P02584 (PROF1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Profilin-1

Alternative name(s):
Profilin I

Gene names

Name:

PFN1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	140 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. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR By similarity.
Subunit structure	Interacts with VASP. Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio. Found in a complex with XPO6, Ran, ACTB and PFN1 By similarity. Interacts with HTT By similarity.
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Phosphorylation at Ser-138 reduces its affinity for G-actin and blocks its interaction with HTT, reducing its ability to inhibit androgen receptor (AR) and HTT aggregation By similarity.
Sequence similarities	Belongs to the profilin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	Actin-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro neural tube closure Inferred from sequence or structural similarity. Source: AgBase regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: AgBase
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: AgBase cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from sequence or structural similarity. Source: AgBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 140

139

Profilin-1

PRO_0000199570

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.3 Ref.4

Modified residue

108

1

N6-acetyllysine By similarity

Modified residue

129

1

Phosphotyrosine By similarity

Modified residue

138

1

Phosphoserine; by ROCK1 By similarity

Cross-link

54

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Secondary structure

1

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140

Helix Strand Turn

Details...

Helix

5 – 12

8

Beta strand

15 – 24

10

Beta strand

26 – 28

3

Beta strand

30 – 34

5

Helix

40 – 42

3

Helix

45 – 51

7

Helix

58 – 62

5

Beta strand

64 – 66

3

Beta strand

69 – 76

8

Turn

81 – 83

3

Beta strand

85 – 90

6

Beta strand

100 – 105

6

Beta strand

107 – 115

9

Helix

121 – 137

17

Sequences

	Sequence		Length	Mass (Da)
	P02584 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E56BFBB5BBB016E3	FASTA	140	15,057
	10 20 30 40 50 60 MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGI LVGKDRSSFF 70 80 90 100 110 120 VNGLTLGGQK CSVIRDSLLQ DGEFTMDLRT KSTGGAPTFN ITVTMTAKTL VLLMGKEGVH 130 140 GGMINKKCYE MASHLRRSQY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.
[3]	"The amino acid sequence of profilin from calf spleen." Nystroem L.-E., Lindberg U., Kendrick-Jones J., Jakes R. FEBS Lett. 101:161-165(1979) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-140, ACETYLATION AT ALA-2. Tissue: Spleen.
[4]	"The primary structure of human platelet profilin: reinvestigation of the calf spleen profilin sequence." Ampe C., Markey F., Lindberg U., Vandekerckhove J. FEBS Lett. 228:17-21(1988) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"The structure of crystalline profilin-beta-actin." Schutt C.E., Myslik J.C., Rozycki M.D., Goonesekere N.C.W., Lindberg U. Nature 365:810-816(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF COMPLEX WITH BETA-ACTIN.
[6]	"The structure of an open state of beta-actin at 2.65-A resolution." Chik J.K., Lindberg U., Schutt C.E. J. Mol. Biol. 263:607-623(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF COMPLEX WITH BETA-ACTIN.
[7]	"Crystallization and structure determination of bovine profilin at 2.0-A resolution." Cedergren-Zeppezauer E.S., Goonesekere N.C., Rozycki M.D., Myslik J.C., Dauter Z., Lindberg U., Schutt C.E. J. Mol. Biol. 240:459-475(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BT021078 mRNA. Translation: AAX09095.1.
BC102240 mRNA. Translation: AAI02241.1.

IPI

IPI00694107.

PIR

FABO. S00308.

RefSeq

NP_001015592.1. NM_001015592.1.

UniGene

Bt.23180.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HLU	X-ray	2.65	P	2-140	[»]
1PNE	X-ray	2.00	A	2-140	[»]
2BTF	X-ray	2.55	P	2-140	[»]
3U4L	X-ray	2.40	P	2-140	[»]
3UB5	X-ray	2.20	P	2-140	[»]

ProteinModelPortal

P02584.

SMR

P02584. Positions 2-140.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17037N.

IntAct

P02584. 1 interaction.

Proteomic databases

PaxDb

P02584.

PRIDE

P02584.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000006465; ENSBTAP00000006465; ENSBTAG00000004915.

GeneID

513895.

KEGG

bta:513895.

Organism-specific databases

CTD

5216.

Phylogenomic databases

eggNOG

NOG269129.

GeneTree

ENSGT00390000010143.

HOGENOM

HOG000171592.

HOVERGEN

HBG053683.

InParanoid

P02584.

KO

K05759.

OMA

HLRRAQY.

OrthoDB

EOG4SN1Q1.

Family and domain databases

InterPro

IPR005454. Profilin_chordates.
IPR027310. Profilin_CS.
IPR005455. Profilin_eukaryotes/bac.
[Graphical view]

Pfam

PF00235. Profilin. 1 hit.
[Graphical view]

PRINTS

PR00392. PROFILIN.
PR01639. PROFILINMAML.

SMART

SM00392. PROF. 1 hit.
[Graphical view]

SUPFAM

SSF55770. Profilin. 1 hit.

PROSITE

PS00414. PROFILIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P02584.

NextBio

20871082.

Entry information

Entry name

PROF1_BOVIN

Accession

Primary (citable) accession number: P02584
Secondary accession number(s): Q3ZCH4, Q5E942

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program