ACTN2_CHICK
ID ACTN2_CHICK Reviewed; 897 AA.
AC P20111; Q90821;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 163.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3197725; DOI=10.1111/j.1432-1033.1988.tb14419.x;
RA Arimura C., Suzuki T., Yanagisawa M., Imamura M., Hamada Y., Masaki T.;
RT "Primary structure of chicken skeletal muscle and fibroblast alpha-actinins
RT deduced from cDNA sequences.";
RL Eur. J. Biochem. 177:649-655(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1720388; DOI=10.1016/0014-4827(91)90418-t;
RA Tokuue Y., Goto S., Imamura M., Obinata T., Masaki T., Endo T.;
RT "Transfection of chicken skeletal muscle alpha-actinin cDNA into nonmuscle
RT and myogenic cells: dimerization is not essential for alpha-actinin to bind
RT to microfilaments.";
RL Exp. Cell Res. 197:158-167(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 662-867 (ISOFORM 2).
RX PubMed=1483465; DOI=10.1111/j.1432-1033.1992.tb17483.x;
RA Parr T., Waites G.T., Patel B., Millake D.B., Critchley D.R.;
RT "A chick skeletal-muscle alpha-actinin gene gives rise to two alternatively
RT spliced isoforms which differ in the EF-hand Ca(2+)-binding domain.";
RL Eur. J. Biochem. 210:801-809(1992).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P20111-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P20111-2; Sequence=VSP_012544;
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; X13874; CAA32078.1; -; mRNA.
DR EMBL; X59247; CAA41935.1; -; mRNA.
DR EMBL; X68797; CAA48702.1; -; Genomic_DNA.
DR EMBL; X68798; CAA48702.1; JOINED; Genomic_DNA.
DR EMBL; X68799; CAA48702.1; JOINED; Genomic_DNA.
DR EMBL; X68800; CAA48702.1; JOINED; Genomic_DNA.
DR EMBL; X68801; CAA48702.1; JOINED; Genomic_DNA.
DR EMBL; X68802; CAA48702.1; JOINED; Genomic_DNA.
DR PIR; S02032; S02032.
DR RefSeq; NP_990654.1; NM_205323.1. [P20111-1]
DR AlphaFoldDB; P20111; -.
DR SMR; P20111; -.
DR STRING; 9031.ENSGALP00000023309; -.
DR PaxDb; P20111; -.
DR PRIDE; P20111; -.
DR Ensembl; ENSGALT00000023354; ENSGALP00000023309; ENSGALG00000014463. [P20111-1]
DR GeneID; 396263; -.
DR KEGG; gga:396263; -.
DR CTD; 88; -.
DR VEuPathDB; HostDB:geneid_396263; -.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000153968; -.
DR HOGENOM; CLU_005217_1_1_1; -.
DR InParanoid; P20111; -.
DR OMA; IMILVDP; -.
DR PhylomeDB; P20111; -.
DR TreeFam; TF352676; -.
DR PRO; PR:P20111; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000014463; Expressed in skeletal muscle tissue and 10 other tissues.
DR ExpressionAtlas; P20111; baseline and differential.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030035; P:microspike assembly; IDA:UniProtKB.
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; 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 Actin-binding; Alternative splicing; Calcium; Cytoplasm; Metal-binding;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..897
FT /note="Alpha-actinin-2"
FT /id="PRO_0000073437"
FT DOMAIN 41..145
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 154..260
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 284..394
FT /note="Spectrin 1"
FT REPEAT 404..509
FT /note="Spectrin 2"
FT REPEAT 519..630
FT /note="Spectrin 3"
FT REPEAT 640..743
FT /note="Spectrin 4"
FT DOMAIN 756..791
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 792..827
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..257
FT /note="Actin-binding"
FT BINDING 769
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 773
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 780
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 805
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 807
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 VAR_SEQ 792
FT /note="L -> LDESDNLHSDEFKACLISLGEVGNDLQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_012544"
SQ SEQUENCE 897 AA; 104275 MW; F4FAC12F7F4C8834 CRC64;
MNSMNQIETN MQYTYNYEED EYMTQEEEWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT
QIENIEEDFR NGLKLMLLLE VISGERLPKP DRGKMRFHKI ANVNKALDYI ASKGVKLVSI
GAEEIVDGNV KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YRNVNIQNFH
LSWKDGLGLC ALIHRHRPDL IDYSKLNKDD PIGNINLAME IAEKHLDIPK MLDAEDIVNT
PKPDERAIMT YVSCFYHAFA GAEQAETAAN RICKVLAVNQ ENERLMEEYE RLASELLEWI
RRTIPWLENR TPEKTMQAMQ KKLEDFRDYR RKHKPPKVQE KCQLEINFNT LQTKLRISNR
PAFMPSEGKM VSDIAGAWQR LEQAEKGYEE WLLNEIRRLE RLEHLAEKFR QKASTHEQWA
YGKEQILLQK DYESASLTEV RAMLRKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYHDAA
SVNDRCQKIC DQWDSLGTLT QKRREALERT EKLLETIDQL HLEFAKRAAP FNNWMEGAME
DLQDMFIVHS IEEIQSLISA HDQFKATLPE ADGERQAILS IQNEVEKVIQ SYSMRISASN
PYSTVTVEEI RTKWEKVKQL VPQRDQSLQE ELARQHANER LRRQFAAQAN VIGPWIQTKM
EEIARSSIEM TGPLEDQMNQ LKQYEQNIIN YKHNIDKLEG DHQLIQEALV FDNKHTNYTM
EHIRVGWELL LTTIARTINE VETQILTRDA KGITQEQMND FRASFNHFDR RKNGLMDHDD
FRACLISMGY DLGEAEFARI MSLVDPNGQG TVTFQSFIDF MTRETADTDT AEQVIASFRI
LASDKPYILA DELRRELPPE QAQYCIKRMP QYTGPGSVPG ALDYTSFSSA LYGESDL
