DTNA_HUMAN
ID DTNA_HUMAN Reviewed; 743 AA.
AC Q9Y4J8; A8K541; A8MSZ0; A8MUY4; B4DGS6; B4DIR0; B4DIU8; M0QYX6; M0R397;
AC O15332; O15333; O75697; Q13197; Q13198; Q13199; Q13498; Q13499; Q13500;
AC Q59GK7; Q9BS59;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Dystrobrevin alpha {ECO:0000305};
DE Short=DTN-A;
DE AltName: Full=Alpha-dystrobrevin;
DE AltName: Full=Dystrophin-related protein 3;
GN Name=DTNA {ECO:0000312|HGNC:HGNC:3057}; Synonyms=DRP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 5; 6; 7 AND 8), AND VARIANT
RP GLU-180.
RX PubMed=8845841; DOI=10.1093/hmg/5.4.489;
RA Sadoulet-Puccio H.M., Khurana T.S., Cohen J.B., Kunkel L.M.;
RT "Cloning and characterization of the human homologue of a dystrophin
RT related phosphoprotein found at the Torpedo electric organ post-synaptic
RT membrane.";
RL Hum. Mol. Genet. 5:489-496(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3 AND 7), AND VARIANT
RP GLU-180.
RX PubMed=10735273; DOI=10.1007/s100480050006;
RA Sadoulet-Puccio H.M., Feener C.A., Schaid D.J., Thibodeau S.N.,
RA Michels V.V., Kunkel L.M.;
RT "The genomic organization of human dystrobrevin.";
RL Neurogenetics 1:37-42(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
RC TISSUE=Fetal brain;
RX PubMed=9701558; DOI=10.1242/jcs.111.17.2595;
RA Nawrotzki R., Loh N.Y., Ruegg M.A., Davies K.E., Blake D.J.;
RT "Characterisation of alpha-dystrobrevin in muscle.";
RL J. Cell Sci. 111:2595-2605(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 10; 11; 12 AND 16).
RC TISSUE=Brain, Hippocampus, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP INTERACTION WITH SNTB1.
RX PubMed=7844150; DOI=10.1083/jcb.128.3.363;
RA Ahn A.H., Kunkel L.M.;
RT "Syntrophin binds to an alternatively spliced exon of dystrophin.";
RL J. Cell Biol. 128:363-371(1995).
RN [11]
RP INTERACTION WITH SNTA1 AND SNTB2.
RX PubMed=8576247; DOI=10.1074/jbc.271.5.2724;
RA Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.;
RT "The three human syntrophin genes are expressed in diverse tissues, have
RT distinct chromosomal locations, and each bind to dystrophin and its
RT relatives.";
RL J. Biol. Chem. 271:2724-2730(1996).
RN [12]
RP INTERACTION WITH SNTG1 AND SNTG2.
RX PubMed=10747910; DOI=10.1074/jbc.m000439200;
RA Piluso G., Mirabella M., Ricci E., Belsito A., Abbondanza C., Servidei S.,
RA Puca A.A., Tonali P., Puca G.A., Nigro V.;
RT "Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins
RT localized in neuronal cells.";
RL J. Biol. Chem. 275:15851-15860(2000).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP STRUCTURE BY NMR OF 237-292.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZZ domain of dystrobrevin alpha.";
RL Submitted (JUN-2007) to the PDB data bank.
RN [15]
RP VARIANT LVNC1 LEU-121.
RX PubMed=11238270; DOI=10.1161/01.cir.103.9.1256;
RA Ichida F., Tsubata S., Bowles K.R., Haneda N., Uese K., Miyawaki T.,
RA Dreyer W.J., Messina J., Li H., Bowles N.E., Towbin J.A.;
RT "Novel gene mutations in patients with left ventricular noncompaction or
RT Barth syndrome.";
RL Circulation 103:1256-1263(2001).
CC -!- FUNCTION: May be involved in the formation and stability of synapses as
CC well as being involved in the clustering of nicotinic acetylcholine
CC receptors.
CC -!- SUBUNIT: Interacts with dystrophin, utrophin and the syntrophins SNTA1,
CC SNTB1, SNTB2, SNTG1 and SNTG2. Isoform 7 and isoform 8 do not interact
CC with dystrophin. Binds dystrobrevin binding protein 1. Interacts with
CC MAGEE1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y4J8; Q9UBT7: CTNNAL1; NbExp=5; IntAct=EBI-949471, EBI-514206;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Synapse. Cell membrane {ECO:0000250}.
