Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9ESD7

- DYSF_MOUSE

UniProt

Q9ESD7 - DYSF_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dysferlin

Gene

Dysf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

GO - Biological processi

  1. plasma membrane repair Source: UniProtKB
  2. vesicle fusion Source: UniProtKB
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 20562056CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei2057 – 207721HelicalSequence AnalysisAdd
BLAST
Topological domaini2078 – 209013ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasmic vesicle Source: UniProtKB
  2. extracellular vesicular exosome Source: Ensembl
  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
Complete GO annotation...

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

BgeeiQ9ESD7.
CleanExiMM_DYSF.
ExpressionAtlasiQ9ESD7. baseline and differential.
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, 218-329, 953-1061, 1162-1251, 1584-1675.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ9ESD7.
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

        10         20         30         40         50
MLRVFILFAE NVHTPDSDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF
60 70 80 90 100
EWDLKGIPLD QSSELLVVVK DHETMGRNRF LGEAKIPLQE VLATPSLSAS
110 120 130 140 150
FNAPLLDAKQ QPTGASLVLQ VSYTPPPGAV PLFPPPASLA PSPTLPDMDL
160 170 180 190 200
VPDTGGEEDT EDQGLTGDEA EPFLDQSAAV GPGGPTTPRK PPSHPPPHYP
210 220 230 240 250
GAKRKRSSAP PRKLLSDKPQ DFQIRVQVIE GRQLPGVNIK PVVKVTAAGQ
260 270 280 290 300
TKRTRIQKGN SPLFNETLFF NVFDSPLELF DEPIFITVVD SRSLRTDALL
310 320 330 340 350
GEFRMDVGTV YREPRHAYLR KWLLLSDPDD FSAGARGYLK ASLCVLGPGD
360 370 380 390 400
EAPLDKKDPS EDKEDIEGNL LRPTGVALRG AHFCLKLFRA EDLPQMDDAV
410 420 430 440 450
MDNVKQIFGF DSNKKNLVDP FVEVSFAGKM LCSKILEKTA NPQWNQNITL
460 470 480 490 500
PAMFPSMCEK MRIRVMDWDR LTHNDTVATT YLGMSKISAT GGEIEEEPAG
510 520 530 540 550
VLKSPQATDL DDNLGFLPTF GPCYVNLYGS PREFTGFPDP YAELNTGKGE
560 570 580 590 600
GVAYRGRVLL SLETKLVEHS EQKVEDLPAD DILRVEKYLR RRKYSLFAAF
610 620 630 640 650
YSATMLQDVD DAIQFEVSIG NYGNKFDTTC LPLASTTQYS RAVFDGGSLP
660 670 680 690 700
LPVGCHYYYL PWGNVKPVVV LSSYWEDISH RIEIQNQLLR VADRLEANLE
710 720 730 740 750
QVHLALKAQC SSEDVDALVA QLTDELLADC SQPLCDIHEI PSATHLDQYL
760 770 780 790 800
LRLRTRHLSQ IKEAALALKL GHSELSTALE QAEDWLLHLR ALAEEPQNSL
810 820 830 840 850
PDIIIWMLQG DKRVAYQRVP AHEVLFSRRG PSYCGRNCGK LQTIFLKYPM
860 870 880 890 900
EGMPGARMPV QIRIKLWFGL SVDEKEFNQF AEGKLSVFAE TYENQTKLAL
910 920 930 940 950
VGNWGTTGLT YPKFSDVTGK IKLPKDSFRP SAGWAWAGDW FVCPEKTLLH
