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P18091 (ACTN_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-actinin, sarcomeric
Alternative name(s):
F-actin cross-linking protein
Gene names
Name:Actn
Synonyms:fliA, l(1)2Cb
ORF Names:CG4376
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length924 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Ref.1 Ref.6

Subunit structure

Homodimer; antiparallel. Interacts with Smn; the interaction occurs in adult thoracic tissues. Ref.7

Subcellular location

CytoplasmmyofibrilsarcomereZ line. Note: Colocalizes with Smn at the Z-line of indirect flight muscles. Ref.7

Tissue specificity

Larval muscle isoform isexpressed in the larval body wall, adult muscles of the head and abdomen and supercontractile muscles of the larva and adult. Adult muscle isoform accumulateswithin adult fibrillar and tubular muscles. Ref.6 Ref.7

Developmental stage

Larval muscle isoform isfound in the larvae and adults, the adult muscle isoform inadults only. Ref.6

Sequence similarities

Belongs to the alpha-actinin family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 2 EF-hand domains.

Contains 4 spectrin repeats.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform Long (identifier: P18091-1)

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.
Isoform Non-muscle (identifier: P18091-2)

The sequence of this isoform differs from the canonical sequence as follows:
     229-260: Missing.
     261-261: N → Q
Isoform Larval muscle (identifier: P18091-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     261-286: NTALPDERAVMTYVSSYYHCFSGAQK → VTHVPEPTRQYTYVPNNYN
Isoform Adult muscle (identifier: P18091-4)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     258-286: Missing.
Isoform A (identifier: P18091-5)

The sequence of this isoform differs from the canonical sequence as follows:
     231-260: INTPKPDERAIMTYVSCYYHAFQGAQQVGN → Q

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 924924Alpha-actinin, sarcomeric
PRO_0000073447

Regions

Domain1 – 250250Actin-binding
Domain34 – 138105CH 1
Domain147 – 250104CH 2
Repeat251 – 395145Spectrin 1
Repeat396 – 510115Spectrin 2
Repeat511 – 631121Spectrin 3
Repeat632 – 744113Spectrin 4
Domain778 – 81336EF-hand 1
Domain819 – 85436EF-hand 2
Calcium binding791 – 802121 By similarity
Calcium binding832 – 843122 By similarity

Natural variations

Alternative sequence229 – 26032Missing in isoform Non-muscle.
VSP_000712
Alternative sequence231 – 26030INTPK…QQVGN → Q in isoform A.
VSP_000713
Alternative sequence258 – 28629Missing in isoform Adult muscle.
VSP_000715
Alternative sequence261 – 28626NTALP…SGAQK → VTHVPEPTRQYTYVPNNYN in isoform Larval muscle.
VSP_000716
Alternative sequence2611N → Q in isoform Non-muscle.
VSP_000714

Experimental info

Sequence conflict4091A → G in CAA36042. Ref.1
Sequence conflict4571C → Y in CAA36042. Ref.1
Sequence conflict4741S → C in CAA36042. Ref.1
Sequence conflict5031S → C in CAA36042. Ref.1
Sequence conflict5741E → V in CAA36042. Ref.1
Sequence conflict6541L → R in CAA36042. Ref.1
Sequence conflict684 – 6918AVTAIGMG → VVTPLVWD in CAA36042. Ref.1
Sequence conflict7111Y → H in CAA36042. Ref.1
Sequence conflict8171D → E in CAA36042. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: 08F8961520328ACE

FASTA924107,019
        10         20         30         40         50         60 
MMMENGLSME YGDGYMEQEE EWEREGLLDP AWEKQQKKTF TAWCNSHLRK AGTAIDNIEE 

        70         80         90        100        110        120 
DFRNGLKLML LLEVISGETL PKPDRGKMRF HKIANVNKAL DFIASKGVHL VSIGAEEIVD 

       130        140        150        160        170        180 
GNLKMTLGMI WTIILRFAIQ DISVEEMTAK EGLLLWCQRK TAPYKNVNVQ NFHLSFKDGL 

       190        200        210        220        230        240 
AFCALIHRHR PDLIDYAKLS KDNPLENLNT AFDVAEKYLD IPRMLDPDDL INTPKPDERA 

       250        260        270        280        290        300 
IMTYVSCYYH AFQGAQQVGN NTALPDERAV MTYVSSYYHC FSGAQKAETA ANRICKVLKV 

       310        320        330        340        350        360 
NQENERLMEE YERLASDLLE WIRRTMPWLN SRQADNSLAG VQKKLEEYRT YRRKHKPPRV 

       370        380        390        400        410        420 
EQKAKLETNF NTLQTKLRLS NRPAYLPTEG KTVSDISNSW KGLELAEKAF EEWLLAETMR 

       430        440        450        460        470        480 
LERLEHLAQK FKHKADAHED WTRGKEEMLQ SQDFRQCKLN ELKALKKKHE AFESDLAAHQ 

       490        500        510        520        530        540 
DRVEQIAAIA QELNTLEYHD CVSVNARCQR ICDQWDRLGA LTQRRRTALD EAERILEKID 