CC Note=In peripheral nerves, colocalizes with MAGEE1 in the Schwann cell
CC membrane. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=17;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=DTN-1;
CC IsoId=Q9Y4J8-1; Sequence=Displayed;
CC Name=2; Synonyms=Dystrobrevin-alpha;
CC IsoId=Q9Y4J8-2; Sequence=VSP_004208;
CC Name=3; Synonyms=DTN-2;
CC IsoId=Q9Y4J8-3; Sequence=VSP_004212, VSP_004213;
CC Name=4; Synonyms=Dystrobrevin-beta;
CC IsoId=Q9Y4J8-4; Sequence=VSP_004207, VSP_004212, VSP_004213;
CC Name=5; Synonyms=Dystrobrevin-gamma;
CC IsoId=Q9Y4J8-5; Sequence=VSP_004208, VSP_004212, VSP_004213;
CC Name=6; Synonyms=Dystrobrevin-epsilon;
CC IsoId=Q9Y4J8-6; Sequence=VSP_004206, VSP_004207, VSP_004211;
CC Name=7; Synonyms=DTN-3, Alpha-dystrobrevin-3, Dystrobrevin-delta;
CC IsoId=Q9Y4J8-7; Sequence=VSP_004209, VSP_004210;
CC Name=8; Synonyms=Dystrobrevin-zeta;
CC IsoId=Q9Y4J8-8; Sequence=VSP_004206, VSP_004207, VSP_004208,
CC VSP_004212, VSP_004213;
CC Name=9;
CC IsoId=Q9Y4J8-9; Sequence=VSP_004207, VSP_004209, VSP_004210;
CC Name=10;
CC IsoId=Q9Y4J8-10; Sequence=VSP_004206, VSP_004207, VSP_043824;
CC Name=11;
CC IsoId=Q9Y4J8-11; Sequence=VSP_004206, VSP_004207, VSP_045444;
CC Name=12;
CC IsoId=Q9Y4J8-12; Sequence=VSP_047532, VSP_004212, VSP_004213;
CC Name=13;
CC IsoId=Q9Y4J8-13; Sequence=VSP_004207, VSP_004208;
CC Name=14;
CC IsoId=Q9Y4J8-14; Sequence=VSP_004207, VSP_004208, VSP_054816;
CC Name=15;
CC IsoId=Q9Y4J8-15; Sequence=VSP_004207, VSP_004208, VSP_054817;
CC Name=16;
CC IsoId=Q9Y4J8-16; Sequence=VSP_004207, VSP_004208, VSP_004212,
CC VSP_004213;
CC Name=17;
CC IsoId=Q9Y4J8-17; Sequence=VSP_004207, VSP_061450;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, skeletal and cardiac
CC muscles, and expressed at lower levels in lung, liver and pancreas.
CC Isoform 2 is not expressed in cardiac muscle. Isoform 7 and isoform 8
CC are only expressed in muscle.
CC -!- DOMAIN: The coiled coil domain mediates the interaction with dystrophin
CC and utrophin. {ECO:0000250}.
CC -!- PTM: Phosphorylation of DTN-1 on tyrosine kinase substrate domain
CC present in the C-terminus. {ECO:0000250}.
CC -!- DISEASE: Left ventricular non-compaction 1 (LVNC1) [MIM:604169]: A form
CC of left ventricular non-compaction, a cardiomyopathy due to myocardial
CC morphogenesis arrest and characterized by a hypertrophic left
CC ventricle, a severely thickened 2-layered myocardium, numerous
CC prominent trabeculations, deep intertrabecular recesses, and poor
CC systolic function. Clinical manifestations are variable. Some affected
CC individuals experience no symptoms at all, others develop heart
CC failure. In some cases, left ventricular non-compaction is associated
CC with other congenital heart anomalies. LVNC1 is an autosomal dominant
CC condition. {ECO:0000269|PubMed:11238270}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the dystrophin family. Dystrobrevin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92339.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U46744; AAC50429.1; -; mRNA.
