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O97592

- DMD_CANFA

UniProt

O97592 - DMD_CANFA

Protein

Dystrophin

Gene

DMD

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri3302 – 334948ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. zinc ion binding Source: InterPro

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dystrophin
    Gene namesi
    Name:DMD
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    Subcellular locationi

    Cell membranesarcolemma; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton By similarity. Cell junctionsynapsepostsynaptic cell membrane By similarity
    Note: In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs) in the presence of ANK2 By similarity.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB-KW
    3. cytoskeleton Source: UniProtKB-SubCell
    4. postsynaptic membrane Source: UniProtKB-SubCell
    5. sarcolemma Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Postsynaptic cell membrane, Synapse

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 36803680DystrophinPRO_0000076074Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3478 – 34781PhosphoserineBy similarity
    Modified residuei3607 – 36071PhosphoserineBy similarity
    Modified residuei3608 – 36081PhosphoserineBy similarity
    Modified residuei3612 – 36121PhosphoserineBy similarity
    Modified residuei3618 – 36181PhosphoserineBy similarity
    Modified residuei3619 – 36191PhosphoserineBy similarity
    Modified residuei3661 – 36611PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO97592.

    Interactioni

    Subunit structurei

    Interacts with SYNM. Interacts with the syntrophins SNTA1, SNTB1, SNTB2, SNTG1 and SNTG2. Interacts with KRT19. Component of the dystrophin-associated glycoprotein complex which is composed of three subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the transmembrane dystroglycan complex, and the sarcoglycan-sarcospan complex. Interacts with DAG1 (betaDAG1) with DMD; the interaction is inhibited by phosphorylation on the PPXY motif of DAG1. Interacts with CMYA5. Directly interacts with ANK2 and ANK3; these interactions do not interfere with betaDAG1-binding and are necessary for proper localization in muscle cells By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000020300.

    Structurei

    3D structure databases

    ProteinModelPortaliO97592.
    SMRiO97592. Positions 9-246, 3042-3301.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 237237Actin-bindingAdd
    BLAST
    Domaini15 – 119105CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini134 – 237104CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati340 – 448109Spectrin 1Add
    BLAST
    Repeati449 – 557109Spectrin 2Add
    BLAST
    Repeati560 – 668109Spectrin 3Add
    BLAST
    Repeati720 – 829110Spectrin 4Add
    BLAST
    Repeati831 – 935105Spectrin 5Add
    BLAST
    Repeati944 – 1047104Spectrin 6Add
    BLAST
    Repeati1050 – 1156107Spectrin 7Add
    BLAST
    Repeati1159 – 1265107Spectrin 8Add
    BLAST
    Repeati1268 – 1369102Spectrin 9Add
    BLAST
    Repeati1370 – 146596Spectrin 10Add
    BLAST
    Repeati1470 – 1570101Spectrin 11Add
    BLAST
    Repeati1573 – 1678106Spectrin 12Add
    BLAST
    Repeati1681 – 1780100Spectrin 13Add
    BLAST
    Repeati1781 – 187696Spectrin 14Add
    BLAST
    Repeati1879 – 1981103Spectrin 15Add
    BLAST
    Repeati1994 – 2103110Spectrin 16Add
    BLAST
    Repeati2106 – 2210105Spectrin 17Add
    BLAST
    Repeati2213 – 2320108Spectrin 18Add
    BLAST
    Repeati2321 – 241898Spectrin 19Add
    BLAST
    Repeati2470 – 2572103Spectrin 20Add
    BLAST
    Repeati2575 – 2681107Spectrin 21Add
    BLAST
    Repeati2684 – 2797114Spectrin 22Add
    BLAST
    Repeati2803 – 2925123Spectrin 23Add
    BLAST
    Repeati2930 – 3035106Spectrin 24Add
    BLAST
    Domaini3050 – 308334WWPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni63 – 7210ANK2- and ANK-3 bindingBy similarity
    Regioni1418 – 1915498Interaction with SYNMBy similarityAdd
    BLAST
    Regioni3053 – 3403351Interaction with SYNMBy similarityAdd
    BLAST
    Regioni3461 – 351353Binds to SNTB1By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 actin-binding domain.Curated
    Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
    Contains 24 spectrin repeats.Curated
    Contains 1 WW domain.PROSITE-ProRule annotation
    Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri3302 – 334948ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5069.
    HOVERGENiHBG005495.
    KOiK10366.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProiIPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR016344. Dystrophin/utrophin.
    IPR011992. EF-hand-dom_pair.
    IPR015153. EF-hand_dom_typ1.
    IPR015154. EF-hand_dom_typ2.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    IPR001202. WW_dom.
    IPR000433. Znf_ZZ.
    [Graphical view]
    PfamiPF00307. CH. 2 hits.
    PF09068. EF-hand_2. 1 hit.
    PF09069. EF-hand_3. 1 hit.
    PF00435. Spectrin. 16 hits.
    PF00397. WW. 1 hit.
    PF00569. ZZ. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002341. Dystrophin/utrophin. 1 hit.
    SMARTiSM00033. CH. 2 hits.
    SM00150. SPEC. 22 hits.
    SM00456. WW. 1 hit.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    SSF51045. SSF51045. 1 hit.
    PROSITEiPS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O97592-1 [UniParc]FASTAAdd to Basket

