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P05095

- ACTNA_DICDI

UniProt

P05095 - ACTNA_DICDI

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Protein
Alpha-actinin A
Gene
abpA, actnA, DDB_G0268632
Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - 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. 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.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi742 – 753121
Add
BLAST
Calcium bindingi778 – 789122
Add
BLAST

GO - Molecular functioni

  1. actin filament binding Source: dictyBase
  2. calcium ion binding Source: dictyBase
  3. protein binding, bridging Source: dictyBase
  4. structural constituent of cytoskeleton Source: dictyBase

GO - Biological processi

  1. actin crosslink formation Source: UniProtKB
  2. actin filament bundle assembly Source: dictyBase
  3. multicellular organismal development Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-actinin A
Alternative name(s):
Actin-binding protein A
F-actin cross-linking protein
Gene namesi
Name:abpA
Synonyms:actnA
ORF Names:DDB_G0268632
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195: Chromosome 1, UP000002195: Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0268632. abpA.

Subcellular locationi

Cytoplasm. Cytoplasmcell cortex. Contractile vacuole. Cytoplasmic vesiclephagosome
Note: Expressed diffusely throughout the cytoplasm. Accumulates in the cell cortex, contractile vesicle and phagosome.1 Publication

GO - Cellular componenti

  1. actin filament Source: dictyBase
  2. cell cortex Source: UniProtKB-SubCell
  3. contractile vacuole Source: UniProtKB-SubCell
  4. phagocytic vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Vacuole

Pathology & Biotechi

Disruption phenotypei

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.6 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi742 – 7421D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-744; A-746 and A-753. 1 Publication
Mutagenesisi744 – 7441D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-746 and A-753. 1 Publication
Mutagenesisi746 – 7461D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-753. 1 Publication
Mutagenesisi753 – 7531E → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-746. 1 Publication
Mutagenesisi778 – 7781D → A: Decreases sensitivity to inhibition by calcium; when associated with A-780; A-786 and A-789. 1 Publication
Mutagenesisi780 – 7801D → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-786 and A-789. 1 Publication
Mutagenesisi786 – 7861S → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-789. 1 Publication
Mutagenesisi789 – 7891E → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-786. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 861861Alpha-actinin A
PRO_0000073445Add
BLAST

Proteomic databases

PRIDEiP05095.

Expressioni

Developmental stagei

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

Interactioni

Subunit structurei

Homodimer; antiparallel.1 Publication

Protein-protein interaction databases

STRINGi44689.DDB_0191133.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi263 – 28119
Turni282 – 2865
Helixi292 – 30817
Helixi311 – 3144
Helixi316 – 32611
Beta strandi328 – 3303
Turni339 – 3413
Helixi342 – 38645
Turni387 – 3893
Helixi390 – 3934
Helixi401 – 41212
Helixi414 – 43724
Turni438 – 4403
Helixi446 – 4538
Turni454 – 4563
Helixi457 – 46812
Helixi470 – 48011
Beta strandi481 – 4833
Helixi484 – 4874
Turni489 – 4946
Turni496 – 5016

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G8XX-ray2.80A/B265-502[»]
2YCUX-ray2.25A263-502[»]
ProteinModelPortaliP05095.
SMRiP05095. Positions 19-244, 265-502.

Miscellaneous databases

EvolutionaryTraceiP05095.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 239239Actin-binding
Add
BLAST
Domaini22 – 127106CH 1
Add
BLAST
Domaini136 – 239104CH 2
Add
BLAST
Repeati240 – 365126Spectrin 1
Add
BLAST
Repeati366 – 480115Spectrin 2
Add
BLAST
Repeati481 – 601121Spectrin 3
Add
BLAST
Repeati602 – 714113Spectrin 4
Add
BLAST
Domaini729 – 76436EF-hand 1
Add
BLAST
Domaini765 – 80036EF-hand 2
Add
BLAST

Sequence similaritiesi

Belongs to the alpha-actinin family.
Contains 2 EF-hand domains.
Contains 4 spectrin repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
KOiK05699.
OMAiDFITEAQ.
PhylomeDBiP05095.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. 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]
PfamiPF00307. 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]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. 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]

Sequencei

Sequence statusi: Complete.

