UTRN_HUMAN
ID UTRN_HUMAN Reviewed; 3433 AA.
AC P46939; Q5SYY1; Q5SZ57; Q9UJ40;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Utrophin {ECO:0000305};
DE AltName: Full=Dystrophin-related protein 1;
DE Short=DRP-1;
GN Name=UTRN {ECO:0000312|HGNC:HGNC:12635}; Synonyms=DMDL, DRP1;
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] (ISOFORM 1).
RX PubMed=1461283; DOI=10.1038/360591a0;
RA Tinsley J.M., Blake D.J., Roche A., Fairbrother U., Riss J., Byth B.C.,
RA Knight A.E., Kendrick-Jones J., Suthers G.K., Love D.R., Edwards Y.H.,
RA Davies K.E.;
RT "Primary structure of dystrophin-related protein.";
RL Nature 360:591-593(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS UP71 AND UP140), ALTERNATIVE PROMOTER
RP USAGE, AND TISSUE SPECIFICITY.
RX PubMed=10369873; DOI=10.1093/hmg/8.7.1271;
RA Wilson J., Putt W., Jimenez C., Edwards Y.H.;
RT "Up71 and up140, two novel transcripts of utrophin that are homologues of
RT short forms of dystrophin.";
RL Hum. Mol. Genet. 8:1271-1278(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31 (ISOFORM 2), AND ALTERNATIVE
RP PROMOTER USAGE.
RX PubMed=10570192; DOI=10.1073/pnas.96.24.14025;
RA Burton E.A., Tinsley J.M., Holzfeind P.J., Rodrigues N.R., Davies K.E.;
RT "A second promoter provides an alternative target for therapeutic up-
RT regulation of utrophin in Duchenne muscular dystrophy.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14025-14030(1999).
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH DAG1.
RX PubMed=10767429; DOI=10.1016/s0014-5793(00)01400-9;
RA Tommasi di Vignano A., Di Zenzo G., Sudol M., Cesareni G., Dente L.;
RT "Contribution of the different modules in the utrophin carboxy-terminal
RT region to the formation and regulation of the DAP complex.";
RL FEBS Lett. 471:229-234(2000).
RN [8]
RP INTERACTION WITH DAG1.
RX PubMed=10769203; DOI=10.1242/jcs.113.10.1717;
RA James M., Nuttall A., Ilsley J.L., Ottersbach K., Tinsley J.M., Sudol M.,
RA Winder S.J.;
RT "Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan
RT regulates its interaction with utrophin.";
RL J. Cell Sci. 113:1717-1726(2000).
RN [9]
RP INTERACTION WITH SYNM.
RX PubMed=16777071; DOI=10.1016/j.bbrc.2006.05.192;
RA Bhosle R.C., Michele D.E., Campbell K.P., Li Z., Robson R.M.;
RT "Interactions of intermediate filament protein synemin with dystrophin and
RT utrophin.";
RL Biochem. Biophys. Res. Commun. 346:768-777(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4; SER-10 AND SER-3297, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP DOMAIN CH, AND ACTIN-BINDING.
RX PubMed=24628267; DOI=10.1021/bi500149q;
RA Singh S.M., Bandi S., Winder S.J., Mallela K.M.;
RT "The actin binding affinity of the utrophin tandem calponin-homology domain
RT is primarily determined by its N-terminal domain.";
RL Biochemistry 53:1801-1809(2014).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-2008 AND SER-2211,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-261.
RX PubMed=9887274; DOI=10.1006/jmbi.1998.2406;
RA Keep N.H., Norwood F.L.M., Moores C.A., Winder S.J., Kendrick-Jones J.;
RT "The 2.0-A structure of the second calponin homology domain from the actin-
RT binding region of the dystrophin homologue utrophin.";
RL J. Mol. Biol. 285:1257-1264(1999).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 31-256, AND SUBUNIT.
RX PubMed=10647184; DOI=10.1016/s0969-2126(00)88344-6;
RA Keep N.H., Winder S.J., Moores C.A., Walke S., Norwood F.L.M.,
RA Kendrick-Jones J.;
RT "Crystal structure of the actin-binding region of utrophin reveals a head-
RT to-tail dimer.";
RL Structure 7:1539-1546(1999).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (20 ANGSTROMS), AND ACTIN-BINDING.
RX PubMed=10715214; DOI=10.1006/jmbi.2000.3583;
RA Moores C.A., Keep N.H., Kendrick-Jones J.;
RT "Structure of the utrophin actin-binding domain bound to F-actin reveals
RT binding by an induced fit mechanism.";
RL J. Mol. Biol. 297:465-480(2000).
CC -!- FUNCTION: May play a role in anchoring the cytoskeleton to the plasma
CC membrane. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with the syntrophins SNTA1; SNTB1 and
CC SNTB2. Interacts with SYNM. Interacts (via its WWW and ZZ domains) with
CC DAG1 (via the PPXY motif of betaDAG1); the interaction is inhibited by
CC the tyrosine phosphorylation of the PPXY motif of DAG1. Interacts with
CC DTNB (By similarity). Interacts with PGM5 (By similarity).
CC {ECO:0000250|UniProtKB:G3V7L1, ECO:0000269|PubMed:10647184,
CC ECO:0000269|PubMed:10767429, ECO:0000269|PubMed:10769203,
CC ECO:0000269|PubMed:16777071, ECO:0000269|PubMed:7844150,
CC ECO:0000269|PubMed:8576247}.
CC -!- INTERACTION:
CC P46939; Q08209-1: PPP3CA; NbExp=3; IntAct=EBI-295856, EBI-15637215;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Neuromuscular
CC junction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=4;
CC Name=1;
CC IsoId=P46939-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P46939-2; Sequence=VSP_047925;
CC Name=Up71;
CC IsoId=P46939-3; Sequence=VSP_054943, VSP_054944;
CC Name=Up140;
CC IsoId=P46939-4; Sequence=VSP_054942;
CC -!- TISSUE SPECIFICITY: Isoform 1 has high expression in muscle. Isoforms
CC Up70 and Up140 were found in all the adult and fetal tissues tested and
CC relatively abundant in lung and kidney. {ECO:0000269|PubMed:10369873}.
CC -!- DOMAIN: Actin binding affinity is primarily determined by CH domain 1.
CC {ECO:0000269|PubMed:24628267}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Up71]: =Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Up140]: =Produced by alternative promoter
CC usage. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Utrophin entry;
CC URL="https://en.wikipedia.org/wiki/Utrophin";
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DR EMBL; X69086; CAA48829.1; -; mRNA.
DR EMBL; AL024474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ250044; CAB61826.1; -; Genomic_DNA.
DR CCDS; CCDS34547.1; -. [P46939-1]
DR PIR; S28381; S28381.
DR RefSeq; NP_009055.2; NM_007124.2. [P46939-1]
DR RefSeq; XP_005267187.1; XM_005267130.2. [P46939-1]
DR RefSeq; XP_011534408.1; XM_011536106.2. [P46939-1]
DR PDB; 1BHD; X-ray; 2.00 A; A/B=144-261.
DR PDB; 1QAG; X-ray; 3.00 A; A/B=31-256.
DR PDB; 6M5G; EM; 3.60 A; F/G/H=1-261.
DR PDBsum; 1BHD; -.
DR PDBsum; 1QAG; -.
DR PDBsum; 6M5G; -.
DR SMR; P46939; -.
DR BioGRID; 113245; 160.
DR CORUM; P46939; -.
DR DIP; DIP-711N; -.
DR IntAct; P46939; 93.
DR MINT; P46939; -.
DR STRING; 9606.ENSP00000356515; -.
DR BindingDB; P46939; -.
DR ChEMBL; CHEMBL4523230; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR GlyGen; P46939; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P46939; -.
DR MetOSite; P46939; -.
DR PhosphoSitePlus; P46939; -.
DR BioMuta; UTRN; -.
DR DMDM; 215274104; -.
DR EPD; P46939; -.
DR jPOST; P46939; -.
DR MassIVE; P46939; -.
DR MaxQB; P46939; -.
DR PaxDb; P46939; -.
DR PeptideAtlas; P46939; -.
DR PRIDE; P46939; -.
DR ProteomicsDB; 55775; -. [P46939-1]
DR ProteomicsDB; 64041; -.
DR ABCD; P46939; 1 sequenced antibody.
DR Antibodypedia; 4282; 90 antibodies from 20 providers.
DR DNASU; 7402; -.
DR Ensembl; ENST00000367545.8; ENSP00000356515.3; ENSG00000152818.19. [P46939-1]
DR GeneID; 7402; -.
DR KEGG; hsa:7402; -.
DR MANE-Select; ENST00000367545.8; ENSP00000356515.3; NM_007124.3; NP_009055.2.
DR UCSC; uc003qkt.4; human. [P46939-1]
DR CTD; 7402; -.
DR DisGeNET; 7402; -.
DR GeneCards; UTRN; -.
