Reviewed, UniProtKB/Swiss-Prot P05095 (ACTNA_DICDI)

Names and origin

Protein names

Recommended 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

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	861 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Cytoplasm › cell cortex. Contractile vacuole. Cytoplasmic vesicle › phagosome. 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.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoplasmic vesicle Vacuole
Domain	Repeat
Ligand	Actin-binding Calcium
Molecular function	Developmental protein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	actin crosslink formation Ref.7 Inferred from direct assay. Source: UniProtKB actin filament bundle formation Ref.4 Inferred from direct assay. Source: dictyBase multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	actin filament Ref.4 Inferred from direct assay. Source: dictyBase cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell contractile vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell phagocytic vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin filament binding Ref.4 Inferred from direct assay. Source: dictyBase calcium ion binding Ref.7 Inferred from direct assay. Source: dictyBase protein binding, bridging Ref.4 Inferred from direct assay. Source: dictyBase structural constituent of cytoskeleton Ref.4 Inferred from direct assay. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 861

861

Alpha-actinin A

PRO_0000073445

Regions

Domain

1 – 239

239

Actin-binding

Domain

22 – 127

106

CH 1

Domain

136 – 239

104

CH 2

Repeat

240 – 365

126

Spectrin 1

Repeat

366 – 480

115

Spectrin 2

Repeat

481 – 601

121

Spectrin 3

Repeat

602 – 714

113

Spectrin 4

Domain

729 – 764

36

EF-hand 1

Domain

765 – 800

36

EF-hand 2

Calcium binding

742 – 753

12

1

Calcium binding

778 – 789

12

2

Experimental info

Mutagenesis

742

1

D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-744; A-746 and A-753. Ref.7

Mutagenesis

744

1

D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-746 and A-753. Ref.7

Mutagenesis

746

1

D → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-753. Ref.7

Mutagenesis

753

1

E → A: Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-746. Ref.7

Mutagenesis

778

1

D → A: Decreases sensitivity to inhibition by calcium; when associated with A-780; A-786 and A-789. Ref.7

Mutagenesis

780

1

D → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-786 and A-789. Ref.7

Mutagenesis

786

1

S → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-789. Ref.7

Mutagenesis

789

1

E → A: Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-786. Ref.7

Sequence conflict

78

1

R → RR in CAA68685. Ref.1

Sequence conflict

359

1

T → P in CAA27855. Ref.3

Sequence conflict

500

1

I → T in CAA27855. Ref.3

Sequence conflict

675

1

A → R in CAA68685. Ref.1

Sequence conflict

696

1

I → L in CAA68685. Ref.1

Secondary structure

1

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861

Helix Strand Turn

Details...

Helix

265 – 290

26

Helix

298 – 313

16

Turn

316 – 318

3

Helix

322 – 338

17

Turn

339 – 341

3

Helix

353 – 404

52

Turn

405 – 408

4

Turn

418 – 421

4

Helix

422 – 424

3

Helix

428 – 431

4

Turn

435 – 437

3

Helix

442 – 455

14

Helix

462 – 472

11

Turn

473 – 476

4

Turn

480 – 483

4

Helix

484 – 487

4

Turn

489 – 494

6

Turn

496 – 501

6

Sequences

	Sequence		Length	Mass (Da)
	P05095-1 [UniParc]. Last modified March 20, 2007. Version 2. Checksum: 17F4364B8059EAFA	FASTA	861	97,358
	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

References

	« Hide 'large scale' referencesShow '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: 3622778] [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: 15875012] [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: 3745276] [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: 6746725] [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: 3956480] [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: 1732064] [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: 8486739] [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: 7820857] [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: 8937986] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]	"Computer-assisted morphometry of cell-substratum contacts." Weber I. Croat. Med. J. 40:334-339(1999) [PubMed: 10411959] [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: 10413681] [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: 10704840] [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: 11226153] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 265-502.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y00689 mRNA. Translation: CAA68685.1.
AAFI02000004 Genomic DNA. Translation: EAL72905.1.
X04324 Genomic DNA. Translation: CAA27855.1.

PIR

FADOAA. S00103.

RefSeq

XP_646979.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G8X	X-ray	2.80	A/B	265-502	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P05095.

Genome annotation databases

GeneID

3398209.

GenomeReviews

Gene locus abpA in contig CM000150_GR.

KEGG

ddi:DDB_0191133.

Organism-specific databases

dictyBase

DDB_G0268632. abpA.

Phylogenomic databases

HOGENOM

HBG314462.

OMA

TETINDR.

Family and domain databases

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR016146. Calponin-homology.
IPR001715. Calponin_act_bd.
IPR014837. EF-hand_Ca_insen.
IPR011992. EF-Hand_type.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR018248. EF_Hand_dom.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]

Gene3D

G3DSA:1.10.418.10. Calponin-homology. 1 hit.
G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

Pfam

PF00307. CH. 2 hits.
PF00036. efhand. 2 hits.
PF08726. efhand_Ca_insen. 1 hit.
PF00435. Spectrin. 3 hits.
[Graphical view]

SMART

SM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Entry information

Entry name

ACTNA_DICDI

Accession

Primary (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:	December 15, 2009
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)