Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Macrophage-capping protein

Gene

Capg

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA. Uncapping occurs either when Ca2+ falls or when the concentration of polyphosphoinositide rises, both at low and high Ca2+ (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Macrophage-capping protein
Alternative name(s):
Actin regulatory protein CAP-G
Gene namesi
Name:Capg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi1311724. Capg.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Macrophage-capping proteinPRO_0000271392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei338 – 3381PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ6AYC4.
PRIDEiQ6AYC4.

PTM databases

iPTMnetiQ6AYC4.
PhosphoSiteiQ6AYC4.

Expressioni

Gene expression databases

GenevisibleiQ6AYC4. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018562.

Structurei

3D structure databases

ProteinModelPortaliQ6AYC4.
SMRiQ6AYC4. Positions 11-349.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati28 – 10780Gelsolin-like 1Add
BLAST
Repeati147 – 22276Gelsolin-like 2Add
BLAST
Repeati264 – 34279Gelsolin-like 3Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi138 – 14710Nuclear localization signalSequence analysis

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated
Contains 3 gelsolin-like repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000235030.
HOVERGENiHBG001093.
InParanoidiQ6AYC4.
KOiK10368.
OMAiTERALNW.
OrthoDBiEOG7288RJ.
PhylomeDBiQ6AYC4.
TreeFamiTF313468.

Family and domain databases

Gene3Di3.40.20.10. 3 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR029917. CapG.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF13. PTHR11977:SF13. 1 hit.
PfamiPF00626. Gelsolin. 3 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6AYC4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYTPIPQSGS PFPASVQDPG LHIWRVEKLK PVPIARENHG IFFSGDSYLV
60 70 80 90 100
LHNGPEEASH LHLWIGQQSS RDEQGACAVL AVHLNTLLGE RPVQHREVQG
110 120 130 140 150
NESDLFMSYF PQGLKYREGG VESAFHKTTS GTTPAAIRKL YQVKGKKNIR
160 170 180 190 200
ATERALSWDS FNTGDCFILD LGQNIFAWCG GKSNILERNK ARDLALAIRD
210 220 230 240 250
SERQGKAQVE IITDGEEPAE MIQVLGPKPA LKEGNPEEDI TADQTNAQAA
260 270 280 290 300
ALYKVSDATG QMNLTKVADS SPFASELLIP DDCFVLDNGL CGKIYIWKGR
310 320 330 340
KANEKERQAA LQVADGFISR MRYSPNTQVE ILPQGRESPI FKQFFKDWK
Length:349
Mass (Da):38,799
Last modified:September 13, 2004 - v1
Checksum:iB1F327DE344BCD22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079104 mRNA. Translation: AAH79104.1.
RefSeqiNP_001013104.1. NM_001013086.1.
XP_006236723.1. XM_006236661.2.
XP_006236724.1. XM_006236662.2.
XP_006236725.1. XM_006236663.2.
XP_006236728.1. XM_006236666.2.
UniGeneiRn.8945.

Genome annotation databases

EnsembliENSRNOT00000018562; ENSRNOP00000018562; ENSRNOG00000013668.
GeneIDi297339.
KEGGirno:297339.
UCSCiRGD:1311724. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079104 mRNA. Translation: AAH79104.1.
RefSeqiNP_001013104.1. NM_001013086.1.
XP_006236723.1. XM_006236661.2.
XP_006236724.1. XM_006236662.2.
XP_006236725.1. XM_006236663.2.
XP_006236728.1. XM_006236666.2.
UniGeneiRn.8945.

3D structure databases

ProteinModelPortaliQ6AYC4.
SMRiQ6AYC4. Positions 11-349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018562.

PTM databases

iPTMnetiQ6AYC4.
PhosphoSiteiQ6AYC4.

Proteomic databases

PaxDbiQ6AYC4.
PRIDEiQ6AYC4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018562; ENSRNOP00000018562; ENSRNOG00000013668.
GeneIDi297339.
KEGGirno:297339.
UCSCiRGD:1311724. rat.

Organism-specific databases

CTDi822.
RGDi1311724. Capg.

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000235030.
HOVERGENiHBG001093.
InParanoidiQ6AYC4.
KOiK10368.
OMAiTERALNW.
OrthoDBiEOG7288RJ.
PhylomeDBiQ6AYC4.
TreeFamiTF313468.

Miscellaneous databases

NextBioi642116.
PROiQ6AYC4.

Gene expression databases

GenevisibleiQ6AYC4. RN.

Family and domain databases

Gene3Di3.40.20.10. 3 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR029917. CapG.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF13. PTHR11977:SF13. 1 hit.
PfamiPF00626. Gelsolin. 3 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  2. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 323-336, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  3. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCAPG_RAT
AccessioniPrimary (citable) accession number: Q6AYC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: September 13, 2004
Last modified: May 11, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.