ID M9PGA7_DROME Unreviewed; 917 AA.
AC M9PGA7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Alpha actinin, isoform G {ECO:0000313|EMBL:AGB95011.1};
DE SubName: Full=Alpha actinin, isoform H {ECO:0000313|EMBL:AGB95012.1};
DE SubName: Full=Alpha actinin, isoform J {ECO:0000313|EMBL:AGB95013.1};
GN Name=Actn {ECO:0000313|EMBL:AGB95013.1,
GN ECO:0000313|FlyBase:FBgn0000667};
GN Synonyms=ACTN {ECO:0000313|EMBL:AGB95013.1}, actn
GN {ECO:0000313|EMBL:AGB95013.1}, alpha-actinin
GN {ECO:0000313|EMBL:AGB95013.1}, alphaActn
GN {ECO:0000313|EMBL:AGB95013.1}, CT14163 {ECO:0000313|EMBL:AGB95013.1},
GN CT14232 {ECO:0000313|EMBL:AGB95013.1}, Dmel\CG4376
GN {ECO:0000313|EMBL:AGB95013.1}, EG:133E12.1
GN {ECO:0000313|EMBL:AGB95013.1}, fliA {ECO:0000313|EMBL:AGB95013.1},
GN GA17 {ECO:0000313|EMBL:AGB95013.1}, HM-29
GN {ECO:0000313|EMBL:AGB95013.1}, l(1)2Cb {ECO:0000313|EMBL:AGB95013.1},
GN l(1)EA82 {ECO:0000313|EMBL:AGB95013.1}, y
GN {ECO:0000313|EMBL:AGB95013.1};
GN ORFNames=CG4376 {ECO:0000313|EMBL:AGB95013.1,
GN ECO:0000313|FlyBase:FBgn0000667}, Dmel_CG4376
GN {ECO:0000313|EMBL:AGB95013.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AGB95013.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AGB95013.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|EMBL:AGB95013.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|EMBL:AGB95013.1, ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000313|EMBL:AGB95013.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AGB95013.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AGB95013.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AGB95013.1}
RP NUCLEOTIDE SEQUENCE.
RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA Svirskas R., Rubin G.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|EMBL:AGB95013.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [9] {ECO:0000313|EMBL:AGB95013.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
RN [10] {ECO:0000313|EMBL:AGB95013.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26109357; DOI=.1534/g3.115.018929;
RG FlyBase Consortium;
RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E.,
RA Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M.,
RA Gelbart W.M., null;
RT "Gene Model Annotations for Drosophila melanogaster: Impact of High-
RT Throughput Data.";
RL G3 (Bethesda) 5:1721-1736(2015).
RN [11] {ECO:0000313|EMBL:AGB95013.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26109356; DOI=.1534/g3.115.018937;
RG FlyBase Consortium;
RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E.,
RA Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.,
RA null;
RT "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.";
RL G3 (Bethesda) 5:1737-1749(2015).
RN [12] {ECO:0000313|EMBL:AGB95013.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25589440;
RA Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E.,
RA Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M.,
RA Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M.,
RA de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M.,
RA Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M.,
RA Karpen G.H., Celniker S.E.;
RT "The Release 6 reference sequence of the Drosophila melanogaster genome.";
RL Genome Res. 25:445-458(2015).
RN [13] {ECO:0000313|EMBL:AGB95013.1}
RP NUCLEOTIDE SEQUENCE.
RG Berkeley Drosophila Genome Project;
RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C.,
RA Rubin G.;
RT "Drosophila melanogaster release 4 sequence.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN [14] {ECO:0000313|EMBL:AGB95013.1}
RP NUCLEOTIDE SEQUENCE.
RG FlyBase;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the alpha-actinin family.
CC {ECO:0000256|ARBA:ARBA00010255}.
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DR EMBL; AE014298; AGB95011.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95012.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95013.1; -; Genomic_DNA.
DR RefSeq; NP_001259165.1; NM_001272236.1.
DR RefSeq; NP_001259166.1; NM_001272237.1.
DR RefSeq; NP_001259167.1; NM_001272238.1.
