Skip Header

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

P68135

- ACTS_RABIT

UniProt

P68135 - ACTS_RABIT

(max 400 entries)x

Your basket is currently empty.

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: 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

  1. ATP binding Source: UniProtKB-KW
  2. calcium-dependent protein binding Source: AgBase
  3. identical protein binding Source: IntAct

GO - Biological processi

  1. skeletal muscle fiber development Source: UniProtKB
  2. skeletal muscle thin filament assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. actin filament Source: UniProtKB
  2. stress fiber Source: UniProtKB
  3. striated muscle thin filament Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature form2 PublicationsPRO_0000000850
Chaini3 – 377375Actin, alpha skeletal musclePRO_0000000851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylaspartate
Modified residuei63 – 631N6-malonyllysineBy similarity
Modified residuei75 – 751Tele-methylhistidineBy similarity
Modified residuei86 – 861N6-methyllysineBy similarity
Modified residuei179 – 1791ADP-ribosylarginine; by SpvB1 Publication

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.

Protein-protein interaction databases

DIPiDIP-29021N.
IntActiP68135. 29 interactions.
MINTiMINT-1489367.
STRINGi9986.ENSOCUP00000006542.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 85Combined sources
Beta strandi10 – 145Combined sources
Beta strandi16 – 238Combined sources
Beta strandi26 – 283Combined sources
Beta strandi30 – 345Combined sources
Beta strandi37 – 404Combined sources
Turni42 – 443Combined sources
Beta strandi49 – 513Combined sources
Beta strandi54 – 563Combined sources
Helixi57 – 626Combined sources
Helixi64 – 663Combined sources
Beta strandi67 – 704Combined sources
Beta strandi72 – 743Combined sources
Helixi81 – 9313Combined sources
Turni94 – 963Combined sources
Helixi100 – 1023Combined sources
Beta strandi105 – 1095Combined sources
Helixi115 – 12713Combined sources
Beta strandi132 – 1387Combined sources
Helixi139 – 1468Combined sources
Beta strandi150 – 1578Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi162 – 1687Combined sources
Helixi174 – 1763Combined sources
Beta strandi178 – 1803Combined sources
Helixi184 – 19613Combined sources
Turni197 – 1993Combined sources
Helixi205 – 21814Combined sources
Helixi225 – 23410Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi249 – 2535Combined sources
Helixi255 – 26410Combined sources
Helixi266 – 2694Combined sources
Helixi276 – 28510Combined sources
Helixi289 – 2913Combined sources
Helixi292 – 2965Combined sources
Beta strandi299 – 3035Combined sources
Helixi304 – 3063Combined sources
Beta strandi308 – 3103Combined sources
Helixi311 – 32212Combined sources
Helixi324 – 3263Combined sources
Helixi337 – 3393Combined sources
Helixi340 – 35011Combined sources
Helixi352 – 3576Combined sources
Beta strandi358 – 3603Combined sources
Helixi361 – 3677Combined sources
Helixi368 – 3703Combined sources
Helixi371 – 3755Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
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[»]
ProteinModelPortaliP68135.
SMRiP68135. Positions 6-377.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68135.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiCOG5277.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP68135.

Family and domain databases

InterProiIPR004000. Actin-related.
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.

