ID   PROF_CUCME              Reviewed;         131 AA.
AC   Q5FX67; Q5FX66;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Profilin;
DE   AltName: Full=Pollen allergen Cuc m 2;
DE   AltName: Allergen=Cuc m 2;
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX   PubMed=16153305; DOI=10.1186/1476-7961-3-13;
RA   Sankian M., Varasteh A., Pazouki N., Mahmoudi M.;
RT   "Sequence homology: a poor predictive value for profilins cross-
RT   reactivity.";
RL   Clin. Mol. Allergy 3:13-13(2005).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-131, AND ALLERGEN.
RX   PubMed=31326654; DOI=10.1016/j.molimm.2019.07.004;
RA   Kapingidza A.B., Pye S.E., Hyduke N., Dolamore C., Pote S.,
RA   Schlachter C.R., Commins S.P., Kowal K., Chruszcz M.;
RT   "Comparative structural and thermal stability studies of Cuc m 2.0101, Art
RT   v 4.0101 and other allergenic profilins.";
RL   Mol. Immunol. 114:19-29(2019).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC       actin in a 1:1 ratio.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. This is a
CC       pollen allergen. {ECO:0000269|PubMed:16153305,
CC       ECO:0000269|PubMed:31326654}.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR   EMBL; AY879597; AAW69549.1; -; mRNA.
DR   EMBL; AY879598; AAW69550.1; -; mRNA.
DR   RefSeq; NP_001284474.1; NM_001297545.1.
DR   PDB; 6MBX; X-ray; 2.40 A; A/B/C=2-131.
DR   PDBsum; 6MBX; -.
DR   AlphaFoldDB; Q5FX67; -.
DR   SMR; Q5FX67; -.
DR   Allergome; 3230; Cuc m 2.0101.
DR   Allergome; 981; Cuc m 2.
DR   GeneID; 103498238; -.
DR   KEGG; cmo:103498238; -.
DR   eggNOG; KOG1755; Eukaryota.
DR   Proteomes; UP000089565; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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   3D-structure; Actin-binding; Allergen; Cytoplasm; Cytoskeleton;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..131
FT                   /note="Profilin"
FT                   /id="PRO_0000199628"
FT   HELIX           3..8
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   TURN            9..11
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   STRAND          21..27
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   HELIX           44..55
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   TURN            57..63
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   STRAND          82..87
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   STRAND          98..106
FT                   /evidence="ECO:0007829|PDB:6MBX"
FT   HELIX           112..128
FT                   /evidence="ECO:0007829|PDB:6MBX"
SQ   SEQUENCE   131 AA;  13924 MW;  DCB90EB85AE1B67B CRC64;
     MSWQVYVDEH LMCEIEGNHL TSAAIIGQDG SVWAQSQNFP QLKPEEVAGI VGDFADPGTL
     APTGLYIGGT KYMVIQGEPG AVIRGKKGPG GATVKKTGMA LVIGIYDEPM TPGQCNMIVE
     RLGDYLIDQG L