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Q9ESD7

- DYSF_MOUSE

UniProt

Q9ESD7 - DYSF_MOUSE

Protein

Dysferlin

Gene

Dysf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    Key calcium ion sensor involved in the Ca2+-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi18 – 181CalciumBy similarity
    Metal bindingi19 – 191Calcium; via carbonyl oxygenBy similarity
    Metal bindingi21 – 211CalciumBy similarity
    Metal bindingi40 – 401CalciumBy similarity

    GO - Molecular functioni

    1. calcium-dependent phospholipid binding Source: Ensembl
    2. calcium ion binding Source: UniProtKB
    3. phospholipid binding Source: UniProtKB
    4. protein binding Source: UniProt

    GO - Biological processi

    1. plasma membrane repair Source: UniProtKB
    2. vesicle fusion Source: UniProtKB

    Keywords - Ligandi

    Calcium, Lipid-binding, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dysferlin
    Alternative name(s):
    Dystrophy-associated fer-1-like protein
    Fer-1-like protein 1
    Gene namesi
    Name:Dysf
    Synonyms:Fer1l1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1349385. Dysf.

    Subcellular locationi

    Cell membranesarcolemma; Single-pass type II membrane protein. Cytoplasmic vesicle membrane; Single-pass type II membrane protein. Cell membrane By similarity
    Note: Colocalizes, during muscle differentiation, with BIN1 in the T-tubule system of myotubules and at the site of contact between two myotubes or a myoblast and a myotube By similarity. Accumulates and colocalizes with fusion vesicles at the sarcolemma disruption sites. Wounding of myotubes led to its focal enrichment to the site of injury and to its relocalization in a Ca2+-dependent manner toward the plasma membrane By similarity. Colocalizes with ANXA1 and ANXA2 at the sarcolemma in skeletal muscle. Colocalizes with PARVB at the sarcolemma of skeletal muscle By similarity. Retained by caveolin at the plasmma membrane. Reaches the plasmma membrane through a caveolin-independent mechanism. Colocalizes, during muscle differentiation, with CACNA1S in the T-tubule system of myotubules. Detected on the apical plasma membrane of the syncytiotrophoblast By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasmic vesicle Source: UniProtKB
    2. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. lamellipodium Source: UniProtKB
    5. plasma membrane Source: UniProtKB
    6. sarcolemma Source: UniProtKB
    7. T-tubule Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Dysf are the cause of a slowly progressive muscular dystrophy observed in SJL mice. It affects primarily the proximal muscles and it is inherited as autosomal recessive trait.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20902090DysferlinPRO_0000057880Add
    BLAST

    Proteomic databases

    MaxQBiQ9ESD7.
    PaxDbiQ9ESD7.
    PRIDEiQ9ESD7.

    PTM databases

    PhosphoSiteiQ9ESD7.

    Expressioni

    Tissue specificityi

    Expressed in skeletal and cardiac muscles (at protein level). Expressed in skeletal muscle and heart. Also found in brain, liver and kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ9ESD7.
    BgeeiQ9ESD7.
    CleanExiMM_DYSF.
    GenevestigatoriQ9ESD7.

    Interactioni

    Subunit structurei

    Interacts with CAV3. Interacts with AHNAK; the interaction is direct and Ca2+-independent. Interacts with AHNAK2; the interaction is direct and Ca2+-independent By similarity. Interacts with ANXA1; the interaction is Ca2+- and injury state-dependent. Interacts with ANXA2; the interaction is Ca2+- and injury state-dependent. Interacts with CACNA1S and PARVB. Interacts with TRIM72/MG53; interaction is required for transport to sites of cell injury during repair patch formation.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi205052. 2 interactions.
    IntActiQ9ESD7. 4 interactions.
    MINTiMINT-4998243.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ESD7.
    SMRiQ9ESD7. Positions 1-124, 223-489, 883-945, 953-1061, 1074-1110, 1156-1275, 1584-1675.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 20562056CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2078 – 209013ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2057 – 207721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8585C2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini209 – 30496C2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini368 – 486119C2 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1149 – 1254106C2 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1346 – 143388C2 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1575 – 167399C2 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1823 – 1936114C2 7PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1048 – 110760Arg-richAdd
    BLAST

    Domaini

    All seven C2 domains associate with lipid membranes in a calcium-dependent manner. Domains C2 1 and 3 have the highest affinity for calcium, the C2 domain 1 seems to be largely unstructured in the absence of bound ligands By similarity.By similarity

    Sequence similaritiesi

    Belongs to the ferlin family.Curated
    Contains 7 C2 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG330124.
    GeneTreeiENSGT00550000074414.
    HOGENOMiHOG000006771.
    HOVERGENiHBG018972.
    InParanoidiQ6KAR3.
    KOiK18261.
    OMAiQVHLALK.
    TreeFamiTF316871.

