ID A0A087WRB8_MOUSE Unreviewed; 1471 AA. AC A0A087WRB8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 13-SEP-2023, entry version 56. DE SubName: Full=Dystonin {ECO:0000313|Ensembl:ENSMUSP00000140560.2}; DE Flags: Fragment; GN Name=Dst {ECO:0000313|Ensembl:ENSMUSP00000140560.2, GN ECO:0000313|MGI:MGI:104627}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000140560.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000140560.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140560.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000140560.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140560.2}; RG Ensembl; RL Submitted (MAY-2023) to UniProtKB. CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. CC {ECO:0000256|ARBA:ARBA00009109}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR SMR; A0A087WRB8; -. DR ProteomicsDB; 355784; -. DR Antibodypedia; 31066; 191 antibodies from 23 providers. DR Ensembl; ENSMUST00000187486.7; ENSMUSP00000140560.2; ENSMUSG00000026131.21. DR AGR; MGI:104627; -. DR MGI; MGI:104627; Dst. DR VEuPathDB; HostDB:ENSMUSG00000026131; -. DR GeneTree; ENSGT00940000155008; -. DR HOGENOM; CLU_004168_0_0_1; -. DR ChiTaRS; Dst; mouse. DR Proteomes; UP000000589; Chromosome 1. DR Bgee; ENSMUSG00000026131; Expressed in aorta tunica media and 256 other tissues. DR ExpressionAtlas; A0A087WRB8; baseline and differential. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEA:InterPro. DR CDD; cd21236; CH_DYST_rpt1; 1. DR CDD; cd21239; CH_DYST_rpt2; 1. DR CDD; cd00176; SPEC; 1. DR Gene3D; 1.20.58.1060; -; 1. DR Gene3D; 1.20.58.60; -; 5. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR041615; Desmoplakin_SH3. DR InterPro; IPR041573; Desmoplakin_Spectrin-like. DR InterPro; IPR043197; Plakin. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR PANTHER; PTHR23169:SF24; DYSTONIN; 1. DR PANTHER; PTHR23169; ENVOPLAKIN; 1. DR Pfam; PF00307; CH; 2. DR Pfam; PF17902; SH3_10; 1. DR Pfam; PF00435; Spectrin; 1. DR Pfam; PF18373; Spectrin_like; 1. DR SMART; SM00033; CH; 2. DR SMART; SM00150; SPEC; 3. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF46966; Spectrin repeat; 5. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW Actin-binding {ECO:0000256|ARBA:ARBA00023203}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Microtubule {ECO:0000256|ARBA:ARBA00022701}; KW Proteomics identification {ECO:0007829|EPD:A0A087WRB8, KW ECO:0007829|MaxQB:A0A087WRB8}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}. FT DOMAIN 75..178 FT /note="Calponin-homology (CH)" FT /evidence="ECO:0000259|PROSITE:PS50021" FT DOMAIN 191..295 FT /note="Calponin-homology (CH)" FT /evidence="ECO:0000259|PROSITE:PS50021" FT DOMAIN 926..983 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT REGION 1..57 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 781..808 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1247..1281 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1..35 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1471 FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000140560.2" SQ SEQUENCE 1471 AA; 170209 MW; 40ECA2095F7219A5 CRC64; MSSGNASYRC SMSSSADFSD EDDFSQKSGS ASPAPGDTLP WNLPKHERSK RKIQGGSVLD PAERAVLRIA DERDKVQKKT FTKWINQHLM KVRKHVNDLY EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL DYLKRRQVKL VNIRNDDITD GNPKLTLGLI WTIILHFQIS DIHVTGESED MSAKERLLLW TQQATEGYAG VRCENFTTCW RDGKLFNAII HKYRPDLIDM NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE KSVITYVSSL YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VVTMSERTFP NNPLELKALY NQYLQFKEKE IPPKEMEKSK IKRLYKLLEI WIEFGRIKLL QGYHPNDIEK EWGKLIIAML EREKALRPEV ERLDMLQQIA TRVQRDSVSC EDKLILARNA LQSDSKRLES GVQFQNEAEI AGYILECENL LRQHVIDVQI LIDGKYYQAD QLVQRVAKLR DEIMALRNEC SSVYSKGRML TTEQTKLMIS GITQSLNSGF AQTLHPSLNS GLTQSLTPSL TSSSVTSGLS SGMTSRLTPS VTPVYAPGFP SVVAPNFSLG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE EEVNMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE FESSLKEAKI SEIQMTAPLK LSYTDKLHRL ESQYAKLLNT SRNQERHLDT LHNFVTRATN ELIWLNEKEE SEVAYDWSER NSSVARKKSY HAELMRELEQ KEESIKAVQE IAEQLLLENH PARLTIEAYR AAMQTQWSWI LQLCQCVEQH IQENSAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI HKLEDLVQES MEKEELLQYR SVVAGLMGRA KTVVQLKPRN PDNPLKTSIP IKAICDYRQI EITIYKDDEC VLANNSHRAK WKVISPTGNE AMVPSVCFTV PPPNKEAVDF ANRIEQQYQS VLTLWHESHI NMKSVVSWHY LVNEIDRIRA SNVASIKTML PGEHQQVLSN LQSRLEDFLE DSQESQIFSG SDISQLEKEV SVCRKYYQEL LKSAEREEQE ESVYNLYISE VRNIRLRLES CEDRLIRQIR TPLERDDLHE SMLRITEQEK LKKELDRLKD DLGTITNKCE EFFSQAADSP SVPALRSELS VVIQSLSQIY SMSSTYIEKL KTVNLVLKNT QAAEALVKLY ETKLCEEEAV IADKNNIENL MSTLKQWRSE VDEKREVFHA LEDELQKAKA ISDEMFKTHK ERDLDFDWHK EKADQLVERW QSVHVQIDNR LRDLEGIGKS LKHYRDSYHP LDDWIQHIET TQRKIQENQP ENSKALALQL NQQKMLVSEI EVKQSKMDEC QKYSEQYSAA VKDYELQTMT YRAMVESQQK SPVKRRRIQS SADLVIQEFM DLRTRYTALV TLMTQYIKFA GDSLKRLEEE E //