ACTO_ACACA
ID ACTO_ACACA Reviewed; 88 AA.
AC P18281;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Actobindin;
OS Acanthamoeba castellanii (Amoeba).
OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC Acanthamoebidae; Acanthamoeba.
OX NCBI_TaxID=5755;
RN [1]
RP PROTEIN SEQUENCE, ACETYLATION AT MET-1, AND METHYLATION AT LYS-35 AND
RP LYS-72.
RX PubMed=2376577; DOI=10.1016/s0021-9258(19)38230-4;
RA Vandekerckhove J., van Damme J., Vancompernolle K., Bubb M.R.,
RA Lambooy P.K., Korn E.D.;
RT "The covalent structure of Acanthamoeba actobindin.";
RL J. Biol. Chem. 265:12801-12805(1990).
CC -!- FUNCTION: Is able to bind two actin monomers at high concentrations of
CC G-actin.
CC -!- SUBUNIT: Monomer.
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DR PIR; A36614; A36614.
DR AlphaFoldDB; P18281; -.
DR ELM; P18281; -.
DR iPTMnet; P18281; -.
DR VEuPathDB; AmoebaDB:ACA1_256510; -.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR InterPro; IPR016365; Actobindin.
DR InterPro; IPR003124; WH2_dom.
DR Pfam; PF02205; WH2; 1.
DR PIRSF; PIRSF002724; Actobindin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Direct protein sequencing; Methylation.
FT CHAIN 1..88
FT /note="Actobindin"
FT /id="PRO_0000064444"
FT DOMAIN 37..54
FT /note="WH2"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:2376577"
FT MOD_RES 35
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:2376577"
FT MOD_RES 72
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:2376577"
SQ SEQUENCE 88 AA; 9554 MW; E814A5C521603DA6 CRC64;
MNPELQSAIG QGAALKHAET VDKSAPQIEN VTVKKVDRSS FLEEVAKPHE LKHAETVDKS
GPAIPEDVHV KKVDRGAFLS EIEKAAKQ