ID   DEPA_ASTAM              Reviewed;         150 AA.
AC   P20690;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Depactin;
OS   Asterias amurensis (Northern Pacific seastar).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC   Forcipulatacea; Forcipulatida; Asteriidae; Asterias.
OX   NCBI_TaxID=7602;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Oocyte;
RX   PubMed=3422641; DOI=10.1016/s0021-9258(18)69040-4;
RA   Takagi T., Konishi K., Mabuchi I.;
RT   "Amino acid sequence of starfish oocyte depactin.";
RL   J. Biol. Chem. 263:3097-3102(1988).
CC   -!- FUNCTION: Depactin interacts with actin at some of its 12 N-terminal
CC       residues and 20 C-terminal residues. Binds to actin monomers from
CC       filaments and in solution.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC       {ECO:0000305}.
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DR   PIR; A29916; A29916.
DR   AlphaFoldDB; P20690; -.
DR   SMR; P20690; -.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.20.10; -; 1.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   SMART; SM00102; ADF; 1.
DR   PROSITE; PS51263; ADF_H; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Direct protein sequencing; Repeat.
FT   CHAIN           1..150
FT                   /note="Depactin"
FT                   /id="PRO_0000214941"
FT   DOMAIN          3..148
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
SQ   SEQUENCE   150 AA;  17234 MW;  7B23BCCDE922C0DE CRC64;
     PQSGTALDEN VKEEIRAFKM DQSKVKVPWM LLEIVQNDDR IDVVKVTKKA GPSDNLETLR
     EELKQREVVY FVLDYEPSEE KRAKHNIPKG KTYPLTCFWS METANIKLKM KYSSTVGTLK
     SATSTLKTYL EAHDFDDLSE EAIGDKIKNF