GenomeNet

Database: UniProt
Entry: A0A0B4KHE2_DROME
LinkDB: A0A0B4KHE2_DROME
Original site: A0A0B4KHE2_DROME 
ID   A0A0B4KHE2_DROME        Unreviewed;      1152 AA.
AC   A0A0B4KHE2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Dystrophin, isoform J {ECO:0000313|EMBL:AGB96111.1};
GN   Name=Dys {ECO:0000313|EMBL:AGB96111.1,
GN   ECO:0000313|FlyBase:FBgn0260003};
GN   Synonyms=CG17750 {ECO:0000313|EMBL:AGB96111.1}, CG31175
GN   {ECO:0000313|EMBL:AGB96111.1}, CG7240 {ECO:0000313|EMBL:AGB96111.1},
GN   CG7243 {ECO:0000313|EMBL:AGB96111.1}, CG7344
GN   {ECO:0000313|EMBL:AGB96111.1}, det {ECO:0000313|EMBL:AGB96111.1}, DLP
GN   {ECO:0000313|EMBL:AGB96111.1}, DLP1 {ECO:0000313|EMBL:AGB96111.1},
GN   DLP186 {ECO:0000313|EMBL:AGB96111.1}, DLP2
GN   {ECO:0000313|EMBL:AGB96111.1}, DLP3 {ECO:0000313|EMBL:AGB96111.1},
GN   DmDLP {ECO:0000313|EMBL:AGB96111.1}, dmDLP
GN   {ECO:0000313|EMBL:AGB96111.1}, dmDp186 {ECO:0000313|EMBL:AGB96111.1},
GN   DmDYS {ECO:0000313|EMBL:AGB96111.1}, dmDys
GN   {ECO:0000313|EMBL:AGB96111.1}, Dmel\CG34157
GN   {ECO:0000313|EMBL:AGB96111.1}, Dp117 {ECO:0000313|EMBL:AGB96111.1},
GN   Dp186 {ECO:0000313|EMBL:AGB96111.1}, Dp205
GN   {ECO:0000313|EMBL:AGB96111.1}, DYS {ECO:0000313|EMBL:AGB96111.1}, dys
GN   {ECO:0000313|EMBL:AGB96111.1}, GI3046716
GN   {ECO:0000313|EMBL:AGB96111.1}, IDLP {ECO:0000313|EMBL:AGB96111.1};
GN   ORFNames=CG34157 {ECO:0000313|EMBL:AGB96111.1,
GN   ECO:0000313|FlyBase:FBgn0260003}, Dmel_CG34157
GN   {ECO:0000313|EMBL:AGB96111.1};
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:AGB96111.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AGB96111.1, 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:AGB96111.1, 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:AGB96111.1, 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:AGB96111.1, 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:AGB96111.1, 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:AGB96111.1, 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:AGB96111.1, 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   [8] {ECO:0000313|EMBL:AGB96111.1, 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).
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC       {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004278}.
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DR   EMBL; AE014297; AGB96111.1; -; Genomic_DNA.
DR   RefSeq; NP_001262731.1; NM_001275802.1.
DR   AlphaFoldDB; A0A0B4KHE2; -.
DR   SMR; A0A0B4KHE2; -.
DR   DNASU; 42327; -.
DR   EnsemblMetazoa; FBtr0334563; FBpp0306630; FBgn0260003.
DR   GeneID; 42327; -.
DR   AGR; FB:FBgn0260003; -.
DR   CTD; 42327; -.
DR   FlyBase; FBgn0260003; Dys.
DR   VEuPathDB; VectorBase:FBgn0260003; -.
DR   GeneTree; ENSGT00940000166230; -.
DR   OrthoDB; 2880153at2759; -.
DR   BioGRID-ORCS; 42327; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 42327; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0260003; Expressed in spermathecum and 62 other cell types or tissues.
