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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
 
 
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