Reviewed, UniProtKB/Swiss-Prot P13466 (GELA_DICDI)

Names and origin

Protein names

Recommended name:
    Gelation factor
Alternative name(s):
    Actin-binding protein 120
      Short name=ABP-120

Gene names

Name:	abpC
ORF Names:	DDB_G0269100

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	857 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	F-actin cross-linking protein.
Subunit structure	Homodimer.
Domain	The rod domain contains six 100-residue motifs that appear to have a cross-beta conformation. Ref.3
Sequence similarities	Contains 2 CH (calponin-homology) domains. Contains 6 filamin repeats.

Ontologies

Keywords
Domain	Repeat
Ligand	Actin-binding
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Inferred from direct assay. Source: dictyBase hyperosmotic response Inferred from expression pattern. Source: dictyBase phototaxis Inferred from mutant phenotype. Source: dictyBase sorocarp development Inferred from mutant phenotype. Source: dictyBase thermotaxis Inferred from mutant phenotype. Source: dictyBase
Cellular component	cortical actin cytoskeleton Inferred from direct assay. Source: dictyBase membrane fraction Inferred from direct assay. Source: dictyBase phagocytic cup Inferred from direct assay. Source: dictyBase
Molecular function	actin filament binding Traceable author statement. Source: dictyBase protein homodimerization activity Traceable author statement. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 857

857

Gelation factor

PRO_0000087454

Regions

Domain

1 – 250

250

Actin-binding

Domain

12 – 117

106

CH 1

Domain

125 – 226

102

CH 2

Repeat

245 – 346

102

Filamin 1

Repeat

347 – 446

100

Filamin 2

Repeat

447 – 545

99

Filamin 3

Repeat

546 – 645

100

Filamin 4

Repeat

646 – 747

102

Filamin 5

Repeat

763 – 837

75

Filamin 6

Region

229 – 246

18

Regulatory site Potential

Amino acid modifications

Modified residue

1

1

Blocked amino end (Met)

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

857

Helix Strand Turn

Details...