DR   ExpressionAtlas; A0A0B4KHE2; baseline and differential.
DR   GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:UniProt.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0007154; P:cell communication; IEA:UniProt.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:UniProt.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:UniProt.
DR   GO; GO:0023052; P:signaling; IEA:UniProt.
DR   CDD; cd16242; EFh_DMD_like; 1.
DR   CDD; cd00201; WW; 1.
DR   CDD; cd02334; ZZ_dystrophin; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR015153; EF-hand_dom_typ1.
DR   InterPro; IPR015154; EF-hand_dom_typ2.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR12268:SF14; DYSTROPHIN-1; 1.
DR   PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR   Pfam; PF09068; EF-hand_2; 1.
DR   Pfam; PF09069; EF-hand_3; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00456; WW; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          403..436
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          661..717
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          870..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          941..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1037..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1114..1152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          264..331
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          835..869
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..168
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        870..896
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..997
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1037..1067
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1122..1152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1152 AA;  127753 MW;  CC9754CC428B112C CRC64;
     MRLFASSGQA ATSPALAHSS SDEAGEVIEN SHTKRAGCSV LQSSGGKSRS LERYSGAPKI
     HQQTLEMLPP YATPTCSTRR RLLAPFRSLK RRSRSSSSSN ESHHFGNHLN NLVVVNVGAA
     AANGGVAKAK AKASSQSGDS GTGGTELEHE MEQDDDEEDE EEGEEMDELS LSYSQLSSSG
     CEEAEAPPED VPDDRQAAVE ATVSACVQHV ANERRRNILS LYSSSSEEQL HCRLGDITLV
     DDTYSNYDPQ NDAERMFLQV VGILRDENEK MRQFQKILED LSSRVALAEQ TKTSWLPPSS
     VGEANEQMQQ LQRLRDKMTT ASALLDDCNE QQSFFTANQV LVPTPCLSKL EDLNTRMKLL
     QIAMDERQKV LCQAGAQQTH ENGDDGRTTS NSGTIGPLPN LGQSVKPPWE RATTAANVPY
     YIDHERETTH WDHPEMIELM KGLADLNEIR FSAYRTAMKL RSVQKRLALD RISMSTACES
     FDRHGLRAQN DKLIDIPDMT TVLHSLYVTI DKIDLTLMLD LAINWILNVY DSQRTGQIRV
     LSFKVGLVLL CKGHLEEKYR YLFRLVADTD RRADQRRLGL LLHDCIQVPR QLGEVAAFGG
     SNIEPSVRSC LEQAGISQEA IDGNQDISIE LQHFLGWLQH EPQSLVWLPV LHRLAAAEAA
     KHQAKCNICK EYPIVGFRYR CLKCFNFDMC QKCFFFGRNA KNHKLTHPMH EYCTTTTSTE
     DVRDFTRALK NKFKSRKYFK KHPRVGYLPV QSVLEGDALE SPAPSPQHTT HQLQNDMHSR
     LEMYASRLAQ VEYGGTGSNS TPDSDDEHQL IAQYCQALPG TSNGSAPKSP VQVMAAMDAE
     QREELEAIIR DLEEENANLQ AEYQQLCSKE QSGMPEDSNG MQHSSSSMTG LSGQGEQGQD
     MMAEAKLLRQ HKGRLEARMQ ILEDHNRQLE AQLQRLRQLL DEPNGGGSSA TSSGLPSAPG
     SALNSKPNTL QTRSVTASQL NTDSPAKMNQ QNGHYEHNSK GIMLPGMNSE IQQQHAQLAS
     LAAKHHQHQL SGALNALHQQ QQQQLQQQPP QQQRSMMTGN GGMDISGGMQ TSGGYLGDDG
     RPPPPPHSSL MQQQHQQHLN ENSSGLVTVI TEQELESIND DLEDSSSSNT TNTTTTTTTT
     ATTEKTCVEL QK
//
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