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Q7TPR4

- ACTN1_MOUSE

UniProt

Q7TPR4 - ACTN1_MOUSE

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Protein
Alpha-actinin-1
Gene
Actn1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 By similarity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi759 – 770121 Reviewed prediction
Add
BLAST
Calcium bindingi800 – 811122 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. actin filament binding Source: MGI
  2. calcium ion binding Source: InterPro
  3. double-stranded RNA binding Source: MGI
  4. protein binding Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. actin crosslink formation Source: InterPro
  2. actin filament bundle assembly Source: UniProtKB
  3. cortical cytoskeleton organization Source: UniProtKB
  4. focal adhesion assembly Source: Ensembl
  5. negative regulation of cellular component movement Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196644. Syndecan interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-actinin-1
Alternative name(s):
Alpha-actinin cytoskeletal isoform
F-actin cross-linking protein
Non-muscle alpha-actinin-1
Gene namesi
Name:Actn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:2137706. Actn1.

Subcellular locationi

Cytoplasmcytoskeleton. CytoplasmmyofibrilsarcomereZ line. Cell membrane. Cell junction. Cell projectionruffle
Note: Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures.3 Publications

GO - Cellular componenti

  1. Z disc Source: MGI
  2. cortical cytoskeleton Source: UniProtKB
  3. dendritic spine Source: Ensembl
  4. dense core granule membrane Source: UniProtKB
  5. extracellular vesicular exosome Source: Ensembl
  6. fascia adherens Source: MGI
  7. focal adhesion Source: UniProtKB
  8. nucleus Source: Ensembl
  9. plasma membrane Source: UniProtKB-SubCell
  10. ruffle Source: UniProtKB-SubCell
  11. secretory granule Source: UniProtKB
  12. stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321Q → K: Shows less organization of the circumferential actin-filament network compared to controls. 1 Publication
Mutagenesisi105 – 1051V → I: Shows less organization of the circumferential actin-filament network compared to controls. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 892892Alpha-actinin-1
PRO_0000073432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei6 – 61Phosphoserine By similarity
Modified residuei12 – 121Phosphotyrosine; by FAK1 By similarity
Modified residuei95 – 951N6-acetyllysine By similarity
Modified residuei195 – 1951N6-acetyllysine By similarity
Modified residuei676 – 6761N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7TPR4.
PaxDbiQ7TPR4.
PRIDEiQ7TPR4.

PTM databases

PhosphoSiteiQ7TPR4.

Expressioni

Gene expression databases

ArrayExpressiQ7TPR4.
BgeeiQ7TPR4.
CleanExiMM_ACTN1.
GenevestigatoriQ7TPR4.

Interactioni

Subunit structurei

Homodimer; antiparallel. Interacts with DDN, MYOZ2, PDLIM2, TTID and LPP By similarity. Interacts with PSD. Interacts with MICALL2.2 Publications

Protein-protein interaction databases

BioGridi224977. 13 interactions.
IntActiQ7TPR4. 7 interactions.
MINTiMINT-1869732.
STRINGi10090.ENSMUSP00000021554.

Structurei

3D structure databases

ProteinModelPortaliQ7TPR4.
SMRiQ7TPR4. Positions 30-254, 267-892.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 247247Actin-binding
Add
BLAST
Domaini31 – 135105CH 1
Add
BLAST
Domaini144 – 247104CH 2
Add
BLAST
Repeati274 – 384111Spectrin 1
Add
BLAST
Repeati394 – 499106Spectrin 2
Add
BLAST
Repeati509 – 620112Spectrin 3
Add
BLAST
Repeati630 – 733104Spectrin 4
Add
BLAST
Domaini746 – 78136EF-hand 1
Add
BLAST
Domaini787 – 82236EF-hand 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni274 – 733460Interaction with DDN By similarity
Add
BLAST

Sequence similaritiesi

Belongs to the alpha-actinin family.
Contains 2 EF-hand domains.
Contains 4 spectrin repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00670000097825.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiQ7TPR4.
KOiK05699.
OMAiWIRRTMP.
OrthoDBiEOG72C4ZJ.
PhylomeDBiQ7TPR4.
TreeFamiTF352676.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR026921. Alpha-actinin_1.
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:SF241. PTHR11915:SF241. 1 hit.
PfamiPF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 2 hits.
[Graphical view]
SUPFAMiSSF47576. 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.