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    MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL     50
    LDLLEGLTGQ KLPKEKGSTR VHALNNVNKA LRVLQKNNVD LVNIGSTDIV 100
    DGNHKLTLGL IWNIILHWQV KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN 150
    YPQVNVINFT TSWSDGLALN ALIHSHRPDL FDWNSVVCQQ SATQRLEHAF 200
    NIAKYQLGIE KLLDPEDVAT TYPDKKSILM YITSLFQVLP QQVSIEAIQE 250
    VEMLPRPSQV TREEHFQIHH QMHYSQQITV SLAQGYERAP SFPKPRFKSY 300
    AYTQAAYVTT SDPTRSPLPS QHLETPEDKS FGRSLTETEA NLDSYQTALE 350
    EVLSWLLSAE DALQAQGEIS NDVEEVKEQF HTHEGYMMDL TSHQGRVGNV 400
    LQLGSQLIGT GKLSEDEETE VQEQMNLLNS RWECLRVASM EKQSNLHKVL 450
    MDLQNQQLKE LNDWLTKTEE RTRKMEKEPL GPDIEDLKRQ VQQHKVLQED 500
    LEQEQVRVNS LTHMVVVVDE SSGDHATAAL EEQLKVLGDR WANICRWTED 550
    RWVLLQDILL KWQRFTEEQC LFSAWLSEKE DAVNKIHTTG FKDQSEVLSN 600
    LQKLAVLKTD LEKKKQTMDK LCSLNQDLLS ALKNTVVAHK MEAWLDNFAQ 650
    RWDNLVQKLE KSSAQISQAV TTTQPSLTQT TVMETVTMVT TREHILVKHA 700
    QEELPPPPPQ KKRQIIVDSE IRKRLDVDIT ELHSWITRSE AVLQSPEFAI 750
    YRKEGNFSDL KEKVNAIERE KAEKFRKLQD ASRSAQALVE QMVNEGVNAD 800
    SIKQASEQLN SRWIEFCQLL SERLNWLEYQ NNIITFYNQL QQLEQMTTTA 850
    ENWLKTQPTT TSEPTAIKSQ LKICKDEINR LSALQPQIER LKIQSIALKE 900
    KGQGPMFLDA DFVAFTNHFN QVFADVQARE KELQTIFDSL PPMRYQETMS 950
    TILTWIQQSE TKLSIPQVTV TEYDIMEQRL GELQALQSSL QEQQNGLNYL 1000
    STTVKEMSKK APLSDISRKY QSEFEEIEGR WKKLSSQLVE HCQKLEEQMA 1050
    KLRKIQNHIK TLKKWITEVD VFLKEEWPAL GDSEILKRQL KQCRLLVNDI 1100
    QTIQPSLNSV NEGAQKMKNE AEPEFAGRLE TELRELNTQW DYMCRQVYAR 1150
    KEALKGGLDK TVSLQKDLSE MHEWMTQAEE EYLERDFEYK TPDELQTAVE 1200
    EMKRAKEEAQ QKEAKVKLLT ESVNSVIAQA PPAAQEALKK ELDTLTTNYQ 1250
    WLCTRLNGKC KTLEEVWACW HELLSYLEKA NKWLSEVEVK LKTTENISGG 1300
    AEEIAEVLDS LENLMQHSED NPNQIRILAQ TLTDGGVMDE LINEELETFN 1350
    SRWRELHEEA VRRQKLLEQS IQSAQEIEKS LHLIQESLSS IDKQLAAYIA 1400
    DKVDAAQMPQ EAQKIQSDLT SHEISLEEMK KHNQGKETAQ RVLSQIDVAQ 1450
    KKLQDVSMKF RLFQKPANFE QRLQESKMIL DEVKMHLPAL ETKSVEQEVV 1500
    QSQLNHCVNL YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL 1550
    KLHYNELGAK VTERKQQLEK CLKLSRKMRK EMNALTEWLA ATDMELTKRS 1600
    AVEGMPSNLD SEVAWGKATQ KEIEKQKVHL KSVTEVGEAL KTVLGKKEML 1650
    VEDKLSLLNS NWIAVTSRAE EWLNLLLEYQ KHMETFDQNV DYITNWIIQA 1700
    DALLDESEKK KPQQKEDILK RLKAEMNDIR PKVDSTRDQA ANLMANRGDH 1750
    CRKVVEPKIS ELNHRFAAIS HRIKTGKASI PLKELEQFNS DIQKLLEPLE 1800
    AEIQQGVNLK EEDFNKDMSE DNEGTVKELL QRGDNLQQRI TDERKREEIK 1850
    IKQQLLQTKH NALKDLRSQR RKKALEISHQ WYQYKRQADD LLKCLDDIEK 1900
