ID A0A1R3H9E7_COCAP Unreviewed; 214 AA.
AC A0A1R3H9E7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=Profilin {ECO:0000256|RuleBase:RU003909};
GN ORFNames=CCACVL1_20953 {ECO:0000313|EMBL:OMO66893.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO66893.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO66893.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO66893.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|RuleBase:RU003908}.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio. {ECO:0000256|RuleBase:RU003908}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the profilin family.
CC {ECO:0000256|ARBA:ARBA00010058, ECO:0000256|RuleBase:RU003909}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO66893.1}.
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DR EMBL; AWWV01012470; OMO66893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3H9E7; -.
DR STRING; 210143.A0A1R3H9E7; -.
DR Gramene; OMO66893; OMO66893; CCACVL1_20953.
DR OrthoDB; 421374at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:TreeGrafter.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003785; F:actin monomer binding; IEA:TreeGrafter.
DR CDD; cd00148; PROF; 1.
DR FunFam; 3.30.450.30:FF:000001; Profilin; 1.
DR Gene3D; 3.30.450.30; Dynein light chain 2a, cytoplasmic; 1.
DR InterPro; IPR005050; Enod93.
DR InterPro; IPR048278; PFN.
DR InterPro; IPR005455; PFN_euk.
DR InterPro; IPR036140; PFN_sf.
DR InterPro; IPR027310; Profilin_CS.
DR PANTHER; PTHR11604; PROFILIN; 1.
DR PANTHER; PTHR11604:SF0; PROFILIN; 1.
DR Pfam; PF03386; ENOD93; 1.
DR Pfam; PF00235; Profilin; 1.
DR PRINTS; PR00392; PROFILIN.
DR PRINTS; PR01640; PROFILINPLNT.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; Profilin (actin-binding protein); 1.
DR PROSITE; PS00414; PROFILIN; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW ECO:0000256|RuleBase:RU003909}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|RuleBase:RU003908}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 136..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 214 AA; 22774 MW; AE546ABEE6387DF8 CRC64;
MSWQAYVDDH LMCDIDGLHL TAAAIIGHDG TVWAQSATFP AFTPQEINAI VNDFAEPGSL
APTGLFLGGV KYMVIQGEPG AVIRGKKGAG GVTVKKTNQA LIIGIYDEPM TPGQCNMIVE
RLDERRLRAA RFSQEGILAG LKAAAITAVV SAVPTLIAVR KIPWAKANLN HTAQALIISG
ASIAAYFITV DKTVLESARS YSRAQLDKTE DPKA
//