DR EMBL; U46745; AAC50430.1; -; mRNA.
DR EMBL; U26744; AAC50426.1; -; mRNA.
DR EMBL; U46746; AAC50431.1; -; mRNA.
DR EMBL; U26742; AAC50424.1; -; mRNA.
DR EMBL; U26743; AAC50425.1; -; mRNA.
DR EMBL; AK294746; BAG57887.1; -; mRNA.
DR EMBL; AK295732; BAG58572.1; -; mRNA.
DR EMBL; AB209102; BAD92339.1; ALT_INIT; mRNA.
DR EMBL; AK291156; BAF83845.1; -; mRNA.
DR EMBL; AK295789; BAG58610.1; -; mRNA.
DR EMBL; U84551; AAB58543.1; -; Genomic_DNA.
DR EMBL; U84529; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84530; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84531; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84532; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84533; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84534; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84535; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84536; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84537; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84538; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84539; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84541; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84542; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84543; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84544; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84545; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84546; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84548; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84549; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84550; AAB58543.1; JOINED; Genomic_DNA.
DR EMBL; U84547; AAB58542.1; -; Genomic_DNA.
DR EMBL; U84529; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84530; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84531; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84532; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84533; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84534; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84535; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84536; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84537; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84538; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84539; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84541; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84542; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84543; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84544; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84545; AAB58542.1; JOINED; Genomic_DNA.
DR EMBL; U84540; AAB58541.1; -; Genomic_DNA.
DR EMBL; U84529; AAB58541.1; JOINED; Genomic_DNA.
DR EMBL; U84530; AAB58541.1; JOINED; Genomic_DNA.
DR EMBL; U84531; AAB58541.1; JOINED; Genomic_DNA.
DR EMBL; U84532; AAB58541.1; JOINED; Genomic_DNA.
DR EMBL; U84533; AAB58541.1; JOINED; Genomic_DNA.
DR EMBL; U84534; AAB58541.1; JOINED; Genomic_DNA.
DR EMBL; U84535; AAB58541.1; JOINED; Genomic_DNA.
DR EMBL; U84536; AAB58541.1; JOINED; Genomic_DNA.
DR EMBL; U84537; AAB58541.1; JOINED; Genomic_DNA.
DR EMBL; U84538; AAB58541.1; JOINED; Genomic_DNA.
DR EMBL; AJ009668; CAA08769.1; -; mRNA.
DR EMBL; BT006937; AAP35583.1; -; mRNA.
