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

Alpha-actinin A

Gene

abpA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Calcium bindingi742 – 7531Add BLAST12
Calcium bindingi778 – 7892Add BLAST12

GO - Molecular functioni

  • actin filament binding Source: dictyBase
  • calcium ion binding Source: dictyBase
  • protein binding, bridging Source: dictyBase
  • structural constituent of cytoskeleton Source: dictyBase

GO - Biological processi

  • actin crosslink formation Source: UniProtKB
  • actin filament bundle assembly Source: dictyBase
  • cell motility Source: dictyBase
  • cellular response to starvation Source: dictyBase
  • hyperosmotic response Source: dictyBase
  • phagocytosis Source: dictyBase
  • sorocarp development Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-DDI-114608. Platelet degranulation.

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
Proteomesi
  • UP000002195 Componentsi: Chromosome 1, 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

  • actin filament Source: dictyBase
  • cell cortex Source: UniProtKB-SubCell
  • cell leading edge Source: dictyBase
  • contractile vacuole Source: UniProtKB-SubCell
  • cytosol Source: dictyBase
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi742D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-744; A-746 and A-753. 1 Publication1
Mutagenesisi744D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-746 and A-753. 1 Publication1
Mutagenesisi746D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-753. 1 Publication1
Mutagenesisi753E → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-746. 1 Publication1
Mutagenesisi778D → A: Decreases sensitivity to inhibition by calcium; when associated with A-780; A-786 and A-789. 1 Publication1
Mutagenesisi780D → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-786 and A-789. 1 Publication1
Mutagenesisi786S → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-789. 1 Publication1
Mutagenesisi789E → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-786. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000734451 – 861Alpha-actinin AAdd BLAST861

Proteomic databases

PaxDbiP05095.
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

GO - Molecular functioni

  • actin filament binding Source: dictyBase
  • protein binding, bridging Source: dictyBase

Protein-protein interaction databases

STRINGi44689.DDB0191133.

Structurei

Secondary structure

1861
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi265 – 290Combined sources26
Helixi298 – 313Combined sources16
Helixi316 – 338Combined sources23
Turni339 – 341Combined sources3
Beta strandi348 – 350Combined sources3
Helixi353 – 404Combined sources52
Helixi406 – 409Combined sources4
Turni418 – 421Combined sources4
Helixi422 – 424Combined sources3
Helixi428 – 431Combined sources4
Turni432 – 436Combined sources5
Helixi437 – 440Combined sources4
Helixi442 – 455Combined sources14
Helixi461 – 472Combined sources12
Helixi475 – 482Combined sources8
Helixi484 – 487Combined sources4
Turni489 – 494Combined sources6
Turni496 – 501Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G8XX-ray2.80A/B265-502[»]
4PD3X-ray2.84A/B265-502[»]
5JLHelectron microscopy3.90F/G265-502[»]
ProteinModelPortaliP05095.
SMRiP05095.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05095.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 239Actin-bindingAdd BLAST239
Domaini22 – 127CH 1PROSITE-ProRule annotationAdd BLAST106
Domaini136 – 239CH 2PROSITE-ProRule annotationAdd BLAST104
Repeati240 – 365Spectrin 1Add BLAST126
Repeati366 – 480Spectrin 2Add BLAST115
Repeati481 – 601Spectrin 3Add BLAST121
Repeati602 – 714Spectrin 4Add BLAST113
Domaini729 – 764EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini765 – 800EF-hand 2PROSITE-ProRule annotationAdd BLAST36

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

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
COG5126. LUCA.
InParanoidiP05095.
KOiK05699.
OMAiIHQEMQE.
PhylomeDBiP05095.

