CAPG_RAT
ID CAPG_RAT Reviewed; 349 AA.
AC Q6AYC4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Macrophage-capping protein;
DE AltName: Full=Actin regulatory protein CAP-G;
GN Name=Capg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [2]
RP PROTEIN SEQUENCE OF 323-336, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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+) (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:P24452}. Cytoplasm
CC {ECO:0000250|UniProtKB:P24452}. 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 -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; BC079104; AAH79104.1; -; mRNA.
DR RefSeq; NP_001013104.1; NM_001013086.1.
DR RefSeq; XP_006236723.1; XM_006236661.3.
DR RefSeq; XP_006236724.1; XM_006236662.3.
DR RefSeq; XP_006236725.1; XM_006236663.3.
DR RefSeq; XP_017448026.1; XM_017592537.1.
DR RefSeq; XP_017448027.1; XM_017592538.1.
DR RefSeq; XP_017448028.1; XM_017592539.1.
DR RefSeq; XP_017448029.1; XM_017592540.1.
DR RefSeq; XP_017448030.1; XM_017592541.1.
DR AlphaFoldDB; Q6AYC4; -.
DR SMR; Q6AYC4; -.
DR STRING; 10116.ENSRNOP00000018562; -.
DR iPTMnet; Q6AYC4; -.
DR PhosphoSitePlus; Q6AYC4; -.
DR PaxDb; Q6AYC4; -.
DR PRIDE; Q6AYC4; -.
DR Ensembl; ENSRNOT00000102328; ENSRNOP00000096107; ENSRNOG00000013668.
DR GeneID; 297339; -.
DR KEGG; rno:297339; -.
DR UCSC; RGD:1311724; rat.
DR CTD; 822; -.
DR RGD; 1311724; Capg.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000159305; -.
DR HOGENOM; CLU_002568_0_0_1; -.
DR InParanoid; Q6AYC4; -.
DR OMA; LHSYKVG; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; Q6AYC4; -.
DR TreeFam; TF313468; -.
DR PRO; PR:Q6AYC4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000013668; Expressed in esophagus and 19 other tissues.
DR Genevisible; Q6AYC4; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; ISO:RGD.
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:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
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:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
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..349
FT /note="Macrophage-capping protein"
FT /id="PRO_0000271392"
FT REPEAT 28..107
FT /note="Gelsolin-like 1"
FT REPEAT 147..222
FT /note="Gelsolin-like 2"
FT REPEAT 264..342
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:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
SQ SEQUENCE 349 AA; 38799 MW; B1F327DE344BCD22 CRC64;
MYTPIPQSGS PFPASVQDPG LHIWRVEKLK PVPIARENHG IFFSGDSYLV LHNGPEEASH
LHLWIGQQSS RDEQGACAVL AVHLNTLLGE RPVQHREVQG NESDLFMSYF PQGLKYREGG
VESAFHKTTS GTTPAAIRKL YQVKGKKNIR ATERALSWDS FNTGDCFILD LGQNIFAWCG
GKSNILERNK ARDLALAIRD SERQGKAQVE IITDGEEPAE MIQVLGPKPA LKEGNPEEDI
TADQTNAQAA ALYKVSDATG QMNLTKVADS SPFASELLIP DDCFVLDNGL CGKIYIWKGR
KANEKERQAA LQVADGFISR MRYSPNTQVE ILPQGRESPI FKQFFKDWK
