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   24-JAN-2024, entry version 170.
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; 15.
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; 9606-ENSP00000472249; -.
DR   PeptideAtlas; O60234; -.
DR   ProteomicsDB; 49260; -.
DR   Pumba; O60234; -.
DR   TopDownProteomics; O60234; -.
DR   Antibodypedia; 16749; 239 antibodies from 27 providers.
DR   DNASU; 9535; -.
DR   Ensembl; ENST00000597595.6; ENSP00000472249.1; ENSG00000130755.13.
DR   Ensembl; ENST00000709032.1; ENSP00000517472.1; ENSG00000291873.1.
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   AGR; HGNC:4374; -.
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; 21121at2759; -.
DR   PhylomeDB; O60234; -.
DR   TreeFam; TF315147; -.
DR   PathwayCommons; O60234; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; O60234; -.
DR   SIGNOR; O60234; -.
DR   BioGRID-ORCS; 9535; 25 hits in 1151 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 161 other cell types or tissues.
DR   ExpressionAtlas; O60234; baseline and differential.
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   CDD; cd11283; ADF_GMF-beta_like; 1.
DR   Gene3D; 3.40.20.10; Severin; 1.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR011171; GMF.
DR   PANTHER; PTHR11249:SF4; GLIA MATURATION FACTOR GAMMA; 1.
DR   PANTHER; PTHR11249; GLIAL FACTOR NATURATION FACTOR; 1.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   PIRSF; PIRSF001788; GMF-beta; 1.
DR   SMART; SM00102; ADF; 1.
DR   SUPFAM; SSF55753; Actin depolymerizing proteins; 1.
DR   PROSITE; PS51263; ADF_H; 1.
DR   Genevisible; O60234; HS.
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
//