PROF1_LOKSG
ID PROF1_LOKSG Reviewed; 134 AA.
AC A0A0F8V8L2;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Loki profilin-1 {ECO:0000303|PubMed:30283132};
GN ORFNames=Lokiarch_47830;
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:5YED, ECO:0007744|PDB:5YEE}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) ALONE AND IN COMPLEX WITH RABBIT
RP ACTIN, 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:0000269|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; JYIM01000447; KKK40842.1; -; Genomic_DNA.
DR PDB; 5YED; X-ray; 1.60 A; A=1-134.
DR PDB; 5YEE; X-ray; 1.81 A; A=1-134.
DR PDBsum; 5YED; -.
DR PDBsum; 5YEE; -.
DR AlphaFoldDB; A0A0F8V8L2; -.
DR SMR; A0A0F8V8L2; -.
DR EnsemblBacteria; KKK40842; KKK40842; Lokiarch_47830.
DR KEGG; loki:Lokiarch_47830; -.
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-1"
FT /id="PRO_0000450549"
FT REGION 55..62
FT /note="Loki loop"
FT /evidence="ECO:0000269|PubMed:30283132"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:5YED"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:5YED"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:5YED"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5YED"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:5YED"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5YED"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:5YED"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:5YED"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:5YED"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:5YED"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:5YED"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:5YED"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:5YED"
SQ SEQUENCE 134 AA; 14701 MW; EFCDEE0FE4C4469F CRC64;
MSEKIEGIID DLLNLEENAH GIAIIGKDGK IITQTENWNI SNDLDKLNEF LNEKLALGKK
GITSLSIQGI KYMIVENTEE RKIGTNITGK GHVVICPIPI GGTGALITYV NPRAGPRDVL
FNVQEYAKKL TDLI