GELA_DICDI
ID GELA_DICDI Reviewed; 857 AA.
AC P13466; Q55C12;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Gelation factor;
DE AltName: Full=Actin-binding protein 120;
DE Short=ABP-120;
GN Name=abpC; ORFNames=DDB_G0269100;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=AX2;
RX PubMed=2668299; DOI=10.1083/jcb.109.2.607;
RA Noegel A.A., Rapp S., Lottspeich F., Schleicher M., Stewart M.;
RT "The Dictyostelium gelation factor shares a putative actin binding site
RT with alpha-actinins and dystrophin and also has a rod domain containing six
RT 100-residue motifs that appear to have a cross-beta conformation.";
RL J. Cell Biol. 109:607-618(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP ACTIN-BINDING MINIMAL DOMAIN.
RX PubMed=2345173; DOI=10.1016/s0021-9258(19)38837-4;
RA Bresnick A.R., Warren V., Condeelis J.;
RT "Identification of a short sequence essential for actin binding by
RT Dictyostelium ABP-120.";
RL J. Biol. Chem. 265:9236-9240(1990).
RN [4]
RP STRUCTURE BY NMR OF 549-648.
RX PubMed=9164464; DOI=10.1038/nsb0397-223;
RA Fucini P., Renner C., Herberhold C., Noegel A.A., Holak T.A.;
RT "The repeating segments of the F-actin cross-linking gelation factor (ABP-
RT 120) have an immunoglobulin-like fold.";
RL Nat. Struct. Biol. 4:223-230(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 646-857.
RX PubMed=9417983; DOI=10.1006/jsbi.1997.3930;
RA Fucini P., McCoy A.J., Gomez-Ortiz M., Schleicher M., Noegel A.A.,
RA Stewart M.;
RT "Crystallization and preliminary X-ray diffraction characterization of a
RT dimerizing fragment of the rod domain of the Dictyostelium gelation factor
RT (ABP-120).";
RL J. Struct. Biol. 120:192-195(1997).
CC -!- FUNCTION: F-actin cross-linking protein.
CC -!- SUBUNIT: Homodimer.
CC -!- DOMAIN: The rod domain contains six 100-residue motifs that appear to
CC have a cross-beta conformation.
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DR EMBL; X15430; CAA33471.1; -; mRNA.
DR EMBL; AAFI02000005; EAL71899.1; -; Genomic_DNA.
DR PIR; A35298; A35298.
DR PIR; S05943; S05943.
DR RefSeq; XP_646669.1; XM_641577.1.
DR PDB; 1KSR; NMR; -; A=549-648.
DR PDB; 1QFH; X-ray; 2.20 A; A/B=646-857.
DR PDB; 1WLH; X-ray; 2.80 A; A/B=547-857.
DR PDB; 2N62; NMR; -; L=646-839.
DR PDB; 6G4A; NMR; -; A=646-750.
DR PDBsum; 1KSR; -.
DR PDBsum; 1QFH; -.
DR PDBsum; 1WLH; -.
DR PDBsum; 2N62; -.
DR PDBsum; 6G4A; -.
DR AlphaFoldDB; P13466; -.
DR SMR; P13466; -.
DR BioGRID; 1242645; 1.
DR STRING; 44689.DDB0201554; -.
DR PaxDb; P13466; -.
DR EnsemblProtists; EAL71899; EAL71899; DDB_G0269100.
DR GeneID; 8617642; -.
DR KEGG; ddi:DDB_G0269100; -.
DR dictyBase; DDB_G0269100; abpC.
DR eggNOG; KOG0518; Eukaryota.
DR HOGENOM; CLU_333569_0_0_1; -.
DR InParanoid; P13466; -.
DR OMA; GWANNYL; -.
DR PhylomeDB; P13466; -.
DR EvolutionaryTrace; P13466; -.
DR PRO; PR:P13466; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0061802; C:anterior cell cortex; IDA:dictyBase.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0097575; C:lateral cell cortex; IDA:dictyBase.
DR GO; GO:0070685; C:macropinocytic cup; IDA:dictyBase.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0061803; C:posterior cell cortex; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0051764; P:actin crosslink formation; IMP:dictyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:dictyBase.
DR GO; GO:0016477; P:cell migration; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IGI:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0006972; P:hyperosmotic response; IGI:dictyBase.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0042331; P:phototaxis; IMP:dictyBase.
DR GO; GO:0031269; P:pseudopodium assembly; IMP:dictyBase.
DR GO; GO:0031272; P:regulation of pseudopodium assembly; IMP:dictyBase.
DR GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IGI:dictyBase.
DR GO; GO:0043052; P:thermotaxis; IMP:dictyBase.