    Family and domain databases

    Gene3Di2.60.40.150. 8 hits.
    InterProiIPR000008. C2_dom.
    IPR012968. FerIin-domain.
    IPR012560. Ferlin_A-domain.
    IPR012561. Ferlin_B-domain.
    IPR010482. Peroxin/Dysferlin.
    IPR006614. Peroxin/Ferlin.
    [Graphical view]
    PfamiPF00168. C2. 7 hits.
    PF08165. FerA. 1 hit.
    PF08150. FerB. 1 hit.
    PF08151. FerI. 1 hit.
    PF06398. Pex24p. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 7 hits.
    SM00694. DysFC. 2 hits.
    SM00693. DysFN. 2 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 7 hits.
    PROSITEiPS50004. C2. 5 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9ESD7-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLRVFILFAE NVHTPDSDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF     50
    EWDLKGIPLD QSSELLVVVK DHETMGRNRF LGEAKIPLQE VLATPSLSAS 100
    FNAPLLDAKQ QPTGASLVLQ VSYTPPPGAV PLFPPPASLA PSPTLPDMDL 150
    VPDTGGEEDT EDQGLTGDEA EPFLDQSAAV GPGGPTTPRK PPSHPPPHYP 200
    GAKRKRSSAP PRKLLSDKPQ DFQIRVQVIE GRQLPGVNIK PVVKVTAAGQ 250
    TKRTRIQKGN SPLFNETLFF NVFDSPLELF DEPIFITVVD SRSLRTDALL 300
    GEFRMDVGTV YREPRHAYLR KWLLLSDPDD FSAGARGYLK ASLCVLGPGD 350
    EAPLDKKDPS EDKEDIEGNL LRPTGVALRG AHFCLKLFRA EDLPQMDDAV 400
    MDNVKQIFGF DSNKKNLVDP FVEVSFAGKM LCSKILEKTA NPQWNQNITL 450
    PAMFPSMCEK MRIRVMDWDR LTHNDTVATT YLGMSKISAT GGEIEEEPAG 500
    VLKSPQATDL DDNLGFLPTF GPCYVNLYGS PREFTGFPDP YAELNTGKGE 550
    GVAYRGRVLL SLETKLVEHS EQKVEDLPAD DILRVEKYLR RRKYSLFAAF 600
    YSATMLQDVD DAIQFEVSIG NYGNKFDTTC LPLASTTQYS RAVFDGGSLP 650
    LPVGCHYYYL PWGNVKPVVV LSSYWEDISH RIEIQNQLLR VADRLEANLE 700
    QVHLALKAQC SSEDVDALVA QLTDELLADC SQPLCDIHEI PSATHLDQYL 750
    LRLRTRHLSQ IKEAALALKL GHSELSTALE QAEDWLLHLR ALAEEPQNSL 800
    PDIIIWMLQG DKRVAYQRVP AHEVLFSRRG PSYCGRNCGK LQTIFLKYPM 850
    EGMPGARMPV QIRIKLWFGL SVDEKEFNQF AEGKLSVFAE TYENQTKLAL 900
