated by phorbol ester. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. GMF
CC subfamily. {ECO:0000305}.
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DR EMBL; AF297220; AAG22803.1; -; mRNA.
DR EMBL; AB050013; BAB41099.1; -; mRNA.
DR EMBL; AK013947; BAB29076.1; -; mRNA.
DR EMBL; AK013970; BAB29092.1; -; mRNA.
DR EMBL; AK142014; BAE24913.1; -; mRNA.
DR EMBL; BC040233; AAH40233.1; -; mRNA.
DR CCDS; CCDS36898.1; -.
DR RefSeq; NP_071306.2; NM_022023.2.
DR PDB; 1V6F; NMR; -; A=2-139.
DR PDBsum; 1V6F; -.
DR AlphaFoldDB; Q9CQI3; -.
DR SMR; Q9CQI3; -.
DR BioGRID; 211011; 7.
DR IntAct; Q9CQI3; 2.
DR STRING; 10090.ENSMUSP00000107448; -.
DR iPTMnet; Q9CQI3; -.
DR PhosphoSitePlus; Q9CQI3; -.
DR SwissPalm; Q9CQI3; -.
DR EPD; Q9CQI3; -.
DR jPOST; Q9CQI3; -.
DR MaxQB; Q9CQI3; -.
DR PaxDb; Q9CQI3; -.
DR PRIDE; Q9CQI3; -.
DR ProteomicsDB; 271404; -.
DR Antibodypedia; 23938; 250 antibodies from 30 providers.
DR DNASU; 63985; -.
DR Ensembl; ENSMUST00000079314; ENSMUSP00000078293; ENSMUSG00000062014.
DR Ensembl; ENSMUST00000111817; ENSMUSP00000107448; ENSMUSG00000062014.
DR GeneID; 63985; -.
DR KEGG; mmu:63985; -.
DR UCSC; uc007thh.2; mouse.
DR CTD; 2764; -.
DR MGI; MGI:1927133; Gmfb.
DR VEuPathDB; HostDB:ENSMUSG00000062014; -.
DR eggNOG; KOG1736; Eukaryota.
DR GeneTree; ENSGT00390000008920; -.
DR HOGENOM; CLU_087056_1_0_1; -.
DR InParanoid; Q9CQI3; -.
DR OMA; PFIVYSY; -.
DR OrthoDB; 1477747at2759; -.
DR PhylomeDB; Q9CQI3; -.
DR TreeFam; TF315147; -.
DR BioGRID-ORCS; 63985; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Gmfb; mouse.
DR EvolutionaryTrace; Q9CQI3; -.
DR PRO; PR:Q9CQI3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CQI3; protein.
DR Bgee; ENSMUSG00000062014; Expressed in otic placode and 247 other tissues.
DR ExpressionAtlas; Q9CQI3; baseline and differential.
DR Genevisible; Q9CQI3; MM.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0071846; P:actin filament debranching; IBA:GO_Central.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
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 PANTHER; PTHR11249; PTHR11249; 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; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P60984"
FT CHAIN 2..142
FT /note="Glia maturation factor beta"
FT /id="PRO_0000214944"
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:P60984"
FT CONFLICT 40
FT /note="E -> K (in Ref. 1; AAG22803)"
FT /evidence="ECO:0000305"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:1V6F"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1V6F"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1V6F"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:1V6F"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1V6F"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1V6F"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1V6F"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1V6F"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1V6F"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:1V6F"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:1V6F"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1V6F"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:1V6F"
SQ SEQUENCE 142 AA; 16723 MW; 89D0E02A826247C6 CRC64;
MSESLVVCDV AEDLVEKLRK FRFRKETHNA AIIMKIDKDE RLVVLDEELE GVSPDELKDE
LPERQPRFIV YSYKYQHDDG RVSYPLCFIF SSPVGCKPEQ QMMYAGSKNK LVQTAELTKV
FEIRNTEDLT EEWLREKLGF FH
