GMFB_RAT
ID GMFB_RAT Reviewed; 142 AA.
AC Q63228;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Glia maturation factor beta;
DE Short=GMF-beta;
GN Name=Gmfb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8436977; DOI=10.1111/j.1471-4159.1993.tb03237.x;
RA Zaheer A., Fink B.D., Lim R.;
RT "Expression of glia maturation factor beta mRNA and protein in rat organs
RT and cells.";
RL J. Neurochem. 60:914-920(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP PROTEIN SEQUENCE OF 42-64, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
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; Z11558; CAA77650.1; -; mRNA.
DR EMBL; BC081778; AAH81778.1; -; mRNA.
DR PIR; S22149; S22149.
DR RefSeq; NP_112294.1; NM_031032.2.
DR AlphaFoldDB; Q63228; -.
DR SMR; Q63228; -.
DR BioGRID; 249561; 3.
DR IntAct; Q63228; 1.
DR MINT; Q63228; -.
DR STRING; 10116.ENSRNOP00000067695; -.
DR iPTMnet; Q63228; -.
DR PhosphoSitePlus; Q63228; -.
DR SwissPalm; Q63228; -.
DR jPOST; Q63228; -.
DR PaxDb; Q63228; -.
DR PRIDE; Q63228; -.
DR Ensembl; ENSRNOT00000101993; ENSRNOP00000089942; ENSRNOG00000064480.
DR GeneID; 81661; -.
DR KEGG; rno:81661; -.
DR UCSC; RGD:70910; rat.
DR CTD; 2764; -.
DR RGD; 70910; Gmfb.
DR eggNOG; KOG1736; Eukaryota.
DR GeneTree; ENSGT00390000008920; -.
DR InParanoid; Q63228; -.
DR OrthoDB; 1477747at2759; -.
DR PRO; PR:Q63228; -.
DR Proteomes; UP000002494; Chromosome 15.
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; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
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 Acetylation; Direct protein sequencing; Growth factor; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..142
FT /note="Glia maturation factor beta"
FT /id="PRO_0000214946"
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:0000269|Ref.4"
SQ SEQUENCE 142 AA; 16736 MW; A36B8D8D82B44F6C CRC64;
MSESLVVCDV AEDLVEKLRK FRFRKETHNA AIIMKIDKDK RLVVLDEELE GVSPDELKDE
LPERQPRFIV YSYKYQHDDG RVSYPLCFIF SSPLGCKPEQ QMMYAGSKNK LVQTAELTKV
FEIRNTEDLT EEWLREKLGF FH