ACTP_ACACA
ID ACTP_ACACA Reviewed; 138 AA.
AC P37167;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Actophorin;
OS Acanthamoeba castellanii (Amoeba).
OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC Acanthamoebidae; Acanthamoeba.
OX NCBI_TaxID=5755;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-106, AND CRYSTALLIZATION.
RX PubMed=8357799; DOI=10.1021/bi00084a019;
RA Quirk S., Maciver S.K., Ampe C., Doberstein S.K., Kaiser D.A.,
RA van Damme J., Vandekerckhove J., Pollard T.D.;
RT "Primary structure of and studies on Acanthamoeba actophorin.";
RL Biochemistry 32:8525-8533(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9145107; DOI=10.1038/nsb0597-369;
RA Leonard S.A., Gittis A.G., Petrella E.C., Pollard T.D., Lattman E.E.;
RT "Crystal structure of the actin-binding protein actophorin from
RT Acanthamoeba.";
RL Nat. Struct. Biol. 4:369-373(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX PubMed=9737968; DOI=10.1074/jbc.273.39.25106;
RA Blanchoin L., Pollard T.D.;
RT "Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin)
RT and profilin.";
RL J. Biol. Chem. 273:25106-25111(1998).
CC -!- FUNCTION: Forms a one to one complex with monomeric actin. Can regulate
CC the pool available for polymerization. Severs actin filaments in a
CC dose-dependent manner.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; M93361; AAA02909.1; -; mRNA.
DR PDB; 1AHQ; X-ray; 2.30 A; A=2-138.
DR PDB; 1CNU; X-ray; 2.25 A; A=2-138.
DR PDB; 7RTX; X-ray; 1.65 A; A=2-138.
DR PDBsum; 1AHQ; -.
DR PDBsum; 1CNU; -.
DR PDBsum; 7RTX; -.
DR AlphaFoldDB; P37167; -.
DR SMR; P37167; -.
DR VEuPathDB; AmoebaDB:ACA1_296340; -.
DR EvolutionaryTrace; P37167; -.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:InterPro.
DR CDD; cd11286; ADF_cofilin_like; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR017904; ADF/Cofilin.
DR PANTHER; PTHR11913; PTHR11913; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR PRINTS; PR00006; COFILIN.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Direct protein sequencing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8357799"
FT CHAIN 2..138
FT /note="Actophorin"
FT /id="PRO_0000214940"
FT DOMAIN 3..134
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT MOD_RES 2
FT /note="Blocked amino end (Ser)"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:7RTX"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:7RTX"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:7RTX"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:7RTX"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:7RTX"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:7RTX"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:7RTX"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:7RTX"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:7RTX"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:7RTX"
SQ SEQUENCE 138 AA; 15554 MW; F071B8C477F63424 CRC64;
MSGIAVSDDC VQKFNELKLG HQHRYVTFKM NASNTEVVVE HVGGPNATYE DFKSQLPERD
CRYAIFDYEF QVDGGQRNKI TFILWAPDSA PIKSKMMYTS TKDSIKKKLV GIQVEVQATD
AAEISEDAVS ERAKKDVK
