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P05095 (ACTNA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-actinin A
Alternative name(s):
Actin-binding protein A
F-actin cross-linking protein
Gene names
Name:abpA
Synonyms:actnA
ORF Names:DDB_G0268632
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length861 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Increases the actin-stimulated ATPase activity of myosin. Involved in vegetative cell growth, phagocytosis, motility and development, probably through stabilization of the actin network in the cortical cytoskeleton. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12

Subunit structure

Homodimer; antiparallel. Ref.5

Subcellular location

Cytoplasm. Cytoplasmcell cortex. Contractile vacuole. Cytoplasmic vesiclephagosome. Note: Expressed diffusely throughout the cytoplasm. Accumulates in the cell cortex, contractile vesicle and phagosome. Ref.8

Developmental stage

Expressed throughout development. Levels increase during aggregation (1-6 hours) and are then maintained until late culmination when they start to decrease. Ref.3

Disruption phenotype

Cells show a minor impairment of growth under conditions of reduced temperature and hyperosmotic stress. Fruiting body development and spore production on soil plates is strongly impaired in mutants lacking abpA, but is only mildly affected in mutants on agar plates. Double mutants lacking both abpA and abpC show a marked reduction in growth, cell size and resistance to osmotic shock, and decreased motility and phagocytosis rates. Development is blocked at the tip stage of aggregation, although expression of developmentally regulated genes does not appear to be affected. Double mutants lacking abpA and abpB show a significant reduction in growth and a slight reduction in motility. Development appears to proceed normally until culmination when aberrant fruiting bodies are formed. The phenotypes of the double mutants suggests a partial redundancy in the microfilament system. Ref.5 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the alpha-actinin family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 2 EF-hand domains.

Contains 4 spectrin repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 861861Alpha-actinin A
PRO_0000073445

Regions

Domain1 – 239239Actin-binding
Domain22 – 127106CH 1
Domain136 – 239104CH 2
Repeat240 – 365126Spectrin 1
Repeat366 – 480115Spectrin 2
Repeat481 – 601121Spectrin 3
Repeat602 – 714113Spectrin 4
Domain729 – 76436EF-hand 1
Domain765 – 80036EF-hand 2
Calcium binding742 – 753121
Calcium binding778 – 789122

Experimental info

Mutagenesis7421D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-744; A-746 and A-753. Ref.7
Mutagenesis7441D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-746 and A-753. Ref.7
Mutagenesis7461D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-753. Ref.7
Mutagenesis7531E → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-746. Ref.7
Mutagenesis7781D → A: Decreases sensitivity to inhibition by calcium; when associated with A-780; A-786 and A-789. Ref.7
Mutagenesis7801D → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-786 and A-789. Ref.7
Mutagenesis7861S → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-789. Ref.7
Mutagenesis7891E → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-786. Ref.7
Sequence conflict781R → RR in CAA68685. Ref.1
Sequence conflict3591T → P in CAA27855. Ref.3
Sequence conflict5001I → T in CAA27855. Ref.3
Sequence conflict6751A → R in CAA68685. Ref.1
Sequence conflict6961I → L in CAA68685. Ref.1

Secondary structure

.................................. 861
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05095 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: 17F4364B8059EAFA

FASTA86197,358
        10         20         30         40         50         60 
MSEEPTPVSG NDKQLLNKAW EITQKKTFTA WCNSHLRKLG SSIEQIDTDF TDGIKLAQLL 

        70         80         90        100        110        120 
EVISNDPVFK VNKTPKLRIH NIQNVGLCLK HIESHGVKLV GIGAEELVDK NLKMTLGMIW 

       130        140        150        160        170        180 
TIILRFAIQD ISIEELSAKE ALLLWCQRKT EGYDRVKVGN FHTSFQDGLA FCALIHKHRP 

       190        200        210        220        230        240 
DLINFDSLNK DDKAGNLQLA FDIAEKELDI PKMLDVSDML DVVRPDERSV MTYVAQYYHH 

       250        260        270        280        290        300 
FSASRKAETA GKQVGKVLDT FMLLEQTKSD YLKRANELVQ WINDKQASLE SRDFGDSIES 

       310        320        330        340        350        360 
VQSFMNAHKE YKKTEKPPKG QEVSELEAIY NSLQTKLRLI KREPFVAPAG LTPNEIDSTW 

       370        380        390        400        410        420 
SALEKAEQEH AEALRIELKR QKKIAVLLQK YNRILKKLEN WATTKSVYLG SNETGDSITA 

       430        440        450        460        470        480 
VQAKLKNLEA FDGECQSLEG QSNSDLLSIL AQLTELNYNG VPELTERKDT FFAQQWTGVK 

       490        500        510        520        530        540 
SSAETYKNTL LAELERLQKI EDSLVEFAKR AAQLNVWIEA ADDHVFDPIN VDSVQGVQEI 

       550        560        570        580        590        600 
QEKFDAFLHD QSQQFAELEA LAALTQQLRE LGRSENDYSV ISYDELSAKW NNLLAGIEER 

