ACT1_AEDAE
ID ACT1_AEDAE Reviewed; 376 AA.
AC P49128; Q17JS1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Actin-1;
DE Flags: Precursor;
GN Name=ACT-1; ORFNames=AAEL001928;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Liverpool / Blackeye;
RX PubMed=8961646; DOI=10.1093/jmedent/33.6.955;
RA Ibrahim M.S., Eisinger S.W., Scott A.L.;
RT "Muscle actin gene from Aedes aegypti (Diptera: Culicidae).";
RL J. Med. Entomol. 33:955-962(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
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: Oxidation of Met-45 to form methionine sulfoxide promotes actin
CC filament depolymerization. Methionine sulfoxide is produced
CC stereospecifically, but it is not known whether the (S)-S-oxide or the
CC (R)-S-oxide is produced (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; U20287; AAA62350.1; -; mRNA.
DR EMBL; CH477231; EAT46902.1; -; Genomic_DNA.
DR RefSeq; XP_001654313.1; XM_001654263.1.
DR AlphaFoldDB; P49128; -.
DR SMR; P49128; -.
DR STRING; 7159.AAEL001928-PA; -.
DR GeneID; 5572986; -.
DR KEGG; aag:5572986; -.
DR VEuPathDB; VectorBase:AAEL001928; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P49128; -.
DR OMA; ERFCASE; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P49128; -.
DR Proteomes; UP000008820; 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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW Oxidation; Reference proteome.
FT PROPEP 1..2
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000604"
FT CHAIN 3..376
FT /note="Actin-1"
FT /id="PRO_0000000605"
FT MOD_RES 3
FT /note="N-acetylaspartate"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 48
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT CONFLICT 4..9
FT /note="EDAAAL -> DDVRRS (in Ref. 1; AAA62350)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="A -> V (in Ref. 1; AAA62350)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="A -> V (in Ref. 1; AAA62350)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="I -> N (in Ref. 1; AAA62350)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..267
FT /note="CPEALFQPSF -> AQKLSSSHPS (in Ref. 1; AAA62350)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41673 MW; F48E3CF5480F3FE2 CRC64;
MCDEDAAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGN KDSYVGDEAQ
SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS
YELPDGQVIT IGNERFRCPE ALFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANTVL
SGGTTMYPGI ADRMQKEITA LAPSSIKIKI IAPPERKYSV WIGGSILASL STFQAMWISK
QEYDESGPAI VHRKCF
