ACTN1_RAT
ID ACTN1_RAT Reviewed; 892 AA.
AC Q9Z1P2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 183.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hippocampus;
RA Schulz T.W., Seeburg P.H.;
RT "Rattus norvegicus non-muscle alpha-actinin 1 mRNA.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH PDLIM4.
RX PubMed=14729062; DOI=10.1016/j.yexcr.2003.09.004;
RA Vallenius T., Scharm B., Vesikansa A., Luukko K., Schaefer R.,
RA Maekelae T.P.;
RT "The PDZ-LIM protein RIL modulates actin stress fiber turnover and enhances
RT the association of alpha-actinin with F-actin.";
RL Exp. Cell Res. 293:117-128(2004).
RN [3]
RP INTERACTION WITH PDLIM2.
RX PubMed=15505042; DOI=10.1167/iovs.04-0721;
RA Torrado M., Senatorov V.V., Trivedi R., Fariss R.N., Tomarev S.I.;
RT "Pdlim2, a novel PDZ-LIM domain protein, interacts with alpha-actinins and
RT filamin A.";
RL Invest. Ophthalmol. Vis. Sci. 45:3955-3963(2004).
RN [4]
RP INTERACTION WITH DDN.
RX PubMed=16464232; DOI=10.1111/j.1471-4159.2006.03679.x;
RA Kremerskothen J., Kindler S., Finger I., Veltel S., Barnekow A.;
RT "Postsynaptic recruitment of Dendrin depends on both dendritic mRNA
RT transport and synaptic anchoring.";
RL J. Neurochem. 96:1659-1666(2006).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CTTN AND DNM2.
RX PubMed=21210813; DOI=10.1111/j.1471-4159.2011.07169.x;
RA Kurklinsky S., Chen J., McNiven M.A.;
RT "Growth cone morphology and spreading are regulated by a dynamin-cortactin
RT complex at point contacts in hippocampal neurons.";
RL J. Neurochem. 117:48-60(2011).
RN [6]
RP INTERACTION WITH PDLIM1.
RX PubMed=22659164; DOI=10.1016/j.yexcr.2012.05.006;
RA Miyazaki K., Ohno K., Tamura N., Sasaki T., Sato K.;
RT "CLP36 and RIL recruit alpha-actinin-1 to stress fibers and differentially
RT regulate stress fiber dynamics in F2408 fibroblasts.";
RL Exp. Cell Res. 318:1716-1725(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). Interacts with DDN (PubMed:16464232). Interacts with
CC PSD. Interacts with MICALL2 (By similarity). Interacts with DNM2 and
CC CTTN (PubMed:21210813). Interacts with PDLIM1 (PubMed:22659164).
CC Interacts with PDLIM2 (PubMed:15505042). Interacts with PDLIM4 (via PDZ
CC domain) (PubMed:14729062). {ECO:0000250|UniProtKB:P12814,
CC ECO:0000250|UniProtKB:Q7TPR4, ECO:0000269|PubMed:14729062,
CC ECO:0000269|PubMed:15505042, ECO:0000269|PubMed:16464232,
CC ECO:0000269|PubMed:21210813, ECO:0000269|PubMed:22659164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21210813}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:P12814}. Cell membrane
CC {ECO:0000269|PubMed:21210813}. Cell junction
CC {ECO:0000269|PubMed:21210813}. 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; AF115386; AAD12064.1; -; mRNA.
DR RefSeq; NP_112267.1; NM_031005.3.
DR AlphaFoldDB; Q9Z1P2; -.
DR SMR; Q9Z1P2; -.
DR BioGRID; 249534; 15.
DR CORUM; Q9Z1P2; -.
DR IntAct; Q9Z1P2; 7.
DR MINT; Q9Z1P2; -.
DR STRING; 10116.ENSRNOP00000061058; -.
DR iPTMnet; Q9Z1P2; -.
DR PhosphoSitePlus; Q9Z1P2; -.
DR jPOST; Q9Z1P2; -.
DR PaxDb; Q9Z1P2; -.
DR PRIDE; Q9Z1P2; -.
DR Ensembl; ENSRNOT00000091560; ENSRNOP00000068851; ENSRNOG00000056756.
DR GeneID; 81634; -.
DR KEGG; rno:81634; -.
DR UCSC; RGD:70907; rat.
DR CTD; 87; -.
DR RGD; 70907; Actn1.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000155548; -.
DR InParanoid; Q9Z1P2; -.
DR OrthoDB; 543832at2759; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:Q9Z1P2; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000056756; Expressed in colon and 19 other tissues.
DR ExpressionAtlas; Q9Z1P2; baseline and differential.
DR Genevisible; Q9Z1P2; RN.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0005916; C:fascia adherens; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0030017; C:sarcomere; ISO:RGD.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005519; F:cytoskeletal regulatory protein binding; IPI:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0099186; F:structural constituent of postsynapse; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0017166; F:vinculin binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; ISO:RGD.
DR GO; GO:0051639; P:actin filament network formation; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:RGD.
DR GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR GO; GO:0030220; P:platelet formation; ISO:RGD.
DR GO; GO:0036344; P:platelet morphogenesis; ISO:RGD.
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 1: Evidence at protein 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_0000073433"
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:0007744|PubMed:22673903"
SQ SEQUENCE 892 AA; 102960 MW; 2360D496D0A84095 CRC64;
MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT QIENIEEDFR
DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI ASKGVKLVSI GAEEIVDGNV
KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC
ALIHRHRPEL IDYGKLRKDD PLTNLNTAFD VAERYLDIPK MLDAEDIVGT ARPDEKAIMT
YVSSFYHAFS GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR
VPENTMQAMQ QKLEDFRDYR RLHKPPKVQE KCQLEINFNT LQTKLRLSNR PAFMPSEGRM
VSDINNAWGC LEQAEKGYEE WLLNEIRRLE RLDHLAEKFR QKASIHEAWT DGKEAMLRQK
DYETATLSEI KALLKKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYYDSP SVNARCQKIC
DQWDNLGALT QKRREALERT EKLLETIDQL YLEYAKRAAP FNNWMEGAME DLQDTFIVHT
IEEIQGLTTA HEQFKATLPD ADKERLAILG IHNEVSKIVQ TYHVNMAGTN PYTTITPQEI
NGKWDHVRQL VPRRDQALTE EHSRQQHNER LRKQFGAQAN VIGPWIQTKM EEIGRISIEM
HGTLEDQLSH LRQYEKSIVN YKPKIDQLEG DHQLIQEALI FDNKHTNYTM EHIRVGWEQL
LTTIARTINE VENQILTRDA KGISQEQMNE FRASFNHFDR DHSGTLGPEE FKACLISLGY
DIGNDPQGEA EFARIMSIVD PNRLGVVTFQ AFIDFMSRET ADTDTADQVM ASFKILAGDK
NYITGDELRR ELPPDQAEYC IARMAPYAGP DSVPGALDYM SFSTALYGES DL
