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)DescriptionActionsGraphical viewLength
ChainiPRO_00000874541 – 857Gelation factorAdd BLAST857

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Blocked amino end (Met)1

Proteomic databases

PaxDbiP13466.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi1242645. 1 interactor.
STRINGi44689.DDB0201554.

Structurei

Secondary structure

1857
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi551 – 553Combined sources3
Beta strandi559 – 561Combined sources3
Beta strandi566 – 568Combined sources3
Beta strandi570 – 575Combined sources6
Beta strandi578 – 580Combined sources3
Beta strandi582 – 585Combined sources4
Beta strandi591 – 599Combined sources9
Beta strandi605 – 607Combined sources3
Beta strandi609 – 617Combined sources9
Beta strandi623 – 635Combined sources13
Beta strandi640 – 646Combined sources7
Turni651 – 653Combined sources3
Beta strandi655 – 658Combined sources4
Helixi659 – 661Combined sources3
Beta strandi663 – 665Combined sources3
Beta strandi670 – 675Combined sources6
Beta strandi677 – 681Combined sources5
Beta strandi691 – 696Combined sources6
Helixi698 – 700Combined sources3
Beta strandi702 – 704Combined sources3
Beta strandi706 – 709Combined sources4
Beta strandi711 – 719Combined sources9
Beta strandi723 – 733Combined sources11
Beta strandi742 – 748Combined sources7
Helixi753 – 755Combined sources3
Beta strandi757 – 766Combined sources10
Beta strandi772 – 774Combined sources3
Beta strandi777 – 781Combined sources5
Beta strandi782 – 788Combined sources7
Beta strandi791 – 799Combined sources9
Beta strandi801 – 823Combined sources23
Beta strandi832 – 838Combined sources7
Helixi840 – 842Combined sources3
Beta strandi850 – 856Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP13466.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 250Actin-bindingAdd BLAST250
Domaini12 – 117CH 1PROSITE-ProRule annotationAdd BLAST106
Domaini125 – 226CH 2PROSITE-ProRule annotationAdd BLAST102
Repeati245 – 346Filamin 1Add BLAST102
Repeati347 – 446Filamin 2Add BLAST100
Repeati447 – 545Filamin 3Add BLAST99
Repeati546 – 645Filamin 4Add BLAST100
Repeati646 – 747Filamin 5Add BLAST102
Repeati763 – 837Filamin 6Add BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni229 – 246Regulatory siteSequence analysisAdd BLAST18

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.
OMAiYGPVETI.
PhylomeDBiP13466.

Family and domain databases

CDDicd00014. CH. 2 hits.
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

EnsemblProtistsiEAL71899; EAL71899; 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KSRNMR-A549-648[»]
1QFHX-ray2.20A/B646-857[»]
1WLHX-ray2.80A/B547-857[»]
2N62NMR-L646-839[»]
ProteinModelPortaliP13466.
SMRiP13466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1242645. 1 interactor.
STRINGi44689.DDB0201554.

Proteomic databases

PaxDbiP13466.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL71899; EAL71899; DDB_G0269100.
GeneIDi8617642.
KEGGiddi:DDB_G0269100.

Organism-specific databases

dictyBaseiDDB_G0269100. abpC.

Phylogenomic databases

eggNOGiKOG0518. Eukaryota.
COG5069. LUCA.
InParanoidiP13466.
KOiK04437.
OMAiYGPVETI.
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

CDDicd00014. CH. 2 hits.
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...

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: November 30, 2016
This is version 130 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.