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Q42449 (PROF1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Profilin-1
Alternative name(s):
Allergen=Ara t 8
Gene names
Name:PRO1
Synonyms:PFN1, PRF1
Ordered Locus Names:At2g19760
ORF Names:F6F22.21
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length131 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity.

Subunit structure

Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio.

Subcellular location

Cytoplasmcytoskeleton By similarity.

Tissue specificity

Ubiquitous.

Allergenic properties

Causes an allergic reaction in human.

Sequence similarities

Belongs to the profilin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 131131Profilin-1
PRO_0000199615

Secondary structure

....................... 131
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q42449 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 84212D4681F83F51

FASTA13114,266
        10         20         30         40         50         60 
MSWQSYVDDH LMCDVEGNHL TAAAILGQDG SVWAQSAKFP QLKPQEIDGI KKDFEEPGFL 

        70         80         90        100        110        120 
APTGLFLGGE KYMVIQGEQG AVIRGKKGPG GVTIKKTNQA LVFGFYDEPM TGGQCNLVVE 

       130 
RLGDYLIESE L 

« Hide

References

« Hide 'large scale' references
[1]"Arabidopsis profilins are functionally similar to yeast profilins: identification of a vascular bundle-specific profilin and a pollen-specific profilin."
Christensen H.E.M., Ramachandran S., Tan C.T., Surana U., Dong C.H., Chua N.-H.
Plant J. 10:269-279(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: cv. Columbia.
[2]"The Arabidopsis profilin gene family. Evidence for an ancient split between constitutive and pollen-specific profilin genes."
Huang S., McDowell J.M., Weise M.J., Meagher R.B.
Plant Physiol. 111:115-126(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: cv. Columbia.
[3]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"The crystal structure of a major allergen from plants."
Thorn K.S., Christensen H.E.M., Shigeta R. Jr., Hudler D. Jr., Shalaby L., Lindnerg U., Chua N.-H., Schutt C.E.
Structure 5:19-32(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43325 mRNA. Translation: AAB39480.1.
U43322 Genomic DNA. Translation: AAB39476.1.
U43593 Genomic DNA. Translation: AAG10090.1.
U43590 mRNA. Translation: AAB46750.1.
AC005169 Genomic DNA. Translation: AAC62140.1.
CP002685 Genomic DNA. Translation: AEC06923.1.
AY072427 mRNA. Translation: AAL62419.1.
BT000264 mRNA. Translation: AAN15583.1.
PIRG84580.
RefSeqNP_179566.1. NM_127534.2.
UniGeneAt.23712.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0KX-ray2.20A1-131[»]
1PLMmodel-A2-131[»]
3NULX-ray1.60A2-131[»]
ProteinModelPortalQ42449.
SMRQ42449. Positions 2-131.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1850. 1 interaction.
IntActQ42449. 1 interaction.
STRING3702.AT2G19760.1-P.

Proteomic databases

PaxDbQ42449.
PRIDEQ42449.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G19760.1; AT2G19760.1; AT2G19760.
GeneID816495.
KEGGath:AT2G19760.

Organism-specific databases

TAIRAT2G19760.

Phylogenomic databases

eggNOGNOG277929.
HOGENOMHOG000171591.
InParanoidQ42449.
KOK05759.
OMAKKDFEEP.
PhylomeDBQ42449.

Gene expression databases

GenevestigatorQ42449.

Family and domain databases

InterProIPR027310. Profilin_CS.
IPR005455. Profilin_eukaryotes/bac.
[Graphical view]
PANTHERPTHR11604. PTHR11604. 1 hit.
PfamPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSPR00392. PROFILIN.
PR01640. PROFILINPLNT.
SMARTSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMSSF55770. SSF55770. 1 hit.
PROSITEPS00414. PROFILIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ42449.

Entry information

Entry namePROF1_ARATH
AccessionPrimary (citable) accession number: Q42449
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 14, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

Allergens

Nomenclature of allergens and list of entries