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Protein

Alpha-actinin-4

Gene

Actn4

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

Functioni

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions. May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi778 – 789121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi819 – 830122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-114608. Platelet degranulation.
R-RNO-373753. Nephrin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-actinin-4Curated
Alternative name(s):
Non-muscle alpha-actinin 4Curated
Gene namesi
Name:Actn4Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi61816. Actn4.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Cell junction By similarity

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Colocalizes with actin stress fibers.By similarity

GO - Cellular componenti

  • brush border Source: Ensembl
  • cell-cell junction Source: Ensembl
  • cortical cytoskeleton Source: Ensembl
  • cytoplasm Source: RGD
  • cytosol Source: Reactome
  • extracellular exosome Source: Ensembl
  • extracellular space Source: Ensembl
  • focal adhesion Source: Ensembl
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • neuron projection Source: UniProtKB
  • nucleus Source: RGD
  • perinuclear region of cytoplasm Source: Ensembl
  • protein complex Source: RGD
  • pseudopodium Source: Ensembl
  • stress fiber Source: Ensembl
  • Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 911911Alpha-actinin-4PRO_0000073443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311PhosphotyrosineBy similarity
Modified residuei114 – 1141N6-acetyllysineBy similarity
Modified residuei214 – 2141N6-acetyllysineBy similarity
Modified residuei249 – 2491PhosphothreonineBy similarity
Modified residuei592 – 5921N6-acetyllysineBy similarity
Modified residuei625 – 6251N6-acetyllysineBy similarity
Modified residuei696 – 6961PhosphoserineBy similarity
Modified residuei779 – 7791N6-acetyllysineBy similarity
Modified residuei859 – 8591N6-acetyllysineBy similarity
Modified residuei909 – 9091PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9QXQ0.
PRIDEiQ9QXQ0.

PTM databases

iPTMnetiQ9QXQ0.
PhosphoSiteiQ9QXQ0.

Expressioni

Tissue specificityi

Expressed in the foot process layer of podocytes in the kidney glomerulus but not in tubules (at protein level).1 Publication

Gene expression databases

ExpressionAtlasiQ9QXQ0. baseline and differential.
GenevisibleiQ9QXQ0. RN.

Interactioni

Subunit structurei

Homodimer; antiparallel (By similarity). Interacts with BAIAP1 (By similarity). Interacts with MICALL2 (preferentially in opened conformation); stimulated by RAB13 activation (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and TRIM3. Binds TRIM3 at the N-terminus. Interacts with PDLIM2. Identified in a complex with CASK, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1. Interacts with PPARG and RARA (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Slc2a4P193573EBI-919056,EBI-915426

GO - Molecular functioni

  • protein complex binding Source: RGD
  • protein N-terminus binding Source: RGD

Protein-protein interaction databases

BioGridi248895. 3 interactions.
IntActiQ9QXQ0. 2 interactions.
MINTiMINT-1775108.
STRINGi10116.ENSRNOP00000027773.

Structurei

3D structure databases

ProteinModelPortaliQ9QXQ0.
SMRiQ9QXQ0. Positions 47-271, 286-758, 841-911.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 269269Actin-bindingAdd
BLAST
Domaini50 – 154105CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini163 – 269107CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati293 – 403111Spectrin 1Add
BLAST
Repeati413 – 518106Spectrin 2Add
BLAST
Repeati528 – 639112Spectrin 3Add
BLAST
Repeati649 – 752104Spectrin 4Add
BLAST
Domaini765 – 80036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini806 – 84136EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni177 – 19216Polyphosphoinositide (PIP2)-bindingSequence analysisAdd
BLAST
Regioni736 – 911176Mediates interaction with MICALL2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi84 – 885LXXLL motifBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 2912Poly-GlyAdd
BLAST

Domaini

Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif that mediates interaction with nuclear receptors.By similarity