DR CDD; cd00014; CH; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.60.40.10; -; 6.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR044801; Filamin.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR38537; PTHR38537; 4.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00630; Filamin; 6.
DR SMART; SM00033; CH; 2.
DR SMART; SM00557; IG_FLMN; 6.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF81296; SSF81296; 6.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50194; FILAMIN_REPEAT; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Direct protein sequencing; Reference proteome;
KW Repeat.
FT CHAIN 1..857
FT /note="Gelation factor"
FT /id="PRO_0000087454"
FT DOMAIN 12..117
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 125..227
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 245..346
FT /note="Filamin 1"
FT REPEAT 347..446
FT /note="Filamin 2"
FT REPEAT 447..545
FT /note="Filamin 3"
FT REPEAT 546..645
FT /note="Filamin 4"
FT REPEAT 646..747
FT /note="Filamin 5"
FT REPEAT 763..837
FT /note="Filamin 6"
FT REGION 1..250
FT /note="Actin-binding"
FT REGION 229..246
FT /note="Regulatory site"
FT /evidence="ECO:0000255"
FT REGION 832..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="Blocked amino end (Met)"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:1WLH"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:1KSR"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:1KSR"
FT STRAND 570..575
FT /evidence="ECO:0007829|PDB:1WLH"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:1WLH"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:1KSR"
FT STRAND 591..599
FT /evidence="ECO:0007829|PDB:1WLH"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:1KSR"
FT STRAND 609..617
FT /evidence="ECO:0007829|PDB:1WLH"
FT STRAND 623..635
FT /evidence="ECO:0007829|PDB:1WLH"
FT STRAND 640..646
FT /evidence="ECO:0007829|PDB:1WLH"
FT TURN 651..653
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 655..658
FT /evidence="ECO:0007829|PDB:1QFH"
FT HELIX 659..661
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 666..668
FT /evidence="ECO:0007829|PDB:6G4A"
FT STRAND 670..675
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 677..681
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 691..696
FT /evidence="ECO:0007829|PDB:1QFH"
FT HELIX 698..700
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:2N62"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 711..719
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 723..733
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 742..748
FT /evidence="ECO:0007829|PDB:1QFH"
FT HELIX 753..755
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 757..766
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 777..781
FT /evidence="ECO:0007829|PDB:2N62"
FT STRAND 782..788
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 791..799
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 801..823
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 832..838
FT /evidence="ECO:0007829|PDB:1QFH"
FT HELIX 840..842
FT /evidence="ECO:0007829|PDB:1QFH"
FT STRAND 850..856
FT /evidence="ECO:0007829|PDB:1QFH"
SQ SEQUENCE 857 AA; 92207 MW; B000809C25D1ECEE CRC64;
MAAAPSGKTW IDVQKKTFTG WANNYLKERI LKIEDLATSL EDGVLLINLL EIISSKKILK
YNKAPKIRMQ KIENNNMAVN FIKSEGLKLV GIGAEDIVDS QLKLILGLIW TLILRYQIQM
SESDNSPKAA LLEWVRKQVA PYKVVVNNFT DSWCDGRVLS ALTDSLKPGV REMSTLTGDA
VQDIDRSMDI ALEEYEIPKI MDANDMNSLP DELSVITYVS YFRDYALNKE KRDADALAAL
EKKRRETSDA SKVEVYGPGV EGGFVNKSAD FHIKAVNYYG EPLANGGEGF TVSVVGADGV
EVPCKLVDNK NGIYDASYTA TVPQDYTVVV QLDDVHCKDS PYNVKIDGSD AQHSNAYGPG
LEGGKVGVPA AFKIQGRNKD GETVTQGGDD FTVKVQSPEG PVDAQIKDNG DGSYDVEYKP
TKGGDHTVEV FLRGEPLAQG PTEVKILNSD SQNSYCDGPG FEKAQAKRPT EFTIHSVGAD
NKPCAAGGDP FQVSISGPHP VNVGITDNDD GTYTVAYTPE QPGDYEIQVT LNDEAIKDIP
KSIHIKPAAD PEKSYAEGPG LDGGECFQPS KFKIHAVDPD GVHRTDGGDG FVVTIEGPAP
VDPVMVDNGD GTYDVEFEPK EAGDYVINLT LDGDNVNGFP KTVTVKPAPS AEHSYAEGEG
LVKVFDNAPA EFTIFAVDTK GVARTDGGDP FEVAINGPDG LVVDAKVTDN NDGTYGVVYD
APVEGNYNVN VTLRGNPIKN MPIDVKCIEG ANGEDSSFGS FTFTVAAKNK KGEVKTYGGD
KFEVSITGPA EEITLDAIDN QDGTYTAAYS LVGNGRFSTG VKLNGKHIEG SPFKQVLGNP
GKKNPEVKSF TTTRTAN
