PROF5_MAIZE
ID PROF5_MAIZE Reviewed; 131 AA.
AC Q9FR39; B4FV68;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Profilin-5 {ECO:0000303|PubMed:10760246};
DE Short=ZmPRO5 {ECO:0000303|PubMed:10760246};
DE AltName: Full=Double B-box zinc finger protein 11;
DE AltName: Full=Pollen allergen Zea m 12 {ECO:0000303|PubMed:27586352};
DE AltName: Allergen=Zea m 12 {ECO:0000303|PubMed:27586352};
GN Name=PRO5 {ECO:0000303|PubMed:10760246}; Synonyms=DBB11, PRF5;
GN ORFNames=ZEAMMB73_Zm00001d045323 {ECO:0000312|EMBL:AQL02054.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, ACTIVITY
RP REGULATION, POLYMORPHISM, AND CHARACTERIZATION.
RC STRAIN=cv. B73;
RX PubMed=10760246; DOI=10.2307/3871071;
RA Kovar D.R., Droebak B.K., Staiger C.J.;
RT "Maize profilin isoforms are functionally distinct.";
RL Plant Cell 12:583-598(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73; TISSUE=Seedling;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [5]
RP MUTAGENESIS OF TYR-6; ASP-8 AND LYS-86.
RX PubMed=11485551; DOI=10.1042/0264-6021:3580049;
RA Kovar D.R., Droebak B.K., Collings D.A., Staiger C.J.;
RT "The characterization of ligand-specific maize (Zea mays) profilin
RT mutants.";
RL Biochem. J. 358:49-57(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), SUBUNIT, AND ALLERGEN.
RX PubMed=27586352; DOI=10.1038/srep32552;
RA Mares-Mejia I., Martinez-Caballero S., Garay-Canales C., Cano-Sanchez P.,
RA Torres-Larios A., Lara-Gonzalez S., Ortega E., Rodriguez-Romero A.;
RT "Structural insights into the IgE mediated responses induced by the
RT allergens Hev b 8 and Zea m 12 in their dimeric forms.";
RL Sci. Rep. 6:32552-32552(2016).
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. Has a high affinity for poly-
CC proline. {ECO:0000269|PubMed:10760246}.
CC -!- ACTIVITY REGULATION: Actin binding is enhanced by calcium Ca(2+).
CC {ECO:0000269|PubMed:10760246}.
CC -!- SUBUNIT: Multimer (PubMed:27586352). Occurs in many kinds of cells as a
CC complex with monomeric actin in a 1:1 ratio (By similarity).
CC {ECO:0000250|UniProtKB:P35081, ECO:0000269|PubMed:27586352}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P35081}.
CC -!- TISSUE SPECIFICITY: Expressed in vegetative tissues. Present in shoots,
CC roots and coleoptiles. Also detected in endosperm and pollen.
CC {ECO:0000269|PubMed:10760246}.
CC -!- PTM: Phosphorylated by MAP kinases. {ECO:0000250|UniProtKB:P35081}.
CC -!- POLYMORPHISM: Several isoforms of the allergen exist due to
CC polymorphism. {ECO:0000305|PubMed:10760246}.
CC -!- ALLERGEN: Causes an allergic reaction in human (Probable). Dimerization
CC considerably increases the IgE-mediated degranulation in rat basophilic
CC leukemia cells (PubMed:27586352). {ECO:0000269|PubMed:27586352,
CC ECO:0000305|PubMed:27586352}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; AF201459; AAG35601.1; -; mRNA.
DR EMBL; CM000785; AQL02054.1; -; Genomic_DNA.
DR EMBL; CM000785; AQL02058.1; -; Genomic_DNA.
DR EMBL; EU952424; ACG24542.1; -; mRNA.
DR EMBL; EU958791; ACG30909.1; -; mRNA.
DR EMBL; EU959080; ACG31198.1; -; mRNA.
DR EMBL; EU960195; ACG32313.1; -; mRNA.
DR EMBL; EU967239; ACG39357.1; -; mRNA.
DR EMBL; BT041006; ACF86011.1; -; mRNA.
DR RefSeq; NP_001105622.1; NM_001112152.1.
DR PDB; 5FEF; X-ray; 2.20 A; A=1-131.
DR PDBsum; 5FEF; -.
DR AlphaFoldDB; Q9FR39; -.
DR SMR; Q9FR39; -.
DR STRING; 4577.GRMZM5G877388_P02; -.
DR Allergome; 3533; Zea m 12.0105.
DR Allergome; 682; Zea m 12.
DR PaxDb; Q9FR39; -.
DR PRIDE; Q9FR39; -.
DR EnsemblPlants; Zm00001eb376740_T001; Zm00001eb376740_P001; Zm00001eb376740.
DR GeneID; 542625; -.
DR Gramene; Zm00001eb376740_T001; Zm00001eb376740_P001; Zm00001eb376740.
DR KEGG; zma:542625; -.
DR MaizeGDB; 314492; -.
DR eggNOG; KOG1755; Eukaryota.
DR HOGENOM; CLU_120772_0_1_1; -.
DR OMA; WASSEGF; -.
DR OrthoDB; 1428600at2759; -.
DR Proteomes; UP000007305; Chromosome 9.
DR ExpressionAtlas; Q9FR39; baseline and differential.
DR Genevisible; Q9FR39; ZM.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003785; F:actin monomer binding; IMP:AgBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; TAS:AgBase.
DR GO; GO:0070064; F:proline-rich region binding; IMP:AgBase.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IMP:AgBase.
DR GO; GO:0030845; P:phospholipase C-inhibiting G protein-coupled receptor signaling pathway; IDA:AgBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; TAS:AgBase.
DR GO; GO:0042989; P:sequestering of actin monomers; IDA:AgBase.
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 Disulfide bond; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..131
FT /note="Profilin-5"
FT /id="PRO_0000199650"
FT MOTIF 81..97
FT /note="Involved in PIP2 interaction"
FT /evidence="ECO:0000250|UniProtKB:P35081"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ST99"
FT DISULFID 13..115
FT /evidence="ECO:0000250|UniProtKB:A4GDU3"
FT DISULFID 13
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9STB6"
FT MUTAGEN 6
FT /note="Y->F: Increased affinity for poly-(L-proline)
FT (PLP)."
FT /evidence="ECO:0000269|PubMed:11485551"
FT MUTAGEN 6
FT /note="Y->Q: Decreased affinity for poly-(L-proline)
FT (PLP)."
FT /evidence="ECO:0000269|PubMed:11485551"
FT MUTAGEN 8
FT /note="D->A: Increased affinity for PtdIns(4,5)P(2)."
FT /evidence="ECO:0000269|PubMed:11485551"
FT MUTAGEN 86
FT /note="K->A: Strongly decreased affinity for G-actin."
FT /evidence="ECO:0000269|PubMed:11485551"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:5FEF"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:5FEF"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:5FEF"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:5FEF"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:5FEF"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:5FEF"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5FEF"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:5FEF"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:5FEF"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:5FEF"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:5FEF"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:5FEF"
FT HELIX 112..129
FT /evidence="ECO:0007829|PDB:5FEF"
SQ SEQUENCE 131 AA; 14114 MW; 0FCCD16023DA1944 CRC64;
MSWQAYVDDH LLCDIEGQHL SAAAIVGHDG SVWAQSENFP ELKPEEVAGM IKDFDEPGTL
APTGLFVGGT KYMVIQGEPG VVIRGKKGTG GITIKKTGMS LIIGIYDEPM TPGQCNMVVE
RLGDYLIEQG F
