ID   ACTN3_MOUSE             Reviewed;         900 AA.
AC   O88990; Q14DS8;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 173.
DE   RecName: Full=Alpha-actinin-3;
DE   AltName: Full=Alpha-actinin skeletal muscle isoform 3;
DE   AltName: Full=F-actin cross-linking protein;
GN   Name=Actn3;
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 [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RA   Birkenmeier C.S., Gifford E.J., Barker J.E.;
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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).
CC   -!- FUNCTION: F-actin cross-linking protein which is thought to anchor
CC       actin to a variety of intracellular structures. This is a bundling
CC       protein (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; antiparallel. Also forms heterodimers with ACTN2.
CC       Interacts with MYOZ1 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR   EMBL; AF093775; AAC62512.1; -; mRNA.
DR   EMBL; BC111890; AAI11891.1; -; mRNA.
DR   CCDS; CCDS29441.1; -.
DR   RefSeq; NP_038484.1; NM_013456.2.
DR   AlphaFoldDB; O88990; -.
DR   SMR; O88990; -.
DR   BioGRID; 197951; 9.
DR   IntAct; O88990; 3.
DR   MINT; O88990; -.
DR   STRING; 10090.ENSMUSP00000006626; -.
DR   GlyGen; O88990; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; O88990; -.
DR   PhosphoSitePlus; O88990; -.
DR   EPD; O88990; -.
DR   jPOST; O88990; -.
DR   MaxQB; O88990; -.
DR   PaxDb; 10090-ENSMUSP00000006626; -.
DR   PeptideAtlas; O88990; -.
DR   ProteomicsDB; 285720; -.
DR   Antibodypedia; 73518; 296 antibodies from 30 providers.
DR   DNASU; 11474; -.
DR   Ensembl; ENSMUST00000006626.5; ENSMUSP00000006626.4; ENSMUSG00000006457.5.
DR   GeneID; 11474; -.
DR   KEGG; mmu:11474; -.
DR   UCSC; uc008gbf.2; mouse.
DR   AGR; MGI:99678; -.
DR   CTD; 89; -.
DR   MGI; MGI:99678; Actn3.
DR   VEuPathDB; HostDB:ENSMUSG00000006457; -.
DR   eggNOG; KOG0035; Eukaryota.
DR   GeneTree; ENSGT00940000153968; -.
DR   HOGENOM; CLU_005217_1_1_1; -.
DR   InParanoid; O88990; -.
DR   OMA; RMTKYTG; -.
DR   OrthoDB; 2872403at2759; -.
DR   PhylomeDB; O88990; -.
DR   TreeFam; TF352676; -.
DR   Reactome; R-MMU-390522; Striated Muscle Contraction.
DR   BioGRID-ORCS; 11474; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Actn3; mouse.
DR   PRO; PR:O88990; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; O88990; Protein.
DR   Bgee; ENSMUSG00000006457; Expressed in triceps brachii and 135 other cell types or tissues.
DR   GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR   GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR   GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030017; C:sarcomere; IDA:MGI.
DR   GO; GO:0005865; C:striated muscle thin filament; TAS:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; TAS:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0060349; P:bone morphogenesis; IMP:UniProtKB.
DR   GO; GO:0048041; P:focal adhesion assembly; ISO:MGI.
DR   GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR   GO; GO:0006936; P:muscle contraction; TAS:MGI.
DR   GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0045820; P:negative regulation of glycolytic process; IMP:UniProtKB.
DR   GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IMP:UniProtKB.
DR   GO; GO:1901078; P:negative regulation of relaxation of muscle; IMP:UniProtKB.
DR   GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; IMP:UniProtKB.
DR   GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; IMP:UniProtKB.
DR   GO; GO:1904025; P:positive regulation of glucose catabolic process to lactate via pyruvate; IMP:UniProtKB.
DR   GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IMP:UniProtKB.
DR   GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; IMP:UniProtKB.
DR   GO; GO:1903715; P:regulation of aerobic respiration; IMP:UniProtKB.
