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

Actin, alpha skeletal muscle

Gene

ACTA1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium-dependent protein binding Source: AgBase
  • identical protein binding Source: IntAct

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKP68135.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, alpha skeletal muscle
Alternative name(s):
Alpha-actin-1
Gene namesi
Name:ACTA1
Synonyms:ACTA
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000008501 – 2Removed in mature form2 Publications2
ChainiPRO_00000008513 – 377Actin, alpha skeletal muscleAdd BLAST375

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylaspartate1 Publication1
Modified residuei63N6-malonyllysineBy similarity1
Modified residuei86N6-methyllysineBy similarity1
Modified residuei179ADP-ribosylarginine; by SpvB1 Publication1

Post-translational modificationi

Can be mono-ADP-ribosylated on Arg-179 by SpvB of Salmonella spp. This modification blocks subsequent polymerization and leads to cell death.
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).By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Methylation

Proteomic databases

PRIDEiP68135.

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

WithEntry#Exp.IntActNotes
itself5EBI-367540,EBI-367540
Q05193-55EBI-367540,EBI-8446026From a different organism.
ARP8Q123862EBI-367540,EBI-2967From a different organism.
CNN1P269325EBI-367540,EBI-8602797From a different organism.
Mkl1Q8K4J615EBI-367540,EBI-8291665From a different organism.

GO - Molecular functioni

  • calcium-dependent protein binding Source: AgBase
  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-29021N.
IntActiP68135. 31 interactors.
MINTiMINT-1489367.
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 strandi45 – 48Combined sources4
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ALMmodel-V/W/X/Y/Z3-374[»]
1ATNX-ray2.80A3-374[»]
1EQYX-ray2.30A1-377[»]
1ESVX-ray2.00A1-377[»]
1H1VX-ray3.00A3-377[»]
1IJJX-ray2.85A/B1-377[»]
1J6ZX-ray1.54A3-377[»]
1KXPX-ray2.10A3-377[»]
1LCUX-ray3.50A/B7-377[»]
1LOTX-ray2.50B3-377[»]
1M8Qelectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1MA9X-ray2.40B3-377[»]
1MVWelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1NWKX-ray1.85A3-377[»]
1O18electron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O19electron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Aelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Belectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Celectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Delectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Eelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Felectron microscopy70.000/1/2/3/4/5/6/7/8/V/W/X/Y/Z3-377[»]
1O1Gelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1P8ZX-ray2.60A1-377[»]
1QZ5X-ray1.45A3-377[»]
1QZ6X-ray1.60A3-377[»]
1RDWX-ray2.30X3-377[»]
1RFQX-ray3.00A/B3-377[»]