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 .
PIRi A92182. ATRB.
I46471.
I46472.
I46473.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ALM model - V/W/X/Y/Z 3-374 [» ]
1ATN X-ray 2.80 A 3-374 [» ]
1EQY X-ray 2.30 A 1-377 [» ]
1ESV X-ray 2.00 A 1-377 [» ]
1H1V X-ray 3.00 A 3-377 [» ]
1IJJ X-ray 2.85 A/B 1-377 [» ]
1J6Z X-ray 1.54 A 3-377 [» ]
1KXP X-ray 2.10 A 3-377 [» ]
1LCU X-ray 3.50 A/B 7-377 [» ]
1LOT X-ray 2.50 B 3-377 [» ]
1M8Q electron microscopy 70.00 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z 3-377 [» ]
1MA9 X-ray 2.40 B 3-377 [» ]
1MVW electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1NWK X-ray 1.85 A 3-377 [» ]
1O18 electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O19 electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1A electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1B electron microscopy 70.00 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1C electron microscopy 70.00 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1D electron microscopy 70.00 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1E electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1F electron microscopy 70.00 0/1/2/3/4/5/6/7/8/V/W/X/Y/Z 3-377 [» ]
1O1G electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1P8Z X-ray 2.60 A 1-377 [» ]
1QZ5 X-ray 1.45 A 3-377 [» ]
1QZ6 X-ray 1.60 A 3-377 [» ]
1RDW X-ray 2.30 X 3-377 [» ]
1RFQ X-ray 3.00 A/B 3-377 [» ]
1RGI X-ray 3.00 A 1-377 [» ]
1S22 X-ray 1.60 A 3-377 [» ]
1SQK X-ray 2.50 A 1-377 [» ]
1T44 X-ray 2.00 A 8-377 [» ]
1UY5 model - A 3-374 [» ]
1WUA X-ray 1.45 A 3-377 [» ]
1Y64 X-ray 3.05 A 3-377 [» ]
1YXQ X-ray 2.01 A/B 3-377 [» ]
2A3Z X-ray 2.08 A 3-377 [» ]
2A40 X-ray 1.80 A/D 3-377 [» ]
2A41 X-ray 2.60 A 3-377 [» ]
2A42 X-ray 1.85 A 3-377 [» ]
2A5X X-ray 2.49 A 3-377 [» ]
2ASM X-ray 1.60 A 3-377 [» ]
2ASO X-ray 1.70 A 3-377 [» ]
2ASP X-ray 1.64 A 3-377 [» ]
2D1K X-ray 2.50 A 3-377 [» ]
2FF3 X-ray 2.00 B 3-377 [» ]
2FF6 X-ray 2.05 A 3-377 [» ]
2FXU X-ray 1.35 A 3-377 [» ]
2GWJ X-ray 1.90 A 7-377 [» ]
2GWK X-ray 2.00 A/B 7-377 [» ]
2HMP X-ray 1.90 A/B 3-377 [» ]
2PAV X-ray 1.80 A 3-377 [» ]
2PBD X-ray 1.50 A 1-377 [» ]
2Q0R X-ray 1.70 A 3-377 [» ]
2Q0U X-ray 1.45 A 3-377 [» ]
2Q1N X-ray 2.70 A/B 3-377 [» ]
2Q31 X-ray 2.70 A/B 3-377 [» ]
2Q36 X-ray 2.50 A 3-377 [» ]
2Q97 X-ray 2.50 A 3-377 [» ]
2V51 X-ray 2.35 B/D 1-377 [» ]
2V52 X-ray 1.45 B 1-377 [» ]
2VCP X-ray 3.20 A/B 3-377 [» ]
2VYP X-ray 2.35 A/B 1-377 [» ]
2W49 electron microscopy 35.00 D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S 3-374 [» ]
2W4U electron microscopy 35.00 D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S 3-374 [» ]
2Y83 electron microscopy 22.90 O/P/Q/R/S/T 3-377 [» ]
2YJE X-ray 3.10 A/B/C 1-377 [» ]
2YJF X-ray 3.50 A/B/C/D/E 1-377 [» ]
2ZWH fiber diffraction 3.30 A 3-377 [» ]
3B5U electron microscopy - A/B/C/D/E/F/G/H/I/J/K/L/M/N 1-377 [» ]
3BUZ X-ray 2.81 B 3-377 [» ]
3CJB X-ray 3.21 A 1-377 [» ]
3CJC X-ray 3.90 A 1-377 [» ]
3DAW X-ray 2.55 A 1-377 [» ]
3FFK X-ray 3.00 B/E 1-377 [» ]
3G37 electron microscopy - O/P/Q/R/S/T/U/V/W/X/Y/Z 3-377 [» ]
3HBT X-ray 2.70 A 3-377 [» ]
3J4K electron microscopy 8.00 A/B/C/D/E 3-377 [» ]
3M1F X-ray 2.89 A 3-377 [» ]
3M3N X-ray 7.00 A/B 3-377 [» ]
3M6G X-ray 2.00 A/B 3-373 [» ]
3MFP electron microscopy - A 3-377 [» ]
3MN5 X-ray 1.50 A 3-377 [» ]
3SJH X-ray 1.75 A 3-377 [» ]
3TPQ X-ray 3.45 A/B/C/D/E 3-377 [» ]
3TU5 X-ray 3.00 A 1-377 [» ]
3U8X X-ray 2.00 A/C 3-377 [» ]
3U9Z X-ray 2.09 A 3-377 [» ]
3UE5 X-ray 2.76 A 3-377 [» ]
4A7F electron microscopy 7.70 A/D/E/F/I 3-377 [» ]
4A7H electron microscopy 7.80 A/D/E/F/G 3-377 [» ]
4A7L electron microscopy 8.10 A/D/E/F/I 3-377 [» ]
4A7N electron microscopy 8.90 A/B/C/D/E 3-377 [» ]
4B1V X-ray 1.75 A/B 2-377 [» ]
4B1W X-ray 1.95 B 2-377 [» ]
4B1X X-ray 1.80 B 2-377 [» ]
4B1Y X-ray 1.29 B 2-377 [» ]
4B1Z X-ray 3.30 A/B/C/D/E/F 2-377 [» ]
4EAH X-ray 3.40 D/F/G/H 1-377 [» ]
4GY2 X-ray 2.71 B 3-377 [» ]
4H03 X-ray 1.75 B 3-377 [» ]
4H0T X-ray 2.20 B 3-377 [» ]
4H0V X-ray 2.03 B 3-377 [» ]
4H0X X-ray 2.33 B 3-377 [» ]
4H0Y X-ray 1.94 B 3-377 [» ]
4K41 X-ray 1.40 A 3-377 [» ]
4K42 X-ray 2.90 A/B/C/D 3-377 [» ]
4K43 X-ray 2.90 A/B 3-377 [» ]
4PKG X-ray 1.80 A 1-377 [» ]
4PKH X-ray 2.15 A/D/F/I 1-377 [» ]
4PKI X-ray 2.30 A 1-377 [» ]
ProteinModelPortali P68135.
SMRi P68135. Positions 6-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29021N.
IntActi P68135. 29 interactions.
MINTi MINT-1489367.
STRINGi 9986.ENSOCUP00000006542.

