ID ACTN1_BOVIN Reviewed; 892 AA.
AC Q3B7N2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 01-MAY-2013, entry version 69.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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).
CC -!- SUBUNIT: Homodimer; antiparallel. Interacts with DDN, MYOZ2,
CC PDLIM2, TTID, LPP and PSD (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC myofibril, sarcomere, Z line. Cell membrane (By similarity). Cell
CC projection, ruffle (By similarity). Note=Colocalizes with MYOZ2
CC and PPP3CA at the Z-line of heart and skeletal muscle (By
CC similarity). Colocalizes with PSD in membrane ruffles and central
CC reticular structures (By similarity).
CC -!- SIMILARITY: Belongs to the alpha-actinin family.
CC -!- SIMILARITY: Contains 1 actin-binding domain.
CC -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -!- SIMILARITY: Contains 4 spectrin repeats.
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DR EMBL; BC107533; AAI07534.1; -; mRNA.
DR IPI; IPI00712562; -.
DR RefSeq; NP_001030428.1; NM_001035351.2.
DR UniGene; Bt.57772; -.
DR HSSP; P46939; 1QAG.
DR ProteinModelPortal; Q3B7N2; -.
DR SMR; Q3B7N2; 30-254, 267-739, 821-892.
DR PaxDb; Q3B7N2; -.
DR PRIDE; Q3B7N2; -.
DR Ensembl; ENSBTAT00000024301; ENSBTAP00000024301; ENSBTAG00000018255.
DR GeneID; 524770; -.
DR KEGG; bta:524770; -.
DR CTD; 87; -.
DR eggNOG; COG5069; -.
DR GeneTree; ENSGT00670000097825; -.
DR HOGENOM; HOG000263418; -.
DR HOVERGEN; HBG050453; -.
DR KO; K05699; -.
DR OMA; MLQSQDF; -.
DR NextBio; 20874035; -.
DR ArrayExpress; Q3B7N2; -.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005916; C:fascia adherens; IEA:Compara.
DR GO; GO:0005925; C:focal adhesion; IEA:Compara.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0012506; C:vesicle membrane; NAS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043495; F:protein anchor; NAS:UniProtKB.
DR GO; GO:0005523; F:tropomyosin binding; IDA:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IEA:Compara.
DR GO; GO:0051234; P:establishment of localization; NAS:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; IEA:Compara.
DR GO; GO:0051271; P:negative regulation of cellular component movement; IEA:Compara.
DR GO; GO:0043462; P:regulation of ATPase activity; IDA:UniProtKB.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; NAS:UniProtKB.
DR Gene3D; 1.10.238.10; -; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR026921; Alpha-actinin.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR011992; EF-hand-like_dom.
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 PANTHER; PTHR11915:SF47; PTHR11915:SF47; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF13405; EF_hand_4; 1.
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; SSF47576; Calponin-homology; 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 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Calcium; Cell membrane; Cell projection;
KW Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1 892 Alpha-actinin-1.
FT /FTId=PRO_0000254032.
FT DOMAIN 1 247 Actin-binding.
FT DOMAIN 31 135 CH 1.
FT DOMAIN 144 247 CH 2.
FT REPEAT 274 384 Spectrin 1.
FT REPEAT 394 499 Spectrin 2.
FT REPEAT 509 620 Spectrin 3.
FT REPEAT 630 733 Spectrin 4.
FT DOMAIN 746 781 EF-hand 1.
FT DOMAIN 787 822 EF-hand 2.
FT CA_BIND 759 770 Potential.
FT CA_BIND 800 811 Potential.
FT REGION 274 733 Interaction with DDN (By similarity).
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT MOD_RES 6 6 Phosphoserine (By similarity).
FT MOD_RES 12 12 Phosphotyrosine; by FAK1 (By similarity).
FT MOD_RES 95 95 N6-acetyllysine (By similarity).
FT MOD_RES 195 195 N6-acetyllysine (By similarity).
FT MOD_RES 676 676 N6-acetyllysine (By similarity).
SQ SEQUENCE 892 AA; 102980 MW; 98A03A62A9AA8E4A CRC64;
MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT QIENIEEDFR
DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI ASKGVKLVSI GAEEIVDGNV
KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC
ALIHRHRPEL IDYGKLRKDD PLTNLNTAFD VAEKYLDIPK MLDAEDIVGT ARPDEKAIMT
YVSSFYHAFS GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR
APENTMHAMQ 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 EHARQQHNER LRKQFGAQAN VIGPWIQTKM EEIGRISIEM
HGTLEDQLNH LRQYEKSIVN YKPKIDQLEG DHQLIQEALI FDNKHTNYTM EHIRVGWEQL
LTTIARTINE VENQILTRDA KGISQEQMNE FRASFNHFDR DHSGTLGPEE FKACLISLGY
DIGNDPQGEA EFARIMSIVD PNRLGVVTFQ AFIDFMSRET ADTDTADQVM ASFKILAGDK
NYITVDELRR ELPPDQAEYC IARMAPYTGP DAVPGALDYM SFSTALYGES DL
//