    VGNWGTTGLT YPKFSDVTGK IKLPKDSFRP SAGWAWAGDW FVCPEKTLLH 950
    DADAGHLSFV EEVFENQTRL PGGQWIYMSD NYTDVNGEKV LPKDDIECPL 1000
    GWKWEDEEWS TDLNRAVDEQ GWEYSITIPP DRKPKHWVPV EKMYYTHRRR 1050
    RWVRLRRRDL SQMEALKRHR QAEAEGEGWE YASLFGWKFH LEYRKTDAFR 1100
    RRRWRRRMEP LEKTGPAAVF ALEGALGGMV DDKSEDSMSV STLSFGVNRP 1150
    TISCIFDYGN RYHLRCYLYQ ARDLPAMDKD SFSDPYAIVS FLHQSQKTVV 1200
    EKNTLNPTWD QTLIFYEIEI FGEPASIAEH PPCIVVELYD HDTYGADEFM 1250
    GRCICQPSLE RMPRLAWFPL TRGSQPAGEL LAAFELIQRE KPAIHHIPGF 1300
    EMHETSRILD ETEDTDLPYP PPQREANIYM VPQNIKPALQ RTAIEILAWG 1350
    LRNMKSYQMA SISSPSLVVE CGGQTVQSCV IRNLRKNPNF DVCTLFMEVM 1400
    LPREDLYCPP IVVKVIDNRQ FGRRPVVGQC TIRSLENFLC DPYSAESPSP 1450
    QGGPDDVSLL SPGEDVLIDI DDKEPLIPVQ EEEFIDWWSK FFASVGEREK 1500
    CGSYLEKDFD TLKVYDTQLE NVEAFGGLSD FCNTFKLYRG RTQEETDDPS 1550
    VIGEFKGLFK IYPLPEDPAI PMPPRQFHQL AAQGPQECLV RIYIVRAFGL 1600
    QPKDPNGKCD PYIKISIGKK SVSDQDNYIP CTLEPVFGKM FELTCTLPLE 1650
    KDLKITLYDY DLLSKDEKIG ETVIDLENRL LSKFGARCGL PQTYCVSGPN 1700
    QWRDQLRPSQ LLHLFCQQHR IKAPVYRTDR VTFQDKDYTI EEIEAGRLPN 1750
    PHLGPVEERL ALHVLQQQGL VPEHVESRPL YSPLQPDIEQ GKLQMWIDIF 1800
    PKVLGRPGPP FNITPRKARR FFLRCIIWNT KDVILDDLSL TGEKMSDIYV 1850
    KGWMVGFEEH KQKTDVHYRS LGGEGNFNWR FVFPFDYLPA EQVCAVAKKD 1900
    AFWRLDKTES KIPARVVFQI WDNDKFSFDD FLGSLQLDLN RMPKPAKTAE 1950
    KCSLDQLDDT FHPEWFVSLF EQKTVKGWWP CVTEEGEKKM LAGKLEMTLE 2000
    IVAESEHEER PAGQGRDEPN MNPKLEDPRR PDTSFLWFTS PYKTMKFILW 2050
    RRFRCAIILF IILFILLLFL GVFVYAFPNY AAMKLVKPFR 2090
    Length:2,090
    Mass (Da):237,911
    Last modified:December 16, 2008 - v3
    Checksum:i0EBD1E2353946143
    GO
    Isoform 2 (identifier: Q9ESD7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: MLRVFILFAENVHTPDSDISDAYCSAVFA → MLCCLLARASNLPNVKKDRRSDPVASLIFR
         152-152: P → PGGGQSRAETWSLLSDSTMDTRYSGKKWPVPT
         496-510: EEPAGVLKSPQATDL → V
         647-654: Missing.