DR HGNC; HGNC:12635; UTRN.
DR HPA; ENSG00000152818; Low tissue specificity.
DR MIM; 128240; gene.
DR neXtProt; NX_P46939; -.
DR OpenTargets; ENSG00000152818; -.
DR PharmGKB; PA37260; -.
DR VEuPathDB; HostDB:ENSG00000152818; -.
DR eggNOG; KOG4286; Eukaryota.
DR GeneTree; ENSGT00940000153467; -.
DR HOGENOM; CLU_000246_2_0_1; -.
DR InParanoid; P46939; -.
DR OMA; NQRWDAI; -.
DR OrthoDB; 72477at2759; -.
DR PhylomeDB; P46939; -.
DR TreeFam; TF320178; -.
DR PathwayCommons; P46939; -.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; P46939; -.
DR SIGNOR; P46939; -.
DR BioGRID-ORCS; 7402; 11 hits in 1086 CRISPR screens.
DR ChiTaRS; UTRN; human.
DR EvolutionaryTrace; P46939; -.
DR GeneWiki; Utrophin; -.
DR GenomeRNAi; 7402; -.
DR Pharos; P46939; Tchem.
DR PRO; PR:P46939; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P46939; protein.
DR Bgee; ENSG00000152818; Expressed in calcaneal tendon and 192 other tissues.
DR ExpressionAtlas; P46939; baseline and differential.
DR Genevisible; P46939; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:BHF-UCL.
DR GO; GO:0031527; C:filopodium membrane; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IDA:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IPI:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0017166; F:vinculin binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 9.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035436; Dystrophin/utrophin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 10.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 18.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative promoter usage; Calcium;
KW Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Metal-binding;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Synapse; Zinc; Zinc-finger.
FT CHAIN 1..3433
FT /note="Utrophin"
FT /id="PRO_0000076082"
FT DOMAIN 31..135
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 150..255
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 312..416
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 421..525
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 532..636
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 690..795
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 801..901
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 910..1012
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 1019..1121
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 1128..1229
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 1236..1333
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT REPEAT 1335..1436
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1438..1540
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1547..1648
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1653..1747
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1748..1848
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1849..1968
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 1979..2080
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 2087..2186
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT REPEAT 2229..2332
FT /note="Spectrin 18"
FT /evidence="ECO:0000255"
FT REPEAT 2349..2439
FT /note="Spectrin 19"
FT /evidence="ECO:0000255"
FT REPEAT 2446..2555
FT /note="Spectrin 20"
FT /evidence="ECO:0000255"
FT REPEAT 2562..2687
FT /note="Spectrin 21"
FT /evidence="ECO:0000255"
FT REPEAT 2694..2796
FT /note="Spectrin 22"
FT /evidence="ECO:0000255"
FT DOMAIN 2812..2845