Proteomic databases

PRIDEi P68135.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG5277.
HOGENOMi HOG000233340.
HOVERGENi HBG003771.
InParanoidi P68135.

Miscellaneous databases

EvolutionaryTracei P68135.

Family and domain databases

InterProi IPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view ]
PANTHERi PTHR11937. PTHR11937. 1 hit.
Pfami PF00022. Actin. 1 hit.
[Graphical view ]
PRINTSi PR00190. ACTIN.
SMARTi SM00268. ACTIN. 1 hit.
[Graphical view ]
PROSITEi PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence."
    Collins J.H., Elzinga M.
    J. Biol. Chem. 250:5915-5920(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-377.
    Tissue: Skeletal muscle.
  2. "Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin."
    Vandekerckhove J., Weber K.
    Eur. J. Biochem. 90:451-462(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 5; 7; 14 AND 75-81.
  3. "Partial amino acid sequence of brain actin and its homology with muscle actin."
    Lu R.C., Elzinga M.
    Biochemistry 16:5801-5806(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing."
    Putney S.D., Herlihy W.C., Schimmel P.R.
    Nature 302:718-721(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-147; 194-283 AND 311-377.
  5. "The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A protein-chemical analysis of muscle actin differentiation."
    Vandekerckhove J., Weber K.
    Differentiation 14:123-133(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-377.
    Tissue: Skeletal muscle.
  6. "Atomic structure of the actin:DNase I complex."
    Kabsch W., Mannherz H.G., Suck D., Pai E.F., Holmes K.C.
    Nature 347:37-44(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  7. "Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics."
    Graceffa P., Dominguez R.
    J. Biol. Chem. 278:34172-34180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
  8. "Actin crystal dynamics: structural implications for F-actin nucleation, polymerization, and branching mediated by the anti-parallel dimer."
    Reutzel R., Yoshioka C., Govindasamy L., Yarmola E.G., Agbandje-McKenna M., Bubb M.R., McKenna R.
    J. Struct. Biol. 146:291-301(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 3-377 IN COMPLEX WITH ATP.
  9. "A steric antagonism of actin polymerization by a Salmonella virulence protein."
    Margarit S.M., Davidson W., Frego L., Stebbins C.E.
    Structure 14:1219-1229(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 7-377, ADP-RIBOSYLATION AT ARG-179 BY SPVB.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH COBL; GSN AND TMSB4X, SUBUNIT.

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 26, 2014
This is version 94 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

External Data

Dasty 3