DR EMBL; AC068506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC013290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471088; EAX01319.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01325.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01328.1; -; Genomic_DNA.
DR EMBL; BC005300; AAH05300.1; -; mRNA.
DR CCDS; CCDS11908.1; -. [Q9Y4J8-4]
DR CCDS; CCDS11909.1; -. [Q9Y4J8-6]
DR CCDS; CCDS42426.1; -. [Q9Y4J8-7]
DR CCDS; CCDS45848.1; -. [Q9Y4J8-2]
DR CCDS; CCDS56060.1; -. [Q9Y4J8-9]
DR CCDS; CCDS56061.1; -. [Q9Y4J8-14]
DR CCDS; CCDS56062.1; -. [Q9Y4J8-11]
DR CCDS; CCDS56063.1; -. [Q9Y4J8-10]
DR CCDS; CCDS59309.1; -. [Q9Y4J8-5]
DR CCDS; CCDS59310.1; -. [Q9Y4J8-16]
DR CCDS; CCDS59311.1; -. [Q9Y4J8-13]
DR CCDS; CCDS59312.1; -. [Q9Y4J8-15]
DR CCDS; CCDS59313.1; -. [Q9Y4J8-12]
DR CCDS; CCDS59314.1; -. [Q9Y4J8-8]
DR RefSeq; NP_001121647.1; NM_001128175.1. [Q9Y4J8-9]
DR RefSeq; NP_001185867.1; NM_001198938.1. [Q9Y4J8-15]
DR RefSeq; NP_001185868.1; NM_001198939.1. [Q9Y4J8-14]
DR RefSeq; NP_001185869.1; NM_001198940.1. [Q9Y4J8-13]
DR RefSeq; NP_001185870.1; NM_001198941.1. [Q9Y4J8-16]
DR RefSeq; NP_001185871.1; NM_001198942.1. [Q9Y4J8-11]
DR RefSeq; NP_001185873.1; NM_001198944.1. [Q9Y4J8-10]
DR RefSeq; NP_001185874.1; NM_001198945.1. [Q9Y4J8-12]
DR RefSeq; NP_001381.2; NM_001390.4. [Q9Y4J8-1]
DR RefSeq; NP_001382.2; NM_001391.5. [Q9Y4J8-3]
DR RefSeq; NP_001383.2; NM_001392.4. [Q9Y4J8-7]
DR RefSeq; NP_116757.2; NM_032975.3. [Q9Y4J8-2]
DR RefSeq; NP_116760.2; NM_032978.6. [Q9Y4J8-4]
DR RefSeq; NP_116761.2; NM_032979.4. [Q9Y4J8-5]
DR RefSeq; NP_116762.2; NM_032980.3. [Q9Y4J8-6]
DR RefSeq; NP_116763.1; NM_032981.4. [Q9Y4J8-8]
DR RefSeq; XP_011524155.1; XM_011525853.2. [Q9Y4J8-16]
DR RefSeq; XP_016881066.1; XM_017025577.1. [Q9Y4J8-15]
DR RefSeq; XP_016881073.1; XM_017025584.1. [Q9Y4J8-2]
DR RefSeq; XP_016881076.1; XM_017025587.1. [Q9Y4J8-13]
DR RefSeq; XP_016881077.1; XM_017025588.1. [Q9Y4J8-13]
DR RefSeq; XP_016881078.1; XM_017025589.1. [Q9Y4J8-13]
DR RefSeq; XP_016881079.1; XM_017025590.1. [Q9Y4J8-13]
DR RefSeq; XP_016881080.1; XM_017025591.1. [Q9Y4J8-13]
DR RefSeq; XP_016881089.1; XM_017025600.1. [Q9Y4J8-7]
DR RefSeq; XP_016881090.1; XM_017025601.1. [Q9Y4J8-9]
DR RefSeq; XP_016881091.1; XM_017025602.1. [Q9Y4J8-9]
DR PDB; 2E5R; NMR; -; A=237-292.
DR PDBsum; 2E5R; -.
DR AlphaFoldDB; Q9Y4J8; -.
DR SMR; Q9Y4J8; -.
DR BioGRID; 108170; 106.
DR CORUM; Q9Y4J8; -.
DR IntAct; Q9Y4J8; 35.
DR MINT; Q9Y4J8; -.
DR STRING; 9606.ENSP00000470152; -.
DR TCDB; 8.A.66.1.7; the dystrophin (dystrophin) family.
DR iPTMnet; Q9Y4J8; -.
DR PhosphoSitePlus; Q9Y4J8; -.
DR SwissPalm; Q9Y4J8; -.
DR BioMuta; DTNA; -.
DR DMDM; 229462840; -.
DR EPD; Q9Y4J8; -.
DR jPOST; Q9Y4J8; -.
DR MassIVE; Q9Y4J8; -.
DR MaxQB; Q9Y4J8; -.
DR PaxDb; Q9Y4J8; -.
DR PeptideAtlas; Q9Y4J8; -.
DR PRIDE; Q9Y4J8; -.
DR ProteomicsDB; 4321; -.
DR ProteomicsDB; 86213; -. [Q9Y4J8-1]
DR ProteomicsDB; 86214; -. [Q9Y4J8-10]
DR ProteomicsDB; 86215; -. [Q9Y4J8-2]
DR ProteomicsDB; 86216; -. [Q9Y4J8-3]
DR ProteomicsDB; 86217; -. [Q9Y4J8-4]
DR ProteomicsDB; 86218; -. [Q9Y4J8-5]
DR ProteomicsDB; 86219; -. [Q9Y4J8-6]
DR ProteomicsDB; 86220; -. [Q9Y4J8-7]
DR ProteomicsDB; 86221; -. [Q9Y4J8-8]
DR ProteomicsDB; 86222; -. [Q9Y4J8-9]
DR Antibodypedia; 22242; 262 antibodies from 26 providers.
DR DNASU; 1837; -.