Beta strand

551 – 553

3

Beta strand

570 – 575

6

Beta strand

578 – 580

3

Beta strand

591 – 599

9

Beta strand

609 – 617

9

Beta strand

623 – 635

13

Beta strand

640 – 645

6

Turn

651 – 653

3

Beta strand

655 – 658

4

Helix

659 – 661

3

Beta strand

663 – 665

3

Beta strand

670 – 675

6

Beta strand

677 – 681

5

Beta strand

691 – 696

6

Helix

698 – 700

3

Beta strand

706 – 709

4

Beta strand

711 – 719

9

Beta strand

723 – 733

11

Beta strand

742 – 748

7

Helix

753 – 755

3

Beta strand

757 – 766

10

Beta strand

772 – 774

3

Beta strand

782 – 788

7

Beta strand

791 – 799

9

Beta strand

801 – 823

23

Beta strand

832 – 838

7

Helix

840 – 842

3

Beta strand

850 – 856

7

Sequences

	Sequence		Length	Mass (Da)
	P13466-1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: B000809C25D1ECEE	FASTA	857	92,207
	10 20 30 40 50 60 MAAAPSGKTW IDVQKKTFTG WANNYLKERI LKIEDLATSL EDGVLLINLL EIISSKKILK 70 80 90 100 110 120 YNKAPKIRMQ KIENNNMAVN FIKSEGLKLV GIGAEDIVDS QLKLILGLIW TLILRYQIQM 130 140 150 160 170 180 SESDNSPKAA LLEWVRKQVA PYKVVVNNFT DSWCDGRVLS ALTDSLKPGV REMSTLTGDA 190 200 210 220 230 240 VQDIDRSMDI ALEEYEIPKI MDANDMNSLP DELSVITYVS YFRDYALNKE KRDADALAAL 250 260 270 280 290 300 EKKRRETSDA SKVEVYGPGV EGGFVNKSAD FHIKAVNYYG EPLANGGEGF TVSVVGADGV 310 320 330 340 350 360 EVPCKLVDNK NGIYDASYTA TVPQDYTVVV QLDDVHCKDS PYNVKIDGSD AQHSNAYGPG 370 380 390 400 410 420 LEGGKVGVPA AFKIQGRNKD GETVTQGGDD FTVKVQSPEG PVDAQIKDNG DGSYDVEYKP 430 440 450 460 470 480 TKGGDHTVEV FLRGEPLAQG PTEVKILNSD SQNSYCDGPG FEKAQAKRPT EFTIHSVGAD 490 500 510 520 530 540 NKPCAAGGDP FQVSISGPHP VNVGITDNDD GTYTVAYTPE QPGDYEIQVT LNDEAIKDIP 550 560 570 580 590 600 KSIHIKPAAD PEKSYAEGPG LDGGECFQPS KFKIHAVDPD GVHRTDGGDG FVVTIEGPAP 610 620 630 640 650 660 VDPVMVDNGD GTYDVEFEPK EAGDYVINLT LDGDNVNGFP KTVTVKPAPS AEHSYAEGEG 670 680 690 700 710 720 LVKVFDNAPA EFTIFAVDTK GVARTDGGDP FEVAINGPDG LVVDAKVTDN NDGTYGVVYD 730 740 750 760 770 780 APVEGNYNVN VTLRGNPIKN MPIDVKCIEG ANGEDSSFGS FTFTVAAKNK KGEVKTYGGD 790 800 810 820 830 840 KFEVSITGPA EEITLDAIDN QDGTYTAAYS LVGNGRFSTG VKLNGKHIEG SPFKQVLGNP 850 GKKNPEVKSF TTTRTAN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Dictyostelium gelation factor shares a putative actin binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation." Noegel A.A., Rapp S., Lottspeich F., Schleicher M., Stewart M. J. Cell Biol. 109:607-618(1989) [PubMed: 2668299] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. 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]	"Identification of a short sequence essential for actin binding by Dictyostelium ABP-120." Bresnick A.R., Warren V., Condeelis J. J. Biol. Chem. 265:9236-9240(1990) [PubMed: 2345173] [Abstract] Cited for: ACTIN-BINDING MINIMAL DOMAIN.
[4]	"The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold." Fucini P., Renner C., Herberhold C., Noegel A.A., Holak T.A. Nat. Struct. Biol. 4:223-230(1997) [PubMed: 9164464] [Abstract] Cited for: STRUCTURE BY NMR OF 549-648.
[5]	"Crystallization and preliminary X-ray diffraction characterization of a dimerizing fragment of the rod domain of the Dictyostelium gelation factor (ABP-120)." Fucini P., McCoy A.J., Gomez-Ortiz M., Schleicher M., Noegel A.A., Stewart M. J. Struct. Biol. 120:192-195(1997) [PubMed: 9417983] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 646-857.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X15430 mRNA. Translation: CAA33471.1.
AAFI02000005 Genomic DNA. Translation: EAL71899.1.

PIR

A35298.
S05943.

RefSeq

XP_646669.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KSR	NMR	-	A	549-648	[»]
1QFH	X-ray	2.20	A/B	646-857	[»]
1WLH	X-ray	2.80	A/B	547-857	[»]

SMR

P13466. Positions 7-225, 246-346, 350-446, 425-558.

ModBase

Search...

Genome annotation databases

GeneID

8617642.

KEGG

ddi:DDB_0201554.

Organism-specific databases

dictyBase

DDB_G0269100. abpC.

Phylogenomic databases

eggNOG

KOG0518.

OMA

PWIANIM.

Family and domain databases

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR016146. Calponin-homology.
IPR001715. Calponin_act_bd.
IPR001298. Filamin.
IPR017868. Filamin/ABP280_repeat-like.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]

Gene3D

G3DSA:1.10.418.10. Calponin-homology. 2 hits.
G3DSA:2.60.40.10. Ig-like_fold. 6 hits.

Pfam

PF00307. CH. 2 hits.
PF00630. Filamin. 6 hits.
[Graphical view]

SMART

SM00033. CH. 2 hits.
SM00557. IG_FLMN. 6 hits.
[Graphical view]

PROSITE

PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 6 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GELA_DICDI

Accession

Primary (citable) accession number: P13466
Secondary accession number(s): Q55C12

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	February 9, 2010
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)