CAPG_BOVIN
ID CAPG_BOVIN Reviewed; 349 AA.
AC Q865V6;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Macrophage-capping protein;
DE AltName: Full=Actin regulatory protein CAP-G;
GN Name=CAPG;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12754261; DOI=10.1074/jbc.m300598200;
RA Pellieux C., Desgeorges A., Pigeon C.H., Chambaz C., Yin H., Hayoz D.,
RA Silacci P.;
RT "Cap G, a gelsolin family protein modulating protective effects of
RT unidirectional shear stress.";
RL J. Biol. Chem. 278:29136-29144(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:P40121}. Cytoplasm
CC {ECO:0000250|UniProtKB:P40121}. Melanosome
CC {ECO:0000250|UniProtKB:P40121}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P24452}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:P24452}. Note=In macrophages, may be
CC predominantly cytoplasmic. Nuclear localization was observed in
CC fibroblasts. In macrophages, present at the membrane-cytoplasm
CC interface. In activated macrophages, concentrated in the ruffles of the
CC leading lamellipodia. {ECO:0000250|UniProtKB:P24452}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; AY219899; AAO38847.1; -; mRNA.
DR EMBL; BC102160; AAI02161.1; -; mRNA.
DR RefSeq; NP_848669.1; NM_178574.2.
DR RefSeq; XP_005212800.1; XM_005212743.2.
DR RefSeq; XP_015328964.1; XM_015473478.1.
DR AlphaFoldDB; Q865V6; -.
DR SMR; Q865V6; -.
DR STRING; 9913.ENSBTAP00000007150; -.
DR PaxDb; Q865V6; -.
DR PeptideAtlas; Q865V6; -.
DR PRIDE; Q865V6; -.
DR Ensembl; ENSBTAT00000007150; ENSBTAP00000007150; ENSBTAG00000005432.
DR Ensembl; ENSBTAT00000077078; ENSBTAP00000065020; ENSBTAG00000005432.
DR GeneID; 353121; -.
DR KEGG; bta:353121; -.
DR CTD; 822; -.
DR VEuPathDB; HostDB:ENSBTAG00000005432; -.
DR VGNC; VGNC:26739; CAPG.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000159305; -.
DR HOGENOM; CLU_002568_0_0_1; -.
DR InParanoid; Q865V6; -.
DR OMA; LHSYKVG; -.
DR OrthoDB; 1376537at2759; -.
DR TreeFam; TF313468; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000005432; Expressed in monocyte and 106 other tissues.
DR ExpressionAtlas; Q865V6; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Actin capping; Actin-binding; Cell projection; Cytoplasm;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..349
FT /note="Macrophage-capping protein"
FT /id="PRO_0000284657"
FT REPEAT 27..75
FT /note="Gelsolin-like 1"
FT REPEAT 149..189
FT /note="Gelsolin-like 2"
FT REPEAT 262..308
FT /note="Gelsolin-like 3"
FT MOTIF 138..147
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 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40121"
SQ SEQUENCE 349 AA; 38876 MW; 981690E3A3DFE4D8 CRC64;
MYSPIPQSGS PFPPTVKLPG LHIWRVEKLK PVPVAPENYG IFFSGDSYLV LHNGPEELSH
LHLWIGQQSS RDEQGGCAIL AVHLNTLLGE RPVQHRESQG NESDLFMSYF PHGLKYQEGG
VESAFHKTSP GTAPAAIKKL YQVKGKKNIR ATERVLSWDS FNTGDCFILD LGQNIFAWCG
AKSNILERNK ARDLALAIRD SERQGKAHVE IVTDGEEPAD MIQVLGPKPS LKEGNPEEDL
TADRTNAQAA ALYKVSDATG QMNLTKLADS SPFALELLIP DDCFVLDNGL CGKIYIWKGR
KANEKERQAA LQVAEDFITR MRYAPNTQVE ILPQGRESAI FKQFFKDWK
