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P05094

- ACTN1_CHICK

UniProt

P05094 - ACTN1_CHICK

Protein

Alpha-actinin-1

Gene

ACTN1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (21 Feb 2001)
      Previous versions | rss
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    Functioni

    F-actin cross-linking protein is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi760 – 771121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi801 – 812122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. actin crosslink formation Source: InterPro
    2. actin filament bundle assembly Source: InterPro

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_197897. Syndecan interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-actinin-1
    Alternative name(s):
    Alpha-actinin cytoskeletal isoform
    F-actin cross-linking protein
    Non-muscle alpha-actinin-1
    Gene namesi
    Name:ACTN1
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. CytoplasmmyofibrilsarcomereZ line By similarity. Cell membrane By similarity. Cell junction By similarity. Cell projectionruffle By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-SubCell
    2. cytoskeleton Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB-SubCell
    4. ruffle Source: UniProtKB-SubCell
    5. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 893893Alpha-actinin-1PRO_0000073434Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131Phosphotyrosine; by FAK1By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP05094.
    PRIDEiP05094.

    Interactioni

    Subunit structurei

    Homodimer; antiparallel.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ICAM5Q9UMF03EBI-5847257,EBI-6398041From a different organism.
    ITGB1P072284EBI-5847257,EBI-5606437
    ITGB3P051062EBI-5847257,EBI-702847From a different organism.
    VCLP120035EBI-6049246,EBI-1039563
    ZYXQ045844EBI-6049246,EBI-6222189

    Protein-protein interaction databases

    BioGridi674968. 1 interaction.
    IntActiP05094. 7 interactions.

    Structurei

    Secondary structure

    1
    893
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 4919
    Helixi64 – 729
    Helixi87 – 10317
    Helixi114 – 1174
    Helixi121 – 13212
    Turni148 – 1514
    Helixi152 – 1598
    Beta strandi169 – 1713
    Helixi172 – 1743
    Helixi178 – 1858
    Beta strandi190 – 1923
    Helixi195 – 1984
    Helixi203 – 2053
    Helixi208 – 21710
    Helixi225 – 2284
    Helixi236 – 24510
    Turni246 – 2505
    Turni267 – 2693
    Helixi270 – 29425
    Helixi295 – 2973
    Helixi307 – 32216
    Helixi326 – 33712
    Turni338 – 3403
    Helixi341 – 3455
    Turni346 – 3494
    Helixi362 – 3643
    Helixi365 – 37612
    Turni377 – 3793
    Helixi380 – 3878
    Helixi390 – 41930
    Turni422 – 4243
    Helixi428 – 44518
    Helixi448 – 46417
    Helixi470 – 51849
    Turni519 – 5224
    Helixi523 – 53412
    Beta strandi540 – 5423
    Helixi543 – 5453
    Helixi546 – 55611
    Helixi559 – 58123
    Beta strandi592 – 5954
    Helixi598 – 61922
    Helixi620 – 6223
    Helixi623 – 65331
    Turni661 – 6633
    Helixi666 – 68015
    Helixi683 – 6853
    Helixi686 – 69712
    Turni698 – 7003
    Helixi712 – 73827
    Helixi746 – 75611
    Turni757 – 7593
    Beta strandi761 – 7699
    Helixi772 – 7798
    Helixi791 – 80010
    Beta strandi806 – 8094
    Helixi812 – 8154
    Helixi817 – 8204
    Beta strandi825 – 8273
    Helixi828 – 8358
    Helixi836 – 8383
    Beta strandi840 – 8456
    Helixi846 – 8527
    Helixi855 – 86410
    Beta strandi865 – 8673
    Beta strandi877 – 8804
    Helixi881 – 8877