    KLASLPEPRD ERKIKEIDRE LQKKKEELNA VRRQAEGLSE DGAAMAVEPT 1950
    QIQLSKRWRE IESKFAQFRR LNFAQIHTVH EESVVAMTED MPLEISYVPS 2000
    TYLTEITHVS QALSEVEELL NAPDLCAQDF EDLFKQEESL KNIKDSLQQI 2050
    SGRIDIIHNK KTAALHSATP AERAKLQEAL SRLDFQWERV NNMYKDRQGR 2100
    FDRSVEKWRR FHYDMKILNQ WLTEAEQFLK KTQIPENWEH AKYKWYLKEL 2150
    QDGIGQRQSV VRVLNATGEE IIQQSSKTDA SILQEKLGSL NLRWQEVCKQ 2200
    LAERKKRLEE QKNILSEFQR DVNEFVLWLE EADNVANIPL EPGNEQQLKE 2250
    KLEQVKLLAE ELPLRQGILK QLNETGGTVL VSAPLSPEEQ DKLENKLKQT 2300
    NLQWIKVSRN LPEKQEEIEA HVKDLGQLEE QLNHLLLWLS PIRNQLEIYN 2350
    QPNQTGPFDI KEIEVAVQAK QPDVEGILSK GQHLYKEKPA TQPAKRKLED 2400
    LSSDWKVVTQ LLQELRAKQP GPAPGLTTVR APPSQTVTLV TQPAVTKETA 2450
    ISKLEMPSSL LLEVPALADF NRAWTELTDW LSLLDRVIKS QRVMVGDLED 2500
    INEMIIKQKA TLQDLEQRRP QLEELITAAQ NLKNKTSNQE ARTIITDRIE 2550
    RIQSQWDEVQ EHLQNRRLQL TEMLKDSTQW LEAKEEAEQV LGQARAKLES 2600
    WKEAPYTVDA IQKKITETKQ LAKDLRQWQI NVDVANDLAL KLLRDYSADD 2650
    TRKVHMITEN INASWASIHK RLSEREAALE ETHRLLQQFP LDLEKFLAWL 2700
    TEAETTANVL QDATHKERLL EDSKGVRELM KQWQDLQGEI EAHTDIYHNL 2750
    DENGQKVLRS LEGSDDAALL QRRLDNMNFK WSELRKKSLN IRSHLEASSD 2800
    QWKRLHLSLQ ELLVWLQLKD DELSRQAPIG GDFPAVQKQN DVHRAFKREL 2850
    KTKEPVIMST LETVRIFLTE QPLEGLEKLY QEPRELPPEE RAQNVTRLLR 2900
    KQAEEVNTQW EKLNVHSADW QRKIDEALER LQELQEATDE LDLKLRQAEV 2950
    IKGSWQPVGD LLIDSLQDHL EKVKALRGEI TPLKENVSYV NDLARQLTTL 3000
    GIQLSPYNLN TLEDLNTRWK LLQVAIEDRI RQLHEAHRDF GPASQHFLST 3050
    SVQGPWERAI SPNKVPYYIN HETQTTCWDH PKMTELYQSL ADLNNVRFSA 3100
    YRTAMKLRRL QKALCLDLLS LSAACDALDQ HNLKQNDQPM DILQVINCLT 3150
    TIYDRLEQEH NNLVNVPLCV DMCLNWLLNV YDTGRTGRIR VLSFKTGIIS 3200
    LCKAHLEDKY RYLFKQVASS TGFCDQRRLG LLLHDSIQIP RQLGEVASFG 3250
    GSNIEPSVRS CFQFANNKPE IEAALFLDWM RLEPQSMVWL PVLHRVAAAE 3300
    TAKHQAKCNI CKECPIIGFR YRSLKHFNYD ICQSCFFSGR VAKGHKMHYP 3350
    MVEYCTPTTS GEDVRDFAKV LKNKFRTKRY FAKHPRMGYL PVQTVLEGDN 3400
    METPVTLINF WPVDSAPASS PQLSHDDTHS RIEHYASRLK KMENSNGSYL 3450
    NDSISPNESI DDEHLLIQHY WRSLNQESPL SQPRSPAQIL ISLESEERGE 3500
    LERILADLEG RNRNLQAEYD RLKQQHEHKG LSPLPSPPEM MPTSPQSPRD 3550
    AELIAEAKLL RQHKGRLEAR MQILEDHNKQ LESQLHRLRQ LLEQPQAEAK 3600
    VNGTTVSSPS TSLQRSDSSQ PMLLRVVGSQ TSESMGEEDL LSPPQDTSTG 3650
    LEEVMEQLNH SFPSSRGRNT PGKPMREDTM 3680
    Length:3,680
    Mass (Da):425,653
    Last modified:May 1, 1999 - v1
    Checksum:i539F1C9D72377872
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF070485 mRNA. Translation: AAC83646.1.
    RefSeqiNP_001003343.1. NM_001003343.1.
    UniGeneiCfa.3738.