       550        560        570        580        590        600 
ILHLEFAKRA APFNNWLDGT REDLVDMFIV HTMEEIQGLI QAHDQFKATL GEADKEFNLI 

       610        620        630        640        650        660 
VNLVREVESI VKQHQIPGGL ENPYTTLTAN DMTRKWSDVR QLVPQRDQTL ANELRKQQNN 

       670        680        690        700        710        720 
EMLRRQFAEK ANIVGPWIER QMDAVTAIGM GLQGSLEDQL HRLKEYEQAV YAYKPNIEEL 

       730        740        750        760        770        780 
EKIHQAVQES MIFENRYTNY TMETLRVGWE QLLTSINRNI NEVENQILTR DSKGISQEQL 

       790        800        810        820        830        840 
NEFRSSFNHF DKNRTGRLSP EEFKSCLVSL GYSIGKDRQG DLDFQRILAV VDPNNTGYVH 

       850        860        870        880        890        900 
FDAFLDFMTR ESTDTDTAEQ VIDSFRILAA DKPYILPDEL RRELPPDQAE YCIQRMPPYK 

       910        920 
GPNGVPGALD YMSFSTALYG ETDL 

« Hide

Isoform Non-muscle [UniParc].

Checksum: CDE214DD3B7E5A72
Show »

FASTA892103,420
Isoform Larval muscle (C) [UniParc].

Checksum: 31573181B7230DAA
Show »

FASTA917106,373
Isoform Adult muscle (B) [UniParc].

Checksum: 196879A84FB0E259
Show »

FASTA895103,828
Isoform A [UniParc].

Checksum: FB2D59D86C6B9619
Show »

FASTA895103,763

References

« Hide 'large scale' references
[1]"Molecular genetics of Drosophila alpha-actinin: mutant alleles disrupt Z disc integrity and muscle insertions."
Fyrberg E.A., Kelly M., Ball E., Fyrberg C., Reedy M.C.
J. Cell Biol. 110:1999-2011(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ADULT MUSCLE), FUNCTION.
Strain: Canton-S.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]"From sequence to chromosome: the tip of the X chromosome of D. melanogaster."
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. expand/collapse author list , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M.
Science 287:2220-2222(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS LONG AND ADULT MUSCLE).
Strain: Oregon-R.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Embryo.
[6]"Perturbations of Drosophila alpha-actinin cause muscle paralysis, weakness, and atrophy but do not confer obvious nonmuscle phenotypes."
Roulier E.M., Fyrberg C., Fyrberg E.
J. Cell Biol. 116:911-922(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 229-286 (ISOFORM NON-MUSCLE), ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Oregon-R.
Tissue: Embryo.
[7]"A Drosophila melanogaster model of spinal muscular atrophy reveals a function for SMN in striated muscle."
Rajendra T.K., Gonsalvez G.B., Walker M.P., Shpargel K.B., Salz H.K., Matera A.G.
J. Cell Biol. 176:831-841(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51753 mRNA. Translation: CAA36042.1.
AE014298 Genomic DNA. Translation: AAF45705.2.
AE014298 Genomic DNA. Translation: AAF45706.2.
AE014298 Genomic DNA. Translation: AAN09068.1.
AL009192, AL031765 Genomic DNA. Translation: CAA15688.1.
AL009192, AL031765 Genomic DNA. Translation: CAA15689.1.
AL031765, AL009192 Genomic DNA. Translation: CAA21120.1.
AL031765, AL009192 Genomic DNA. Translation: CAA21121.1.
AY069615 mRNA. Translation: AAL39760.1.
X64419 mRNA. Translation: CAA45764.1.
PIRFAFFAA. A35598.
T13413.
T13414.
RefSeqNP_001188532.1. NM_001201603.2.
NP_001188533.1. NM_001201604.2.
NP_001259165.1. NM_001272236.1.
NP_001259166.1. NM_001272237.1.
NP_001259167.1. NM_001272238.1.
NP_477484.2. NM_058136.4.
NP_477485.1. NM_058137.5.
NP_726784.1. NM_166920.2.
UniGeneDm.25.

3D structure databases

ProteinModelPortalP18091.
SMRP18091. Positions 31-255, 300-924.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid57710. 35 interactions.
DIPDIP-22313N.

Proteomic databases

PaxDbP18091.
PRIDEP18091.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID31166.
KEGGdme:Dmel_CG4376.

Organism-specific databases

CTD31166.
FlyBaseFBgn0000667. Actn.

Phylogenomic databases

eggNOGCOG5069.
InParanoidP18091.
KOK05699.
OMAWIRRTMP.
OrthoDBEOG72C4ZJ.
PhylomeDBP18091.

Gene expression databases

BgeeP18091.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProIPR001589. Actinin_actin-bd_CS.
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]
PfamPF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS00019. 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]
ProtoNetSearch...

Other

ChiTaRSActn. drosophila.
GenomeRNAi31166.
NextBio772252.
PROP18091.

Entry information

Entry nameACTN_DROME
AccessionPrimary (citable) accession number: P18091
Secondary accession number(s): O46044 expand/collapse secondary AC list , O46045, Q24370, Q8T024, Q9W536, Q9W537
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 21, 2001
Last modified: April 16, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase