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P05095

- ACTNA_DICDI

UniProt

P05095 - ACTNA_DICDI

Protein

Alpha-actinin A

Gene

abpA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (20 Mar 2007)
      Previous versions | rss
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    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 – 753121Add
    BLAST
    Calcium bindingi778 – 789122Add
    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

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

    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

    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 APRO_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

    1
    861
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05095.

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Belongs to the alpha-actinin family.Curated
    Contains 1 actin-binding domain.Curated
    Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
    Contains 2 EF-hand domains.PROSITE-ProRule annotation
    Contains 4 spectrin repeats.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti78 – 781R → RR in CAA68685. (PubMed:3622778)Curated
    Sequence conflicti359 – 3591T → P in CAA27855. (PubMed:3745276)Curated
    Sequence conflicti500 – 5001I → T in CAA27855. (PubMed:3745276)Curated
    Sequence conflicti675 – 6751A → R in CAA68685. (PubMed:3622778)Curated
    Sequence conflicti696 – 6961I → L in CAA68685. (PubMed:3622778)Curated

    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

    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: October 1, 2014
    This is version 125 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