ACTN1_MACFA
ID ACTN1_MACFA Reviewed; 892 AA.
AC Q2PFV7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Alpha-actinin-1;
DE AltName: Full=Alpha-actinin cytoskeletal isoform;
DE AltName: Full=F-actin cross-linking protein;
DE AltName: Full=Non-muscle alpha-actinin-1;
GN Name=ACTN1; ORFNames=QmoA-13496;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Medulla oblongata;
RA Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA Hashimoto K.;
RT "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT oligo-chips.";
RL Submitted (JUL-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. Interacts with MYOZ2, TTID and LPP.
CC Interacts with DDN (By similarity). Interacts with PSD. Interacts with
CC MICALL2 (By similarity). Interacts with DNM2 and CTTN. Interacts with
CC PDLIM1. Interacts with PDLIM2. Interacts with PDLIM4 (via PDZ domain)
CC (By similarity). {ECO:0000250|UniProtKB:P12814,
CC ECO:0000250|UniProtKB:Q7TPR4, ECO:0000250|UniProtKB:Q9Z1P2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9Z1P2}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:P12814}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9Z1P2}. Cell junction
CC {ECO:0000250|UniProtKB:Q9Z1P2}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:Q7TPR4}. Note=Colocalizes with MYOZ2 and PPP3CA
CC at the Z-line of heart and skeletal muscle. Colocalizes with PSD in
CC membrane ruffles and central reticular structures.
CC {ECO:0000250|UniProtKB:Q7TPR4}.
CC -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR EMBL; AB220480; BAE73013.1; -; mRNA.
DR RefSeq; NP_001306279.1; NM_001319350.1.
DR AlphaFoldDB; Q2PFV7; -.
DR SMR; Q2PFV7; -.
DR STRING; 9541.XP_005561643.1; -.
DR PRIDE; Q2PFV7; -.
DR GeneID; 102127552; -.
DR CTD; 87; -.
DR VEuPathDB; HostDB:ENSMFAG00000003078; -.
DR eggNOG; KOG0035; Eukaryota.
DR OMA; QRFENVN; -.
DR Proteomes; UP000233100; Chromosome 7.
DR GO; GO:0005923; C:bicellular tight junction; ISS:AgBase.
DR GO; GO:0031252; C:cell leading edge; ISS:AgBase.
DR GO; GO:0097433; C:dense body; ISS:AgBase.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0090637; C:inner dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:AgBase.
DR GO; GO:0090636; C:outer dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; ISS:AgBase.
DR GO; GO:0030486; C:smooth muscle dense body; ISS:AgBase.
DR GO; GO:0001725; C:stress fiber; ISS:AgBase.
DR GO; GO:1990357; C:terminal web; ISS:AgBase.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0005915; C:zonula adherens; ISS:AgBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0051393; F:alpha-actinin binding; ISS:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:AgBase.
DR GO; GO:0017166; F:vinculin binding; ISS:AgBase.
DR GO; GO:0045214; P:sarcomere organization; ISS:AgBase.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISS:AgBase.
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; IPR018247; EF_Hand_1_Ca_BS.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Calcium; Cell junction; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..892
FT /note="Alpha-actinin-1"
FT /id="PRO_0000312774"
FT DOMAIN 31..135
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 144..250
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 274..384
FT /note="Spectrin 1"
FT REPEAT 394..499
FT /note="Spectrin 2"
FT REPEAT 509..620
FT /note="Spectrin 3"
FT REPEAT 630..733
FT /note="Spectrin 4"
FT DOMAIN 746..781
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 787..822
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..247
FT /note="Actin-binding"
FT REGION 274..733
FT /note="Interaction with DDN"
FT /evidence="ECO:0000250"
FT BINDING 759
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 761
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 763
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 765
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 770
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P12814"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12814"
FT MOD_RES 12
FT /note="Phosphotyrosine; by FAK1"
FT /evidence="ECO:0000250|UniProtKB:P12814"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12814"
FT MOD_RES 195
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12814"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12814"
FT MOD_RES 676
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12814"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12814"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1P2"
SQ SEQUENCE 892 AA; 103025 MW; 3DA3F4C1A0289505 CRC64;
MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT QIENIEEDFR
DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI ASKGVKLVSI GAEEIVDGNV
KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC
ALIHRHRPEL IDYGKLRKDD PLTNLNTAFD VAEKYLDIPK MLDAEDIVGT ARPDEKAIMT
YVSSFYHAFS GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR
VPENTMHAMQ QKLEDFRDYR RLHKPPKVQE KCQLEINFNT LQTKLRLSNR PAFMPSEGRM
VSDINNAWGC LEQVEKGYEE WLLNEIRRLE RLDHLAEKFR QKASIHEAWT DGKEAMLRQK
DYETATLSEI KALLKKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYYDSP SVNARCQKIC
DQWDNLGALT QKRREALERT EKLLETIDQL YLEYAKRAAP FNNWMEGAME DLQDTFIVHT
IEEIQGLTTA HEQFKATLPD ADKERLAILG IHNEVSKIVQ TYHVNMAGTN PYTTITPQEI
NGKWDHVRQL VPRRDQALTE EHARQQHNER LRKQFGAQAN VIGPWIQTKM EEIGRISIEM
HGTLEDQLSH LRQYEKSIVN YKPKIDQLEG DHQLIQEALI FDNKHTNYTM EHIRVGWEQL
LTTIARTINE VENQILTRDA KGISQEQMNE FRASFNHFDR DHSGTLGPEE FKACLISLGY
DIGNDPQGEA EFARIMSIVD PNRLGVVTFQ AFIDFMSRET ADTDTADQVM ASFKILAGDK
NYITVDELRR ELPPDQAEYC IARMAPYTGP DSVPGALDYM SFSTALYGES DL