1RGIX-ray3.00A1-377[»]
1S22X-ray1.60A3-377[»]
1SQKX-ray2.50A1-377[»]
1T44X-ray2.00A8-377[»]
1UY5model-A3-374[»]
1WUAX-ray1.45A3-377[»]
1Y64X-ray3.05A3-377[»]
1YXQX-ray2.01A/B3-377[»]
2A3ZX-ray2.08A3-377[»]
2A40X-ray1.80A/D3-377[»]
2A41X-ray2.60A3-377[»]
2A42X-ray1.85A3-377[»]
2A5XX-ray2.49A3-377[»]
2ASMX-ray1.60A3-377[»]
2ASOX-ray1.70A3-377[»]
2ASPX-ray1.64A3-377[»]
2D1KX-ray2.50A3-377[»]
2FF3X-ray2.00B3-377[»]
2FF6X-ray2.05A3-377[»]
2FXUX-ray1.35A3-377[»]
2GWJX-ray1.90A7-377[»]
2GWKX-ray2.00A/B7-377[»]
2HMPX-ray1.90A/B3-377[»]
2PAVX-ray1.80A3-377[»]
2PBDX-ray1.50A1-377[»]
2Q0RX-ray1.70A3-377[»]
2Q0UX-ray1.45A3-377[»]
2Q1NX-ray2.70A/B3-377[»]
2Q31X-ray2.70A/B3-377[»]
2Q36X-ray2.50A3-377[»]
2Q97X-ray2.50A3-377[»]
2V51X-ray2.35B/D1-377[»]
2V52X-ray1.45B1-377[»]
2VCPX-ray3.20A/B3-377[»]
2VYPX-ray2.35A/B1-377[»]
2W49electron microscopy35.00D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S3-374[»]
2W4Uelectron microscopy35.00D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S3-374[»]
2Y83electron microscopy22.90O/P/Q/R/S/T3-377[»]
2YJEX-ray3.10A/B/C1-377[»]
2YJFX-ray3.50A/B/C/D/E1-377[»]
2ZWHfiber diffraction3.30A3-377[»]
3B5Uelectron microscopy-A/B/C/D/E/F/G/H/I/J/K/L/M/N1-377[»]
3BUZX-ray2.81B3-377[»]
3CJBX-ray3.21A1-377[»]
3CJCX-ray3.90A1-377[»]
3DAWX-ray2.55A1-377[»]
3FFKX-ray3.00B/E1-377[»]
3G37electron microscopy-O/P/Q/R/S/T/U/V/W/X/Y/Z3-377[»]
3HBTX-ray2.70A3-377[»]
3J4Kelectron microscopy8.00A/B/C/D/E3-377[»]
3J8Aelectron microscopy3.70A/B/C/D/E3-377[»]
3J8Ielectron microscopy4.70D/E/F/G/H1-377[»]
3J8Jelectron microscopy12.00A/B/C/D/E/F/G/H/I/J/K1-377[»]
3J8Kelectron microscopy12.00A/B/C/D/E/F/G/H/I/J1-377[»]
3JBIelectron microscopy8.50A/B3-377[»]
3JBJelectron microscopy7.60A/B3-377[»]
3JBKelectron microscopy8.20A/B3-377[»]
3M1FX-ray2.89A3-377[»]
3M3NX-ray7.00A/B3-377[»]
3M6GX-ray2.00A/B3-373[»]
3MFPelectron microscopy-A3-377[»]
3MN5X-ray1.50A3-377[»]
3SJHX-ray1.75A3-377[»]
3TPQX-ray3.45A/B/C/D/E3-377[»]
3TU5X-ray3.00A1-377[»]
3U8XX-ray2.00A/C3-377[»]
3U9ZX-ray2.09A3-377[»]
3UE5X-ray2.76A3-377[»]
4A7Felectron microscopy7.70A/D/E/F/I3-377[»]
4A7Helectron microscopy7.80A/D/E/F/G3-377[»]
4A7Lelectron microscopy8.10A/D/E/F/I3-377[»]
4A7Nelectron microscopy8.90A/B/C/D/E3-377[»]
4B1VX-ray1.75A/B2-377[»]
4B1WX-ray1.95B2-377[»]
4B1XX-ray1.80B2-377[»]
4B1YX-ray1.29B2-377[»]
4B1ZX-ray3.30A/B/C/D/E/F2-377[»]
4EAHX-ray3.40D/F/G/H1-377[»]
4GY2X-ray2.71B3-377[»]
4H03X-ray1.75B3-377[»]
4H0TX-ray2.20B3-377[»]
4H0VX-ray2.03B3-377[»]
4H0XX-ray2.33B3-377[»]
4H0YX-ray1.94B3-377[»]
4K41X-ray1.40A3-377[»]
4K42X-ray2.90A/B/C/D3-377[»]
4K43X-ray2.90A/B3-377[»]
4PKGX-ray1.80A1-377[»]
4PKHX-ray2.15A/D/F/I1-377[»]
4PKIX-ray2.30A1-377[»]
4PL8X-ray2.00A/B3-377[»]
4V0UX-ray7.88A/B/C/L/M3-377[»]
4WYBX-ray3.49A/C/E/G/I/K/M/O/Q/S/U/X1-377[»]
4Z94X-ray2.40A1-377[»]
5JLFelectron microscopy3.60A/B/C/D/E3-377[»]
5KG8electron microscopy9.10B/C/D3-377[»]
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