DR Ensembl; ENST00000269192.11; ENSP00000269192.7; ENSG00000134769.23. [Q9Y4J8-11]
DR Ensembl; ENST00000283365.14; ENSP00000283365.10; ENSG00000134769.23. [Q9Y4J8-13]
DR Ensembl; ENST00000315456.10; ENSP00000322519.5; ENSG00000134769.23. [Q9Y4J8-7]
DR Ensembl; ENST00000348997.9; ENSP00000336682.4; ENSG00000134769.23. [Q9Y4J8-4]
DR Ensembl; ENST00000399113.7; ENSP00000382064.3; ENSG00000134769.23. [Q9Y4J8-1]
DR Ensembl; ENST00000399121.9; ENSP00000382072.5; ENSG00000134769.23. [Q9Y4J8-14]
DR Ensembl; ENST00000444659.6; ENSP00000405819.2; ENSG00000134769.23. [Q9Y4J8-17]
DR Ensembl; ENST00000554864.7; ENSP00000451516.2; ENSG00000134769.23. [Q9Y4J8-9]
DR Ensembl; ENST00000556414.7; ENSP00000452255.2; ENSG00000134769.23. [Q9Y4J8-10]
DR Ensembl; ENST00000591182.5; ENSP00000467720.1; ENSG00000134769.23. [Q9Y4J8-6]
DR Ensembl; ENST00000595022.5; ENSP00000473078.1; ENSG00000134769.23. [Q9Y4J8-13]
DR Ensembl; ENST00000596745.5; ENSP00000469121.1; ENSG00000134769.23. [Q9Y4J8-12]
DR Ensembl; ENST00000597599.5; ENSP00000473119.1; ENSG00000134769.23. [Q9Y4J8-16]
DR Ensembl; ENST00000597674.5; ENSP00000471783.1; ENSG00000134769.23. [Q9Y4J8-8]
DR Ensembl; ENST00000598142.5; ENSP00000470716.1; ENSG00000134769.23. [Q9Y4J8-2]
DR Ensembl; ENST00000598334.5; ENSP00000470152.1; ENSG00000134769.23. [Q9Y4J8-15]
DR Ensembl; ENST00000598774.6; ENSP00000472031.1; ENSG00000134769.23. [Q9Y4J8-5]
DR Ensembl; ENST00000679796.1; ENSP00000506659.1; ENSG00000134769.23. [Q9Y4J8-17]
DR Ensembl; ENST00000679936.1; ENSP00000506586.1; ENSG00000134769.23. [Q9Y4J8-5]
DR Ensembl; ENST00000680346.1; ENSP00000505947.1; ENSG00000134769.23. [Q9Y4J8-5]
DR Ensembl; ENST00000681241.1; ENSP00000506495.1; ENSG00000134769.23. [Q9Y4J8-13]
DR Ensembl; ENST00000682483.1; ENSP00000508159.1; ENSG00000134769.23. [Q9Y4J8-16]
DR Ensembl; ENST00000683370.1; ENSP00000507104.1; ENSG00000134769.23. [Q9Y4J8-16]
DR Ensembl; ENST00000683379.1; ENSP00000507995.1; ENSG00000134769.23. [Q9Y4J8-2]
DR Ensembl; ENST00000683705.1; ENSP00000507911.1; ENSG00000134769.23. [Q9Y4J8-13]
DR Ensembl; ENST00000683876.1; ENSP00000507423.1; ENSG00000134769.23. [Q9Y4J8-8]
DR Ensembl; ENST00000684359.1; ENSP00000507300.1; ENSG00000134769.23. [Q9Y4J8-2]
DR Ensembl; ENST00000684610.1; ENSP00000508348.1; ENSG00000134769.23. [Q9Y4J8-9]
DR Ensembl; ENST00000684734.1; ENSP00000506928.1; ENSG00000134769.23. [Q9Y4J8-9]
DR GeneID; 1837; -.
DR KEGG; hsa:1837; -.
DR MANE-Select; ENST00000444659.6; ENSP00000405819.2; NM_001386795.1; NP_001373724.1. [Q9Y4J8-17]
DR UCSC; uc002kxu.3; human. [Q9Y4J8-1]
DR CTD; 1837; -.
DR DisGeNET; 1837; -.
DR GeneCards; DTNA; -.
DR HGNC; HGNC:3057; DTNA.
