ACT_KOMPG
ID ACT_KOMPG Reviewed; 376 AA.
AC Q9P4D1; C4R3Y1;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Actin;
GN Name=ACT1; OrderedLocusNames=PAS_chr3_1169;
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10923020;
RX DOI=10.1002/1097-0061(200008)16:11<979::aid-yea594>3.0.co;2-c;
RA Payne W.E., Kaiser C.A., Bevis B.J., Soderholm J., Fu D., Sears I.B.,
RA Glick B.S.;
RT "Isolation of Pichia pastoris genes involved in ER-to-Golgi transport.";
RL Yeast 16:979-993(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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 -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; AF216956; AAF27627.1; -; Genomic_DNA.
DR EMBL; FN392321; CAY70252.1; -; Genomic_DNA.
DR RefSeq; XP_002492446.1; XM_002492401.1.
DR PDB; 4PL7; X-ray; 2.30 A; A/B=2-376.
DR PDBsum; 4PL7; -.
DR AlphaFoldDB; Q9P4D1; -.
DR SMR; Q9P4D1; -.
DR STRING; 644223.Q9P4D1; -.
DR PRIDE; Q9P4D1; -.
DR EnsemblFungi; CAY70252; CAY70252; PAS_chr3_1169.
DR GeneID; 8200200; -.
DR KEGG; ppa:PAS_chr3_1169; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; Q9P4D1; -.
DR OMA; PNIMVGM; -.
DR Proteomes; UP000000314; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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;
KW Reference proteome.
FT CHAIN 1..376
FT /note="Actin"
FT /id="PRO_0000088991"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:4PL7"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:4PL7"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:4PL7"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:4PL7"
FT HELIX 360..365
FT /evidence="ECO:0007829|PDB:4PL7"
SQ SEQUENCE 376 AA; 41691 MW; D94BFF302B345884 CRC64;
MDGEDVAALV IDNGSGMCKA GYAGDDAPHT VFPSVVGRPR HQGVMVGMGQ KDSFVGDEAQ
SKRGILTLRY PIEHGIVTNW DDMEKIWHHT FYNELRLAPE EHPVLLTEAP MNPKSNREKM
TQIMFETFNV PAFYVSIQAV LSLYASGRTT GIVLDSGDGV THVVPIYAGF SLPHAILRID
LAGRDLTDYL MKILSERGYT FSTSAEREIV RDIKEKLCYV ALDFDQELQT SSQSSSIEKS
YELPDGQVIT IGNERFRAPE ALFHPSVLGL EASGIDQTTY NSIMKCDVDV RKELYSNIVM
SGGTTMFPGI AERMQKELTA LAPSSMKVKI SAPPERKYSV WIGGSILASL GTFQQMWISK
QEYDESGPSI VHLKCF
