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Protein

Alpha-actinin-1

Gene

Actn1

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 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi759 – 770121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi800 – 811122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • protein domain specific binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-114608. Platelet degranulation.
R-RNO-3000170. Syndecan interactions.
R-RNO-373753. Nephrin interactions.
R-RNO-446388. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi70907. Actn1.

Subcellular locationi

  • Cytoplasmcytoskeleton 1 Publication
  • CytoplasmmyofibrilsarcomereZ line By similarity
  • Cell membrane 1 Publication
  • Cell junction 1 Publication
  • Cell projectionruffle By similarity

  • 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.By similarity

GO - Cellular componenti

  • cell junction Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • dendritic spine Source: UniProtKB
  • nucleus Source: RGD
  • plasma membrane Source: UniProtKB-SubCell
  • ruffle Source: UniProtKB-SubCell
  • Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 892892Alpha-actinin-1PRO_0000073433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei12 – 121Phosphotyrosine; by FAK1By similarity
Modified residuei95 – 951N6-acetyllysineBy similarity
Modified residuei195 – 1951N6-acetyllysineBy similarity
Modified residuei471 – 4711PhosphoserineBy similarity
Modified residuei676 – 6761N6-acetyllysineBy similarity
Modified residuei677 – 6771PhosphoserineBy similarity
Modified residuei890 – 8901PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9Z1P2.
PRIDEiQ9Z1P2.

PTM databases

iPTMnetiQ9Z1P2.
PhosphoSiteiQ9Z1P2.

Expressioni

Gene expression databases

BgeeiENSRNOG00000004309.
ExpressionAtlasiQ9Z1P2. differential.
GenevisibleiQ9Z1P2. RN.

Interactioni

Subunit structurei

Homodimer; antiparallel. Interacts with MYOZ2, TTID, LPP and PSD. Interacts with MICALL2 (By similarity). Interacts with DDN and PDLIM2. Interacts with DNM2 and CTTN (PubMed:21210813).By similarity3 Publications

GO - Molecular functioni

  • protein domain specific binding Source: RGD

Protein-protein interaction databases

BioGridi249534. 5 interactions.
IntActiQ9Z1P2. 5 interactions.
MINTiMINT-132434.
STRINGi10116.ENSRNOP00000061058.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1P2.
SMRiQ9Z1P2. Positions 30-254, 267-739, 821-892.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni274 – 733460Interaction with DDNBy similarityAdd
BLAST

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.
InParanoidiQ9Z1P2.
KOiK05699.

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.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 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.

Q9Z1P2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT
60 70 80 90 100
QIENIEEDFR DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI
110 120 130 140 150
ASKGVKLVSI GAEEIVDGNV KMTLGMIWTI ILRFAIQDIS VEETSAKEGL
160 170 180 190 200
LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC ALIHRHRPEL IDYGKLRKDD
210 220 230 240 250
PLTNLNTAFD VAERYLDIPK MLDAEDIVGT ARPDEKAIMT YVSSFYHAFS
260 270 280 290 300
GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR
310 320 330 340 350
VPENTMQAMQ QKLEDFRDYR RLHKPPKVQE KCQLEINFNT LQTKLRLSNR
360 370 380 390 400
PAFMPSEGRM VSDINNAWGC LEQAEKGYEE WLLNEIRRLE RLDHLAEKFR
410 420 430 440 450
QKASIHEAWT DGKEAMLRQK DYETATLSEI KALLKKHEAF ESDLAAHQDR
460 470 480 490 500
VEQIAAIAQE LNELDYYDSP SVNARCQKIC DQWDNLGALT QKRREALERT
510 520 530 540 550
EKLLETIDQL YLEYAKRAAP FNNWMEGAME DLQDTFIVHT IEEIQGLTTA
560 570 580 590 600
HEQFKATLPD ADKERLAILG IHNEVSKIVQ TYHVNMAGTN PYTTITPQEI
610 620 630 640 650
NGKWDHVRQL VPRRDQALTE EHSRQQHNER LRKQFGAQAN VIGPWIQTKM
660 670 680 690 700
EEIGRISIEM HGTLEDQLSH LRQYEKSIVN YKPKIDQLEG DHQLIQEALI
710 720 730 740 750
FDNKHTNYTM EHIRVGWEQL LTTIARTINE VENQILTRDA KGISQEQMNE
760 770 780 790 800
FRASFNHFDR DHSGTLGPEE FKACLISLGY DIGNDPQGEA EFARIMSIVD
810 820 830 840 850
PNRLGVVTFQ AFIDFMSRET ADTDTADQVM ASFKILAGDK NYITGDELRR
860 870 880 890
ELPPDQAEYC IARMAPYAGP DSVPGALDYM SFSTALYGES DL
Length:892
Mass (Da):102,960
Last modified:May 1, 1999 - v1
Checksum:i2360D496D0A84095
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF115386 mRNA. Translation: AAD12064.1.
RefSeqiNP_112267.1. NM_031005.3.
UniGeneiRn.6401.

Genome annotation databases

EnsembliENSRNOT00000088795; ENSRNOP00000069598; ENSRNOG00000056756.
GeneIDi81634.
KEGGirno:81634.
UCSCiRGD:70907. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF115386 mRNA. Translation: AAD12064.1.
RefSeqiNP_112267.1. NM_031005.3.
UniGeneiRn.6401.

3D structure databases

ProteinModelPortaliQ9Z1P2.
SMRiQ9Z1P2. Positions 30-254, 267-739, 821-892.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249534. 5 interactions.
IntActiQ9Z1P2. 5 interactions.
MINTiMINT-132434.
STRINGi10116.ENSRNOP00000061058.

PTM databases

iPTMnetiQ9Z1P2.
PhosphoSiteiQ9Z1P2.

Proteomic databases

PaxDbiQ9Z1P2.
PRIDEiQ9Z1P2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000088795; ENSRNOP00000069598; ENSRNOG00000056756.
GeneIDi81634.
KEGGirno:81634.
UCSCiRGD:70907. rat.

Organism-specific databases

CTDi87.
RGDi70907. Actn1.

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiQ9Z1P2.
KOiK05699.

Enzyme and pathway databases

ReactomeiR-RNO-114608. Platelet degranulation.
R-RNO-3000170. Syndecan interactions.
R-RNO-373753. Nephrin interactions.
R-RNO-446388. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.

Miscellaneous databases

PROiQ9Z1P2.

Gene expression databases

BgeeiENSRNOG00000004309.
ExpressionAtlasiQ9Z1P2. differential.
GenevisibleiQ9Z1P2. RN.

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.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 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...

Entry informationi

Entry nameiACTN1_RAT
AccessioniPrimary (citable) accession number: Q9Z1P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1999
Last modified: September 7, 2016
This is version 146 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. 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.