CAPG_MOUSE
ID CAPG_MOUSE Reviewed; 352 AA.
AC P24452;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Macrophage-capping protein;
DE AltName: Full=Actin regulatory protein CAP-G;
DE AltName: Full=Actin-capping protein GCAP39 {ECO:0000303|PubMed:8293478};
DE AltName: Full=Myc basic motif homolog 1;
GN Name=Capg; Synonyms=Mbh1;
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=NIH Swiss;
RX PubMed=1849072; DOI=10.1002/j.1460-2075.1991.tb08007.x;
RA Prendergast G.C., Ziff E.B.;
RT "Mbh 1: a novel gelsolin/severin-related protein which binds actin in vitro
RT and exhibits nuclear localization in vivo.";
RL EMBO J. 10:757-766(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2255912; DOI=10.1126/science.2255912;
RA Yu F.-X., Johnston P.A., Suedhof T.C., Yin H.L.;
RT "gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping
RT protein.";
RL Science 250:1413-1415(1990).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2211671; DOI=10.1016/s0021-9258(18)38255-3;
RA Johnston P.A., Yu F.-X., Reynolds G.A., Yin H.L., Moomaw C.R.,
RA Slaughter C.A., Suedhof T.C.;
RT "Purification and expression of gCap39. An intracellular and secreted
RT Ca2(+)-dependent actin-binding protein enriched in mononuclear
RT phagocytes.";
RL J. Biol. Chem. 265:17946-17952(1990).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8293478; DOI=10.1002/cm.970260306;
RA Onoda K., Yu F.-X., Yin H.L.;
RT "gCap39 is a nuclear and cytoplasmic protein.";
RL Cell Motil. Cytoskeleton 26:227-238(1993).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, 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).
CC -!- FUNCTION: Calcium-sensitive protein which reversibly blocks the barbed
CC ends of actin filaments but does not sever preformed actin filaments.
CC May play an important role in macrophage function. May play a role in
CC regulating cytoplasmic and/or nuclear structures through potential
CC interactions with actin. May bind DNA. Uncapping occurs either when
CC Ca(2+) falls or when the concentration of polyphosphoinositide rises,
CC both at low and high Ca(2+).
CC -!- SUBUNIT: Interacts with NUP62. Interacts with NUTF2 and RAN; involved
CC in CAPG nuclear import. {ECO:0000250|UniProtKB:P40121}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8293478}. Cytoplasm
CC {ECO:0000269|PubMed:8293478}. Melanosome
CC {ECO:0000250|UniProtKB:P40121}. Cell projection, lamellipodium. Cell
CC projection, ruffle. Note=In macrophages, may be predominantly
CC cytoplasmic. Nuclear localization was observed in fibroblasts. In
CC macrophages, present at the membrane-cytoplasm interface. In activated
CC macrophages, concentrated in the ruffles of the leading lamellipodia.
CC {ECO:0000269|PubMed:8293478}.
CC -!- TISSUE SPECIFICITY: Present in a large variety of tissues and is
CC particularly abundant in kidney and lung. Highly expressed in
CC macrophages (at protein level) (PubMed:8293478).
CC {ECO:0000269|PubMed:8293478}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during HL60 cell differentiation into
CC macrophages (at protein level). {ECO:0000269|PubMed:8293478}.
CC -!- PTM: Phosphorylated. Nuclear GCAP39 is more highly phosphorylated than
CC cytoplasmic GCAP39.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
CC -!- CAUTION: This protein was originally thought to be a DNA-binding
CC protein with a helix-loop-helix domain. {ECO:0000305}.
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DR EMBL; X54511; CAA38370.1; -; mRNA.
DR PIR; A39834; A39834.
DR PIR; S15011; S15011.
DR AlphaFoldDB; P24452; -.
DR SMR; P24452; -.
DR DIP; DIP-61550N; -.
DR IntAct; P24452; 2.
DR STRING; 10090.ENSMUSP00000109705; -.
DR CarbonylDB; P24452; -.
DR iPTMnet; P24452; -.
DR PhosphoSitePlus; P24452; -.
DR SwissPalm; P24452; -.
DR EPD; P24452; -.
DR jPOST; P24452; -.
DR MaxQB; P24452; -.
DR PaxDb; P24452; -.
DR PeptideAtlas; P24452; -.
DR PRIDE; P24452; -.
DR ProteomicsDB; 281771; -.
DR MGI; MGI:1098259; Capg.
DR eggNOG; KOG0443; Eukaryota.
DR InParanoid; P24452; -.
DR ChiTaRS; Capg; mouse.
DR PRO; PR:P24452; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P24452; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IDA:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR Gene3D; 3.40.20.10; -; 3.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR029917; CapG.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF29; PTHR11977:SF29; 1.
DR Pfam; PF00626; Gelsolin; 3.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 3.
PE 1: Evidence at protein level;
KW Acetylation; Actin capping; Actin-binding; Cell projection; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..352
FT /note="Macrophage-capping protein"
FT /id="PRO_0000218754"
FT REPEAT 27..75
FT /note="Gelsolin-like 1"
FT REPEAT 150..190
FT /note="Gelsolin-like 2"
FT REPEAT 265..311
FT /note="Gelsolin-like 3"
FT MOTIF 139..148
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P40121"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 32
FT /note="V -> W (in Ref. 1; CAA38370)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="V -> L (in Ref. 1; CAA38370)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="Missing (in Ref. 1; CAA38370)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..135
FT /note="VESAFHKTTSGARG -> GRVGISQDNLRATP (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="P -> A (in Ref. 1; CAA38370)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 247..248
FT /note="Missing (in Ref. 1 and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 295..296
FT /note="AQ -> GK (in Ref. 1; CAA38370)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="P -> R (in Ref. 1; CAA38370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 39240 MW; 332CF78CD43B8057 CRC64;
MYTPIPQSGS PFPASVQDPG LHIWRVEKLK PVPIARESHG IFFSGDSYLV LHNGPEEASH
LHLWIGQQSS RDEQGACAVL AVHLNTLLGE RPVQHREVQG NESDLFMSYF PRGLKYYREG
GVESAFHKTT SGARGAAIRK LYQVKGKKNI RATERPLSWD SFNTGDCFIL DLGQNIFAWC
GGKSNILERN KARDLALAIR DSERQGKAQV EIITDGEEPA EMIQVLGPKP ALKEGNPEED
ITADQTRPNA QAAALYKVSD ATGQMNLTKV ADSSPFASEL LIPDDCFVLD NGLCAQIYIW
KGRKANEKER QAALQVADGF ISRMRYSPNT QVEILPQGRE SPIFKQFFKN WK
