ACT1_ACACA
ID ACT1_ACACA Reviewed; 375 AA.
AC P02578;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Actin-1;
OS Acanthamoeba castellanii (Amoeba).
OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC Acanthamoebidae; Acanthamoeba.
OX NCBI_TaxID=5755;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6290670; DOI=10.1016/0022-2836(82)90028-6;
RA Nellen W., Gallwitz D.;
RT "Actin genes and actin messenger RNA in Acanthamoeba castellanii.
RT Nucleotide sequence of the split actin gene I.";
RL J. Mol. Biol. 159:1-18(1982).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility and are ubiquitously expressed in all
CC eukaryotic cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Met-1 may be removed after translation.
CC -!- MISCELLANEOUS: There are at least three actin genes in A.castellanii.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; V00002; CAA23399.1; -; Genomic_DNA.
DR PIR; A92886; ATAX.
DR PDB; 4EFH; X-ray; 2.48 A; A=1-375.
DR PDBsum; 4EFH; -.
DR AlphaFoldDB; P02578; -.
DR SMR; P02578; -.
DR ELM; P02578; -.
DR PRIDE; P02578; -.
DR VEuPathDB; AmoebaDB:ACA1_361250; -.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProt.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
FT CHAIN 1..375
FT /note="Actin-1"
FT /id="PRO_0000088884"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:4EFH"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4EFH"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:4EFH"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:4EFH"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:4EFH"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:4EFH"
FT TURN 350..355
FT /evidence="ECO:0007829|PDB:4EFH"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:4EFH"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:4EFH"
SQ SEQUENCE 375 AA; 41676 MW; 5AED1CDC9366795C CRC64;
MGDEVQALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH TGVMVGMGQK DSYVGDEAQS
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVLDSGDGVT HTVPIYEGYA LPHAILRLDL
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMHTA ASSSALEKSY
ELPDGQVITI GNERFRAPEA LFQPSFLGME SAGIHETTYN SIMKCDVDIR KDLYGNVVLS
GGTTMFPGIA DRMQKELTAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKE
EYDESGPSIV HRKCF