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SJJelectron microscopy20.00A/B26-893[»]
    ProteinModelPortaliP05094.
    SMRiP05094. Positions 31-255, 268-740, 822-893.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05094.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 248248Actin-bindingAdd
    BLAST
    Domaini32 – 136105CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini145 – 248104CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati275 – 385111Spectrin 1Add
    BLAST
    Repeati395 – 500106Spectrin 2Add
    BLAST
    Repeati510 – 621112Spectrin 3Add
    BLAST
    Repeati631 – 734104Spectrin 4Add
    BLAST
    Domaini747 – 78236EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini788 – 82336EF-hand 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the alpha-actinin family.Curated
    Contains 1 actin-binding domain.Curated
    Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
    Contains 2 EF-hand domains.PROSITE-ProRule annotation
    Contains 4 spectrin repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5069.
    HOGENOMiHOG000263418.
    HOVERGENiHBG050453.
    InParanoidiP05094.
    KOiK05699.
    OMAiWIRRTMP.
    OrthoDBiEOG72C4ZJ.
    PhylomeDBiP05094.
    TreeFamiTF352676.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProiIPR001589. Actinin_actin-bd_CS.
    IPR026921. Alpha-actinin_1.
    IPR001715. CH-domain.
    IPR011992. EF-hand-dom_pair.
    IPR014837. EF-hand_Ca_insen.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    [Graphical view]
    PANTHERiPTHR11915:SF241. PTHR11915:SF241. 1 hit.
    PfamiPF00307. CH. 2 hits.
    PF13405. EF-hand_6. 1 hit.
    PF08726. EFhand_Ca_insen. 1 hit.
    PF00435. Spectrin. 4 hits.
    [Graphical view]
    SMARTiSM00033. CH. 2 hits.
    SM00054. EFh. 2 hits.
    SM00150. SPEC. 3 hits.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    PROSITEiPS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Isoforms only differ in the region of the first EF-hand calcium-binding motif.

    Isoform 1 (identifier: P05094-1) [UniParc]FASTAAdd to Basket

    Also known as: Brain

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDHHYDPQQT NDYMQPEEDW DRDLLLDPAW EKQQRKTFTA WCNSHLRKAG    50
    TQIENIEEDF RDGLKLMLLL EVISGERLAK PERGKMRVHK ISNVNKALDF 100
    IASKGVKLVS IGAEEIVDGN VKMTLGMIWT IILRFAIQDI SVEETSAKEG 150
    LLLWCQRKTA PYKNVNIQNF HISWKDGLGF CALIHRHRPE LIDYGKLRKD 200
    DPLTNLNTAF DVAEKYLDIP KMLDAEDIVG TARPDEKAIM TYVSSFYHAF 250
    SGAQKAETAA NRICKVLAVN QENEQLMEDY EKLASDLLEW IRRTIPWLEN 300
    RAPENTMQAM QQKLEDFRDY RRLHKPPKVQ EKCQLEINFN TLQTKLRLSN 350
    RPAFMPSEGK MVSDINNAWG GLEQAEKGYE EWLLNEIRRL ERLDHLAEKF 400
    RQKASIHESW TDGKEAMLQQ KDYETATLSE IKALLKKHEA FESDLAAHQD 450
    RVEQIAAIAQ ELNELDYYDS PSVNARCQKI CDQWDNLGAL TQKRREALER 500
    TEKLLETIDQ LYLEYAKRAA PFNNWMEGAM EDLQDTFIVH TIEEIQGLTT 550
    AHEQFKATLP DADKERQAIL GIHNEVSKIV QTYHVNMAGT NPYTTITPQE 600
    INGKWEHVRQ LVPRRDQALM EEHARQQQNE RLRKQFGAQA NVIGPWIQTK 650
    MEEIGRISIE MHGTLEDQLN HLRQYEKSIV NYKPKIDQLE GDHQQIQEAL 700
    IFDNKHTNYT MEHIRVGWEQ LLTTIARTIN EVENQILTRD AKGISQEQMN 750
    EFRASFNHFD RDHSGTLGPE EFKACLISLG YDIGNDAQGE AEFARIMSIV 800
    DPNRMGVVTF QAFIDFMSRE TADTDTADQV MASFKILAGD KNYITVDELR 850
    RELPPDQAEY CIARMAPYNG RDAVPGALDY MSFSTALYGE SDL 893
    Length:893
    Mass (Da):103,162
    Last modified:February 21, 2001 - v3
    Checksum:iB9D1CE5A2C6F8821
    GO
    Isoform 2 (identifier: P05094-2) [UniParc]FASTAAdd to Basket

    Also known as: Smooth muscle

    The sequence of this isoform differs from the canonical sequence as follows:
         762-773: DHSGTLGPEEFK → KKTGMMDCEDFR
         779-788: LGYDIGNDAQ → MGYNM

