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PROF2_LOKSG
ID   PROF2_LOKSG             Reviewed;         134 AA.
AC   A0A0F8XMN8;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Loki profilin-2 {ECO:0000303|PubMed:30283132};
GN   ORFNames=Lokiarch_27400;
OS   Lokiarchaeum sp. (strain GC14_75).
OC   Archaea; Asgard group; Candidatus Lokiarchaeota; Lokiarchaeum;
OC   unclassified Lokiarchaeum.
OX   NCBI_TaxID=1538547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GC14_75;
RX   PubMed=25945739; DOI=10.1038/nature14447;
RA   Spang A., Saw J.H., Jorgensen S.L., Zaremba-Niedzwiedzka K., Martijn J.,
RA   Lind A.E., van Eijk R., Schleper C., Guy L., Ettema T.J.;
RT   "Complex archaea that bridge the gap between prokaryotes and eukaryotes.";
RL   Nature 521:173-179(2015).
RN   [2] {ECO:0007744|PDB:5ZZB}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH RABBIT ACTIN,
RP   FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND DOMAIN.
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   -!- DOMAIN: The Loki loop (specific to some members) becomes ordered on
CC       binding to rabbit actin. {ECO:0000305|PubMed:30283132}.
CC   -!- MISCELLANEOUS: It is not clear if Loki profilins 1, 2 and 3 are from
CC       the same strain. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Asgard profilin family. {ECO:0000305}.
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DR   EMBL; JYIM01000257; KKK43364.1; -; Genomic_DNA.
DR   PDB; 5ZZB; X-ray; 2.30 A; A/C=1-134.
DR   PDBsum; 5ZZB; -.
DR   AlphaFoldDB; A0A0F8XMN8; -.
DR   SMR; A0A0F8XMN8; -.
DR   EnsemblBacteria; KKK43364; KKK43364; Lokiarch_27400.
DR   KEGG; loki:Lokiarch_27400; -.
DR   Proteomes; UP000034722; 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; IPR005455; PFN.
DR   InterPro; IPR036140; PFN_sf.
DR   Pfam; PF00235; Profilin; 1.
DR   SUPFAM; SSF55770; SSF55770; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Cytoplasm; Cytoskeleton.
FT   CHAIN           1..134
FT                   /note="Loki profilin-2"
FT                   /id="PRO_0000450550"
FT   REGION          55..62
FT                   /note="Loki loop"
FT                   /evidence="ECO:0000269|PubMed:30283132"
FT   HELIX           3..15
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   STRAND          19..25
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   STRAND          29..34
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   HELIX           44..51
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   STRAND          70..77
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   STRAND          82..85
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   STRAND          92..99
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   STRAND          102..110
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   HELIX           116..119
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   HELIX           120..129
FT                   /evidence="ECO:0007829|PDB:5ZZB"
FT   TURN            130..133
FT                   /evidence="ECO:0007829|PDB:5ZZB"
SQ   SEQUENCE   134 AA;  14622 MW;  01DEEF58943492B2 CRC64;
     MSEKIEGIID DLLNVEENAD AIAIIGKDGQ IVTQTENWNV SNDLEIINEL LNEKLALGEK
     GITSLSIQGI KYMIVENTEE RKIGTNITGK GHVLICPIPI GGPGALIAYV NPRAGPRDLL
     FNVQEYAKKL INLI
 
 
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