    Genome annotation databases

    GeneIDi606758.
    KEGGicfa:606758.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF070485 mRNA. Translation: AAC83646.1 .
    RefSeqi NP_001003343.1. NM_001003343.1.
    UniGenei Cfa.3738.

    3D structure databases

    ProteinModelPortali O97592.
    SMRi O97592. Positions 9-246, 3042-3301.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000020300.

    Proteomic databases

    PaxDbi O97592.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 606758.
    KEGGi cfa:606758.

    Organism-specific databases

    CTDi 1756.

    Phylogenomic databases

    eggNOGi COG5069.
    HOVERGENi HBG005495.
    KOi K10366.

    Miscellaneous databases

    NextBioi 20892530.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR016344. Dystrophin/utrophin.
    IPR011992. EF-hand-dom_pair.
    IPR015153. EF-hand_dom_typ1.
    IPR015154. EF-hand_dom_typ2.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    IPR001202. WW_dom.
    IPR000433. Znf_ZZ.
    [Graphical view ]
    Pfami PF00307. CH. 2 hits.
    PF09068. EF-hand_2. 1 hit.
    PF09069. EF-hand_3. 1 hit.
    PF00435. Spectrin. 16 hits.
    PF00397. WW. 1 hit.
    PF00569. ZZ. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002341. Dystrophin/utrophin. 1 hit.
    SMARTi SM00033. CH. 2 hits.
    SM00150. SPEC. 22 hits.
    SM00456. WW. 1 hit.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    SSF51045. SSF51045. 1 hit.
    PROSITEi PS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Alternative dystrophin gene transcripts in golden retriever muscular dystrophy."
      Schatzberg S.J., Anderson L.V., Wilton S.D., Kornegay J.N., Mann C.J., Solomon G.G., Sharp N.J.
      Muscle Nerve 21:991-998(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
      Strain: Golden retriever.

    Entry informationi

    Entry nameiDMD_CANFA
    AccessioniPrimary (citable) accession number: O97592
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3