Q7TPR4-1 [UniParc]FASTAAdd to Basket

« Hide

MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT    50
QIENIEEDFR DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI 100
ASKGVKLVSI GAEEIVDGNV KMTLGMIWTI ILRFAIQDIS VEETSAKEGL 150
LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC ALIHRHRPEL IDYGKLRKDD 200
PLTNLNTAFD VAERFLDIPK MLDAEDIVGT ARPDEKAIMT YVSSFYHAFS 250
GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR 300
VPENTMHAMQ QKLEDFRDYR RLHKPPKVQE KCQLEINFNT LQTKLRLSNR 350
PAFMPSEGRM VSDINNAWGC LEQAEKGYEE WLLNEIRRLE RLDHLAEKFR 400
QKASIHEAWT DGKEAMLRQK DYETATLSEI KALLKKHEAF ESDLAAHQDR 450
VEQIAAIAQE LNELDYYDSP SVNARCQKIC DQWDNLGALT QKRREALERT 500
EKLLETIDQL YLEYAKRAAP FNNWMEGAME DLQDTFIVHT IEEIQGLTTA 550
HEQFKATLPD ADKERLAILG IHNEVSKIVQ TYHVNMAGTN PYTTITPQEI 600
NGKWDHVRQL VPRRDQALTE EHARQQHNER LRKQFGAQAN VIGPWIQTKM 650
EEIGRISIEM HGTLEDQLSH LRQYEKSIVN YKPKIDQLEC DHQLIQEALI 700
FDNKHTNYNM EHIRVGWEQL LTTIARTINE VENQILTRDA KGISQEQMNE 750
FRASFNHFDR DHSGTLGPEE FKACLISLGY DIGNDPQGEA EFARIMSIVD 800
PNRLGVVTFQ AFIDFMSRET ADTDTADQVM ASFKILAGDK NYITEDELRR 850
ELPPDQAEYC IARMAPYAGP DSVPGALDYM SFSTALYGES DL 892
Length:892
Mass (Da):103,068
Last modified:October 1, 2003 - v1
Checksum:i652DA065A5F38E7C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC054830 mRNA. Translation: AAH54830.1.
CCDSiCCDS26011.1.
RefSeqiNP_598917.1. NM_134156.2.
UniGeneiMm.253564.
Mm.403477.

Genome annotation databases

EnsembliENSMUST00000021554; ENSMUSP00000021554; ENSMUSG00000015143.
GeneIDi109711.
KEGGimmu:109711.
UCSCiuc007oap.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC054830 mRNA. Translation: AAH54830.1 .
CCDSi CCDS26011.1.
RefSeqi NP_598917.1. NM_134156.2.
UniGenei Mm.253564.
Mm.403477.

3D structure databases

ProteinModelPortali Q7TPR4.
SMRi Q7TPR4. Positions 30-254, 267-892.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 224977. 13 interactions.
IntActi Q7TPR4. 7 interactions.
MINTi MINT-1869732.
STRINGi 10090.ENSMUSP00000021554.

PTM databases

PhosphoSitei Q7TPR4.

Proteomic databases

MaxQBi Q7TPR4.
PaxDbi Q7TPR4.
PRIDEi Q7TPR4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021554 ; ENSMUSP00000021554 ; ENSMUSG00000015143 .
GeneIDi 109711.
KEGGi mmu:109711.
UCSCi uc007oap.2. mouse.

Organism-specific databases

CTDi 87.
MGIi MGI:2137706. Actn1.

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00670000097825.
HOGENOMi HOG000263418.
HOVERGENi HBG050453.
InParanoidi Q7TPR4.
KOi K05699.
OMAi WIRRTMP.
OrthoDBi EOG72C4ZJ.
PhylomeDBi Q7TPR4.
TreeFami TF352676.

Enzyme and pathway databases

Reactomei REACT_196644. Syndecan interactions.

Miscellaneous databases

ChiTaRSi ACTN1. mouse.
NextBioi 362623.
PROi Q7TPR4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q7TPR4.
Bgeei Q7TPR4.
CleanExi MM_ACTN1.
Genevestigatori Q7TPR4.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR026921. Alpha-actinin_1.
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 ]
PANTHERi PTHR11915:SF241. PTHR11915:SF241. 1 hit.
Pfami PF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 2 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
PROSITEi PS00019. 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 ]
ProtoNeti Search...

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: Olfactory epithelium.
  2. "Calsarcins, a novel family of sarcomeric calcineurin-binding proteins."
    Frey N., Richardson J.A., Olson E.N.
    Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  3. "Somatodendritic localization of EFA6A, a guanine nucleotide exchange factor for ADP-ribosylation factor 6, and its possible interaction with alpha-actinin in dendritic spines."
    Sakagami H., Honma T., Sukegawa J., Owada Y., Yanagisawa T., Kondo H.
    Eur. J. Neurosci. 25:618-628(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSD, SUBCELLULAR LOCATION.
  4. "Rab13 small G protein and junctional Rab13-binding protein (JRAB) orchestrate actin cytoskeletal organization during epithelial junctional development."
    Sakane A., Abdallah A.A., Nakano K., Honda K., Ikeda W., Nishikawa Y., Matsumoto M., Matsushita N., Kitamura T., Sasaki T.
    J. Biol. Chem. 287:42455-42468(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MICALL2, SUBCELLULAR LOCATION.
  5. Cited for: MUTAGENESIS OF GLN-32 AND VAL-105.

Entry informationi

Entry nameiACTN1_MOUSE
AccessioniPrimary (citable) accession number: Q7TPR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: September 3, 2014
This is version 106 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi