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Protein

Profilin-5

Gene

PRO5

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 5 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. Has a high affinity for poly-proline.

GO - Molecular functioni

  • actin monomer binding Source: AgBase
  • phosphatidylinositol-4,5-bisphosphate binding Source: AgBase
  • proline-rich region binding Source: AgBase

GO - Biological processi

  • nuclear migration Source: AgBase
  • phospholipase C-inhibiting G-protein coupled receptor signaling pathway Source: AgBase
  • regulation of actin cytoskeleton organization Source: AgBase
  • sequestering of actin monomers Source: AgBase

Keywordsi

Molecular functionActin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Profilin-5
Alternative name(s):
Pollen allergen Zea m 12
ZmPRO5
Allergen: Zea m 12
Gene namesi
Name:PRO5
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Chromosome 9

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3533. Zea m 12.0105.
682. Zea m 12.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001996502 – 131Profilin-5Add BLAST130

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi13 ↔ 115Curated
Modified residuei111PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylated by MAP kinases.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ9FR39.
PRIDEiQ9FR39.

Expressioni

Tissue specificityi

Expressed in vegetative cells.

Gene expression databases

ExpressionAtlasiQ9FR39. baseline and differential.
GenevisibleiQ9FR39. ZM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • actin monomer binding Source: AgBase
  • proline-rich region binding Source: AgBase

Protein-protein interaction databases

STRINGi4577.GRMZM5G877388_P02.

Structurei

Secondary structure

1131
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 10Combined sources8
Beta strandi21 – 27Combined sources7
Beta strandi32 – 35Combined sources4
Helixi46 – 55Combined sources10
Turni57 – 59Combined sources3
Helixi60 – 63Combined sources4
Beta strandi65 – 67Combined sources3
Beta strandi70 – 78Combined sources9
Turni79 – 81Combined sources3
Beta strandi82 – 87Combined sources6
Beta strandi90 – 96Combined sources7
Beta strandi98 – 106Combined sources9
Helixi112 – 129Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FEFX-ray2.20A1-131[»]
ProteinModelPortaliQ9FR39.
SMRiQ9FR39.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi81 – 97Involved in PIP2 interactionAdd BLAST17

Sequence similaritiesi

Belongs to the profilin family.Curated

Phylogenomic databases

eggNOGiKOG1755. Eukaryota.
ENOG41126PD. LUCA.
HOGENOMiHOG000171591.
KOiK05759.
OMAiKKSNMAL.
OrthoDBiEOG09360WEB.

Family and domain databases

CDDicd00148. PROF. 1 hit.
InterProiView protein in InterPro
IPR005455. PFN.
IPR036140. PFN_sf.
IPR027310. Profilin_CS.
PANTHERiPTHR11604. PTHR11604. 1 hit.
PfamiView protein in Pfam
PF00235. Profilin. 1 hit.
PRINTSiPR00392. PROFILIN.
PR01640. PROFILINPLNT.
SMARTiView protein in SMART
SM00392. PROF. 1 hit.
SUPFAMiSSF55770. SSF55770. 1 hit.
PROSITEiView protein in PROSITE
PS00414. PROFILIN. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9FR39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWQAYVDDH LLCDIEGQHL SAAAIVGHDG SVWAQSENFP ELKPEEVAGM
60 70 80 90 100
IKDFDEPGTL APTGLFVGGT KYMVIQGEPG VVIRGKKGTG GITIKKTGMS
110 120 130
LIIGIYDEPM TPGQCNMVVE RLGDYLIEQG F
Length:131
Mass (Da):14,114
Last modified:March 1, 2001 - v1
Checksum:i0FCCD16023DA1944
GO

Polymorphismi

Several isoforms of the allergen exist due to polymorphism.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF201459 mRNA. Translation: AAG35601.1.
RefSeqiNP_001105622.1. NM_001112152.1.
UniGeneiZm.23253.
Zm.567.

Genome annotation databases

EnsemblPlantsiZm00001d045323_T008; Zm00001d045323_P008; Zm00001d045323.
Zm00001d045323_T009; Zm00001d045323_P009; Zm00001d045323.
GeneIDi542625.
GrameneiZm00001d045323_T008; Zm00001d045323_P008; Zm00001d045323.
Zm00001d045323_T009; Zm00001d045323_P009; Zm00001d045323.
KEGGizma:542625.

Similar proteinsi

Entry informationi

Entry nameiPROF5_MAIZE
AccessioniPrimary (citable) accession number: Q9FR39
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: March 1, 2001
Last modified: October 25, 2017
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families