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Protein

Profilin-2

Gene

PRO2

Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Profilin-2
Alternative name(s):
Pollen allergen Hev b 8.0102
Allergen: Hev b 8.0102
Gene namesi
Name:PRO2
OrganismiHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifieri3981 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Involved in latex allergic reactions.1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei397. Hev b 8.
399. Hev b 8.0102.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001996342 – 131Profilin-2Add BLAST130

Proteomic databases

PRIDEiQ9STB6.

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1131
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 8Combined sources6
Turni9 – 12Combined sources4
Beta strandi21 – 30Combined sources10
Beta strandi32 – 35Combined sources4
Helixi46 – 53Combined sources8
Turni57 – 59Combined sources3
Helixi60 – 63Combined sources4
Beta strandi65 – 67Combined sources3
Beta strandi70 – 74Combined sources5
Turni79 – 81Combined sources3
Beta strandi82 – 87Combined sources6
Beta strandi90 – 96Combined sources7
Beta strandi98 – 106Combined sources9
Helixi112 – 126Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FDSX-ray1.90A1-131[»]
5FEGX-ray2.80A/B1-131[»]
ProteinModelPortaliQ9STB6.
SMRiQ9STB6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the profilin family.Curated

Family and domain databases

CDDicd00148. PROF. 1 hit.
InterProiIPR005455. PFN.
IPR027310. Profilin_CS.
[Graphical view]
PANTHERiPTHR11604. PTHR11604. 1 hit.
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR00392. PROFILIN.
PR01640. PROFILINPLNT.
SMARTiSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMiSSF55770. SSF55770. 1 hit.
PROSITEiPS00414. PROFILIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9STB6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWQAYVDDH LMCEIEGNHL SAAAIIGQDG SVWAQSANFP QFKSEEITGI
60 70 80 90 100
MSDFHEPGTL APTGLYIGGT KYMVIQGEPG AVIRGKKGPG GVTVKKTNQA
110 120 130
LIIGIYDEPM TPGQCNMIVE RLGDYLIDQG Y
Length:131
Mass (Da):14,151
Last modified:May 1, 2000 - v1
Checksum:i4AC33760CFEDC87D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132397 mRNA. Translation: CAB51914.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132397 mRNA. Translation: CAB51914.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FDSX-ray1.90A1-131[»]
5FEGX-ray2.80A/B1-131[»]
ProteinModelPortaliQ9STB6.
SMRiQ9STB6.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei397. Hev b 8.
399. Hev b 8.0102.

Proteomic databases

PRIDEiQ9STB6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd00148. PROF. 1 hit.
InterProiIPR005455. PFN.
IPR027310. Profilin_CS.
[Graphical view]
PANTHERiPTHR11604. PTHR11604. 1 hit.
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR00392. PROFILIN.
PR01640. PROFILINPLNT.
SMARTiSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMiSSF55770. SSF55770. 1 hit.
PROSITEiPS00414. PROFILIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPROF2_HEVBR
AccessioniPrimary (citable) accession number: Q9STB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.