Sequence similaritiesi

Belongs to the alpha-actinin family.Curated
Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 4 spectrin repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiQ9QXQ0.
KOiK05699.
OMAiIVGPWIQ.
OrthoDBiEOG72C4ZJ.
PhylomeDBiQ9QXQ0.
TreeFamiTF352676.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR029637. ACTN4.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PANTHERiPTHR11915:SF271. PTHR11915:SF271. 1 hit.
PfamiPF00307. CH. 2 hits.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QXQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDYHAANQA YQYGPSSGGN GTGGGGGMGD YMAQEDDWDR DLLLDPAWEK
60 70 80 90 100
QQRKTFTAWC NSHLRKAGTQ IENIDEDFRD GLKLMLLLEV ISGERLPKPE
110 120 130 140 150
RGKMRVHKIN NVNKALDFIA SKGVKLVSIG AEEIVDGNAK MTLGMIWTII
160 170 180 190 200
LRFAIQDISV EETSAKEGLL LWCQRKTAPY KNVNVQNFHI SWKDGLAFNA
210 220 230 240 250
LIHRHRPELI EYDKLRKDDP VTNLNNAFEV AEKYLDIPKM LDAEDIVNTA
260 270 280 290 300
RPDEKAIMTY VSSFYHAFSG AQKAETAANR ICKVLAVNQE NEHLMEDYER
310 320 330 340 350
LASDLLEWIR RTIPWLEDRV PQKTIQEMQQ KLEDFRDYRR VHKPPKVQEK
360 370 380 390 400
CQLEINFNTL QTKLRLSNRP AFMPSEGRMV SDINNGWQHL EQAEKGYEEW
410 420 430 440 450
LLNEIRRLER LDHLAEKFRQ KASIHEAWTD GKEAMLKHRD YETATLSDIK
460 470 480 490 500
ALIRKHEAFE SDLAAHQDRV EQIAAIAQEL NELDYYDSHN VNTRCQKICD
510 520 530 540 550
QWDNLGSLTH SRREALEKTE KQLETIDQLH LEYAKRAAPF NNWMESAMED
560 570 580 590 600
LQDMFIVHTI EEIEGLISAH DQFKSTLPDA DREREAILAI HKEAQRIAES
610 620 630 640 650
NHIKLSGSNP YTSVTPQIIN SKWEKVQQLV PKRDHALLEE QSKQQSNEHL
660 670 680 690 700
RRQFASQANM VGPWIQTKME EIGRISIEMN GTLEDQLSHL KQYERSIVDY
710 720 730 740 750
KPNLDLLEQQ HQLIQEALIF DNKHTNYTME HLRVGWEQLL TTIARTINEV
760 770 780 790 800
ENQILTRDAK GISQEQMQEF RASFNHFDKD HGGALGPEEF KACLISLGYD
810 820 830 840 850
VENDRQGDAE FNRIMSVVDP NHSGLVTFQA FIDFMSRETT DTDTADQVIA
860 870 880 890 900
SFKVLAGDKN FITAEELRRE LPPDQAEYCI ARMAPYQGPD AAPGALDYKS
910
FSTALYGESD L
Length:911
Mass (Da):104,915
Last modified:December 4, 2007 - v2
Checksum:i0C5FC2E43B5D8FD2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti250 – 2501A → G in AAF20064 (PubMed:10673389).Curated
Sequence conflicti406 – 4061R → P in AAF20064 (PubMed:10673389).Curated
Sequence conflicti792 – 7921A → G in AAF20064 (PubMed:10673389).Curated
Sequence conflicti837 – 8371R → K in AAF20064 (PubMed:10673389).Curated
Sequence conflicti850 – 8501A → G in AAF20064 (PubMed:10673389).Curated
Sequence conflicti864 – 8641A → V in AAF20064 (PubMed:10673389).Curated
Sequence conflicti869 – 8691R → K in AAF20064 (PubMed:10673389).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190909 mRNA. Translation: AAF20064.1.
BC061788 mRNA. Translation: AAH61788.1.
PIRiJC7186.
RefSeqiNP_113863.2. NM_031675.2.
UniGeneiRn.15777.

Genome annotation databases

EnsembliENSRNOT00000027773; ENSRNOP00000027773; ENSRNOG00000020433.
GeneIDi63836.
KEGGirno:63836.
UCSCiRGD:61816. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190909 mRNA. Translation: AAF20064.1.
BC061788 mRNA. Translation: AAH61788.1.
PIRiJC7186.
RefSeqiNP_113863.2. NM_031675.2.
UniGeneiRn.15777.

3D structure databases

ProteinModelPortaliQ9QXQ0.
SMRiQ9QXQ0. Positions 47-271, 286-758, 841-911.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248895. 3 interactions.
IntActiQ9QXQ0. 2 interactions.
MINTiMINT-1775108.
STRINGi10116.ENSRNOP00000027773.

PTM databases

iPTMnetiQ9QXQ0.
PhosphoSiteiQ9QXQ0.

Proteomic databases

PaxDbiQ9QXQ0.
PRIDEiQ9QXQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027773; ENSRNOP00000027773; ENSRNOG00000020433.
GeneIDi63836.
KEGGirno:63836.
UCSCiRGD:61816. rat.

Organism-specific databases

CTDi81.
RGDi61816. Actn4.

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiQ9QXQ0.
KOiK05699.
OMAiIVGPWIQ.
OrthoDBiEOG72C4ZJ.
PhylomeDBiQ9QXQ0.
TreeFamiTF352676.

Enzyme and pathway databases

ReactomeiR-RNO-114608. Platelet degranulation.
R-RNO-373753. Nephrin interactions.

Miscellaneous databases

PROiQ9QXQ0.

Gene expression databases

ExpressionAtlasiQ9QXQ0. baseline and differential.
GenevisibleiQ9QXQ0. RN.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR029637. ACTN4.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PANTHERiPTHR11915:SF271. PTHR11915:SF271. 1 hit.
PfamiPF00307. CH. 2 hits.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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: Prostate.
  3. "Pdlim2, a novel PDZ-LIM domain protein, interacts with alpha-actinins and filamin A."
    Torrado M., Senatorov V.V., Trivedi R., Fariss R.N., Tomarev S.I.
    Invest. Ophthalmol. Vis. Sci. 45:3955-3963(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDLIM2.
  4. "Cell junction-associated proteins IQGAP1, MAGI-2, CASK, spectrins, and alpha-actinin are components of the nephrin multiprotein complex."
    Lehtonen S., Ryan J.J., Kudlicka K., Iino N., Zhou H., Farquhar M.G.
    Proc. Natl. Acad. Sci. U.S.A. 102:9814-9819(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CASK; IQGAP1; MAGI2; NPHS1; SPTAN1 AND SPTBN1, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Renal glomerulus.

Entry informationi

Entry nameiACTN4_RAT
AccessioniPrimary (citable) accession number: Q9QXQ0
Secondary accession number(s): Q6P786
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: December 4, 2007
Last modified: June 8, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.