P05095-1 [UniParc]FASTAAdd to Basket

« Hide

MSEEPTPVSG NDKQLLNKAW EITQKKTFTA WCNSHLRKLG SSIEQIDTDF    50
TDGIKLAQLL EVISNDPVFK VNKTPKLRIH NIQNVGLCLK HIESHGVKLV 100
GIGAEELVDK NLKMTLGMIW TIILRFAIQD ISIEELSAKE ALLLWCQRKT 150
EGYDRVKVGN FHTSFQDGLA FCALIHKHRP DLINFDSLNK DDKAGNLQLA 200
FDIAEKELDI PKMLDVSDML DVVRPDERSV MTYVAQYYHH FSASRKAETA 250
GKQVGKVLDT FMLLEQTKSD YLKRANELVQ WINDKQASLE SRDFGDSIES 300
VQSFMNAHKE YKKTEKPPKG QEVSELEAIY NSLQTKLRLI KREPFVAPAG 350
LTPNEIDSTW SALEKAEQEH AEALRIELKR QKKIAVLLQK YNRILKKLEN 400
WATTKSVYLG SNETGDSITA VQAKLKNLEA FDGECQSLEG QSNSDLLSIL 450
AQLTELNYNG VPELTERKDT FFAQQWTGVK SSAETYKNTL LAELERLQKI 500
EDSLVEFAKR AAQLNVWIEA ADDHVFDPIN VDSVQGVQEI QEKFDAFLHD 550
QSQQFAELEA LAALTQQLRE LGRSENDYSV ISYDELSAKW NNLLAGIEER 600
KVQLANELTT QTNNDVLCQS FSVKANEISD YVRVTLDAIS QNTSSDPQEQ 650
LNNIRAIITA HAEKKPELDE LYTIASQLEE AQVVDNKHTQ HSLESIKLKW 700
DKLNTLAKKN EQVVEGEILA KQLTGVTAEE LSEFKACFSH FDKDNDNKLN 750
RLEFSSCLKS IGDELTEEQL NQVISKIDTD GNGTISFEEF IDYMVSSRKG 800
TDSVESTKAA FKVMAEDKDF ITEAQIRAAI SDSKQIDYLL ASMPAVEGGF 850
DYNSFAEKLY Q 861
Length:861
Mass (Da):97,358
Last modified:March 20, 2007 - v2
Checksum:i17F4364B8059EAFA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781R → RR in CAA68685. 1 Publication
Sequence conflicti359 – 3591T → P in CAA27855. 1 Publication
Sequence conflicti500 – 5001I → T in CAA27855. 1 Publication
Sequence conflicti675 – 6751A → R in CAA68685. 1 Publication
Sequence conflicti696 – 6961I → L in CAA68685. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00689 mRNA. Translation: CAA68685.1.
AAFI02000004 Genomic DNA. Translation: EAL72905.1.
X04324 Genomic DNA. Translation: CAA27855.1.
PIRiS00103. FADOAA.
RefSeqiXP_646979.1. XM_641887.1.

Genome annotation databases

EnsemblProtistsiDDB0191133; DDB0191133; DDB_G0268632.
GeneIDi8616670.
KEGGiddi:DDB_G0268632.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00689 mRNA. Translation: CAA68685.1 .
AAFI02000004 Genomic DNA. Translation: EAL72905.1 .
X04324 Genomic DNA. Translation: CAA27855.1 .
PIRi S00103. FADOAA.
RefSeqi XP_646979.1. XM_641887.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G8X X-ray 2.80 A/B 265-502 [» ]
2YCU X-ray 2.25 A 263-502 [» ]
ProteinModelPortali P05095.
SMRi P05095. Positions 19-244, 265-502.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 44689.DDB_0191133.

Proteomic databases

PRIDEi P05095.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblProtistsi DDB0191133 ; DDB0191133 ; DDB_G0268632 .
GeneIDi 8616670.
KEGGi ddi:DDB_G0268632.

Organism-specific databases

dictyBasei DDB_G0268632. abpA.

Phylogenomic databases

eggNOGi COG5069.
KOi K05699.
OMAi DFITEAQ.
PhylomeDBi P05095.

Miscellaneous databases

EvolutionaryTracei P05095.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProi IPR001589. 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 ]
Pfami PF00307. 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 ]
SMARTi SM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
PROSITEi PS00019. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiACTNA_DICDI
AccessioniPrimary (citable) accession number: P05095
Secondary accession number(s): Q55EP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: March 20, 2007
Last modified: September 3, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi