ID   PROF_CITLA              Reviewed;         131 AA.
AC   Q5XWE1;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Profilin {ECO:0000255|RuleBase:RU003909, ECO:0000303|PubMed:12642849, ECO:0000303|PubMed:19295232, ECO:0000303|PubMed:20484919};
DE   AltName: Allergen=Citr l 2.0101 {ECO:0000305};
OS   Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Citrullus.
OX   NCBI_TaxID=3654 {ECO:0000312|EMBL:AAU43733.1};
RN   [1] {ECO:0000312|EMBL:AAU43733.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 72-84 AND 122-131,
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX   PubMed=20484919; DOI=10.1159/000314361;
RA   Cases B., Pastor-Vargas C., Dones F.G., Perez-Gordo M., Maroto A.S.,
RA   de las Heras M., Vivanco F., Cuesta-Herranz J.;
RT   "Watermelon profilin: characterization of a major allergen as a model for
RT   plant-derived food profilins.";
RL   Int. Arch. Allergy Immunol. 153:215-222(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 72-84 AND 122-131, IDENTIFICATION BY MASS SPECTROMETRY,
RP   AND ALLERGEN.
RX   PubMed=19295232; DOI=10.1159/000205574;
RA   Pastor C., Cuesta-Herranz J., Cases B., Perez-Gordo M., Figueredo E.,
RA   de las Heras M., Vivanco F.;
RT   "Identification of major allergens in watermelon.";
RL   Int. Arch. Allergy Immunol. 149:291-298(2009).
RN   [3]
RP   ALLERGEN.
RX   PubMed=12642849; DOI=10.1067/mai.2003.74;
RA   Rodriguez-Perez R., Crespo J.F., Rodriguez J., Salcedo G.;
RT   "Profilin is a relevant melon allergen susceptible to pepsin digestion in
RT   patients with oral allergy syndrome.";
RL   J. Allergy Clin. Immunol. 111:634-639(2003).
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 similarity). Has a
CC       high affinity for poly-proline (PubMed:20484919).
CC       {ECO:0000250|UniProtKB:Q9FR39, ECO:0000269|PubMed:20484919}.
CC   -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC       actin in a 1:1 ratio. {ECO:0000255|RuleBase:RU003908}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P35081}.
CC   -!- ALLERGEN: Causes an allergic reaction in human (PubMed:20484919,
CC       PubMed:19295232, PubMed:12642849). Binds to IgE of patients allergic to
CC       melon (Cucumis melo) (PubMed:12642849). Binds to IgE of patients with
CC       oral allergy symptoms and pollen allergy to watermelon
CC       (PubMed:20484919, PubMed:19295232). Binds to IgE in 100% of the 17
CC       patients tested (PubMed:20484919). Binds to IgE in 56% of the 23
CC       patients tested. IgE-binding is lost by digestion with pepsin
CC       (PubMed:19295232). Induces degranulation of human basophils
CC       (PubMed:20484919). {ECO:0000269|PubMed:12642849,
CC       ECO:0000269|PubMed:19295232, ECO:0000269|PubMed:20484919}.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000255,
CC       ECO:0000255|RuleBase:RU003909}.
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; AY730591; AAU43733.1; -; mRNA.
DR   AlphaFoldDB; Q5XWE1; -.
DR   SMR; Q5XWE1; -.
DR   Allergome; 11978; Citr l 2.0101.
DR   Allergome; 984; Citr l 2.
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:0070064; F:proline-rich region binding; 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;
KW   Direct protein sequencing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P84177"
FT   CHAIN           2..131
FT                   /note="Profilin"
FT                   /id="PRO_0000450612"
FT   CONFLICT        127
FT                   /note="I -> V (in Ref. 1; AA sequence and 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   131 AA;  14079 MW;  42858AE060F9825E CRC64;
     MSWQAYVDDH LMCEIEGNHL TSAAIIGQDG SVWAKSENFP QLKPEEITGI LNDFNEPGTL
     APTGLYIGGS KYMVIQGEPG AVIRGKKGPG GVTVKKTALA LVIGIYDEPM TPGQCNMIVE
     RLGDYLIEQG L