LOCUS       NP_001163796             894 aa            linear   ROD 11-SEP-2024
DEFINITION  alpha-actinin-2 [Rattus norvegicus].
ACCESSION   NP_001163796 XP_001061664 XP_214499
VERSION     NP_001163796.1
DBSOURCE    REFSEQ: accession NM_001170325.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 894)
  AUTHORS   Wang,K., Wang,Y., Wan,H., Wang,J., Hu,L., Huang,S., Sheng,M.,
            Wu,J., Han,X., Yu,Y., Chen,P. and Chen,F.
  TITLE     Actn2 defects accelerates H9c2 hypertrophy via ERK phosphorylation
            under chronic stress
  JOURNAL   Genes Genomics 46 (9), 1013-1022 (2024)
   PUBMED   38990270
  REMARK    GeneRIF: Actn2 defects accelerates H9c2 hypertrophy via ERK
            phosphorylation under chronic stress.
REFERENCE   2  (residues 1 to 894)
  AUTHORS   Sbai,O., Soussi,R., Bole,A., Khrestchatisky,M., Esclapez,M. and
            Ferhat,L.
  TITLE     The actin binding protein alpha-actinin-2 expression is associated
            with dendritic spine plasticity and migrating granule cells in the
            rat dentate gyrus following pilocarpine-induced seizures
  JOURNAL   Exp Neurol 335, 113512 (2021)
   PUBMED   33098872
  REMARK    GeneRIF: The actin binding protein alpha-actinin-2 expression is
            associated with dendritic spine plasticity and migrating granule
            cells in the rat dentate gyrus following pilocarpine-induced
            seizures.
REFERENCE   3  (residues 1 to 894)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 894)
  AUTHORS   van Eldik,W., den Adel,B., Monshouwer-Kloots,J., Salvatori,D.,
            Maas,S., van der Made,I., Creemers,E.E., Frank,D., Frey,N.,
            Boontje,N., van der Velden,J., Steendijk,P., Mummery,C., Passier,R.
            and Beqqali,A.
  TITLE     Z-disc protein CHAPb induces cardiomyopathy and contractile
            dysfunction in the postnatal heart
  JOURNAL   PLoS One 12 (12), e0189139 (2017)
   PUBMED   29206857
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 894)
  AUTHORS   Qi,L., Yu,Y., Chi,X., Xu,W., Lu,D., Song,Y., Zhang,Y. and Zhang,H.
  TITLE     Kindlin-2 interacts with alpha-actinin-2 and beta1 integrin to
            maintain the integrity of the Z-disc in cardiac muscles
  JOURNAL   FEBS Lett 589 (16), 2155-2162 (2015)
   PUBMED   26143257
  REMARK    GeneRIF: Data suggest that kindlin-2 (Kind2/Fermt2) interacts with
            actin alpha 2 (Actn2) and integrin beta 1 (Itgb1) and co-localizes
            to cardiac sarcomere at Z-disc; knockdown of Kind2 leads to
            dissociation of Actn2 and Itgb1.
REFERENCE   6  (residues 1 to 894)
  AUTHORS   Zhou,Q., Ruiz-Lozano,P., Martone,M.E. and Chen,J.
  TITLE     Cypher, a striated muscle-restricted PDZ and LIM domain-containing
            protein, binds to alpha-actinin-2 and protein kinase C
  JOURNAL   J Biol Chem 274 (28), 19807-19813 (1999)
   PUBMED   10391924
REFERENCE   7  (residues 1 to 894)
  AUTHORS   Young,P., Ferguson,C., Banuelos,S. and Gautel,M.
  TITLE     Molecular structure of the sarcomeric Z-disk: two types of titin
            interactions lead to an asymmetrical sorting of alpha-actinin
  JOURNAL   EMBO J 17 (6), 1614-1624 (1998)
   PUBMED   9501083
REFERENCE   8  (residues 1 to 894)
  AUTHORS   Wyszynski,M., Kharazia,V., Shanghvi,R., Rao,A., Beggs,A.H.,
            Craig,A.M., Weinberg,R. and Sheng,M.
  TITLE     Differential regional expression and ultrastructural localization
            of alpha-actinin-2, a putative NMDA receptor-anchoring protein, in
            rat brain
  JOURNAL   J Neurosci 18 (4), 1383-1392 (1998)
   PUBMED   9454847
REFERENCE   9  (residues 1 to 894)
  AUTHORS   Kato,M., Sasaki,T., Ohya,T., Nakanishi,H., Nishioka,H., Imamura,M.
            and Takai,Y.