Family and domain databases

CDDicd00014. CH. 2 hits.
cd00051. EFh. 1 hit.
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.
PF13499. EF-hand_7. 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]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47576. 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

        10         20         30         40         50
MSEEPTPVSG NDKQLLNKAW EITQKKTFTA WCNSHLRKLG SSIEQIDTDF
60 70 80 90 100
TDGIKLAQLL EVISNDPVFK VNKTPKLRIH NIQNVGLCLK HIESHGVKLV
110 120 130 140 150
GIGAEELVDK NLKMTLGMIW TIILRFAIQD ISIEELSAKE ALLLWCQRKT
160 170 180 190 200
EGYDRVKVGN FHTSFQDGLA FCALIHKHRP DLINFDSLNK DDKAGNLQLA
210 220 230 240 250
FDIAEKELDI PKMLDVSDML DVVRPDERSV MTYVAQYYHH FSASRKAETA
260 270 280 290 300
GKQVGKVLDT FMLLEQTKSD YLKRANELVQ WINDKQASLE SRDFGDSIES
310 320 330 340 350
VQSFMNAHKE YKKTEKPPKG QEVSELEAIY NSLQTKLRLI KREPFVAPAG
360 370 380 390 400
LTPNEIDSTW SALEKAEQEH AEALRIELKR QKKIAVLLQK YNRILKKLEN
410 420 430 440 450
WATTKSVYLG SNETGDSITA VQAKLKNLEA FDGECQSLEG QSNSDLLSIL
460 470 480 490 500
AQLTELNYNG VPELTERKDT FFAQQWTGVK SSAETYKNTL LAELERLQKI
510 520 530 540 550
EDSLVEFAKR AAQLNVWIEA ADDHVFDPIN VDSVQGVQEI QEKFDAFLHD
560 570 580 590 600
QSQQFAELEA LAALTQQLRE LGRSENDYSV ISYDELSAKW NNLLAGIEER
610 620 630 640 650
KVQLANELTT QTNNDVLCQS FSVKANEISD YVRVTLDAIS QNTSSDPQEQ
660 670 680 690 700
LNNIRAIITA HAEKKPELDE LYTIASQLEE AQVVDNKHTQ HSLESIKLKW
710 720 730 740 750
DKLNTLAKKN EQVVEGEILA KQLTGVTAEE LSEFKACFSH FDKDNDNKLN
760 770 780 790 800
RLEFSSCLKS IGDELTEEQL NQVISKIDTD GNGTISFEEF IDYMVSSRKG
810 820 830 840 850
TDSVESTKAA FKVMAEDKDF ITEAQIRAAI SDSKQIDYLL ASMPAVEGGF
860
DYNSFAEKLY Q
Length:861
Mass (Da):97,358
Last modified:March 20, 2007 - v2
Checksum:i17F4364B8059EAFA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti78R → RR in CAA68685 (PubMed:3622778).Curated1
Sequence conflicti359T → P in CAA27855 (PubMed:3745276).Curated1
Sequence conflicti500I → T in CAA27855 (PubMed:3745276).Curated1
Sequence conflicti675A → R in CAA68685 (PubMed:3622778).Curated1
Sequence conflicti696I → L in CAA68685 (PubMed:3622778).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsemblProtistsiEAL72905; EAL72905; DDB_G0268632.
GeneIDi8616670.
KEGGiddi:DDB_G0268632.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G8XX-ray2.80A/B265-502[»]
4PD3X-ray2.84A/B265-502[»]
5JLHelectron microscopy3.90F/G265-502[»]
ProteinModelPortaliP05095.
SMRiP05095.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0191133.

Proteomic databases

PaxDbiP05095.
PRIDEiP05095.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL72905; EAL72905; DDB_G0268632.
GeneIDi8616670.
KEGGiddi:DDB_G0268632.

Organism-specific databases

dictyBaseiDDB_G0268632. abpA.

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
COG5126. LUCA.
InParanoidiP05095.
KOiK05699.
OMAiIHQEMQE.
PhylomeDBiP05095.

Enzyme and pathway databases

ReactomeiR-DDI-114608. Platelet degranulation.

Miscellaneous databases

EvolutionaryTraceiP05095.
PROiP05095.

Family and domain databases

CDDicd00014. CH. 2 hits.
cd00051. EFh. 1 hit.
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.
PF13499. EF-hand_7. 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]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47576. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 140 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

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.