ID   PROF2_ACACA             Reviewed;         126 AA.
AC   P19984;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Profilin-2;
DE   AltName: Full=Basic profilin;
DE   AltName: Full=Profilin II;
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, AND METHYLATION AT LYS-104.
RX   PubMed=3338456; DOI=10.1111/j.1432-1033.1988.tb13739.x;
RA   Ampe C., Sato M., Pollard T.D., Vandekerckhove J.;
RT   "The primary structure of the basic isoform of Acanthamoeba profilin.";
RL   Eur. J. Biochem. 170:597-601(1988).
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 (2.8 ANGSTROMS).
RX   PubMed=8078936; DOI=10.1073/pnas.91.18.8636;
RA   Fedorov A.A., Magnus K.A., Graupe M.H., Lattman E.E., Pollard T.D.,
RA   Almo S.C.;
RT   "X-ray structures of isoforms of the actin-binding protein profilin that
RT   differ in their affinity for phosphatidylinositol phosphates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:8636-8640(1994).
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; L27486; AAA27711.1; -; mRNA.
DR   PIR; A48405; FAAX2.
DR   PDB; 1F2K; X-ray; 2.30 A; A/B=2-126.
DR   PDB; 2ACG; X-ray; 2.50 A; A=2-126.
DR   PDBsum; 1F2K; -.
DR   PDBsum; 2ACG; -.
DR   AlphaFoldDB; P19984; -.
DR   SMR; P19984; -.
DR   VEuPathDB; AmoebaDB:ACA1_066130; -.
DR   EvolutionaryTrace; P19984; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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:3338456"
FT   CHAIN           2..126
FT                   /note="Profilin-2"
FT                   /id="PRO_0000199585"
FT   SITE            116
FT                   /note="Actin binding"
FT   MOD_RES         2
FT                   /note="Blocked amino end (Ser)"
FT   MOD_RES         104
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:1751969,
FT                   ECO:0000269|PubMed:3338456"
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   HELIX           3..8
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   TURN            9..11
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   STRAND          18..24
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   STRAND          29..32
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   HELIX           40..51
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   HELIX           54..59
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   STRAND          66..82
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   STRAND          93..101
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   HELIX           107..122
FT                   /evidence="ECO:0007829|PDB:1F2K"
FT   TURN            123..125
FT                   /evidence="ECO:0007829|PDB:1F2K"
SQ   SEQUENCE   126 AA;  13057 MW;  2EE3B61A0B3DA9A4 CRC64;
     MSWQTYVDTN LVGTGAVTQA AIIGHDGNTW ATSAGFAVSP ANGAALANAF KDATAIRSNG
     FELAGTRYVT IRADDRSVYG KKGSAGVITV KTSKAILIGV YNEKIQPGTA ANVVEKLADY
     LIGQGF