  TITLE     Physical and functional interaction of rabphilin-3A with
            alpha-actinin
  JOURNAL   J Biol Chem 271 (50), 31775-31778 (1996)
   PUBMED   8943213
REFERENCE   10 (residues 1 to 894)
  AUTHORS   Schiaffino,S. and Reggiani,C.
  TITLE     Molecular diversity of myofibrillar proteins: gene regulation and
            functional significance
  JOURNAL   Physiol Rev 76 (2), 371-423 (1996)
   PUBMED   8618961
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK355337.1, DY315226.1, CK358853.1, CK600096.1, FM118105.1,
            FM123616.1 and CR461659.1.
            
            On or before Dec 18, 2009 this sequence version replaced
            XP_214499.4, XP_001061664.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760384,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..894
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..894
                     /product="alpha-actinin-2"
                     /calculated_mol_wt=103703
     Region          35..139
                     /region_name="CH_ACTN_rpt1"
                     /note="first calponin homology (CH) domain found in the
                     alpha-actinin family; cd21214"
                     /db_xref="CDD:409063"
     Site            order(40,44,88,92..94,97..98,113..121,129,131..132,
                     135..136,138..139)
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:409063"
     Site            order(55,57,81..83)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409063"
     Region          143..257
                     /region_name="CH_ACTN_rpt2"
                     /note="second calponin homology (CH) domain found in the
                     alpha-actinin family; cd21216"
                     /db_xref="CDD:409065"
     Site            order(153,157,204..206,209..210,225..233,244,246..247,
                     250..251,253..254)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409065"
     Region          281..391
                     /region_name="Spectrin"
                     /note="Spectrin repeat; pfam00435"
                     /db_xref="CDD:395348"
     Region          402..629
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            507..512
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          637..739
                     /region_name="Spectrin"
                     /note="Spectrin repeat; pfam00435"
                     /db_xref="CDD:395348"
     Region          747..>851
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     Region          824..890
                     /region_name="EFhand_Ca_insen"
                     /note="Ca2+ insensitive EF hand; pfam08726"
                     /db_xref="CDD:430177"
     CDS             1..894
                     /gene="Actn2"
                     /coded_by="NM_001170325.1:190..2874"
                     /db_xref="GeneID:291245"
                     /db_xref="RGD:1308097"
ORIGIN      
        1 mnqiepgvqy nyvydedeym iqeeewdrdl lldpawekqq rktftawcns hlrkagtqie
       61 nieedfrngl klmlllevis gerlpkpdrg kmrfhkianv nkaldyiask gvklvsigae
      121 eivdgnvkmt lgmiwtiilr faiqdisvee tsakeglllw cqrktapyrn vniqnfhtsw
      181 kdglglcali hrhrpdlidy sklnkddpig ninlameiae khldipkmld aedivntpkp
      241 deraimtyvs cfyhafagae qaetaanric kvlavnqene rlmeeyerla sellewirrt
      301 ipwlenrtpe ktmqamqkkl edfrdyrrkh kppkvqekcq leinfntlqt klrisnrpaf
      361 mpsegkmvsd iagawqrleq aekgyeewll neirrlerle hlaekfrqka sthetwaygk
      421 eqillqkdye sasltevral lrkheafesd laahqdrveq iaaiaqelne ldyhdavnvn
      481 drcqkicdqw drlgtltqkr realertekl letidqlhle fakraapfnn wmegamedlq
      541 dmfivhsiee iqslitaheq fkatlpeadg erqsilaiqn evekviqsys irisssnpys
      601 tvtmdelrnk wdkvkqlvpv rdqslqeela rqhanerlrr qfaaqanaig pwiqnkmeei
      661 arssiqitga ledqmnqlkq yehniinykn nidklegdhq liqealvfdn khtnytmehi
      721 rvgwellltt iartinevet qiltrdakgi tqeqmnefra sfnhfdrrkn glmdhedfra
      781 clismgydlg eaefarimtl vdpngqgtvt fqsfidfmtr etadtdtaeq viasfrilas
      841 dkpyilaeel rrelppdqaq ycikrmppys gpgsvpgald ytafssalyg esdl
//