DR RefSeq; NP_477485.1; NM_058137.6.
DR AlphaFoldDB; M9PGA7; -.
DR SMR; M9PGA7; -.
DR EnsemblMetazoa; FBtr0070345; FBpp0070331; FBgn0000667.
DR EnsemblMetazoa; FBtr0310658; FBpp0302778; FBgn0000667.
DR EnsemblMetazoa; FBtr0310659; FBpp0302779; FBgn0000667.
DR EnsemblMetazoa; FBtr0333802; FBpp0305936; FBgn0000667.
DR GeneID; 31166; -.
DR KEGG; dme:Dmel_CG4376; -.
DR AGR; FB:FBgn0000667; -.
DR CTD; 31166; -.
DR FlyBase; FBgn0000667; Actn.
DR VEuPathDB; VectorBase:FBgn0000667; -.
DR OMA; CYEGVEV; -.
DR OrthoDB; 2872403at2759; -.
DR BioGRID-ORCS; 31166; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Actn; fly.
DR GenomeRNAi; 31166; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000667; Expressed in crop (Drosophila) and 36 other cell types or tissues.
DR ExpressionAtlas; M9PGA7; baseline and differential.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd21214; CH_ACTN_rpt1; 1.
DR CDD; cd21216; CH_ACTN_rpt2; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 3.
DR Gene3D; 1.20.58.60; -; 4.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
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:SF442; ALPHA-ACTININ, SARCOMERIC-RELATED; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 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; SM01184; efhand_Ca_insen; 1.
DR SMART; SM00150; SPEC; 4.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 4.
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 1: Evidence at protein level;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9PGA7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 34..138
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 147..253
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 771..806
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 812..847
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 290..317
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 448..475
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 917 AA; 106373 MW; 31573181B7230DAA CRC64;
MMMENGLSME YGDGYMEQEE EWEREGLLDP AWEKQQKKTF TAWCNSHLRK AGTAIDNIEE
DFRNGLKLML LLEVISGETL PKPDRGKMRF HKIANVNKAL DFIASKGVHL VSIGAEEIVD
GNLKMTLGMI WTIILRFAIQ DISVEEMTAK EGLLLWCQRK TAPYKNVNVQ NFHLSFKDGL
AFCALIHRHR PDLIDYAKLS KDNPLENLNT AFDVAEKYLD IPRMLDPDDL INTPKPDERA
IMTYVSCYYH AFQGAQQVGN VTHVPEPTRQ YTYVPNNYNA ETAANRICKV LKVNQENERL
MEEYERLASD LLEWIRRTMP WLNSRQADNS LAGVQKKLEE YRTYRRKHKP PRVEQKAKLE
TNFNTLQTKL RLSNRPAYLP TEGKTVSDIS NSWKGLELAE KAFEEWLLAE TMRLERLEHL
AQKFKHKADA HEDWTRGKEE MLQSQDFRQC KLNELKALKK KHEAFESDLA AHQDRVEQIA
AIAQELNTLE YHDCVSVNAR CQRICDQWDR LGALTQRRRT ALDEAERILE KIDILHLEFA
KRAAPFNNWL DGTREDLVDM FIVHTMEEIQ GLIQAHDQFK ATLGEADKEF NLIVNLVREV
ESIVKQHQIP GGLENPYTTL TANDMTRKWS DVRQLVPQRD QTLANELRKQ QNNEMLRRQF
AEKANIVGPW IERQMDAVTA IGMGLQGSLE DQLHRLKEYE QAVYAYKPNI EELEKIHQAV
QESMIFENRY TNYTMETLRV GWEQLLTSIN RNINEVENQI LTRDSKGISQ EQLNEFRSSF
NHFDKNRTGR LSPEEFKSCL VSLGYSIGKD RQGDLDFQRI LAVVDPNNTG YVHFDAFLDF
MTRESTDTDT AEQVIDSFRI LAADKPYILP DELRRELPPD QAEYCIQRMP PYKGPNGVPG
ALDYMSFSTA LYGETDL
//
