ID   ACTBL_MOUSE             Reviewed;         376 AA.
AC   Q8BFZ3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Beta-actin-like protein 2;
DE   AltName: Full=Kappa-actin;
GN   Name=Actbl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   OXIDATION AT MET-45 AND MET-48, AND DEOXIDATION AT MET-45 AND MET-48.
RX   PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019;
RA   Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A.,
RA   Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R.,
RA   Gladyshev V.N.;
RT   "MsrB1 and MICALs regulate actin assembly and macrophage function via
RT   reversible stereoselective methionine oxidation.";
RL   Mol. Cell 51:397-404(2013).
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. {ECO:0000250}.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix. Each
CC       actin can bind to 4 others (By similarity). Interacts with PFN1 and
CC       PFDN1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- PTM: Oxidation of Met-45 and Met-48 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. {ECO:0000269|PubMed:23911929}.
CC   -!- PTM: Monomethylation at Lys-85 (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 (By
CC       similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, alpha,
CC       beta and gamma have been identified. The alpha actins are found in
CC       muscle tissues and are a major constituent of the contractile
CC       apparatus. The beta and gamma actins coexist in most cell types as
CC       components of the cytoskeleton and as mediators of internal cell
CC       motility.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK029110; BAC26303.1; -; mRNA.
DR   EMBL; AK029130; BAC26313.1; -; mRNA.
DR   EMBL; BC111904; AAI11905.1; -; mRNA.
DR   EMBL; BC112429; AAI12430.1; -; mRNA.
DR   CCDS; CCDS26768.1; -.
DR   RefSeq; NP_780706.1; NM_175497.3.
DR   AlphaFoldDB; Q8BFZ3; -.
DR   SMR; Q8BFZ3; -.
DR   BioGRID; 232025; 14.
DR   IntAct; Q8BFZ3; 7.
DR   MINT; Q8BFZ3; -.
DR   STRING; 10090.ENSMUSP00000052086; -.
DR   iPTMnet; Q8BFZ3; -.
DR   PhosphoSitePlus; Q8BFZ3; -.
DR   SwissPalm; Q8BFZ3; -.
DR   UCD-2DPAGE; Q8BFZ3; -.
DR   EPD; Q8BFZ3; -.
DR   jPOST; Q8BFZ3; -.
DR   MaxQB; Q8BFZ3; -.
DR   PaxDb; Q8BFZ3; -.
DR   PeptideAtlas; Q8BFZ3; -.
DR   PRIDE; Q8BFZ3; -.
DR   ProteomicsDB; 285750; -.
DR   Antibodypedia; 56201; 71 antibodies from 18 providers.
DR   DNASU; 238880; -.
DR   Ensembl; ENSMUST00000054716; ENSMUSP00000052086; ENSMUSG00000055194.
DR   GeneID; 238880; -.
DR   KEGG; mmu:238880; -.
DR   UCSC; uc007rvu.1; mouse.
DR   CTD; 345651; -.
DR   MGI; MGI:2444552; Actbl2.
DR   VEuPathDB; HostDB:ENSMUSG00000055194; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   GeneTree; ENSGT00940000162627; -.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; Q8BFZ3; -.
DR   OMA; SNMKIKI; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; Q8BFZ3; -.
DR   TreeFam; TF354237; -.
DR   BioGRID-ORCS; 238880; 1 hit in 73 CRISPR screens.
DR   PRO; PR:Q8BFZ3; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q8BFZ3; protein.
DR   Bgee; ENSMUSG00000055194; Expressed in lip and 3 other tissues.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR   GO; GO:0048870; P:cell motility; 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; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding; Oxidation;
KW   Reference proteome.
FT   CHAIN           1..376
FT                   /note="Beta-actin-like protein 2"
FT                   /id="PRO_0000318850"
FT   MOD_RES         45
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:23911929"
FT   MOD_RES         48
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:23911929"
SQ   SEQUENCE   376 AA;  42004 MW;  DB6C8377BAE3A8BA CRC64;
     MVDDELTALV VDNGSGMCKA GFGGDDAPRA VFPSMVGRPR HQGVMVGMGQ KDCYVGDEAQ
     SKRGILTLKY PIEHGVVTNW DDMEKIWYHT FYNELRVAPD EHPILLTEAP LNPKINREKM
     TQIMFEAFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV THTVPIYEGY ALPHAILRLD
     LAGRDLTDYL MKILTERGYN FTTTAEREIV RDVKEKLCYV ALDFEQEMVT AAASSSLERS
     YELPDGQVIT IGNERFRCPE AIFQPSFLGI ESRGIHETTF NSIMKCDVDI RKDLFANTVL
     SGGSTMYPGI ADRMQKEIVT LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDEAGPPI VHRKCF