Skip Header

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

UniProtKB - P68135 (ACTS_RABIT)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Actin, alpha skeletal muscle

Gene

ACTA1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Miscellaneous

In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility.

GO - Molecular functioni

  • actin monomer binding Source: CAFA
  • ATP binding Source: UniProtKB-KW
  • calcium-dependent protein binding Source: AgBase
  • calcium ion binding Source: CAFA
  • identical protein binding Source: IntAct
  • magnesium ion binding Source: CAFA
  • myosin heavy chain binding Source: CAFA
  • protein domain specific binding Source: CAFA
  • titin binding Source: CAFA
  • tropomyosin binding Source: CAFA
  • troponin I binding Source: CAFA
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionMuscle protein
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKiP68135

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, alpha skeletal muscle
Alternative name(s):
Alpha-actin-1
Cleaved into the following chain:
Actin, alpha skeletal muscle, intermediate form
Gene namesi
Name:ACTA1
Synonyms:ACTA
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00004428112 – 377Actin, alpha skeletal muscle, intermediate formBy similarityAdd BLAST376
ChainiPRO_00004428123 – 377Actin, alpha skeletal muscle2 PublicationsAdd BLAST375

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylcysteine; in intermediate formBy similarity1
Modified residuei3N-acetylaspartate; in Actin, alpha skeletal muscle1 Publication1
Modified residuei46Methionine (R)-sulfoxideBy similarity1
Modified residuei49Methionine (R)-sulfoxideBy similarity1
Modified residuei63N6-malonyllysineBy similarity1
Modified residuei75Tele-methylhistidineCombined sources5 Publications1
Modified residuei86N6-methyllysineBy similarity1
Modified residuei179ADP-ribosylarginine; by SpvB1 Publication1

Post-translational modificationi

Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization.By similarity
Can be mono-ADP-ribosylated on Arg-179 by SpvB of Salmonella spp. This modification blocks subsequent polymerization and leads to cell death.1 Publication
Monomethylation at Lys-86 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Methylation, Oxidation

Proteomic databases

PRIDEiP68135

PTM databases

CarbonylDBiP68135
iPTMnetiP68135

Interactioni

Subunit structurei

Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Interacts with TTID. Interacts (via its C-terminus) with USP25 (By similarity). Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X.By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin monomer binding Source: CAFA
  • calcium-dependent protein binding Source: AgBase
  • identical protein binding Source: IntAct
  • myosin heavy chain binding Source: CAFA
  • protein domain specific binding Source: CAFA
  • titin binding Source: CAFA
  • tropomyosin binding Source: CAFA
  • troponin I binding Source: CAFA
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

DIPiDIP-29021N
ELMiP68135
IntActiP68135, 86 interactors
MINTiP68135
STRINGi9986.ENSOCUP00000006542

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 8Combined sources5
Beta strandi10 – 14Combined sources5
Beta strandi16 – 23Combined sources8
Beta strandi26 – 28Combined sources3
Beta strandi30 – 34Combined sources5
Beta strandi37 – 40Combined sources4
Turni42 – 44Combined sources3
Beta strandi46 – 48Combined sources3
Beta strandi49 – 51Combined sources3
Beta strandi54 – 56Combined sources3
Helixi57 – 62Combined sources6
Helixi64 – 66Combined sources3
Beta strandi67 – 70Combined sources4
Beta strandi72 – 74Combined sources3
Helixi81 – 93Combined sources13
Turni94 – 96Combined sources3
Helixi100 – 102Combined sources3
Beta strandi105 – 109Combined sources5
Helixi115 – 127Combined sources13
Beta strandi132 – 138Combined sources7
Helixi139 – 146Combined sources8
Beta strandi150 – 157Combined sources8
Beta strandi158 – 160Combined sources3
Beta strandi162 – 168Combined sources7
Helixi174 – 176Combined sources3
Beta strandi178 – 180Combined sources3
Helixi184 – 196Combined sources13
Turni197 – 199Combined sources3
Helixi205 – 218Combined sources14
Helixi225 – 234Combined sources10
Beta strandi236 – 238Combined sources3
Beta strandi240 – 243Combined sources4
Beta strandi245 – 247Combined sources3
Beta strandi249 – 253Combined sources5
Helixi255 – 264Combined sources10
Helixi266 – 269Combined sources4
Helixi276 – 285Combined sources10
Helixi289 – 291Combined sources3
Helixi292 – 296Combined sources5
Beta strandi299 – 303Combined sources5
Helixi304 – 306Combined sources3
Beta strandi308 – 310Combined sources3
Helixi311 – 322Combined sources12
Helixi324 – 326Combined sources3
Helixi337 – 339Combined sources3
Helixi340 – 350Combined sources11
Helixi352 – 357Combined sources6
Beta strandi358 – 360Combined sources3
Helixi361 – 367Combined sources7
Helixi368 – 370Combined sources3
Helixi371 – 375Combined sources5

3D structure databases

ProteinModelPortaliP68135
SMRiP68135
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68135

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676 Eukaryota
COG5277 LUCA
HOGENOMiHOG000233340
HOVERGENiHBG003771
InParanoidiP68135

Family and domain databases

InterProiView protein in InterPro
IPR004000 Actin
IPR020902 Actin/actin-like_CS
IPR004001 Actin_CS
PANTHERiPTHR11937 PTHR11937, 1 hit
PfamiView protein in Pfam
PF00022 Actin, 1 hit
PRINTSiPR00190 ACTIN
SMARTiView protein in SMART
SM00268 ACTIN, 1 hit
PROSITEiView protein in PROSITE
PS00406 ACTINS_1, 1 hit
PS00432 ACTINS_2, 1 hit
PS01132 ACTINS_ACT_LIKE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P68135-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG 
        60         70         80         90        100
QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP 
       110        120        130        140        150
EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT 
       160        170        180        190        200
TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY 
       210        220        230        240        250
SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI 
       260        270        280        290        300
TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV 
       310        320        330        340        350
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS 
       360        370 
LSTFQQMWIT KQEYDEAGPS IVHRKCF
Length:377
Mass (Da):42,051
Last modified:July 21, 1986 - v1
Checksum:iDF2A3A046346A179
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00872 mRNA Translation: CAA24241.1
V00873 mRNA Translation: CAA24242.1
V00874 mRNA Translation: CAA24243.1
PIRiA92182 ATRB
I46471
I46472
I46473
UniGeneiOcu.1731

Similar proteinsi

Entry informationi

Entry nameiACTS_RABIT
AccessioniPrimary (citable) accession number: P68135
Secondary accession number(s): P02568, P99020
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 18, 2018
This is version 118 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health