    Show »
    Length:2,100
    Mass (Da):239,289
    Checksum:i3C8A7837C2F78273
    GO
    Isoform 3 (identifier: Q9ESD7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: MLRVFILFAENVHTPDSDISDAYCSAVFA → MLCCLLARASNLPNVKKDRRSDPVASLIFR
         496-510: EEPAGVLKSPQATDL → V
         647-654: Missing.

    Show »
    Length:2,069
    Mass (Da):235,908
    Checksum:iBA9E838D870C6396
    GO

    Sequence cautioni

    The sequence CAB63111.1 differs from that shown. Reason: The sequence differs significantly from amino acid position 1855.
    The sequence BAD21394.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti467 – 4671D → G in CAB63111. (PubMed:10508505)Curated
    Sequence conflicti476 – 4761T → I in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti510 – 5101L → V in CAB63111. (PubMed:10508505)Curated
    Sequence conflicti684 – 6841I → T in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti690 – 6912RV → GI in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti698 – 6981N → G in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti712 – 7121S → T in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti717 – 7171A → S in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti727 – 7271L → I in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti885 – 8851L → F in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti909 – 9102LT → FS in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti931 – 9311S → T in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti953 – 9531D → A in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti1175 – 11751P → A in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti1187 – 11871A → S in CAB63111. (PubMed:10508505)Curated
    Sequence conflicti1694 – 16941Y → C in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti1701 – 17011Q → K in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti1705 – 17051Q → K in AAG17046. (PubMed:11234777)Curated
    Sequence conflicti1806 – 18061R → Q in AAG17046. (PubMed:11234777)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2929MLRVF…SAVFA → MLCCLLARASNLPNVKKDRR SDPVASLIFR in isoform 2 and isoform 3. 2 PublicationsVSP_035930Add
    BLAST
    Alternative sequencei152 – 1521P → PGGGQSRAETWSLLSDSTMD TRYSGKKWPVPT in isoform 2. 1 PublicationVSP_035931
    Alternative sequencei496 – 51015EEPAG…QATDL → V in isoform 2 and isoform 3. 2 PublicationsVSP_035932Add
    BLAST
    Alternative sequencei647 – 6548Missing in isoform 2 and isoform 3. 2 PublicationsVSP_035933

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF188290 mRNA. Translation: AAG17046.2.
    AK131144 mRNA. Translation: BAD21394.1. Different initiation.
    AC153607 Genomic DNA. No translation available.
    AC153608 Genomic DNA. No translation available.
    AJ242954 mRNA. Translation: CAB63111.1. Sequence problems.
    BC043692 mRNA. Translation: AAH43692.1.
    CCDSiCCDS39536.1. [Q9ESD7-2]
    RefSeqiNP_001071162.1. NM_001077694.2.
    NP_067444.2. NM_021469.3. [Q9ESD7-2]
    XP_006506243.1. XM_006506180.1. [Q9ESD7-3]
    UniGeneiMm.220982.

    Genome annotation databases

    EnsembliENSMUST00000081904; ENSMUSP00000080579; ENSMUSG00000033788. [Q9ESD7-2]
    ENSMUST00000113818; ENSMUSP00000109449; ENSMUSG00000033788. [Q9ESD7-3]
    ENSMUST00000168387; ENSMUSP00000132297; ENSMUSG00000033788. [Q9ESD7-1]
    GeneIDi26903.
    KEGGimmu:26903.
    UCSCiuc009cos.2. mouse. [Q9ESD7-3]
    uc009cot.1. mouse. [Q9ESD7-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF188290 mRNA. Translation: AAG17046.2 .
    AK131144 mRNA. Translation: BAD21394.1 . Different initiation.
    AC153607 Genomic DNA. No translation available.
    AC153608 Genomic DNA. No translation available.
    AJ242954 mRNA. Translation: CAB63111.1 . Sequence problems.
    BC043692 mRNA. Translation: AAH43692.1 .
    CCDSi CCDS39536.1. [Q9ESD7-2 ]
    RefSeqi NP_001071162.1. NM_001077694.2.
    NP_067444.2. NM_021469.3. [Q9ESD7-2 ]
    XP_006506243.1. XM_006506180.1. [Q9ESD7-3 ]
    UniGenei Mm.220982.

    3D structure databases

    ProteinModelPortali Q9ESD7.
    SMRi Q9ESD7. Positions 1-124, 223-489, 883-945, 953-1061, 1074-1110, 1156-1275, 1584-1675.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 205052. 2 interactions.
    IntActi Q9ESD7. 4 interactions.
    MINTi MINT-4998243.

    PTM databases

    PhosphoSitei Q9ESD7.

    Proteomic databases

    MaxQBi Q9ESD7.
    PaxDbi Q9ESD7.
    PRIDEi Q9ESD7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000081904 ; ENSMUSP00000080579 ; ENSMUSG00000033788 . [Q9ESD7-2 ]
    ENSMUST00000113818 ; ENSMUSP00000109449 ; ENSMUSG00000033788 . [Q9ESD7-3 ]
    ENSMUST00000168387 ; ENSMUSP00000132297 ; ENSMUSG00000033788 . [Q9ESD7-1 ]
    GeneIDi 26903.
    KEGGi mmu:26903.
    UCSCi uc009cos.2. mouse. [Q9ESD7-3 ]
    uc009cot.1. mouse. [Q9ESD7-2 ]

    Organism-specific databases

    CTDi 8291.
    MGIi MGI:1349385. Dysf.