DR   GO; GO:0090257; P:regulation of muscle system process; IMP:UniProtKB.
DR   GO; GO:0014728; P:regulation of the force of skeletal muscle contraction; IMP:UniProtKB.
DR   GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IMP:UniProtKB.
DR   GO; GO:0014732; P:skeletal muscle atrophy; IMP:UniProtKB.
DR   GO; GO:0014883; P:transition between fast and slow fiber; IMP:UniProtKB.
DR   CDD; cd21214; CH_ACTN_rpt1; 1.
DR   CDD; cd21216; CH_ACTN_rpt2; 1.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd00176; SPEC; 3.
DR   Gene3D; 1.20.58.60; -; 4.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF432; ALPHA-ACTININ-3; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF08726; EFhand_Ca_insen; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM01184; efhand_Ca_insen; 1.
DR   SMART; SM00150; SPEC; 2.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 4.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   Genevisible; O88990; MM.
PE   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Calcium; Metal-binding; Reference proteome;
KW   Repeat.
FT   CHAIN           1..900
FT                   /note="Alpha-actinin-3"
FT                   /id="PRO_0000073439"
FT   DOMAIN          44..148
FT                   /note="Calponin-homology (CH) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          157..263
FT                   /note="Calponin-homology (CH) 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REPEAT          287..397
FT                   /note="Spectrin 1"
FT   REPEAT          407..512
FT                   /note="Spectrin 2"
FT   REPEAT          522..633
FT                   /note="Spectrin 3"
FT   REPEAT          643..746
FT                   /note="Spectrin 4"
FT   DOMAIN          759..794
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          795..830
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..260
FT                   /note="Actin-binding"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         772
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         776
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         778
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         783
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         808
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         810
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08043"
SQ   SEQUENCE   900 AA;  103043 MW;  7F795002CB2B7F8B CRC64;
     MMMVMQPEGL GAGEGPFSGG GGGEYMEQEE DWDRDLLLDP AWEKQQRKTF TAWCNSHLRK
     AGTQIENIEE DFRNGLKLML LLEVISGERL PRPDKGKMRF HKIANVNKAL DFIASKGVKL
     VSIGAEEIVD GNLKMTLGMI WTIILRFAIQ DISVEETSAK EGLLLWCQRK TAPYRNVNVQ
     NFHTSWKDGL ALCALIHRHR PDLIDYAKLR KDDPIGNLNT AFEVAEKYLD IPKMLDAEDI
     VNTPKPDEKA IMTYVSCFYH AFAGAEQAET AANRICKVLA VNQENEKLME EYEKLASELL
     EWIRRTVPWL ENRVGEPSMS AMQRKLEDFR DYRRLHKPPR VQEKCQLEIN FNTLQTKLRL
     SHRPAFMPSE GKLVSDIANA WRGLEQVEKG YEDWLLSEIR RLQRLQHLAE KFQQKASLHE
     AWTRGKEEML NQHDYESASL QEVRALLRRH EAFESDLAAH QDRVEHIAAL AQELNELDYH
     EAASVNSRCQ AICDQWDNLG TLTQKRRDAL ERMEKLLETI DQLQLEFARR AAPFNNWLDG
     AIEDLQDVWL VHSVEETQSL LTAHEQFKAT LPEADRERGA ILGIQGEIQK ICQTYGLRPK
     SGNPYITLSS QDINNKWDTV RKLVPSRDQT LQEELARQQV NERLRRQFAA QANAIGPWIQ
     GKVEEVGRLA AGLAGSLEEQ MAGLRQQEQN IINYKSNIDR LEGDHQLLQE SLVFDNKHTV
     YSMEHIRVGW EQLLTSIART INEVENQVLT RDAKGLSQEQ LNEFRASFNH FDRKRNGMME
     PDDFRACLIS MGYDLGEVEF ARIMTMVDPN AAGVVTFQAF IDFMTRETAE TDTAEQVVAS
     FKILAGDKNY ITPEELRREL PAEQAEYCIR RMAPYKGSGA PSGALDYVAF SSALYGESDL
//