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ALMmodel-V/W/X/Y/Z3-374[»]
1ATNX-ray2.80A3-374[»]
1EQYX-ray2.30A1-377[»]
1ESVX-ray2.00A1-377[»]
1H1VX-ray3.00A3-377[»]
1IJJX-ray2.85A/B1-377[»]
1J6ZX-ray1.54A3-377[»]
1KXPX-ray2.10A3-377[»]
1LCUX-ray3.50A/B7-377[»]
1LOTX-ray2.50B3-377[»]
1M8Qelectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1MA9X-ray2.40B3-377[»]
1MVWelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1NWKX-ray1.85A3-377[»]
1O18electron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O19electron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Aelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Belectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Celectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Delectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Eelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Felectron microscopy70.000/1/2/3/4/5/6/7/8/V/W/X/Y/Z3-377[»]
1O1Gelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1P8ZX-ray2.60A1-377[»]
1QZ5X-ray1.45A3-377[»]
1QZ6X-ray1.60A3-377[»]
1RDWX-ray2.30X3-377[»]
1RFQX-ray3.00A/B3-377[»]
1RGIX-ray3.00A1-377[»]
1S22X-ray1.60A3-377[»]
1SQKX-ray2.50A1-377[»]
1T44X-ray2.00A8-377[»]
1UY5model-A3-374[»]
1WUAX-ray1.45A3-377[»]
1Y64X-ray3.05A3-377[»]
1YXQX-ray2.01A/B3-377[»]
2A3ZX-ray2.08A3-377[»]
2A40X-ray1.80A/D3-377[»]
2A41X-ray2.60A3-377[»]
2A42X-ray1.85A3-377[»]
2A5XX-ray2.49A3-377[»]
2ASMX-ray1.60A3-377[»]
2ASOX-ray1.70A3-377[»]
2ASPX-ray1.64A3-377[»]
2D1KX-ray2.50A3-377[»]
2FF3X-ray2.00B3-377[»]
2FF6X-ray2.05A3-377[»]
2FXUX-ray1.35A3-377[»]
2GWJX-ray1.90A7-377[»]
2GWKX-ray2.00A/B7-377[»]
2HMPX-ray1.90A/B3-377[»]
2PAVX-ray1.80A3-377[»]
2PBDX-ray1.50A1-377[»]
2Q0RX-ray1.70A3-377[»]
2Q0UX-ray1.45A3-377[»]
2Q1NX-ray2.70A/B3-377[»]
2Q31X-ray2.70A/B3-377[»]
2Q36X-ray2.50A3-377[»]
2Q97X-ray2.50A3-377[»]
2V51X-ray2.35B/D1-377[»]
2V52X-ray1.45B1-377[»]
2VCPX-ray3.20A/B3-377[»]
2VYPX-ray2.35A/B1-377[»]
2W49electron microscopy35.00D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S3-374[»]
2W4Uelectron microscopy35.00D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S3-374[»]
2Y83electron microscopy22.90O/P/Q/R/S/T3-377[»]
2YJEX-ray3.10A/B/C1-377[»]
2YJFX-ray3.50A/B/C/D/E1-377[»]
2ZWHfiber diffraction3.30A3-377[»]
3B5Uelectron microscopy-A/B/C/D/E/F/G/H/I/J/K/L/M/N1-377[»]
3BUZX-ray2.81B3-377[»]
3CJBX-ray3.21A1-377[»]
3CJCX-ray3.90A1-377[»]
3DAWX-ray2.55A1-377[»]
3FFKX-ray3.00B/E1-377[»]
3G37electron microscopy-O/P/Q/R/S/T/U/V/W/X/Y/Z3-377[»]
3HBTX-ray2.70A3-377[»]
3J4Kelectron microscopy8.00A/B/C/D/E3-377[»]
3J8Aelectron microscopy3.70A/B/C/D/E3-377[»]
3J8Ielectron microscopy4.70D/E/F/G/H1-377[»]
3J8Jelectron microscopy12.00A/B/C/D/E/F/G/H/I/J/K1-377[»]
3J8Kelectron microscopy12.00A/B/C/D/E/F/G/H/I/J1-377[»]
3JBIelectron microscopy8.50A/B3-377[»]
3JBJelectron microscopy7.60A/B3-377[»]
3JBKelectron microscopy8.20A/B3-377[»]
3M1FX-ray2.89A3-377[»]
3M3NX-ray7.00A/B3-377[»]
3M6GX-ray2.00A/B3-373[»]
3MFPelectron microscopy-A3-377[»]
3MN5X-ray1.50A3-377[»]
3SJHX-ray1.75A3-377[»]
3TPQX-ray3.45A/B/C/D/E3-377[»]
3TU5X-ray3.00A1-377[»]
3U8XX-ray2.00A/C3-377[»]
3U9ZX-ray2.09A3-377[»]
3UE5X-ray2.76A3-377[»]
4A7Felectron microscopy7.70A/D/E/F/I3-377[»]
4A7Helectron microscopy7.80A/D/E/F/G3-377[»]
4A7Lelectron microscopy8.10A/D/E/F/I3-377[»]
4A7Nelectron microscopy8.90A/B/C/D/E3-377[»]
4B1VX-ray1.75A/B2-377[»]
4B1WX-ray1.95B2-377[»]
4B1XX-ray1.80B2-377[»]
4B1YX-ray1.29B2-377[»]
4B1ZX-ray3.30A/B/C/D/E/F2-377[»]
4EAHX-ray3.40D/F/G/H1-377[»]
4GY2X-ray2.71B3-377[»]
4H03X-ray1.75B3-377[»]
4H0TX-ray2.20B3-377[»]
4H0VX-ray2.03B3-377[»]
4H0XX-ray2.33B3-377[»]
4H0YX-ray1.94B3-377[»]
4K41X-ray1.40A3-377[»]
4K42X-ray2.90A/B/C/D3-377[»]
4K43X-ray2.90A/B3-377[»]
4PKGX-ray1.80A1-377[»]
4PKHX-ray2.15A/D/F/I1-377[»]
4PKIX-ray2.30A1-377[»]
4PL8X-ray2.00A/B3-377[»]
4V0UX-ray7.88A/B/C/L/M3-377[»]
4WYBX-ray3.49A/C/E/G/I/K/M/O/Q/S/U/X1-377[»]
4Z94X-ray2.40A1-377[»]
5JLFelectron microscopy3.60A/B/C/D/E3-377[»]
5KG8electron microscopy9.10B/C/D3-377[»]
ProteinModelPortaliP68135.
SMRiP68135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29021N.
IntActiP68135. 31 interactors.
MINTiMINT-1489367.
STRINGi9986.ENSOCUP00000006542.

Proteomic databases

PRIDEiP68135.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP68135.

Enzyme and pathway databases

SABIO-RKP68135.

Miscellaneous databases

EvolutionaryTraceiP68135.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACTS_RABIT
AccessioniPrimary (citable) accession number: P68135
Secondary accession number(s): P02568, P99020
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

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

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.