ACTN3_MOUSE
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 03-AUG-2022, entry version 165.
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 iPTMnet; O88990; -.
DR PhosphoSitePlus; O88990; -.
DR EPD; O88990; -.
DR jPOST; O88990; -.
DR MaxQB; O88990; -.
DR PaxDb; O88990; -.
DR PeptideAtlas; O88990; -.
DR PRIDE; O88990; -.
DR ProteomicsDB; 285720; -.
DR Antibodypedia; 73518; 262 antibodies from 30 providers.
DR DNASU; 11474; -.
DR Ensembl; ENSMUST00000006626; ENSMUSP00000006626; ENSMUSG00000006457.
DR GeneID; 11474; -.
DR KEGG; mmu:11474; -.
DR UCSC; uc008gbf.2; mouse.
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; MLNQRDY; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; O88990; -.
DR TreeFam; TF352676; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 11474; 0 hits in 73 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 132 other tissues.
DR Genevisible; O88990; MM.
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; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 3.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
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 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; SM00150; SPEC; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
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
