ACTN4_CHICK
ID ACTN4_CHICK Reviewed; 904 AA.
AC Q90734;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Alpha-actinin-4 {ECO:0000305};
DE AltName: Full=Non-muscle alpha-actinin 4 {ECO:0000305};
GN Name=ACTN4 {ECO:0000305};
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].
RX PubMed=8055908; DOI=10.1111/j.1432-1033.1994.tb19006.x;
RA Imamura M., Sakurai T., Ogawa Y., Ishikawa T., Goto K., Masaki T.;
RT "Molecular cloning of low-Ca(2+)-sensitive-type non-muscle alpha-actinin.";
RL Eur. J. Biochem. 223:395-401(1994).
RN [2]
RP PROTEIN SEQUENCE OF 294-316.
RX PubMed=1334489; DOI=10.1016/s0021-9258(18)35697-7;
RA Imamura M., Masaki T.;
RT "A novel nonmuscle alpha-actinin. Purification and characterization of
RT chicken lung alpha-actinin.";
RL J. Biol. Chem. 267:25927-25933(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. Probably involved in vesicular trafficking via its association
CC with the CART complex. Involved in tight junction assembly in
CC epithelial cells. May also function as a transcriptional coactivator,
CC stimulating transcription mediated by nuclear hormone receptors.
CC {ECO:0000250|UniProtKB:O43707}.
CC -!- SUBUNIT: Homodimer; antiparallel. Component of the CART complex. May
CC interact with nuclear receptors. {ECO:0000250|UniProtKB:O43707}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm
CC {ECO:0000250|UniProtKB:O43707}. Cell junction
CC {ECO:0000250|UniProtKB:P57780}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P57780}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif that may mediate
CC interaction with nuclear receptors. {ECO:0000250|UniProtKB:O43707}.
CC -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR EMBL; D26597; BAA05644.1; -; mRNA.
DR PIR; S45673; S45673.
DR RefSeq; NP_990457.1; NM_205126.1.
DR AlphaFoldDB; Q90734; -.
DR BMRB; Q90734; -.
DR SMR; Q90734; -.
DR STRING; 9031.ENSGALP00000023085; -.
DR PRIDE; Q90734; -.
DR GeneID; 396024; -.
DR KEGG; gga:396024; -.
DR CTD; 81; -.
DR VEuPathDB; HostDB:geneid_396024; -.
DR eggNOG; KOG0035; Eukaryota.
DR InParanoid; Q90734; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; Q90734; -.
DR PRO; PR:Q90734; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
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:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; 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:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903506; P:regulation of nucleic acid-templated transcription; ISS:UniProtKB.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISS:UniProtKB.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 3.
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; 4.
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 1: Evidence at protein level;
KW Actin-binding; Calcium; Cell junction; Cytoplasm;
KW Direct protein sequencing; Metal-binding; Nucleus; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..904
FT /note="Alpha-actinin-4"
FT /id="PRO_0000073444"
FT DOMAIN 43..147
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 156..262
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 286..396
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 406..511
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 521..632
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 642..745
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT DOMAIN 758..793
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 799..834
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..259
FT /note="Actin-binding"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 771
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 782
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 812
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 814
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 816
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 818
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 104207 MW; 691AA2D84C852D23 CRC64;
MVDYHSAGQP YPYGGNGPGP NGDYMAQEDD WDRDLLLDPA WEKQQRKTFT AWCNSHLRKA
GTQIENIDED FRDGLKLMLL LEVISGERLP KPERGKMRVH KINNVNKALD FIASKGVNVV
SIGAEEIVDG NAKMTLGMIW TIILRFAIQD ISVEETSAKE GLLLWCQRKT APYKNVNVQN
FHISWKDGLA FNALIHRHRP ELIEYDKLRK DDPVTNLNNA FEVAEKYLDI PKMLDAEDIV
NTARPDEKAI MTYVSSFYHA FSGAQKAETA ANRICKVLAV NQENEHLMED YEKLASDLLE
WIRRTIPWLE DRSPQKTIQE MQQKLEDFRD YRRVHKPPKV QEKCQLEINF NTLQTKLRLS
NRPAFMPSEG RMVSDINTGW QHLEQAEKGY EEWLLNEIRR LEPLDHLAEK FRQKASIHEA
WTEGKEAMLK QKDYETATLS DIKALIRKHE AFESDLAAHQ DRVEQIAAIA QELNELDYYD
SPSVNARCQK ICDQWDVLGS LTHSRREALE KTEKQLETID ELHLEYAKRA APFNNWMESA
MEDLQDMFIV HTIEEIEGLI AAHDQFKATL PDADREREAI LGIQREAQRI ADLHSIKLSG
NNPYTSVTPQ VINSKWERVQ QLVPTRDRAL QDEQSRQQCN ERLRRQFAGQ ANIVGPWMQT
KMEEIGRISI EMHGTLEDQL QHLKHYEQSI VDYKPNLELL EHEHQLVEEA LIFDNKHTNY
TMEHIRVGWE QLLTTIARTI NEVENQILTR DAKGISQEQM QEFRASFNHF DKDHCGALGP
EEFKACLISL GYDVENDRQG DAEFNRIMSL VDPNGSGSVT FQAFIDFMSR ETTDTDTADQ
VIASFKVLAG DKNYITAEEL RRELPPEQAE YCIARMAPYR GPDAAPGALD YKSFSTALYG
ESDL