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 3065..3121
FT /note="ZZ-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..246
FT /note="Actin-binding"
FT REGION 268..905
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000269|PubMed:16777071"
FT REGION 284..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1768
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000269|PubMed:16777071"
FT REGION 2798..3165
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000269|PubMed:16777071"
FT REGION 3357..3390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3357..3381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3070
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3073
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3094
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3097
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 4
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2008
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 3297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..2086
FT /note="Missing (in isoform Up140)"
FT /evidence="ECO:0000303|PubMed:10369873"
FT /id="VSP_054942"
FT VAR_SEQ 1..23
FT /note="MAKYGEHEASPDNGQNEFSDIIK -> MKFFDFLFIFKILPPYYINFFSS
FT (in isoform Up71)"
FT /evidence="ECO:0000303|PubMed:10369873"
FT /id="VSP_054943"
FT VAR_SEQ 1..22
FT /note="MAKYGEHEASPDNGQNEFSDII -> MSGLAATTFHWKKCRLDLPGHVALQA
FT C (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047925"
FT VAR_SEQ 24..2832
FT /note="Missing (in isoform Up71)"
FT /evidence="ECO:0000303|PubMed:10369873"
FT /id="VSP_054944"
FT VARIANT 1880
FT /note="L -> I (in dbSNP:rs12204715)"
FT /id="VAR_047794"
FT VARIANT 1974
FT /note="A -> T (in dbSNP:rs12204734)"
FT /id="VAR_047795"
FT VARIANT 2060
FT /note="G -> D (in dbSNP:rs35676466)"
FT /id="VAR_047796"
FT VARIANT 2202
FT /note="N -> S (in dbSNP:rs1534443)"
FT /id="VAR_047797"
FT CONFLICT 236
FT /note="Q -> R (in Ref. 1; CAA48829)"
FT /evidence="ECO:0000305"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:1QAG"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1QAG"
FT TURN 56..62
FT /evidence="ECO:0007829|PDB:1QAG"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:1QAG"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:1QAG"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:1QAG"
FT HELIX 120..134
FT /evidence="ECO:0007829|PDB:1QAG"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:1QAG"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:1BHD"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1BHD"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1BHD"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:1BHD"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1BHD"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:1BHD"
FT HELIX 207..222
FT /evidence="ECO:0007829|PDB:1BHD"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:1BHD"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:1BHD"
FT CONFLICT P46939-3:5
FT /note="D -> N (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3433 AA; 394466 MW; C72CADE8CD666993 CRC64;
MAKYGEHEAS PDNGQNEFSD IIKSRSDEHN DVQKKTFTKW INARFSKSGK PPINDMFTDL
KDGRKLLDLL EGLTGTSLPK ERGSTRVHAL NNVNRVLQVL HQNNVELVNI GGTDIVDGNH
KLTLGLLWSI ILHWQVKDVM KDVMSDLQQT NSEKILLSWV RQTTRPYSQV NVLNFTTSWT
DGLAFNAVLH RHKPDLFSWD KVVKMSPIER LEHAFSKAQT YLGIEKLLDP EDVAVQLPDK
KSIIMYLTSL FEVLPQQVTI DAIREVETLP RKYKKECEEE AINIQSTAPE EEHESPRAET
