GMFG_HUMAN
ID GMFG_HUMAN Reviewed; 142 AA.
AC O60234; Q6IB37;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Glia maturation factor gamma;
DE Short=GMF-gamma;
GN Name=GMFG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9545571; DOI=10.1016/s0167-4781(97)00222-4;
RA Asai K., Fujita K., Yamamoto M., Hotta T., Morikawa M., Kokubo M.,
RA Moriyama A., Kato T.;
RT "Isolation of novel human cDNA (hGMF-gamma) homologous to glia maturation
RT factor-beta gene.";
RL Biochim. Biophys. Acta 1396:242-244(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10541589; DOI=10.1007/s100480050077;
RA Peters N., Smith J.S., Tachibana I., Lee H.K., Pohl U., Portier B.P.,
RA Louis D.N., Jenkins R.B.;
RT "The human glia maturation factor-gamma gene: genomic structure and
RT mutation analysis in gliomas with chromosome 19q loss.";
RL Neurogenetics 2:163-166(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Lymph;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 7-140.
RG Structural genomics consortium (SGC);
RT "The crystal structure of human glia maturation factor, gamma (GMFG).";
RL Submitted (FEB-2010) to the PDB data bank.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in lung, heart and
CC placenta.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. GMF
CC subfamily. {ECO:0000305}.
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DR EMBL; AB001993; BAA25572.1; -; mRNA.
DR EMBL; AF108027; AAD27807.1; -; Genomic_DNA.
DR EMBL; AF108022; AAD27807.1; JOINED; Genomic_DNA.
DR EMBL; AF108023; AAD27807.1; JOINED; Genomic_DNA.
DR EMBL; AF108024; AAD27807.1; JOINED; Genomic_DNA.
DR EMBL; AF108025; AAD27807.1; JOINED; Genomic_DNA.
DR EMBL; AF108026; AAD27807.1; JOINED; Genomic_DNA.
DR EMBL; AF038956; AAC39870.1; -; mRNA.
DR EMBL; CR456967; CAG33248.1; -; mRNA.
DR EMBL; CR542114; CAG46911.1; -; mRNA.
DR EMBL; CH471126; EAW56874.1; -; Genomic_DNA.
DR EMBL; BC032819; AAH32819.2; -; mRNA.
DR EMBL; BC080180; AAH80180.1; -; mRNA.
DR EMBL; BC093799; AAH93799.1; -; mRNA.
DR EMBL; BC101818; AAI01819.1; -; mRNA.
DR EMBL; BC143543; AAI43544.1; -; mRNA.
DR EMBL; BC143546; AAI43547.1; -; mRNA.
DR EMBL; BC143548; AAI43549.1; -; mRNA.
DR CCDS; CCDS12532.1; -.
DR RefSeq; NP_001287937.1; NM_001301008.1.
DR RefSeq; NP_004868.1; NM_004877.3.
DR PDB; 3L50; X-ray; 1.90 A; A/B=7-140.
DR PDBsum; 3L50; -.
DR AlphaFoldDB; O60234; -.
DR SMR; O60234; -.
DR BioGRID; 114911; 14.
DR IntAct; O60234; 7.
DR STRING; 9606.ENSP00000472249; -.
DR iPTMnet; O60234; -.
DR MetOSite; O60234; -.
DR PhosphoSitePlus; O60234; -.
DR BioMuta; GMFG; -.
DR OGP; O60234; -.
DR EPD; O60234; -.
DR jPOST; O60234; -.
DR MassIVE; O60234; -.
DR PaxDb; O60234; -.
DR PeptideAtlas; O60234; -.
DR PRIDE; O60234; -.
DR ProteomicsDB; 49260; -.
DR TopDownProteomics; O60234; -.
DR Antibodypedia; 16749; 223 antibodies from 27 providers.
DR DNASU; 9535; -.
DR Ensembl; ENST00000597595.6; ENSP00000472249.1; ENSG00000130755.13.
DR GeneID; 9535; -.
DR KEGG; hsa:9535; -.
DR MANE-Select; ENST00000597595.6; ENSP00000472249.1; NM_004877.4; NP_004868.1.
DR UCSC; uc002okz.5; human.
DR CTD; 9535; -.
DR DisGeNET; 9535; -.
DR GeneCards; GMFG; -.
DR HGNC; HGNC:4374; GMFG.
DR HPA; ENSG00000130755; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 604104; gene.
DR neXtProt; NX_O60234; -.
DR OpenTargets; ENSG00000130755; -.
DR PharmGKB; PA28759; -.
DR VEuPathDB; HostDB:ENSG00000130755; -.
DR eggNOG; KOG1736; Eukaryota.
DR GeneTree; ENSGT00390000008920; -.
DR HOGENOM; CLU_087056_1_0_1; -.
DR InParanoid; O60234; -.
DR OMA; EWKMLYA; -.
DR OrthoDB; 1477747at2759; -.
DR PhylomeDB; O60234; -.
DR TreeFam; TF315147; -.
DR PathwayCommons; O60234; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O60234; -.
DR BioGRID-ORCS; 9535; 24 hits in 1074 CRISPR screens.
DR ChiTaRS; GMFG; human.
DR EvolutionaryTrace; O60234; -.
DR GenomeRNAi; 9535; -.
DR Pharos; O60234; Tbio.
DR PRO; PR:O60234; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O60234; protein.
DR Bgee; ENSG00000130755; Expressed in monocyte and 159 other tissues.
DR ExpressionAtlas; O60234; baseline and differential.
DR Genevisible; O60234; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004860; F:protein kinase inhibitor activity; TAS:ProtInc.
DR GO; GO:0071846; P:actin filament debranching; IBA:GO_Central.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
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:0007744|PubMed:25944712"
FT CHAIN 2..142
FT /note="Glia maturation factor gamma"
FT /id="PRO_0000214947"
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:0007744|PubMed:25944712"
FT VARIANT 122
FT /note="E -> K (in dbSNP:rs36110047)"
FT /id="VAR_048196"
FT VARIANT 136
FT /note="E -> K (in dbSNP:rs34035414)"
FT /id="VAR_048197"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:3L50"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3L50"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:3L50"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:3L50"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:3L50"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3L50"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3L50"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3L50"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:3L50"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:3L50"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3L50"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:3L50"
SQ SEQUENCE 142 AA; 16801 MW; DB64BD8DE4F88170 CRC64;
MSDSLVVCEV DPELTEKLRK FRFRKETDNA AIIMKVDKDR QMVVLEEEFQ NISPEELKME
LPERQPRFVV YSYKYVHDDG RVSYPLCFIF SSPVGCKPEQ QMMYAGSKNR LVQTAELTKV
FEIRTTDDLT EAWLQEKLSF FR
