PROFX_ORYSI
ID PROFX_ORYSI Reviewed; 131 AA.
AC P83647; A2Y9G1;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Profilin LP04;
GN ORFNames=OsI_020954;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 57-61 AND 72-79.
RC STRAIN=cv. IR64; TISSUE=Panicle {ECO:0000305};
RA Salekdeh G.H., Bennett J.;
RT "Proteome analysis of rice panicle.";
RL Submitted (JUL-2003) to UniProtKB.
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 -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; CM000131; EAY99721.1; -; Genomic_DNA.
DR AlphaFoldDB; P83647; -.
DR SMR; P83647; -.
DR STRING; 39946.P83647; -.
DR Allergome; 996; Ory s 12.
DR PRIDE; P83647; -.
DR EnsemblPlants; BGIOSGA022333-TA; BGIOSGA022333-PA; BGIOSGA022333.
DR Gramene; BGIOSGA022333-TA; BGIOSGA022333-PA; BGIOSGA022333.
DR HOGENOM; CLU_120772_0_1_1; -.
DR OMA; WAQSSGF; -.
DR Proteomes; UP000007015; Chromosome 6.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IC:Gramene.
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 Actin-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..131
FT /note="Profilin LP04"
FT /id="PRO_0000199660"
SQ SEQUENCE 131 AA; 14133 MW; 83584FF859E6F62C CRC64;
MSWQAYVDDH LMCEIDGNHL TAAAIVGHDG SVWAQSPNFP QYKPEEITGI MKDFDEPGSL
APTGLFLGGT KYMVIQGEPG VVIRGKKGTG GICVKKTGLS LILGIYDEPM TPGQCNMIVE
RLGDYLIEQG C