P68696 (PRO1A_ACACA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Profilin-1A Alternative name(s): Acidic profilin IA Profilin IA
Organism	Acanthamoeba castellanii (Amoeba)
Taxonomic identifier	5755 [NCBI]
Taxonomic lineage	Eukaryota › Amoebozoa › Centramoebida › Acanthamoebidae › Acanthamoeba

Protein attributes

Sequence length	126 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
Subunit structure	Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio.
Subcellular location	Cytoplasm › cytoskeleton.
Sequence similarities	Belongs to the profilin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	Actin-binding
PTM	Methylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Inferred from mutant phenotype Ref.3. Source: UniProtKB
Cellular component	actin cytoskeleton Inferred from direct assay Ref.3. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	actin monomer binding Inferred from mutant phenotype Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 126

125

Profilin-1A

PRO_0000199583

Regions

Region

2 – 36

35

Actin-binding Potential

Sites

Binding site

116

1

Actin

Amino acid modifications

Modified residue

104

1

N6,N6,N6-trimethyllysine

Experimental info

Sequence conflict

2

1

S → T AA sequence Ref.2

Sequence conflict

5

1

T → S AA sequence Ref.2

Sequence conflict

32 – 33

2

TS → SF AA sequence Ref.2

Secondary structure

1

.

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126

Helix Strand Turn

Details...

Helix

3 – 8

6

Turn

9 – 11

3

Helix

12 – 14

3

Beta strand

18 – 24

7

Beta strand

29 – 32

4

Helix

40 – 49

10

Helix

54 – 57

4

Beta strand

61 – 63

3

Beta strand

66 – 73

8

Beta strand

75 – 82

8

Beta strand

85 – 91

7

Beta strand

93 – 101

9

Helix

107 – 123

17

Sequences

	Sequence		Length	Mass (Da)
	P68696 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 69EA51991FE3D58B	FASTA	126	13,084
	10 20 30 40 50 60 MSWQTYVDTN LVGTGAVTQA AILGLDGNTW ATSAGFAVTP AQGQTLASAF NNADPIRASG 70 80 90 100 110 120 FDLAGVHYVT LRADDRSIYG KKGSAGVITV KTSKSILVGV YNEKIQPGTA ANVVEKLADY LIGQGF

References

[1]	"Analysis of cDNA clones for Acanthamoeba profilin-I and profilin-II shows end to end homology with vertebrate profilins and a small family of profilin genes." Pollard T.D., Rimm D.L. Cell Motil. Cytoskeleton 20:169-177(1991) [PubMed: 1751969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The amino acid sequence of Acanthamoeba profilin." Ampe C., Vandekerckhove J., Brenner S.L., Tobacman L., Korn E.D. J. Biol. Chem. 260:834-840(1985) [PubMed: 3881427] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-126.
[3]	"Acanthamoeba actin and profilin can be cross-linked between glutamic acid 364 of actin and lysine 115 of profilin." Vandekerckhove J., Kaiser D.A., Pollard T.D. J. Cell Biol. 109:619-626(1989) [PubMed: 2569469] [Abstract] Cited for: CROSS-LINKING TO ACTIN.
[4]	"Crystal packing induces a conformational change in profilin-I from Acanthamoeba castellanii." Liu S., Fedorov A.A., Pollard T.D., Lattman E.E., Almo S.C., Magnus K.A. J. Struct. Biol. 123:22-29(1998) [PubMed: 9774541] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]	"Three-dimensional solution structure of Acanthamoeba profilin-I." Vinson V.K., Archer S.J., Lattman E.E., Pollard T.D., Torchia D.A. J. Cell Biol. 122:1277-1283(1993) [PubMed: 8397216] [Abstract] Cited for: STRUCTURE BY NMR.
[6]	"Secondary structure and topology of Acanthamoeba profilin I as determined by heteronuclear nuclear magnetic resonance spectroscopy." Archer S.J., Vinson V.K., Pollard T.D., Torchia D.A. Biochemistry 32:6680-6687(1993) [PubMed: 8329394] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L27485 mRNA. Translation: AAA27710.1.

PIR

B48405.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PRQ	X-ray	2.50	A	2-126	[»]
2PRF	NMR	-	A	2-126	[»]

ProteinModelPortal

P68696.

SMR

P68696. Positions 2-126.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002097. Profilin.
IPR005455. Profilin_plant.
[Graphical view]

PANTHER

PTHR11604. Profilin_plant. 1 hit.

Pfam

PF00235. Profilin. 1 hit.
[Graphical view]

PRINTS

PR00392. PROFILIN.
PR01640. PROFILINPLNT.

SMART

SM00392. PROF. 1 hit.
[Graphical view]

SUPFAM

SSF55770. Profilin. 1 hit.

PROSITE

PS00414. PROFILIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PRO1A_ACACA

Accession

Primary (citable) accession number: P68696
Secondary accession number(s): P07763

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 30, 2010
This is version 43 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)