ACTN2_BOVIN
ID ACTN2_BOVIN Reviewed; 894 AA.
AC Q3ZC55;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Alpha-actinin-2;
DE AltName: Full=Alpha-actinin skeletal muscle isoform 2;
DE AltName: Full=F-actin cross-linking protein;
GN Name=ACTN2;
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=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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 ACTN3.
CC Interacts with ADAM12, MYOZ1, MYOZ2 and MYOZ3. Interacts via its C-
CC terminal region with the LDB3 PDZ domain. Interacts with XIRP2.
CC Interacts with DST (via N-terminus). Interacts with PARVB. Interacts
CC with SYNPO2 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P35609}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250}. Note=Colocalizes with MYOZ1 and FLNC at the Z-lines of
CC skeletal muscle. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR EMBL; BC102908; AAI02909.1; -; mRNA.
DR RefSeq; NP_001029807.1; NM_001034635.1.
DR AlphaFoldDB; Q3ZC55; -.
DR BMRB; Q3ZC55; -.
DR SMR; Q3ZC55; -.
DR STRING; 9913.ENSBTAP00000012786; -.
DR PaxDb; Q3ZC55; -.
DR PeptideAtlas; Q3ZC55; -.
DR PRIDE; Q3ZC55; -.
DR Ensembl; ENSBTAT00000012786; ENSBTAP00000012786; ENSBTAG00000009696.
DR GeneID; 536607; -.
DR KEGG; bta:536607; -.
DR CTD; 88; -.
DR VEuPathDB; HostDB:ENSBTAG00000009696; -.
DR VGNC; VGNC:25582; ACTN2.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000153968; -.
DR InParanoid; Q3ZC55; -.
DR OMA; IMILVDP; -.
DR OrthoDB; 543832at2759; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000009696; Expressed in gluteus medius and 95 other tissues.
DR ExpressionAtlas; Q3ZC55; baseline.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 1.
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; 3.
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 Actin-binding; Calcium; Cytoplasm; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..894
FT /note="Alpha-actinin-2"
FT /id="PRO_0000268163"
FT DOMAIN 38..142
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 151..257
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 281..391
FT /note="Spectrin 1"
FT REPEAT 401..506
FT /note="Spectrin 2"
FT REPEAT 516..627
FT /note="Spectrin 3"
FT REPEAT 637..740
FT /note="Spectrin 4"
FT DOMAIN 753..788
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 789..824
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..254
FT /note="Actin-binding"
FT BINDING 766
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 770
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 802
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 804
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JI91"
SQ SEQUENCE 894 AA; 103779 MW; 0CC70A8AEB8363BC CRC64;
MNQIEPGVQY NYVYEDDEYM IQEEEWDRDL LLDPAWEKQQ RKTFTAWCNS HLRKAGTQIE
NIEEDFRNGL KLMLLLEVIS GERLPKPDRG KMRFHKIANV NKALDYIASK GVKLVSIGAE
EIVDGNVKMT LGMIWTIILR FAIQDISVEE TSAKEGLLLW CQRKTAPYRN VNIQNFHTSW
KDGLGLCALI HRHRPDLIDY SKLNKDDPIG NINLAMEIAE KHLDIPKMLD AEDIVNTPKP
DERAIMTYVS CFYHAFAGAE QAETAANRIC KVLAVNQENE RLMEEYERLA SELLEWIRRT
IPWLENRTPE KTMQAMQKKL EDFRDYRRKH KPPKVQEKCQ LEINFNTLQT KLRISNRPAF
MPSEGKMVSD IAGAWQRLEQ AEKGYEEWLL NEIRRLERVE HLAEKFRQKA STHETWAYGK
EQILLQKDYE SSTLTEVRAL LRKHEAFESD LAAHQDRVEQ IAAIAQELNE LDYHDAVNVN
DRCQKICDQW DRLGTLTQKR REALERTEKL LETIDQLHLE FAKRAAPFNN WMEGAMEDLQ
DMFIVHSIEE IQSLITAHEQ FKATLPEADG ERQSILAIQN EVEKVIQSYS IRISSSNPYS
TVTVDEIRSK WDKVKQLVPI RDQSLQEELA RQHANERLRR QFAAQANAIG PWIQNKMEEI
ARSSIQITGA LEDQMNQLKQ YEHNIINYKN NIDKLEGDHQ LIQEALVFDN KHTNYTMEHI
RVGWELLLTT IARTINEVET QILTRDAKGI TQEQMNEFRA SFNHFDRRKN GLMDHEDFRA
CLISMGYDLG EAEFARIMTL VDPNGQGTVT FQSFIDFMTR ETADTDTAEQ VIASFRILAS
DKPYILAEEL RRELPPDQAQ YCIKRMPAYS GPGSVPGALD YTAFSSALYG ESDL
