PRO1A_ACACA
ID PRO1A_ACACA Reviewed; 126 AA.
AC P68696; P07763;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Profilin-1A;
DE AltName: Full=Acidic profilin IA;
DE AltName: Full=Profilin IA;
OS Acanthamoeba castellanii (Amoeba).
OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC Acanthamoebidae; Acanthamoeba.
OX NCBI_TaxID=5755;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND METHYLATION AT LYS-104.
RX PubMed=1751969; DOI=10.1002/cm.970200209;
RA Pollard T.D., Rimm D.L.;
RT "Analysis of cDNA clones for Acanthamoeba profilin-I and profilin-II shows
RT end to end homology with vertebrate profilins and a small family of
RT profilin genes.";
RL Cell Motil. Cytoskeleton 20:169-177(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-126.
RX PubMed=3881427; DOI=10.1016/s0021-9258(20)71174-9;
RA Ampe C., Vandekerckhove J., Brenner S.L., Tobacman L., Korn E.D.;
RT "The amino acid sequence of Acanthamoeba profilin.";
RL J. Biol. Chem. 260:834-840(1985).
RN [3]
RP CROSS-LINKING TO ACTIN.
RX PubMed=2569469; DOI=10.1083/jcb.109.2.619;
RA Vandekerckhove J., Kaiser D.A., Pollard T.D.;
RT "Acanthamoeba actin and profilin can be cross-linked between glutamic acid
RT 364 of actin and lysine 115 of profilin.";
RL J. Cell Biol. 109:619-626(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9774541; DOI=10.1006/jsbi.1998.4009;
RA Liu S., Fedorov A.A., Pollard T.D., Lattman E.E., Almo S.C., Magnus K.A.;
RT "Crystal packing induces a conformational change in profilin-I from
RT Acanthamoeba castellanii.";
RL J. Struct. Biol. 123:22-29(1998).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=8397216; DOI=10.1083/jcb.122.6.1277;
RA Vinson V.K., Archer S.J., Lattman E.E., Pollard T.D., Torchia D.A.;
RT "Three-dimensional solution structure of Acanthamoeba profilin-I.";
RL J. Cell Biol. 122:1277-1283(1993).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=8329394; DOI=10.1021/bi00077a022;
RA Archer S.J., Vinson V.K., Pollard T.D., Torchia D.A.;
RT "Secondary structure and topology of Acanthamoeba profilin I as determined
RT by heteronuclear nuclear magnetic resonance spectroscopy.";
RL Biochemistry 32:6680-6687(1993).
CC -!- FUNCTION: Binds to actin and affects the structure of the cytoskeleton.
CC At high concentrations, profilin prevents the polymerization of actin,
CC whereas it enhances it at low concentrations. By binding to PIP2, it
CC inhibits the formation of IP3 and DG.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; L27485; AAA27710.1; -; mRNA.
DR PIR; B48405; B48405.
DR PDB; 1PRQ; X-ray; 2.50 A; A=2-126.
DR PDB; 2PRF; NMR; -; A=2-126.
DR PDBsum; 1PRQ; -.
DR PDBsum; 2PRF; -.
DR AlphaFoldDB; P68696; -.
DR BMRB; P68696; -.
DR SMR; P68696; -.
DR VEuPathDB; AmoebaDB:ACA1_396950; -.
DR EvolutionaryTrace; P68696; -.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003785; F:actin monomer binding; IMP:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR CDD; cd00148; PROF; 1.
DR InterPro; IPR005455; PFN.
DR InterPro; IPR036140; PFN_sf.
DR InterPro; IPR027310; Profilin_CS.
DR PANTHER; PTHR11604; PTHR11604; 1.
DR Pfam; PF00235; Profilin; 1.
DR PRINTS; PR00392; PROFILIN.
DR PRINTS; PR01640; PROFILINPLNT.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
DR PROSITE; PS00414; PROFILIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Methylation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3881427"
FT CHAIN 2..126
FT /note="Profilin-1A"
FT /id="PRO_0000199583"
FT REGION 2..36
FT /note="Actin binding"
FT /evidence="ECO:0000255"
FT SITE 116
FT /note="Actin binding"
FT MOD_RES 104
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:1751969"
FT CONFLICT 2
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 5
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 32..33
FT /note="TS -> SF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:1PRQ"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1PRQ"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1PRQ"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:1PRQ"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1PRQ"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:1PRQ"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1PRQ"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1PRQ"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:1PRQ"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:1PRQ"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1PRQ"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:1PRQ"
FT HELIX 107..123
FT /evidence="ECO:0007829|PDB:1PRQ"
SQ SEQUENCE 126 AA; 13084 MW; 69EA51991FE3D58B CRC64;
MSWQTYVDTN LVGTGAVTQA AILGLDGNTW ATSAGFAVTP AQGQTLASAF NNADPIRASG
FDLAGVHYVT LRADDRSIYG KKGSAGVITV KTSKSILVGV YNEKIQPGTA ANVVEKLADY
LIGQGF