DR HPA; ENSG00000134769; Group enriched (brain, choroid plexus, heart muscle, skeletal muscle, tongue).
DR MalaCards; DTNA; -.
DR MIM; 601239; gene.
DR MIM; 604169; phenotype.
DR neXtProt; NX_Q9Y4J8; -.
DR OpenTargets; ENSG00000134769; -.
DR Orphanet; 54260; Left ventricular noncompaction.
DR PharmGKB; PA27510; -.
DR VEuPathDB; HostDB:ENSG00000134769; -.
DR eggNOG; KOG4301; Eukaryota.
DR GeneTree; ENSGT00940000153897; -.
DR HOGENOM; CLU_868655_0_0_1; -.
DR InParanoid; Q9Y4J8; -.
DR OMA; KFRYIYS; -.
DR PhylomeDB; Q9Y4J8; -.
DR TreeFam; TF343849; -.
DR PathwayCommons; Q9Y4J8; -.
DR SignaLink; Q9Y4J8; -.
DR SIGNOR; Q9Y4J8; -.
DR BioGRID-ORCS; 1837; 13 hits in 1060 CRISPR screens.
DR ChiTaRS; DTNA; human.
DR EvolutionaryTrace; Q9Y4J8; -.
DR GeneWiki; DTNA; -.
DR GenomeRNAi; 1837; -.
DR Pharos; Q9Y4J8; Tbio.
DR PRO; PR:Q9Y4J8; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9Y4J8; protein.
DR Bgee; ENSG00000134769; Expressed in medial globus pallidus and 176 other tissues.
DR ExpressionAtlas; Q9Y4J8; baseline and differential.
DR Genevisible; Q9Y4J8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006941; P:striated muscle contraction; TAS:ProtInc.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR017432; Distrobrevin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF038204; Distrobrevin; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cardiomyopathy; Cell membrane;
KW Coiled coil; Cytoplasm; Disease variant; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..743
FT /note="Dystrobrevin alpha"
FT /id="PRO_0000080036"
FT ZN_FING 238..294
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..288
FT /note="Interaction with MAGEE1"
FT /evidence="ECO:0000250"
FT REGION 400..450
FT /note="Syntrophin-binding region"
FT REGION 556..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 461..556
FT /evidence="ECO:0000255"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2N4"
FT VAR_SEQ 1..318
FT /note="Missing (in isoform 6, isoform 8, isoform 10 and
FT isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8845841"
FT /id="VSP_004206"
FT VAR_SEQ 202..451
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047532"
FT VAR_SEQ 335..337
FT /note="Missing (in isoform 4, isoform 6, isoform 8, isoform
FT 9, isoform 10, isoform 11, isoform 13, isoform 14, isoform
FT 15, isoform 16 and isoform 17)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8845841,
FT ECO:0000303|Ref.4, ECO:0000303|Ref.6"
FT /id="VSP_004207"
FT VAR_SEQ 364..365
FT /note="RS -> RRLPEGISASSPVAEEHSLIKLYVNQLDHGAR (in isoform
FT 11)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045444"
FT VAR_SEQ 365..422
FT /note="SSPPKDSEVEQNKLLARAAPAFLKGKGIQYSLNVADRLADEHVLIGLYVNML
FT RNNPSC -> RLPEGISASSPVAEEHSLIKLYVNQLDHGAR (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043824"
FT VAR_SEQ 365
FT /note="S -> RLPEGISASSPVAEEHSLIKLYVNQLDHGAR (in isoform
FT 17)"
FT /id="VSP_061450"
FT VAR_SEQ 366..422
FT /note="Missing (in isoform 2, isoform 5, isoform 8, isoform
FT 13, isoform 14, isoform 15 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8845841, ECO:0000303|Ref.6"
FT /id="VSP_004208"
FT VAR_SEQ 367..374
FT /note="PPKDSEVE -> DGAFGGCV (in isoform 7 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8845841, ECO:0000303|PubMed:9701558,
FT ECO:0000303|Ref.4"
FT /id="VSP_004209"
FT VAR_SEQ 375..743
FT /note="Missing (in isoform 7 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8845841, ECO:0000303|PubMed:9701558,
FT ECO:0000303|Ref.4"
FT /id="VSP_004210"
FT VAR_SEQ 392..422
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:8845841"
FT /id="VSP_004211"
FT VAR_SEQ 554
FT /note="K -> KEEELKQG (in isoform 14)"
FT /evidence="ECO:0000305"
FT /id="VSP_054816"
FT VAR_SEQ 555..570
FT /note="TQGAGSPRSSPSHTIS -> EEELKQGVSYVPYCRS (in isoform 3,
FT isoform 4, isoform 5, isoform 8, isoform 12 and isoform
FT 16)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8845841"
FT /id="VSP_004212"
FT VAR_SEQ 571..743
FT /note="Missing (in isoform 3, isoform 4, isoform 5, isoform
FT 8, isoform 12 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8845841"
FT /id="VSP_004213"
FT VAR_SEQ 739..743
FT /note="VSLQG -> LHVSTETRLEHPCPVSETKWRVLFWGFVFFGGFLSLALQIYFW
FT GLF (in isoform 15)"
FT /evidence="ECO:0000305"
FT /id="VSP_054817"
FT VARIANT 121
FT /note="P -> L (in LVNC1; unknown pathological significance;
FT dbSNP:rs104894654)"
FT /evidence="ECO:0000269|PubMed:11238270"
FT /id="VAR_026744"
FT VARIANT 180
FT /note="A -> E (in dbSNP:rs1048081)"
FT /evidence="ECO:0000269|PubMed:10735273,
FT ECO:0000269|PubMed:8845841"
FT /id="VAR_055320"
FT CONFLICT 45
FT /note="Q -> H (in Ref. 2; AAB58541/AAB58542/AAB58543)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="E -> K (in Ref. 3; CAA08769)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="F -> L (in Ref. 1; AAC50426 and 2; AAB58541/
FT AAB58542/AAB58543)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="E -> K (in Ref. 1; AAC50430)"
FT /evidence="ECO:0000305"
FT CONFLICT 558..561
FT /note="AGSP -> SGTH (in Ref. 1; AAC50429)"
FT /evidence="ECO:0000305"
FT CONFLICT 558..559
FT /note="AG -> GV (in Ref. 1; AAC50431)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="P -> R (in Ref. 1; AAC50429)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="T -> S (in Ref. 1; AAC50429)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="T -> S (in Ref. 1; AAC50429)"
FT /evidence="ECO:0000305"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:2E5R"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:2E5R"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:2E5R"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:2E5R"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:2E5R"
SQ SEQUENCE 743 AA; 83901 MW; CFD77DAA57D050EC CRC64;
MIEDSGKRGN TMAERRQLFA EMRAQDLDRI RLSTYRTACK LRFVQKKCNL HLVDIWNVIE
ALRENALNNL DPNTELNVSR LEAVLSTIFY QLNKRMPTTH QIHVEQSISL LLNFLLAAFD
PEGHGKISVF AVKMALATLC GGKIMDKLRY IFSMISDSSG VMVYGRYDQF LREVLKLPTA
VFEGPSFGYT EQSARSCFSQ QKKVTLNGFL DTLMSDPPPQ CLVWLPLLHR LANVENVFHP
VECSYCHSES MMGFRYRCQQ CHNYQLCQDC FWRGHAGGSH SNQHQMKEYT SWKSPAKKLT
NALSKSLSCA SSREPLHPMF PDQPEKPLNL AHIVDTWPPR PVTSMNDTLF SHSVPSSGSP
FITRSSPPKD SEVEQNKLLA RAAPAFLKGK GIQYSLNVAD RLADEHVLIG LYVNMLRNNP
SCMLESSNRL DEEHRLIARY AARLAAESSS SQPPQQRSAP DISFTIDANK QQRQLIAELE
NKNREILQEI QRLRLEHEQA SQPTPEKAQQ NPTLLAELRL LRQRKDELEQ RMSALQESRR
ELMVQLEGLM KLLKTQGAGS PRSSPSHTIS RPIPMPIRSA SACSTPTHTP QDSLTGVGGD
VQEAFAQSSR RNLRNDLLVA ADSITNTMSS LVKELNSEVG SETESNVDSE FARTQFEDLV
PSPTSEKAFL AQIHARKPGY IHSGATTSTM RGDMVTEDAD PYVQPEDENY ENDSVRQLEN
ELQMEEYLKQ KLQDEAYQVS LQG
