ID   ABP41_LILDA             Reviewed;         146 AA.
AC   P84994;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Villin-like protein ABP41;
DE   AltName: Full=Calcium-dependent actin-binding protein ABP41;
DE   Flags: Fragments;
OS   Lilium davidii (David's lily).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Lilium.
OX   NCBI_TaxID=82316;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Pollen {ECO:0000269|PubMed:15557101};
RX   PubMed=15557101; DOI=10.1104/pp.104.046326;
RA   Fan X., Hou J., Chen X., Chaudhry F., Staiger C.J., Ren H.;
RT   "Identification and characterization of a Ca2+-dependent actin filament-
RT   severing protein from lily pollen.";
RL   Plant Physiol. 136:3979-3989(2004).
CC   -!- FUNCTION: Ca(2+)-dependent actin filament-severing protein that is
CC       required for pollen tube growth. Probably regulates the dynamics of the
CC       actin cytoskeleton. It can promote the assembly of monomers into
CC       filaments (nucleation) as well as sever filaments already formed.
CC       {ECO:0000269|PubMed:15557101}.
CC   -!- SUBUNIT: Binds to actin. {ECO:0000269|PubMed:15557101}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level).
CC       {ECO:0000269|PubMed:15557101}.
CC   -!- DEVELOPMENTAL STAGE: Detected at high levels at the tube tip during
CC       early pollen germination. In germinated pollen tubes it is localized in
CC       a punctate pattern throughout the cytoplasm but most prominently at the
CC       tip region. {ECO:0000269|PubMed:15557101}.
CC   -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000255}.
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:15557101}.
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DR   AlphaFoldDB; P84994; -.
DR   SMR; P84994; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
DR   GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB.
DR   GO; GO:0051014; P:actin filament severing; IDA:UniProtKB.
DR   GO; GO:0009860; P:pollen tube growth; IDA:UniProtKB.
DR   InterPro; IPR007122; Villin/Gelsolin.
DR   PANTHER; PTHR11977; PTHR11977; 2.
PE   1: Evidence at protein level;
KW   Actin capping; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing.
FT   CHAIN           1..>146
FT                   /note="Villin-like protein ABP41"
FT                   /id="PRO_0000252246"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000303|PubMed:15557101"
FT   NON_CONS        27..28
FT                   /evidence="ECO:0000303|PubMed:15557101"
FT   NON_CONS        38..39
FT                   /evidence="ECO:0000303|PubMed:15557101"
FT   NON_CONS        48..49
FT                   /evidence="ECO:0000303|PubMed:15557101"
FT   NON_CONS        62..63
FT                   /evidence="ECO:0000303|PubMed:15557101"
FT   NON_CONS        71..72
FT                   /evidence="ECO:0000303|PubMed:15557101"
FT   NON_CONS        86..87
FT                   /evidence="ECO:0000303|PubMed:15557101"
FT   NON_CONS        99..100
FT                   /evidence="ECO:0000303|PubMed:15557101"
FT   NON_CONS        108..109
FT                   /evidence="ECO:0000303|PubMed:15557101"
FT   NON_CONS        118..119
FT                   /evidence="ECO:0000303|PubMed:15557101"
FT   NON_CONS        133..134
FT                   /evidence="ECO:0000303|PubMed:15557101"
FT   NON_TER         146
FT                   /evidence="ECO:0000303|PubMed:15557101"
SQ   SEQUENCE   146 AA;  16166 MW;  C27A3862F5BBD5DC CRC64;
     PAFQGVGQRL GTEIESSKDE AATAALKTVE LDAVLGGRTP EEETFETRLY QFNGANSNLQ
     ERALEVLQYL KVMGDPTVTL ETTPGKSAEE FLLDENRPKD VALLDDGRVV EEETMETRLY
     QFNGANSNLG AERSAEEMLL NENRPK