ID A0A087WRB8_MOUSE Unreviewed; 1471 AA.
AC A0A087WRB8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family.
CC {ECO:0000256|ARBA:ARBA00009109}.
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DR SMR; A0A087WRB8; -.
DR ProteomicsDB; 355784; -.
DR Antibodypedia; 31066; 193 antibodies from 23 providers.
DR Ensembl; ENSMUST00000187486.7; ENSMUSP00000140560.2; ENSMUSG00000026131.22.
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 259 other cell types or tissues.
DR ExpressionAtlas; A0A087WRB8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IPR049538; PCN-like_spectrin-like_rpt.
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_2; 1.
DR Pfam; PF21019; Spectrin_3; 1.
DR Pfam; PF21020; Spectrin_4; 1.
DR Pfam; PF21097; SR_plectin_7; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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
//