PSTVTEVDMD LDSYQIALEE VLTWLLSAED TFQEQDDISD DVEEVKDQFA THEAFMMELT
AHQSSVGSVL QAGNQLITQG TLSDEEEFEI QEQMTLLNAR WEALRVESMD RQSRLHDVLM
ELQKKQLQQL SAWLTLTEER IQKMETCPLD DDVKSLQKLL EEHKSLQSDL EAEQVKVNSL
THMVVIVDEN SGESATAILE DQLQKLGERW TAVCRWTEER WNRLQEINIL WQELLEEQCL
LKAWLTEKEE ALNKVQTSNF KDQKELSVSV RRLAILKEDM EMKRQTLDQL SEIGQDVGQL
LDNSKASKKI NSDSEELTQR WDSLVQRLED SSNQVTQAVA KLGMSQIPQK DLLETVRVRE
QAITKKSKQE LPPPPPPKKR QIHVDIEAKK KFDAISAELL NWILKWKTAI QTTEIKEYMK
MQDTSEMKKK LKALEKEQRE RIPRADELNQ TGQILVEQMG KEGLPTEEIK NVLEKVSSEW
KNVSQHLEDL ERKIQLQEDI NAYFKQLDEL EKVIKTKEEW VKHTSISESS RQSLPSLKDS
CQRELTNLLG LHPKIEMARA SCSALMSQPS APDFVQRGFD SFLGRYQAVQ EAVEDRQQHL
ENELKGQPGH AYLETLKTLK DVLNDSENKA QVSLNVLNDL AKVEKALQEK KTLDEILENQ
KPALHKLAEE TKALEKNVHP DVEKLYKQEF DDVQGKWNKL KVLVSKDLHL LEEIALTLRA
FEADSTVIEK WMDGVKDFLM KQQAAQGDDA GLQRQLDQCS AFVNEIETIE SSLKNMKEIE
TNLRSGPVAG IKTWVQTRLG DYQTQLEKLS KEIATQKSRL SESQEKAANL KKDLAEMQEW
MTQAEEEYLE RDFEYKSPEE LESAVEEMKR AKEDVLQKEV RVKILKDNIK LLAAKVPSGG
QELTSELNVV LENYQLLCNR IRGKCHTLEE VWSCWIELLH YLDLETTWLN TLEERMKSTE
VLPEKTDAVN EALESLESVL RHPADNRTQI RELGQTLIDG GILDDIISEK LEAFNSRYED
LSHLAESKQI SLEKQLQVLR ETDQMLQVLQ ESLGELDKQL TTYLTDRIDA FQVPQEAQKI
QAEISAHELT LEELRRNMRS QPLTSPESRT ARGGSQMDVL QRKLREVSTK FQLFQKPANF
EQRMLDCKRV LDGVKAELHV LDVKDVDPDV IQTHLDKCMK LYKTLSEVKL EVETVIKTGR
HIVQKQQTDN PKGMDEQLTS LKVLYNDLGA QVTEGKQDLE RASQLARKMK KEAASLSEWL
SATETELVQK STSEGLLGDL DTEISWAKNV LKDLEKRKAD LNTITESSAA LQNLIEGSEP
ILEERLCVLN AGWSRVRTWT EDWCNTLMNH QNQLEIFDGN VAHISTWLYQ AEALLDEIEK
KPTSKQEEIV KRLVSELDDA NLQVENVRDQ ALILMNARGS SSRELVEPKL AELNRNFEKV
SQHIKSAKLL IAQEPLYQCL VTTETFETGV PFSDLEKLEN DIENMLKFVE KHLESSDEDE
KMDEESAQIE EVLQRGEEML HQPMEDNKKE KIRLQLLLLH TRYNKIKAIP IQQRKMGQLA
SGIRSSLLPT DYLVEINKIL LCMDDVELSL NVPELNTAIY EDFSFQEDSL KNIKDQLDKL
GEQIAVIHEK QPDVILEASG PEAIQIRDTL TQLNAKWDRI NRMYSDRKGC FDRAMEEWRQ
FHCDLNDLTQ WITEAEELLV DTCAPGGSLD LEKARIHQQE LEVGISSHQP SFAALNRTGD
GIVQKLSQAD GSFLKEKLAG LNQRWDAIVA EVKDRQPRLK GESKQVMKYR HQLDEIICWL
TKAEHAMQKR STTELGENLQ ELRDLTQEME VHAEKLKWLN RTELEMLSDK SLSLPERDKI
SESLRTVNMT WNKICREVPT TLKECIQEPS SVSQTRIAAH PNVQKVVLVS SASDIPVQSH
RTSEISIPAD LDKTITELAD WLVLIDQMLK SNIVTVGDVE EINKTVSRMK ITKADLEQRH
PQLDYVFTLA QNLKNKASSS DMRTAITEKL ERVKNQWDGT QHGVELRQQQ LEDMIIDSLQ
WDDHREETEE LMRKYEARLY ILQQARRDPL TKQISDNQIL LQELGPGDGI VMAFDNVLQK
LLEEYGSDDT RNVKETTEYL KTSWINLKQS IADRQNALEA EWRTVQASRR DLENFLKWIQ
EAETTVNVLV DASHRENALQ DSILARELKQ QMQDIQAEID AHNDIFKSID GNRQKMVKAL
GNSEEATMLQ HRLDDMNQRW NDLKAKSASI RAHLEASAEK WNRLLMSLEE LIKWLNMKDE
ELKKQMPIGG DVPALQLQYD HCKALRRELK EKEYSVLNAV DQARVFLADQ PIEAPEEPRR
NLQSKTELTP EERAQKIAKA MRKQSSEVKE KWESLNAVTS NWQKQVDKAL EKLRDLQGAM
DDLDADMKEA ESVRNGWKPV GDLLIDSLQD HIEKIMAFRE EIAPINFKVK TVNDLSSQLS
PLDLHPSLKM SRQLDDLNMR WKLLQVSVDD RLKQLQEAHR DFGPSSQHFL STSVQLPWQR
SISHNKVPYY INHQTQTTCW DHPKMTELFQ SLADLNNVRF SAYRTAIKIR RLQKALCLDL
LELSTTNEIF KQHKLNQNDQ LLSVPDVINC LTTTYDGLEQ MHKDLVNVPL CVDMCLNWLL
NVYDTGRTGK IRVQSLKIGL MSLSKGLLEE KYRYLFKEVA GPTEMCDQRQ LGLLLHDAIQ
IPRQLGEVAA FGGSNIEPSV RSCFQQNNNK PEISVKEFID WMHLEPQSMV WLPVLHRVAA
AETAKHQAKC NICKECPIVG FRYRSLKHFN YDVCQSCFFS GRTAKGHKLH YPMVEYCIPT
TSGEDVRDFT KVLKNKFRSK KYFAKHPRLG YLPVQTVLEG DNLETPITLI SMWPEHYDPS
QSPQLFHDDT HSRIEQYATR LAQMERTNGS FLTDSSSTTG SVEDEHALIQ QYCQTLGGES
PVSQPQSPAQ ILKSVEREER GELERIIADL EEEQRNLQVE YEQLKDQHLR RGLPVGSPPE
SIISPHHTSE DSELIAEAKL LRQHKGRLEA RMQILEDHNK QLESQLHRLR QLLEQPESDS
RINGVSPWAS PQHSALSYSL DPDASGPQFH QAAGEDLLAP PHDTSTDLTE VMEQIHSTFP
SCCPNVPSRP QAM