    Phylogenomic databases

    eggNOGi NOG330124.
    GeneTreei ENSGT00550000074414.
    HOGENOMi HOG000006771.
    HOVERGENi HBG018972.
    InParanoidi Q6KAR3.
    KOi K18261.
    OMAi QVHLALK.
    TreeFami TF316871.

    Miscellaneous databases

    NextBioi 304757.
    PROi Q9ESD7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ESD7.
    Bgeei Q9ESD7.
    CleanExi MM_DYSF.
    Genevestigatori Q9ESD7.

    Family and domain databases

    Gene3Di 2.60.40.150. 8 hits.
    InterProi IPR000008. C2_dom.
    IPR012968. FerIin-domain.
    IPR012560. Ferlin_A-domain.
    IPR012561. Ferlin_B-domain.
    IPR010482. Peroxin/Dysferlin.
    IPR006614. Peroxin/Ferlin.
    [Graphical view ]
    Pfami PF00168. C2. 7 hits.
    PF08165. FerA. 1 hit.
    PF08150. FerB. 1 hit.
    PF08151. FerI. 1 hit.
    PF06398. Pex24p. 1 hit.
    [Graphical view ]
    SMARTi SM00239. C2. 7 hits.
    SM00694. DysFC. 2 hits.
    SM00693. DysFN. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 7 hits.
    PROSITEi PS50004. C2. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the mouse dysferlin gene and genomic characterization of the SJL-Dysf mutation."
      Vafiadaki E., Reis A., Keers S., Harrison R., Anderson L.V.B., Raffelsberger T., Ivanova S., Hoeger H., Bittner R.E., Bushby K.M.D., Bashir R.
      NeuroReport 12:625-629(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
      Strain: BALB/c, C57BL/10 and SJL/J.
      Tissue: Skeletal muscle.
    2. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
      DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Thymus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 467-1854 (ISOFORMS 1/2).
      Strain: B6C3FE, BALB/c, C3H, C57BL/10 and C57BL/6.
      Tissue: Muscle.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1490-2090 (ISOFORMS 1/2/3).
      Tissue: Mammary tumor.
    6. "Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing."
      Lennon N.J., Kho A., Bacskai B.J., Perlmutter S.L., Hyman B.T., Brown R.H. Jr.
      J. Biol. Chem. 278:50466-50473(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ANXA1 AND ANXA2, SUBCELLULAR LOCATION.
    7. "Defective membrane repair in dysferlin-deficient muscular dystrophy."
      Bansal D., Miyake K., Vogel S.S., Groh S., Chen C.C., Williamson R., McNeil P.L., Campbell K.P.
      Nature 423:168-172(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "Intracellular localization of dysferlin and its association with the dihydropyridine receptor."
      Ampong B.N., Imamura M., Matsumiya T., Yoshida M., Takeda S.
      Acta Myol. 24:134-144(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CACNA1S, SUBCELLULAR LOCATION.
    9. "Dysferlin interacts with affixin (beta-parvin) at the sarcolemma."
      Matsuda C., Kameyama K., Tagawa K., Ogawa M., Suzuki A., Yamaji S., Okamoto H., Nishino I., Hayashi Y.K.
      J. Neuropathol. Exp. Neurol. 64:334-340(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARVB.
    10. "Dysferlin-mediated membrane repair protects the heart from stress-induced left ventricular injury."
      Han R., Bansal D., Miyake K., Muniz V.P., Weiss R.M., McNeil P.L., Campbell K.P.
      J. Clin. Invest. 117:1805-1813(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Caveolin regulates endocytosis of the muscle repair protein, dysferlin."
      Hernandez-Deviez D.J., Howes M.T., Laval S.H., Bushby K., Hancock J.F., Parton R.G.
      J. Biol. Chem. 283:6476-6488(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin."
      Cai C., Weisleder N., Ko J.-K., Komazaki S., Sunada Y., Nishi M., Takeshima H., Ma J.
      J. Biol. Chem. 284:15894-15902(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM72.

    Entry informationi

    Entry nameiDYSF_MOUSE
    AccessioniPrimary (citable) accession number: Q9ESD7
    Secondary accession number(s): Q6KAR3, Q80VT0, Q9QXC0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 120 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Mice lacking Dysf maintain a functional dystrophin glycoprotein complex (DGC) but their muscle cells are defective in repairing the plasma membrane disruptions and accumulates vesicles at the sarcolemma. They develop a progressive muscular dystrophy and cardiomyopathy.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3