ACTBM_HUMAN
ID ACTBM_HUMAN Reviewed; 375 AA.
AC Q9BYX7; Q562N5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Putative beta-actin-like protein 3;
DE AltName: Full=Kappa-actin;
DE AltName: Full=POTE ankyrin domain family member K;
GN Name=POTEKP; Synonyms=ACTBL3; ORFNames=FKSG30;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang Y.-G., Gong L.;
RT "Cloning and characterization of FKSG30, a novel gene encoding a protein
RT similar to ACTG1.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-186, INTERACTION WITH PFN1 AND
RP PFDN1, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=16824795; DOI=10.1016/j.hepres.2006.05.003;
RA Chang K.-W., Yang P.-Y., Lai H.-Y., Yeh T.-S., Chen T.-C., Yeh C.-T.;
RT "Identification of a novel actin isoform in hepatocellular carcinoma.";
RL Hepatol. Res. 36:33-39(2006).
RN [3]
RP METHYLATION AT LYS-84, AND DEMETHYLATION BY ALKBH4.
RX PubMed=23673617; DOI=10.1038/ncomms2863;
RA Li M.M., Nilsen A., Shi Y., Fusser M., Ding Y.H., Fu Y., Liu B., Niu Y.,
RA Wu Y.S., Huang C.M., Olofsson M., Jin K.X., Lv Y., Xu X.Z., He C.,
RA Dong M.Q., Rendtlew Danielsen J.M., Klungland A., Yang Y.G.;
RT "ALKBH4-dependent demethylation of actin regulates actomyosin dynamics.";
RL Nat. Commun. 4:1832-1832(2013).
CC -!- SUBUNIT: Interacts with PFN1 and PFDN1. Does not interact with PFN2.
CC {ECO:0000269|PubMed:16824795}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in some hepatocellular carcinomas.
CC {ECO:0000269|PubMed:16824795}.
CC -!- PTM: Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or
CC MICAL3) to form methionine sulfoxide promotes actin filament
CC depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The
CC (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin
CC repolymerization (By similarity). {ECO:0000250}.
CC -!- PTM: Monomethylation at Lys-84 (K84me1) regulates actin-myosin
CC interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC is required for maintaining actomyosin dynamics supporting normal
CC cleavage furrow ingression during cytokinesis and cell migration.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AY014272; AAG50355.1; -; mRNA.
DR EMBL; AY970480; AAX82286.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9BYX7; -.
DR SMR; Q9BYX7; -.
DR IntAct; Q9BYX7; 25.
DR MINT; Q9BYX7; -.
DR GlyGen; Q9BYX7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BYX7; -.
DR PhosphoSitePlus; Q9BYX7; -.
DR SwissPalm; Q9BYX7; -.
DR BioMuta; HGNC:30182; -.
DR DMDM; 74739412; -.
DR EPD; Q9BYX7; -.
DR jPOST; Q9BYX7; -.
DR MassIVE; Q9BYX7; -.
DR MaxQB; Q9BYX7; -.
DR PeptideAtlas; Q9BYX7; -.
DR PRIDE; Q9BYX7; -.
DR ProteomicsDB; 79742; -.
DR TopDownProteomics; Q9BYX7; -.
DR GeneCards; POTEKP; -.
DR HGNC; HGNC:30182; POTEKP.
DR MIM; 611266; gene.
DR neXtProt; NX_Q9BYX7; -.
DR InParanoid; Q9BYX7; -.
DR PathwayCommons; Q9BYX7; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q9BYX7; -.
DR Pharos; Q9BYX7; Tdark.
DR PRO; PR:Q9BYX7; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9BYX7; protein.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IBA:GO_Central.
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; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 5: Uncertain;
KW ATP-binding; Cytoplasm; Cytoskeleton; Methylation; Nucleotide-binding;
KW Oxidation; Reference proteome.
FT CHAIN 1..375
FT /note="Putative beta-actin-like protein 3"
FT /id="PRO_0000307865"
FT MOD_RES 44
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 47
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 84
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:23673617"
FT CONFLICT 159
FT /note="F -> V (in Ref. 2; AAX82286)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="R -> P (in Ref. 2; AAX82286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 42016 MW; 98127B88A9983B7D CRC64;
MDDDTAVLVI DNGSGMCKAG FAGDDAPQAV FPSIVGRPRH QGMMEGMHQK ESYVGKEAQS
KRGMLTLKYP MEHGIITNWD DMEKIWHHTF YNELRVAPEE HPILLTEAPL NPKANREKMT
QIMFETFNTP AMYVAIQAVL SLYTSGRTTG IVMDSGDGFT HTVPIYEGNA LPHATLRLDL
AGRELTDYLM KILTERGYRF TTTAEQEIVR DIKEKLCYVA LDSEQEMAMA ASSSSVEKSY
ELPDGQVITI GNERFRCPEA LFQPCFLGME SCGIHKTTFN SIVKSDVDIR KDLYTNTVLS
GGTTMYPGIA HRMQKEITAL APSIMKIKII APPKRKYSVW VGGSILASLS TFQQMWISKQ
EYDESGPSIV HRKCF
