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P18091

- ACTN_DROME

UniProt

P18091 - ACTN_DROME

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Protein

Alpha-actinin, sarcomeric

Gene
Actn, fliA, l(1)2Cb, CG4376
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi791 – 802121 By similarityAdd
BLAST
Calcium bindingi832 – 843122 By similarityAdd
BLAST

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. actin crosslink formation Source: InterPro
  2. actin cytoskeleton reorganization Source: FlyBase
  3. actin filament bundle assembly Source: InterPro
  4. cytoskeletal anchoring at plasma membrane Source: FlyBase
  5. flight behavior Source: FlyBase
  6. sarcomere organization Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_184300. Syndecan interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-actinin, sarcomeric
Alternative name(s):
F-actin cross-linking protein
Gene namesi
Name:Actn
Synonyms:fliA, l(1)2Cb
ORF Names:CG4376
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0000667. Actn.

Subcellular locationi

CytoplasmmyofibrilsarcomereZ line
Note: Colocalizes with Smn at the Z-line of indirect flight muscles.1 Publication

GO - Cellular componenti

  1. focal adhesion Source: FlyBase
  2. Z disc Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 924924Alpha-actinin, sarcomericPRO_0000073447Add
BLAST

Proteomic databases

PaxDbiP18091.
PRIDEiP18091.

Expressioni

Tissue specificityi

Larval muscle isoform is expressed in the larval body wall, adult muscles of the head and abdomen and supercontractile muscles of the larva and adult. Adult muscle isoform accumulates within adult fibrillar and tubular muscles.2 Publications

Developmental stagei

Larval muscle isoform is found in the larvae and adults, the adult muscle isoform in adults only.1 Publication

Gene expression databases

BgeeiP18091.

Interactioni

Subunit structurei

Homodimer; antiparallel. Interacts with Smn; the interaction occurs in adult thoracic tissues.1 Publication

Protein-protein interaction databases

BioGridi57710. 35 interactions.
DIPiDIP-22313N.

Structurei

3D structure databases

ProteinModelPortaliP18091.
SMRiP18091. Positions 31-255, 300-924.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 250250Actin-bindingAdd
BLAST
Domaini34 – 138105CH 1Add
BLAST
Domaini147 – 250104CH 2Add
BLAST
Repeati251 – 395145Spectrin 1Add
BLAST
Repeati396 – 510115Spectrin 2Add
BLAST
Repeati511 – 631121Spectrin 3Add
BLAST
Repeati632 – 744113Spectrin 4Add
BLAST
Domaini778 – 81336EF-hand 1Add
BLAST
Domaini819 – 85436EF-hand 2Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
InParanoidiP18091.
KOiK05699.
OMAiWIRRTMP.
OrthoDBiEOG72C4ZJ.
PhylomeDBiP18091.

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. 4 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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform Long (identifier: P18091-1) [UniParc]FASTAAdd to Basket

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

MMMENGLSME YGDGYMEQEE EWEREGLLDP AWEKQQKKTF TAWCNSHLRK    50
AGTAIDNIEE DFRNGLKLML LLEVISGETL PKPDRGKMRF HKIANVNKAL 100
DFIASKGVHL VSIGAEEIVD GNLKMTLGMI WTIILRFAIQ DISVEEMTAK 150
EGLLLWCQRK TAPYKNVNVQ NFHLSFKDGL AFCALIHRHR PDLIDYAKLS 200
KDNPLENLNT AFDVAEKYLD IPRMLDPDDL INTPKPDERA IMTYVSCYYH 250
AFQGAQQVGN NTALPDERAV MTYVSSYYHC FSGAQKAETA ANRICKVLKV 300
NQENERLMEE YERLASDLLE WIRRTMPWLN SRQADNSLAG VQKKLEEYRT 350
YRRKHKPPRV EQKAKLETNF NTLQTKLRLS NRPAYLPTEG KTVSDISNSW 400
KGLELAEKAF EEWLLAETMR LERLEHLAQK FKHKADAHED WTRGKEEMLQ 450
SQDFRQCKLN ELKALKKKHE AFESDLAAHQ DRVEQIAAIA QELNTLEYHD 500
CVSVNARCQR ICDQWDRLGA LTQRRRTALD EAERILEKID ILHLEFAKRA 550
APFNNWLDGT REDLVDMFIV HTMEEIQGLI QAHDQFKATL GEADKEFNLI 600
VNLVREVESI VKQHQIPGGL ENPYTTLTAN DMTRKWSDVR QLVPQRDQTL 650
ANELRKQQNN EMLRRQFAEK ANIVGPWIER QMDAVTAIGM GLQGSLEDQL 700
HRLKEYEQAV YAYKPNIEEL EKIHQAVQES MIFENRYTNY TMETLRVGWE 750
QLLTSINRNI NEVENQILTR DSKGISQEQL NEFRSSFNHF DKNRTGRLSP 800
EEFKSCLVSL GYSIGKDRQG DLDFQRILAV VDPNNTGYVH FDAFLDFMTR 850
ESTDTDTAEQ VIDSFRILAA DKPYILPDEL RRELPPDQAE YCIQRMPPYK 900
GPNGVPGALD YMSFSTALYG ETDL 924
Length:924
Mass (Da):107,019
Last modified:February 21, 2001 - v2
Checksum:i08F8961520328ACE
GO
Isoform Non-muscle (identifier: P18091-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     229-260: Missing.
     261-261: N → Q

