ACTN3_BOVIN
ID ACTN3_BOVIN Reviewed; 901 AA.
AC Q0III9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; BC122618; AAI22619.1; -; mRNA.
DR RefSeq; NP_001069625.1; NM_001076157.1.
DR RefSeq; XP_010819427.1; XM_010821125.2.
DR AlphaFoldDB; Q0III9; -.
DR SMR; Q0III9; -.
DR STRING; 9913.ENSBTAP00000030018; -.
DR PaxDb; Q0III9; -.
DR PeptideAtlas; Q0III9; -.
DR PRIDE; Q0III9; -.
DR Ensembl; ENSBTAT00000030030; ENSBTAP00000030018; ENSBTAG00000022244.
DR GeneID; 539375; -.
DR KEGG; bta:539375; -.
DR CTD; 89; -.
DR VEuPathDB; HostDB:ENSBTAG00000022244; -.
DR VGNC; VGNC:53654; ACTN3.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000153968; -.
DR InParanoid; Q0III9; -.
DR OMA; MLNQRDY; -.
DR OrthoDB; 543832at2759; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000022244; Expressed in biceps femoris and 94 other tissues.
DR ExpressionAtlas; Q0III9; baseline and differential.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR GO; GO:0048041; P:focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0045820; P:negative regulation of glycolytic process; IEA:Ensembl.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IEA:Ensembl.
DR GO; GO:1901078; P:negative regulation of relaxation of muscle; IEA:Ensembl.
DR GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; IEA:Ensembl.
DR GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; IEA:Ensembl.
DR GO; GO:1904025; P:positive regulation of glucose catabolic process to lactate via pyruvate; IEA:Ensembl.
DR GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IEA:Ensembl.
DR GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; IEA:Ensembl.
DR GO; GO:0014728; P:regulation of the force of skeletal muscle contraction; IEA:Ensembl.
DR GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IEA:Ensembl.
DR GO; GO:0014732; P:skeletal muscle atrophy; IEA:Ensembl.
DR GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 2.
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..901
FT /note="Alpha-actinin-3"
FT /id="PRO_0000284524"
FT DOMAIN 45..149
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 158..264
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 288..398
FT /note="Spectrin 1"
FT REPEAT 408..513
FT /note="Spectrin 2"
FT REPEAT 523..634
FT /note="Spectrin 3"
FT REPEAT 644..747
FT /note="Spectrin 4"
FT DOMAIN 760..795
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 796..831
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..261
FT /note="Actin-binding"
FT BINDING 773
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 777
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 779
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 784
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 809
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 811
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 901 AA; 103151 MW; A5BCD793B20415A8 CRC64;
MMMVLQPEGL GTGEGPFAGG RGGGEYMEQE EDWDRDLLLD PAWEKQQRKT FTAWCNSHLR
KAGTQIENIE EDFRNGLKLM LLLEVISGER LPRPDKGKMR FHKIANVNKA LDFIASKGVK
LVSIGAEEIV DGNLKMTLGM IWTIILRFAI QDISVEETSA KEGLLLWCQR KTAPYRNVNV
QNFHTSWKDG LALCALIHRH RPDLIDYAKL RKDDPIGNLN TAFEVAEKYL DIPKMLDAED
IVNTPKPDEK AIMTYVSCFY HAFAGAEQAE TAANRICKVL AVNQENEKLM EEYEKLASEL
LEWIRRTVPW LENRVGEPSM SAMQRKLEDF RDYRRLHKPP RVQEKCQLEI NFNTLQTKLR
LSHRPAFMPS EGKLVSDIAN AWRGLEQAEK GYEDWLLSEI RRLQRLQHLA EKFQQKASLH
EAWTRGKEDM LSQRDYETAS LQEVRALLRR HEAFESDLAA HQDRVEHIAA LAQELNELDY
HEAASVNSRC QAICDQWDNL GTLTQKRRDA LERMEKLLET IDQLQLEFAR RAAPFNNWLD
GAVEDLQDVW LVHSVEETQS LVTAHDQFKA TLPEADRERG AILGIQGEIQ KICQTYGLRP
SSTNPYITLT PQDINTKWDT VRKLVPSRDQ MLQEELTRQQ VNERLRRQFA AQANAIGPWI
QGKVEEVGRL AAGMAGSLEE QMAGLRQQEQ NIINYKSNID RLEGDHQLLQ ESLVFDNKHT
VYSMEHIRVG WEQLLTSIAR TINEVENQVL TRDAKGLSQE QLNEFRASFN HFDRKRNGMM
EPDDFRACLI SMGYDLGEVE FARIMTMVDP NAAGVVTFQA FIDFMTRETA ETDTAEQVVA
SFKILAGDKN YITAEELRRE LPAEQAEYCI RRMAPYKGAG APAGALDYVA FSSALYGESD
L