    Show »
    Length:888
    Mass (Da):102,855
    Checksum:i5F2485A047EA644C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti155 – 1551C → Y in AAA48567. (PubMed:1556133)Curated
    Sequence conflicti501 – 5011T → S in AAA48570. (PubMed:2826427)Curated
    Sequence conflicti852 – 8532EL → DV in CAA32079. (PubMed:3197725)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei762 – 77312DHSGT…PEEFK → KKTGMMDCEDFR in isoform 2. 1 PublicationVSP_000710Add
    BLAST
    Alternative sequencei779 – 78810LGYDIGNDAQ → MGYNM in isoform 2. 1 PublicationVSP_000711

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74143 mRNA. Translation: AAA48570.1.
    X13875 mRNA. Translation: CAA32079.1.
    J02666 mRNA. Translation: AAA48566.1.
    J03486 mRNA. Translation: AAA48567.1.
    PIRiA42162.
    RefSeqiNP_989458.1. NM_204127.1.
    UniGeneiGga.4993.

    Genome annotation databases

    GeneIDi373918.
    KEGGigga:373918.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74143 mRNA. Translation: AAA48570.1 .
    X13875 mRNA. Translation: CAA32079.1 .
    J02666 mRNA. Translation: AAA48566.1 .
    J03486 mRNA. Translation: AAA48567.1 .
    PIRi A42162.
    RefSeqi NP_989458.1. NM_204127.1.
    UniGenei Gga.4993.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SJJ electron microscopy 20.00 A/B 26-893 [» ]
    ProteinModelPortali P05094.
    SMRi P05094. Positions 31-255, 268-740, 822-893.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 674968. 1 interaction.
    IntActi P05094. 7 interactions.

    Proteomic databases

    PaxDbi P05094.
    PRIDEi P05094.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 373918.
    KEGGi gga:373918.

    Organism-specific databases

    CTDi 87.

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000263418.
    HOVERGENi HBG050453.
    InParanoidi P05094.
    KOi K05699.
    OMAi WIRRTMP.
    OrthoDBi EOG72C4ZJ.
    PhylomeDBi P05094.
    TreeFami TF352676.

    Enzyme and pathway databases

    Reactomei REACT_197897. Syndecan interactions.

    Miscellaneous databases

    EvolutionaryTracei P05094.
    NextBioi 20813450.
    PROi P05094.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR026921. Alpha-actinin_1.
    IPR001715. CH-domain.
    IPR011992. EF-hand-dom_pair.
    IPR014837. EF-hand_Ca_insen.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    [Graphical view ]
    PANTHERi PTHR11915:SF241. PTHR11915:SF241. 1 hit.
    Pfami PF00307. CH. 2 hits.
    PF13405. EF-hand_6. 1 hit.
    PF08726. EFhand_Ca_insen. 1 hit.
    PF00435. Spectrin. 4 hits.
    [Graphical view ]
    SMARTi SM00033. CH. 2 hits.
    SM00054. EFh. 2 hits.
    SM00150. SPEC. 3 hits.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    PROSITEi PS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequence of chick alpha-actinin reveals homologies to spectrin and calmodulin."
      Baron M.D., Davison M.D., Jones P., Critchley D.R.
      J. Biol. Chem. 262:17623-17629(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Mutually exclusive splicing of calcium-binding domain exons in chick alpha-actinin."
      Waites G.T., Graham I.R., Jackson P., Millake D.B., Patel B., Blanchard A.D., Weller P., Eperon I.C., Critchley D.R.
      J. Biol. Chem. 267:6263-6271(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "Primary structure of chicken skeletal muscle and fibroblast alpha-actinins deduced from cDNA sequences."
      Arimura C., Suzuki T., Yanagisawa M., Imamura M., Hamada Y., Masaki T.
      Eur. J. Biochem. 177:649-655(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-893 (ISOFORM 1).
      Tissue: Fibroblast.
    4. "Isolation and characterization of a cDNA encoding a chick alpha-actinin."
      Baron M.D., Davison M.D., Jones P., Patel B., Critchley D.R.
      J. Biol. Chem. 262:2558-2561(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-769 (ISOFORM 1).
      Tissue: Fibroblast.

    Entry informationi

    Entry nameiACTN1_CHICK
    AccessioniPrimary (citable) accession number: P05094
    Secondary accession number(s): Q99001
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: February 21, 2001
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3