Show »
Length:892
Mass (Da):103,420
Checksum:iCDE214DD3B7E5A72
GO
Isoform Larval muscle (identifier: P18091-3) [UniParc]FASTAAdd to Basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     261-286: NTALPDERAVMTYVSSYYHCFSGAQK → VTHVPEPTRQYTYVPNNYN

Show »
Length:917
Mass (Da):106,373
Checksum:i31573181B7230DAA
GO
Isoform Adult muscle (identifier: P18091-4) [UniParc]FASTAAdd to Basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     258-286: Missing.

Show »
Length:895
Mass (Da):103,828
Checksum:i196879A84FB0E259
GO
Isoform A (identifier: P18091-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:895
Mass (Da):103,763
Checksum:iFB2D59D86C6B9619
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei229 – 26032Missing in isoform Non-muscle. VSP_000712Add
BLAST
Alternative sequencei231 – 26030INTPK…QQVGN → Q in isoform A. VSP_000713Add
BLAST
Alternative sequencei258 – 28629Missing in isoform Adult muscle. VSP_000715Add
BLAST
Alternative sequencei261 – 28626NTALP…SGAQK → VTHVPEPTRQYTYVPNNYN in isoform Larval muscle. VSP_000716Add
BLAST
Alternative sequencei261 – 2611N → Q in isoform Non-muscle. VSP_000714

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti409 – 4091A → G in CAA36042. 1 Publication
Sequence conflicti457 – 4571C → Y in CAA36042. 1 Publication
Sequence conflicti474 – 4741S → C in CAA36042. 1 Publication
Sequence conflicti503 – 5031S → C in CAA36042. 1 Publication
Sequence conflicti574 – 5741E → V in CAA36042. 1 Publication
Sequence conflicti654 – 6541L → R in CAA36042. 1 Publication
Sequence conflicti684 – 6918AVTAIGMG → VVTPLVWD in CAA36042. 1 Publication
Sequence conflicti711 – 7111Y → H in CAA36042. 1 Publication
Sequence conflicti817 – 8171D → E in CAA36042. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA35598. FAFFAA.
T13413.
T13414.
RefSeqiNP_001188532.1. NM_001201603.2. [P18091-4]
NP_001188533.1. NM_001201604.2. [P18091-4]
NP_001259165.1. NM_001272236.1. [P18091-3]
NP_001259166.1. NM_001272237.1. [P18091-3]
NP_001259167.1. NM_001272238.1. [P18091-3]
NP_477484.2. NM_058136.4. [P18091-5]
NP_477485.1. NM_058137.5. [P18091-3]
NP_726784.1. NM_166920.2. [P18091-4]
UniGeneiDm.25.

Genome annotation databases

GeneIDi31166.
KEGGidme:Dmel_CG4376.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A35598. FAFFAA.
T13413.
T13414.
RefSeqi NP_001188532.1. NM_001201603.2. [P18091-4 ]
NP_001188533.1. NM_001201604.2. [P18091-4 ]
NP_001259165.1. NM_001272236.1. [P18091-3 ]
NP_001259166.1. NM_001272237.1. [P18091-3 ]
NP_001259167.1. NM_001272238.1. [P18091-3 ]
NP_477484.2. NM_058136.4. [P18091-5 ]
NP_477485.1. NM_058137.5. [P18091-3 ]
NP_726784.1. NM_166920.2. [P18091-4 ]
UniGenei Dm.25.

3D structure databases

ProteinModelPortali P18091.
SMRi P18091. Positions 31-255, 300-924.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 57710. 35 interactions.
DIPi DIP-22313N.

Proteomic databases

PaxDbi P18091.
PRIDEi P18091.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 31166.
KEGGi dme:Dmel_CG4376.

Organism-specific databases

CTDi 31166.
FlyBasei FBgn0000667. Actn.

Phylogenomic databases

eggNOGi COG5069.
InParanoidi P18091.
KOi K05699.
OMAi WIRRTMP.
OrthoDBi EOG72C4ZJ.
PhylomeDBi P18091.

Enzyme and pathway databases

Reactomei REACT_184300. Syndecan interactions.

Miscellaneous databases

ChiTaRSi Actn. drosophila.
GenomeRNAii 31166.
NextBioi 772252.
PROi P18091.

Gene expression databases

Bgeei P18091.

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. 4 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

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS LONG AND ADULT MUSCLE).
    Strain: Oregon-R.
  5. 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.

Entry informationi

Entry nameiACTN_DROME
AccessioniPrimary (citable) accession number: P18091
Secondary accession number(s): O46044
, O46045, Q24370, Q8T024, Q9W536, Q9W537
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 21, 2001
Last modified: September 3, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi