ACTN1_CHICK
ID ACTN1_CHICK Reviewed; 893 AA.
AC P05094; Q99001;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 3.
DT 03-AUG-2022, entry version 184.
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 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=2826427; DOI=10.1016/s0021-9258(18)45426-9;
RA Baron M.D., Davison M.D., Jones P., Critchley D.R.;
RT "The sequence of chick alpha-actinin reveals homologies to spectrin and
RT calmodulin.";
RL J. Biol. Chem. 262:17623-17629(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=1556133; DOI=10.1016/s0021-9258(18)42690-7;
RA Waites G.T., Graham I.R., Jackson P., Millake D.B., Patel B.,
RA Blanchard A.D., Weller P., Eperon I.C., Critchley D.R.;
RT "Mutually exclusive splicing of calcium-binding domain exons in chick
RT alpha-actinin.";
RL J. Biol. Chem. 267:6263-6271(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-893 (ISOFORM 1).
RC TISSUE=Fibroblast;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-769 (ISOFORM 1).
RC TISSUE=Fibroblast;
RX PubMed=3818609; DOI=10.1016/s0021-9258(18)61541-8;
RA Baron M.D., Davison M.D., Jones P., Patel B., Critchley D.R.;
RT "Isolation and characterization of a cDNA encoding a chick alpha-actinin.";
RL J. Biol. Chem. 262:2558-2561(1987).
RN [5]
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).
CC -!- FUNCTION: F-actin cross-linking protein is thought to anchor actin to a
CC variety of intracellular structures. This is a bundling protein.
CC -!- SUBUNIT: Homodimer; antiparallel (By similarity). Interacts with PDLIM4
CC (via PDZ domain) (PubMed:14729062). {ECO:0000250|UniProtKB:P12814,
CC ECO:0000269|PubMed:14729062}.
CC -!- INTERACTION:
CC P05094; P07228: ITGB1; NbExp=4; IntAct=EBI-5847257, EBI-5606437;
CC P05094; Q9UMF0: ICAM5; Xeno; NbExp=3; IntAct=EBI-5847257, EBI-6398041;
CC P05094; P05106: ITGB3; Xeno; NbExp=2; IntAct=EBI-5847257, EBI-702847;
CC P05094-2; P12003: VCL; NbExp=5; IntAct=EBI-6049246, EBI-1039563;
CC P05094-2; Q04584: ZYX; NbExp=4; IntAct=EBI-6049246, EBI-6222189;
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Isoforms only differ in the region of the first EF-hand
CC calcium-binding motif.;
CC Name=1; Synonyms=Brain;
CC IsoId=P05094-1; Sequence=Displayed;
CC Name=2; Synonyms=Smooth muscle;
CC IsoId=P05094-2; Sequence=VSP_000710, VSP_000711;
CC -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR EMBL; M74143; AAA48570.1; -; mRNA.
DR EMBL; X13875; CAA32079.1; -; mRNA.
DR EMBL; J02666; AAA48566.1; -; mRNA.
DR EMBL; J03486; AAA48567.1; -; mRNA.
DR PIR; A42162; A42162.
DR RefSeq; NP_989458.1; NM_204127.1.
DR RefSeq; XP_015142744.1; XM_015287258.1. [P05094-1]
DR PDB; 1SJJ; EM; 20.00 A; A/B=26-893.
DR PDBsum; 1SJJ; -.
DR AlphaFoldDB; P05094; -.
DR SMR; P05094; -.
DR BioGRID; 674968; 1.
DR IntAct; P05094; 7.
DR STRING; 9031.ENSGALP00000031979; -.
DR PaxDb; P05094; -.
DR Ensembl; ENSGALT00000061392; ENSGALP00000051864; ENSGALG00000042458. [P05094-2]
DR Ensembl; ENSGALT00000090288; ENSGALP00000064789; ENSGALG00000042458. [P05094-1]
DR GeneID; 373918; -.
DR KEGG; gga:373918; -.
DR CTD; 87; -.
DR VEuPathDB; HostDB:geneid_373918; -.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000155548; -.
DR InParanoid; P05094; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; P05094; -.
DR TreeFam; TF352676; -.
DR SABIO-RK; P05094; -.
DR EvolutionaryTrace; P05094; -.
DR PRO; PR:P05094; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000042458; Expressed in colon and 14 other tissues.
DR ExpressionAtlas; P05094; baseline and differential.
DR GO; GO:0005923; C:bicellular tight junction; IDA:AgBase.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0031252; C:cell leading edge; IDA:AgBase.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0097433; C:dense body; IDA:AgBase.
DR GO; GO:0005925; C:focal adhesion; IDA:AgBase.
DR GO; GO:0090637; C:inner dense plaque of desmosome; IDA:AgBase.
DR GO; GO:0030027; C:lamellipodium; IDA:AgBase.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:AgBase.
DR GO; GO:0090636; C:outer dense plaque of desmosome; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IMP:AgBase.
DR GO; GO:0030486; C:smooth muscle dense body; IDA:AgBase.
DR GO; GO:0001725; C:stress fiber; IDA:AgBase.
DR GO; GO:1990357; C:terminal web; IDA:AgBase.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0005915; C:zonula adherens; IDA:AgBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0051393; F:alpha-actinin binding; IDA:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030274; F:LIM domain binding; IPI:AgBase.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:AgBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
DR GO; GO:0017166; F:vinculin binding; IDA:AgBase.
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:0045214; P:sarcomere organization; IMP:AgBase.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP: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 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Calcium; Cell junction;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..893
FT /note="Alpha-actinin-1"
FT /id="PRO_0000073434"
FT DOMAIN 32..136
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 145..251
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 275..385
FT /note="Spectrin 1"
FT REPEAT 395..500
FT /note="Spectrin 2"
FT REPEAT 510..621
FT /note="Spectrin 3"
FT REPEAT 631..734
FT /note="Spectrin 4"
FT DOMAIN 747..782
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 788..823
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..248
FT /note="Actin-binding"
FT BINDING 760
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 762
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 764
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 766
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 771
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 13
FT /note="Phosphotyrosine; by FAK1"
FT /evidence="ECO:0000250"
FT VAR_SEQ 762..773
FT /note="DHSGTLGPEEFK -> KKTGMMDCEDFR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1556133"
FT /id="VSP_000710"
FT VAR_SEQ 779..788
FT /note="LGYDIGNDAQ -> MGYNM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1556133"
FT /id="VSP_000711"
FT CONFLICT 155
FT /note="C -> Y (in Ref. 2; AAA48567)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="T -> S (in Ref. 1; AAA48570)"
FT /evidence="ECO:0000305"
FT CONFLICT 852..853
FT /note="EL -> DV (in Ref. 3; CAA32079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 893 AA; 103162 MW; B9D1CE5A2C6F8821 CRC64;
MDHHYDPQQT NDYMQPEEDW DRDLLLDPAW EKQQRKTFTA WCNSHLRKAG TQIENIEEDF
RDGLKLMLLL EVISGERLAK PERGKMRVHK ISNVNKALDF IASKGVKLVS IGAEEIVDGN
VKMTLGMIWT IILRFAIQDI SVEETSAKEG LLLWCQRKTA PYKNVNIQNF HISWKDGLGF
CALIHRHRPE LIDYGKLRKD DPLTNLNTAF DVAEKYLDIP KMLDAEDIVG TARPDEKAIM
TYVSSFYHAF SGAQKAETAA NRICKVLAVN QENEQLMEDY EKLASDLLEW IRRTIPWLEN
RAPENTMQAM QQKLEDFRDY RRLHKPPKVQ EKCQLEINFN TLQTKLRLSN RPAFMPSEGK
MVSDINNAWG GLEQAEKGYE EWLLNEIRRL ERLDHLAEKF RQKASIHESW TDGKEAMLQQ
KDYETATLSE IKALLKKHEA FESDLAAHQD RVEQIAAIAQ ELNELDYYDS PSVNARCQKI
CDQWDNLGAL TQKRREALER TEKLLETIDQ LYLEYAKRAA PFNNWMEGAM EDLQDTFIVH
TIEEIQGLTT AHEQFKATLP DADKERQAIL GIHNEVSKIV QTYHVNMAGT NPYTTITPQE
INGKWEHVRQ LVPRRDQALM EEHARQQQNE RLRKQFGAQA NVIGPWIQTK MEEIGRISIE
MHGTLEDQLN HLRQYEKSIV NYKPKIDQLE GDHQQIQEAL IFDNKHTNYT MEHIRVGWEQ
LLTTIARTIN EVENQILTRD AKGISQEQMN EFRASFNHFD RDHSGTLGPE EFKACLISLG
YDIGNDAQGE AEFARIMSIV DPNRMGVVTF QAFIDFMSRE TADTDTADQV MASFKILAGD
KNYITVDELR RELPPDQAEY CIARMAPYNG RDAVPGALDY MSFSTALYGE SDL
