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

Gelation factor

Gene

abpC

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.

GO - Molecular functioni

  • actin filament binding Source: dictyBase
  • protein homodimerization activity Source: dictyBase

GO - Biological processi

  • actin cytoskeleton organization Source: dictyBase
  • cell migration Source: dictyBase
  • cell motility Source: dictyBase
  • hyperosmotic response Source: dictyBase
  • phagocytosis Source: dictyBase
  • phototaxis Source: dictyBase
  • sorocarp development Source: dictyBase
  • thermotaxis Source: dictyBase
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-DDI-114608. Platelet degranulation.
R-DDI-446353. Cell-extracellular matrix interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Gelation factor
Alternative name(s):
Actin-binding protein 120
Short name:
ABP-120
Gene namesi
Name:abpC
ORF Names:DDB_G0269100
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 1, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0269100. abpC.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: dictyBase
  • cell leading edge Source: dictyBase
  • cortical actin cytoskeleton Source: dictyBase
  • cytoplasm Source: dictyBase
  • phagocytic cup Source: dictyBase
  • plasma membrane Source: dictyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 857857Gelation factorPRO_0000087454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Blocked amino end (Met)

Proteomic databases

PaxDbiP13466.
PRIDEiP13466.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • actin filament binding Source: dictyBase
  • protein homodimerization activity Source: dictyBase

Protein-protein interaction databases

BioGridi1242645. 1 interaction.
STRINGi44689.DDB0201554.

Structurei

Secondary structure

1
857
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi551 – 5533Combined sources
Beta strandi559 – 5613Combined sources
Beta strandi566 – 5683Combined sources
Beta strandi570 – 5756Combined sources
Beta strandi578 – 5803Combined sources
Beta strandi582 – 5854Combined sources
Beta strandi591 – 5999Combined sources
Beta strandi605 – 6073Combined sources
Beta strandi609 – 6179Combined sources
Beta strandi623 – 63513Combined sources
Beta strandi640 – 6467Combined sources
Turni651 – 6533Combined sources
Beta strandi655 – 6584Combined sources
Helixi659 – 6613Combined sources
Beta strandi663 – 6653Combined sources
Beta strandi670 – 6756Combined sources
Beta strandi677 – 6815Combined sources
Beta strandi691 – 6966Combined sources
Helixi698 – 7003Combined sources
Beta strandi702 – 7043Combined sources
Beta strandi706 – 7094Combined sources
Beta strandi711 – 7199Combined sources
Beta strandi723 – 73311Combined sources
Beta strandi742 – 7487Combined sources
Helixi753 – 7553Combined sources
Beta strandi757 – 76610Combined sources
Beta strandi772 – 7743Combined sources
Beta strandi777 – 7815Combined sources
Beta strandi782 – 7887Combined sources
Beta strandi791 – 7999Combined sources
Beta strandi801 – 82323Combined sources
Beta strandi832 – 8387Combined sources
Helixi840 – 8423Combined sources
Beta strandi850 – 8567Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KSRNMR-A549-648[»]
1QFHX-ray2.20A/B646-857[»]
1WLHX-ray2.80A/B547-857[»]
2N62NMR-L646-839[»]
ProteinModelPortaliP13466.
SMRiP13466. Positions 547-857.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13466.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 250250Actin-bindingAdd
BLAST
Domaini12 – 117106CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini125 – 226102CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati245 – 346102Filamin 1Add
BLAST
Repeati347 – 446100Filamin 2Add
BLAST
Repeati447 – 54599Filamin 3Add
BLAST
Repeati546 – 645100Filamin 4Add
BLAST
Repeati646 – 747102Filamin 5Add
BLAST
Repeati763 – 83775Filamin 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni229 – 24618Regulatory siteSequence analysisAdd
BLAST

Domaini

The rod domain contains six 100-residue motifs that appear to have a cross-beta conformation.

Sequence similaritiesi

Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 6 filamin repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0518. Eukaryota.
COG5069. LUCA.
InParanoidiP13466.
KOiK04437.
OMAiPKVHATI.
PhylomeDBiP13466.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
2.60.40.10. 6 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF00630. Filamin. 6 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00557. IG_FLMN. 6 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 6 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13466-1 [UniParc]FASTAAdd to basket

« Hide

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

TTTRTAN
Length:857
Mass (Da):92,207
Last modified:January 1, 1990 - v1
Checksum:iB000809C25D1ECEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15430 mRNA. Translation: CAA33471.1.
AAFI02000005 Genomic DNA. Translation: EAL71899.1.
PIRiA35298.
S05943.
RefSeqiXP_646669.1. XM_641577.1.

Genome annotation databases

EnsemblProtistsiDDB0201554; DDB0201554; DDB_G0269100.
GeneIDi8617642.
KEGGiddi:DDB_G0269100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15430 mRNA. Translation: CAA33471.1.
AAFI02000005 Genomic DNA. Translation: EAL71899.1.
PIRiA35298.
S05943.
RefSeqiXP_646669.1. XM_641577.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KSRNMR-A549-648[»]
1QFHX-ray2.20A/B646-857[»]
1WLHX-ray2.80A/B547-857[»]
2N62NMR-L646-839[»]
ProteinModelPortaliP13466.
SMRiP13466. Positions 547-857.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1242645. 1 interaction.
STRINGi44689.DDB0201554.

Proteomic databases

PaxDbiP13466.
PRIDEiP13466.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0201554; DDB0201554; DDB_G0269100.
GeneIDi8617642.
KEGGiddi:DDB_G0269100.

Organism-specific databases

dictyBaseiDDB_G0269100. abpC.

Phylogenomic databases

eggNOGiKOG0518. Eukaryota.
COG5069. LUCA.
InParanoidiP13466.
KOiK04437.
OMAiPKVHATI.
PhylomeDBiP13466.

Enzyme and pathway databases

ReactomeiR-DDI-114608. Platelet degranulation.
R-DDI-446353. Cell-extracellular matrix interactions.

Miscellaneous databases

EvolutionaryTraceiP13466.
PROiP13466.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
2.60.40.10. 6 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF00630. Filamin. 6 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00557. IG_FLMN. 6 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 6 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 646-857.

Entry informationi

Entry nameiGELA_DICDI
AccessioniPrimary (citable) accession number: P13466
Secondary accession number(s): Q55C12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 11, 2016
This is version 126 of the entry and version 1 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.