PROF_CROSA
ID PROF_CROSA Reviewed; 131 AA.
AC Q5EF31;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Profilin {ECO:0000303|PubMed:18791282, ECO:0000303|PubMed:19628979};
DE AltName: Full=Pollen allergen Cro s 2 {ECO:0000305};
DE AltName: Allergen=Cro s 2 {ECO:0000303|PubMed:18791282, ECO:0000303|PubMed:19628979};
OS Crocus sativus (Saffron).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Iridaceae;
OC Crocoideae; Croceae; Crocus.
OX NCBI_TaxID=82528;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ALLERGEN.
RC TISSUE=Pollen {ECO:0000303|PubMed:19628979};
RX PubMed=19628979; DOI=10.2332/allergolint.09-oa-0088;
RA Varasteh A.R., Moghadam M., Vahedi F., Kermani T., Sankian M.;
RT "Cloning and expression of the allergen Cro s 2 profilin from saffron
RT (Crocus sativus).";
RL Allergol. Int. 58:429-435(2009).
RN [2]
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=18791282;
RA Sankian M., Glosaz-Shirazi F., Arafi M., Moghadam M., Varasteh A.;
RT "Production and characterization of monoclonal antibody against Saffron
RT pollen profilin, Cro s 2.";
RL Iran. J. Immunol. 5:156-162(2008).
CC -!- FUNCTION: Binds to actin and affects the structure of the cytoskeleton.
CC At high concentrations, profilin prevents the polymerization of actin,
CC whereas it enhances it at low concentrations. By binding to PIP2, it
CC inhibits the formation of IP3 and DG. {ECO:0000250|UniProtKB:P35081}.
CC -!- SUBUNIT: Exists as monomer and tetramer (PubMed:18791282). Occurs in
CC many kinds of cells as a complex with monomeric actin in a 1:1 ratio
CC (By similarity). {ECO:0000250|UniProtKB:P35081,
CC ECO:0000269|PubMed:18791282}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P35081}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level)
CC (PubMed:18791282). Expressed in pollen (PubMed:19628979).
CC {ECO:0000269|PubMed:18791282, ECO:0000269|PubMed:19628979}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of saffron
CC pollen-sensitized patients. {ECO:0000269|PubMed:19628979}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY898658; AAW81034.1; -; mRNA.
DR AlphaFoldDB; Q5EF31; -.
DR SMR; Q5EF31; -.
DR Allergome; 1475; Cro s 2.
DR Allergome; 3222; Cro s 2.0101.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0042989; P:sequestering of actin monomers; ISS:UniProtKB.
DR CDD; cd00148; PROF; 1.
DR InterPro; IPR005455; PFN.
DR InterPro; IPR036140; PFN_sf.
DR InterPro; IPR027310; Profilin_CS.
DR PANTHER; PTHR11604; PTHR11604; 1.
DR Pfam; PF00235; Profilin; 1.
DR PRINTS; PR00392; PROFILIN.
DR PRINTS; PR01640; PROFILINPLNT.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
DR PROSITE; PS00414; PROFILIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Allergen; Cytoplasm; Cytoskeleton; Disulfide bond.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8H2C9"
FT CHAIN 2..131
FT /note="Profilin"
FT /id="PRO_0000199627"
FT DISULFID 13..115
FT /evidence="ECO:0000250|UniProtKB:A4K9Z8"
SQ SEQUENCE 131 AA; 14139 MW; 95D5F1658E906FEB CRC64;
MSWQTYVDEH LMCDMDGHVL TSAAILGHDG SVWAQSAGFP ELKPAEITAI LNDFNEPGSL
APTGMYINGA KYMVIQGEPG VVIRGKKGSG GVTIKKSNMA LIFGLYDEPM TPGQCNLVVE
RLGDYLIEQG Y