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P05094

- ACTN1_CHICK

UniProt

P05094 - ACTN1_CHICK

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Protein
Alpha-actinin-1
Gene
ACTN1
Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 771121 Reviewed prediction
Add
BLAST
Calcium bindingi801 – 812122 Reviewed prediction
Add
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
Complete GO annotation...

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

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-1
PRO_0000073434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphotyrosine; by FAK1 By 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

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.

Miscellaneous databases

EvolutionaryTraceiP05094.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the alpha-actinin family.
Contains 2 EF-hand domains.
Contains 4 spectrin repeats.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei762 – 77312DHSGT…PEEFK → KKTGMMDCEDFR in isoform 2.
VSP_000710Add
BLAST
Alternative sequencei779 – 78810LGYDIGNDAQ → MGYNM in isoform 2.
VSP_000711

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551C → Y in AAA48567. 1 Publication
Sequence conflicti501 – 5011T → S in AAA48570. 1 Publication
Sequence conflicti852 – 8532EL → DV in CAA32079. 1 Publication

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: September 3, 2014
This is version 140 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

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