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Database: UniProt
Entry: ACTN1_BOVIN
LinkDB: ACTN1_BOVIN
Original site: ACTN1_BOVIN 
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   03-SEP-2014, entry version 81.
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. Interacts with MICALL2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC       myofibril, sarcomere, Z line. Cell membrane (By similarity). Cell
CC       junction (By similarity). Cell projection, ruffle (By similarity).
CC       Note=Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and
CC       skeletal muscle (By similarity). Colocalizes with PSD in membrane
CC       ruffles and central 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   RefSeq; NP_001030428.1; NM_001035351.2.
DR   UniGene; Bt.57772; -.
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; WIRRTMP; -.
DR   OrthoDB; EOG72C4ZJ; -.
DR   TreeFam; TF352676; -.
DR   Reactome; REACT_204848; Syndecan interactions.
DR   Reactome; REACT_211504; Nephrin interactions.
DR   Reactome; REACT_214421; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR   NextBio; 20874035; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl.
DR   GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
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:0003725; F:double-stranded RNA binding; IEA:Ensembl.
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:Ensembl.
DR   GO; GO:0051234; P:establishment of localization; NAS:UniProtKB.
DR   GO; GO:0048041; P:focal adhesion assembly; IEA:Ensembl.
DR   GO; GO:0051271; P:negative regulation of cellular component movement; IEA:Ensembl.
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_1.
DR   InterPro; IPR001715; CH-domain.
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   PANTHER; PTHR11915:SF241; PTHR11915:SF241; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF13405; EF-hand_6; 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; 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   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Calcium; Cell junction; Cell membrane;
KW   Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Membrane;
KW   Metal-binding; 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
//
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