960 970 980 990 1000
DADAGHLSFV EEVFENQTRL PGGQWIYMSD NYTDVNGEKV LPKDDIECPL
1010 1020 1030 1040 1050
GWKWEDEEWS TDLNRAVDEQ GWEYSITIPP DRKPKHWVPV EKMYYTHRRR
1060 1070 1080 1090 1100
RWVRLRRRDL SQMEALKRHR QAEAEGEGWE YASLFGWKFH LEYRKTDAFR
1110 1120 1130 1140 1150
RRRWRRRMEP LEKTGPAAVF ALEGALGGMV DDKSEDSMSV STLSFGVNRP
1160 1170 1180 1190 1200
TISCIFDYGN RYHLRCYLYQ ARDLPAMDKD SFSDPYAIVS FLHQSQKTVV
1210 1220 1230 1240 1250
EKNTLNPTWD QTLIFYEIEI FGEPASIAEH PPCIVVELYD HDTYGADEFM
1260 1270 1280 1290 1300
GRCICQPSLE RMPRLAWFPL TRGSQPAGEL LAAFELIQRE KPAIHHIPGF
1310 1320 1330 1340 1350
EMHETSRILD ETEDTDLPYP PPQREANIYM VPQNIKPALQ RTAIEILAWG
1360 1370 1380 1390 1400
LRNMKSYQMA SISSPSLVVE CGGQTVQSCV IRNLRKNPNF DVCTLFMEVM
1410 1420 1430 1440 1450
LPREDLYCPP IVVKVIDNRQ FGRRPVVGQC TIRSLENFLC DPYSAESPSP
1460 1470 1480 1490 1500
QGGPDDVSLL SPGEDVLIDI DDKEPLIPVQ EEEFIDWWSK FFASVGEREK
1510 1520 1530 1540 1550
CGSYLEKDFD TLKVYDTQLE NVEAFGGLSD FCNTFKLYRG RTQEETDDPS
1560 1570 1580 1590 1600
VIGEFKGLFK IYPLPEDPAI PMPPRQFHQL AAQGPQECLV RIYIVRAFGL
1610 1620 1630 1640 1650
QPKDPNGKCD PYIKISIGKK SVSDQDNYIP CTLEPVFGKM FELTCTLPLE
1660 1670 1680 1690 1700
KDLKITLYDY DLLSKDEKIG ETVIDLENRL LSKFGARCGL PQTYCVSGPN
1710 1720 1730 1740 1750
QWRDQLRPSQ LLHLFCQQHR IKAPVYRTDR VTFQDKDYTI EEIEAGRLPN
1760 1770 1780 1790 1800
PHLGPVEERL ALHVLQQQGL VPEHVESRPL YSPLQPDIEQ GKLQMWIDIF
1810 1820 1830 1840 1850
PKVLGRPGPP FNITPRKARR FFLRCIIWNT KDVILDDLSL TGEKMSDIYV
1860 1870 1880 1890 1900
KGWMVGFEEH KQKTDVHYRS LGGEGNFNWR FVFPFDYLPA EQVCAVAKKD
1910 1920 1930 1940 1950
AFWRLDKTES KIPARVVFQI WDNDKFSFDD FLGSLQLDLN RMPKPAKTAE
1960 1970 1980 1990 2000
KCSLDQLDDT FHPEWFVSLF EQKTVKGWWP CVTEEGEKKM LAGKLEMTLE
2010 2020 2030 2040 2050
IVAESEHEER PAGQGRDEPN MNPKLEDPRR PDTSFLWFTS PYKTMKFILW
2060 2070 2080 2090
RRFRCAIILF IILFILLLFL GVFVYAFPNY AAMKLVKPFR
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 BAD21394.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB63111.1 differs from that shown. Reason: The sequence differs significantly from amino acid position 1855.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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, 218-329, 953-1061, 1162-1251, 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 Q9ESD7.
KOi K18261.
OMAi QVHLALK.
TreeFami TF316871.

Miscellaneous databases

NextBioi 304757.
PROi Q9ESD7.
SOURCEi Search...

Gene expression databases

Bgeei Q9ESD7.
CleanExi MM_DYSF.
ExpressionAtlasi Q9ESD7. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 122 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