ID   PROF_ODILC              Reviewed;         119 AA.
AC   A0A1Q9N7W7;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Odin profilin {ECO:0000303|PubMed:30283132};
GN   ORFNames=OdinLCB4_14170;
OS   Odinarchaeota archaeon (strain LCB_4).
OC   Archaea; Asgard group; Candidatus Odinarchaeota.
OX   NCBI_TaxID=1841599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCB_4;
RX   PubMed=28077874; DOI=10.1038/nature21031;
RA   Zaremba-Niedzwiedzka K., Caceres E.F., Saw J.H., Backstrom D.,
RA   Juzokaite L., Vancaester E., Seitz K.W., Anantharaman K., Starnawski P.,
RA   Kjeldsen K.U., Scott M.B., Nunoura T., Banfield J.F., Schramm A.,
RA   Baker B.J., Spang A., Ettema T.J.G.;
RT   "Asgard archaea illuminate the origin of eukaryotic cellular complexity.";
RL   Nature 541:353-358(2017).
RN   [2] {ECO:0007744|PDB:5ZZA}
RP   X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) IN COMPLEX WITH RABBIT ACTIN,
RP   FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=30283132; DOI=10.1038/s41586-018-0548-6;
RA   Akil C., Robinson R.C.;
RT   "Genomes of Asgard archaea encode profilins that regulate actin.";
RL   Nature 562:439-443(2018).
CC   -!- FUNCTION: Binds to actin and affects the structure of the cytoskeleton.
CC       At high concentrations inhibits spontaneous rabbit actin nucleation.
CC       This strongly suggests this archaea has a profilin-regulated actin
CC       system, and actin-type genes can be identified in this organism.
CC       {ECO:0000269|PubMed:30283132}.
CC   -!- ACTIVITY REGULATION: Inhibition of rabbit actin polymerization is
CC       reduced by phosphatidylinositol-(4,5)-P2(1,2-dipalmitoyl), a soluble
CC       form of the phospholipid phosphatidylinositol, suggesting an unknown
CC       lipid might regulate actin-profilin interaction in vivo.
CC       {ECO:0000305|PubMed:30283132}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000305|PubMed:30283132}.
CC   -!- SIMILARITY: Belongs to the Asgard profilin family. {ECO:0000305}.
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DR   EMBL; MDVT01000007; OLS18178.1; -; Genomic_DNA.
DR   PDB; 5ZZA; X-ray; 1.53 A; P=1-119.
DR   PDBsum; 5ZZA; -.
DR   AlphaFoldDB; A0A1Q9N7W7; -.
DR   SMR; A0A1Q9N7W7; -.
DR   EnsemblBacteria; OLS18178; OLS18178; OdinLCB4_14170.
DR   Proteomes; UP000186851; Unassembled WGS sequence.
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   InterPro; IPR036140; PFN_sf.
DR   SUPFAM; SSF55770; SSF55770; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Cytoplasm; Cytoskeleton.
FT   CHAIN           1..119
FT                   /note="Odin profilin"
FT                   /id="PRO_0000450553"
FT   HELIX           3..9
FT                   /evidence="ECO:0007829|PDB:5ZZA"
FT   STRAND          15..22
FT                   /evidence="ECO:0007829|PDB:5ZZA"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:5ZZA"
FT   HELIX           38..47
FT                   /evidence="ECO:0007829|PDB:5ZZA"
FT   STRAND          50..54
FT                   /evidence="ECO:0007829|PDB:5ZZA"
FT   STRAND          57..73
FT                   /evidence="ECO:0007829|PDB:5ZZA"
FT   TURN            74..77
FT                   /evidence="ECO:0007829|PDB:5ZZA"
FT   STRAND          78..85
FT                   /evidence="ECO:0007829|PDB:5ZZA"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:5ZZA"
FT   STRAND          89..95
FT                   /evidence="ECO:0007829|PDB:5ZZA"
FT   HELIX           101..116
FT                   /evidence="ECO:0007829|PDB:5ZZA"
SQ   SEQUENCE   119 AA;  12648 MW;  0D1E858346680BAE CRC64;
     MSLEQLAGRL ISGDIGATAV IKMTGEIIYQ SPNWSVDGVH AINVYKNREP SIIIQGVKYS
     VIDVNEDRLI ATNVGGQGHI VGAVAGGKAL LIGYVSPNGD ARTAYIQIDK TARQLSKIL