       610        620        630        640        650        660 
KVQLANELTT QTNNDVLCQS FSVKANEISD YVRVTLDAIS QNTSSDPQEQ LNNIRAIITA 

       670        680        690        700        710        720 
HAEKKPELDE LYTIASQLEE AQVVDNKHTQ HSLESIKLKW DKLNTLAKKN EQVVEGEILA 

       730        740        750        760        770        780 
KQLTGVTAEE LSEFKACFSH FDKDNDNKLN RLEFSSCLKS IGDELTEEQL NQVISKIDTD 

       790        800        810        820        830        840 
GNGTISFEEF IDYMVSSRKG TDSVESTKAA FKVMAEDKDF ITEAQIRAAI SDSKQIDYLL 

       850        860 
ASMPAVEGGF DYNSFAEKLY Q 

« Hide

References

« Hide 'large scale' references
[1]"Calcium-sensitive non-muscle alpha-actinin contains EF-hand structures and highly conserved regions."
Noegel A., Witke W., Schleicher M.
FEBS Lett. 221:391-396(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: AX2.
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[3]"Studies on the transcription, translation, and structure of alpha-actinin in Dictyostelium discoideum."
Witke W., Schleicher M., Lottspeich F., Noegel A.
J. Cell Biol. 103:969-975(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 91-504, PROTEIN SEQUENCE OF 126-139; 275-285; 293-309; 313-328; 397-405 AND 481-487, DEVELOPMENTAL STAGE.
Strain: AX2.
[4]"Properties of the 120,000- and 95,000-dalton actin-binding proteins from Dictyostelium discoideum and their possible functions in assembling the cytoplasmic matrix."
Condeelis J., Vahey M., Carboni J.M., DeMey J., Ogihara S.
J. Cell Biol. 99:119-126(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Selection of Dictyostelium mutants defective in cytoskeletal proteins: use of an antibody that binds to the ends of alpha-actinin rods."
Wallraff E., Schleicher M., Modersitzki M., Rieger D., Isenberg G., Gerisch G.
EMBO J. 5:61-67(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE.
[6]"Redundancy in the microfilament system: abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins."
Witke W., Schleicher M., Noegel A.A.
Cell 68:53-62(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]"The Ca(2+)-binding domains in non-muscle type alpha-actinin: biochemical and genetic analysis."
Witke W., Hofmann A., Koeppel B., Schleicher M., Noegel A.A.
J. Cell Biol. 121:599-606(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-742; ASP-744; ASP-746; GLU-753; ASP-778; ASP-780; SER-786 AND GLU-789.
[8]"Differential localization of alpha-actinin and the 30 kD actin-bundling protein in the cleavage furrow, phagocytic cup, and contractile vacuole of Dictyostelium discoideum."
Furukawa R., Fechheimer M.
Cell Motil. Cytoskeleton 29:46-56(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development."
Rivero F., Koeppel B., Peracino B., Bozzaro S., Siegert F., Weijer C.J., Schleicher M., Albrecht R., Noegel A.A.
J. Cell Sci. 109:2679-2691(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]"Computer-assisted morphometry of cell-substratum contacts."
Weber I.
Croat. Med. J. 40:334-339(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[11]"Three actin cross-linking proteins, the 34 kDa actin-bundling protein, alpha-actinin and gelation factor (ABP-120), have both unique and redundant roles in the growth and development of Dictyostelium."
Rivero F., Furukawa R., Fechheimer M., Noegel A.A.
J. Cell Sci. 112:2737-2751(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[12]"Severe developmental defects in Dictyostelium null mutants for actin-binding proteins."
Ponte E., Rivero F., Fechheimer M., Noegel A., Bozzaro S.
Mech. Dev. 91:153-161(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[13]"Structure of a genetically engineered molecular motor."
Kliche W., Fujita-Becker S., Kollmar M., Manstein D.J., Kull F.J.
EMBO J. 20:40-46(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 265-502.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00689 mRNA. Translation: CAA68685.1.
AAFI02000004 Genomic DNA. Translation: EAL72905.1.
X04324 Genomic DNA. Translation: CAA27855.1.
PIRFADOAA. S00103.
RefSeqXP_646979.1. XM_641887.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G8XX-ray2.80A/B265-502[»]
2YCUX-ray2.25A263-502[»]
ProteinModelPortalP05095.
SMRP05095. Positions 19-244, 265-502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0191133.

Proteomic databases

PRIDEP05095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0191133; DDB0191133; DDB_G0268632.
GeneID8616670.
KEGGddi:DDB_G0268632.

Organism-specific databases

dictyBaseDDB_G0268632. abpA.

Phylogenomic databases

eggNOGCOG5069.
OMADFITEAQ.
PhylomeDBP05095.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProIPR001589. Actinin_actin-bd_CS.
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]
PfamPF00307. CH. 2 hits.
PF00036. EF-hand_1. 1 hit.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 3 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05095.

Entry information

Entry nameACTNA_DICDI
AccessionPrimary (citable) accession number: P05095
Secondary accession number(s): Q55EP1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: March 20, 2007
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase