(data stored in ACNUC13749 zone)

HOGENOM: HS18_PE333

ID   HS18_PE333                           STANDARD;      PRT;   743 AA.
AC   HS18_PE333;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Dystrobrevin alpha; Short=DTN-A;AltName:
DE   Full=Alpha-dystrobrevin;AltName: Full=Dystrophin-related protein 3;
DE   (HS18.PE333).
GN   Name=DTNA; Synonyms=DRP3;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS18.PE333.
CC       Homo sapiens chromosome 18 GRCh37  sequence 1..78017248 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:DTNA_HUMAN
CC   -!- FUNCTION: May be involved in the formation and stability of
CC       synapses as well as being involved in the clustering of nicotinic
CC       acetylcholine receptors.
CC   -!- SUBUNIT: Interacts with dystrophin, utrophin and the syntrophins
CC       SNTA1, SNTB1, SNTB2, SNTG1 and SNTG2. Isoform 7 and isoform 8 do
CC       not interact with dystrophin. Binds dystrobrevin binding protein
CC       1. Interacts with MAGEE1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse. Cell
CC       membrane (By similarity). Note=In peripheral nerves, co-localizes
CC       with MAGEE1 in the Schwann cell membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
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   -!- TISSUE SPECIFICITY: Highly expressed in brain, skeletal and
CC       cardiac muscles, and expressed at lower levels in lung, liver and
CC       pancreas. Isoform 2 is not expressed in cardiac muscle. Isoform 7
CC       and isoform 8 are only expressed in muscle.
CC   -!- DOMAIN: The coiled coil domain mediates the interaction with
CC       dystrophin and utrophin (By similarity).
CC   -!- PTM: Phosphorylation of DTN-1 on tyrosine kinase substrate domain
CC       present in the C-terminus (By similarity).
CC   -!- DISEASE: Defects in DTNA are the cause of left ventricular non-
CC       compaction type 1 (LVNC1) [MIM:604169]. Left ventricular non-
CC       compaction is due to an arrest of myocardial morphogenesis. The
CC       disorder is characterized by a hypertrophic left ventricule with
CC       deep trabeculations and with poor systolic function, with or
CC       without associated left ventricular dilation. In some cases, it is
CC       associated with other congenital heart anomalies such as
CC       ventricular septal defects, pulmonic stenosis and atrial septal
CC       defects. The right ventricle may also be affected.
CC   -!- SIMILARITY: Belongs to the dystrophin family. Dystrobrevin
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/DTNA";
CC   -!- GENE_FAMILY: HOG000230684 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000134769;ENST00000399121;ENSP00000382072.
DR   EMBL; AC013290; - ;
DR   EMBL; AC022601; - ;
DR   EMBL; AC068506; - ;
DR   EMBL; AC103768; - ;
DR   EMBL; AJ009668; - ;
DR   EMBL; U26742; - ;
DR   EMBL; U26743; - ;
DR   EMBL; U26744; - ;
DR   EMBL; U46744; - ;
DR   EMBL; U46745; - ;
DR   EMBL; U46746; - ;
DR   EMBL; U84529; - ;
DR   EMBL; U84530; - ;
DR   EMBL; U84531; - ;
DR   EMBL; U84532; - ;
DR   EMBL; U84533; - ;
DR   EMBL; U84534; - ;
DR   EMBL; U84535; - ;
DR   EMBL; U84536; - ;
DR   EMBL; U84537; - ;
DR   EMBL; U84538; - ;
DR   EMBL; U84539; - ;
DR   EMBL; U84540; - ;
DR   EMBL; U84541; - ;
DR   EMBL; U84542; - ;
DR   EMBL; U84543; - ;
DR   EMBL; U84544; - ;
DR   EMBL; U84545; - ;
DR   EMBL; U84546; - ;
DR   EMBL; U84547; - ;
DR   EMBL; U84548; - ;
DR   EMBL; U84549; - ;
DR   EMBL; U84550; - ;
DR   EMBL; U84551; - ;
DR   UniProtKB/Swiss-Prot; Q9Y4J8; A8MSZ0; A8MUY4; O15332; O15333; O75697; Q13197; Q13198; -.
DR   UniProtKB/Swiss-Prot; Q13199; Q13498; Q13499; Q13500; -.
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; 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; 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   IPI; IPI00177936; -.
DR   IPI; IPI00218653; -.
DR   IPI; IPI00218655; -.
DR   IPI; IPI00296091; -.
DR   IPI; IPI00402365; -.
DR   IPI; IPI00749235; -.
DR   IPI; IPI00929645; -.
DR   IPI; IPI00942739; -.
DR   RefSeq; NP_001381.2; NM_001390.4.
DR   RefSeq; NP_001382.2; NM_001391.5.
DR   RefSeq; NP_001383.2; NM_001392.4.
DR   RefSeq; NP_116757.2; NM_032975.3.
DR   RefSeq; NP_116760.2; NM_032978.6.
DR   RefSeq; NP_116761.2; NM_032979.4.
DR   RefSeq; NP_116762.2; NM_032980.3.
DR   RefSeq; NP_116763.1; NM_032981.4.
DR   UniGene; Hs.643454; -.
DR   PDB; 2E5R; NMR; -; A=237-292.
DR   PDBsum; 2E5R; -.
DR   ProteinModelPortal; Q9Y4J8; -.
DR   SMR; Q9Y4J8; 2-292.
DR   IntAct; Q9Y4J8; 3.
DR   MINT; MINT-129318; -.
DR   STRING; Q9Y4J8; -.
DR   PhosphoSite; Q9Y4J8; -.
DR   PRIDE; Q9Y4J8; -.
DR   Ensembl; ENST00000399113; ENSP00000382064; ENSG00000134769.
DR   Ensembl; ENST00000399121; ENSP00000382072; ENSG00000134769.
DR   Ensembl; ENST00000444659; ENSP00000405819; ENSG00000134769.
DR   GeneID; 1837; -.
DR   KEGG; hsa:1837; -.
DR   UCSC; uc002kxv.2; human.
DR   UCSC; uc002kyd.2; human.
DR   UCSC; uc002kye.2; human.
DR   UCSC; uc010dmm.1; human.
DR   CTD; 1837; -.
DR   GeneCards; GC18P028932; -.
DR   HGNC; HGNC:3057; DTNA.
DR   MIM; 601239; gene.
DR   MIM; 604169; phenotype.
DR   neXtProt; NX_Q9Y4J8; -.
DR   Orphanet; 54260; Left ventricular noncompaction.
DR   eggNOG; prNOG04866; -.
DR   GeneTree; ENSGT00550000074400; -.
DR   NextBio; 7499; -.
DR   ArrayExpress; Q9Y4J8; -.
DR   Bgee; Q9Y4J8; -.
DR   Genevestigator; Q9Y4J8; -.
DR   GermOnline; ENSG00000134769; Homo sapiens.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   InterPro; IPR017432; Distrobrevin.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR015153; EF-hand_dom_typ1.
DR   InterPro; IPR015154; EF-hand_dom_typ2.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF09068; efhand_1; 1.
DR   Pfam; PF09069; efhand_2; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   PIRSF; PIRSF038204; Distrobrevin; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
DR   HOGENOMDNA; HS18.PE333; -.
KW   ENSG000001347691755old_1320000031; ENSP000003820727901old_1320000031;
KW   AC013290; AC022601; AC068506; AC103768; AJ009668; U26742; U26743; U26744;
KW   U46745; U46746; U84529; U84530; U84531; U84532; U84533; U84534; U84535;
KW   U84537; U84538; U84539; U84540; U84541; U84542; U84543; U84544; U84545;
KW   U84547; U84548; U84549; U84550; U84551;
KW   3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW   Coiled coil; Complete proteome; Cytoplasm; Disease mutation; Membrane;
KW   Metal-binding; Phosphoprotein; Reference proteome; Synapse; Zinc;
KW   Zinc-finger.
SQ   SEQUENCE   743 AA;  UNKNOWN MW;  UNKNOWN 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
//

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