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Protein

Dysferlin

Gene

DYSF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi18Calcium1 Publication1
Metal bindingi19Calcium; via carbonyl oxygen1 Publication1
Metal bindingi21Calcium1 Publication1
Metal bindingi40Calcium1 Publication1

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • phospholipid binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Lipid-binding, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000135636-MONOMER.
ReactomeiR-HSA-445355. Smooth Muscle Contraction.
SIGNORiO75923.

Protein family/group databases

TCDBi1.F.1.2.1. the synaptosomal vesicle fusion pore (svf-pore) family.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3097. DYSF.

Subcellular locationi

  • Cell membranesarcolemma; Single-pass type II membrane protein
  • Cytoplasmic vesicle membrane By similarity; Single-pass type II membrane protein By similarity
  • Cell membrane

  • 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. 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. Colocalizes with AHNAK, AHNAK2 and PARVB at the sarcolemma of skeletal muscle. Detected on the apical plasma membrane of the syncytiotrophoblast. Reaches the plasmma membrane through a caveolin-independent mechanism. Retained by caveolin at the plasmma membrane (By similarity). Colocalizes, during muscle differentiation, with CACNA1S in the T-tubule system of myotubules (By similarity). Accumulates and colocalizes with fusion vesicles at the sarcolemma disruption sites (By similarity).By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 2046CytoplasmicSequence analysisAdd BLAST2046
Transmembranei2047 – 2067HelicalSequence analysisAdd BLAST21
Topological domaini2068 – 2080ExtracellularSequence analysisAdd BLAST13

GO - Cellular componenti

  • cytoplasmic vesicle membrane Source: Reactome
  • early endosome Source: UniProtKB
  • endocytic vesicle Source: UniProtKB
  • endosome Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • lamellipodium Source: Ensembl
  • late endosome Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • sarcolemma Source: UniProtKB
  • T-tubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Involvement in diseasei

Limb-girdle muscular dystrophy 2B (LGMD2B)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive degenerative myopathy characterized by weakness and atrophy starting in the proximal pelvifemoral muscles, with onset in the late teens or later, massive elevation of serum creatine kinase levels and slow progression. Scapular muscle involvement is minor and not present at onset. Upper limb girdle involvement follows some years after the onset in lower limbs.
See also OMIM:253601
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05783452W → R in LGMD2B. 1 Publication1
Natural variantiVAR_05783567V → D in MMD1 and LGMD2B; Reduces calcium-sensitive phospholipid binding and interaction with AHNAK and AHNAK2. 2 PublicationsCorresponds to variant rs121908957dbSNPEnsembl.1
Natural variantiVAR_057837155G → R in LGMD2B. 1 PublicationCorresponds to variant rs200970855dbSNPEnsembl.1
Natural variantiVAR_024853170A → E in MMD1 and LGMD2B; also found in patients with isolated hyperCKemia. 3 PublicationsCorresponds to variant rs34999029dbSNPEnsembl.1
Natural variantiVAR_057838234G → E in LGMD2B. 1 PublicationCorresponds to variant rs141497053dbSNPEnsembl.1
Natural variantiVAR_057839284I → T in LGMD2B. 1 Publication1
Natural variantiVAR_057840299G → R in LGMD2B and proximodistal myopathy. 3 PublicationsCorresponds to variant rs121908963dbSNPEnsembl.1
Natural variantiVAR_024859555R → W in LGMD2B and MMD1; also found in patients with isolated hyperCKemia. 2 PublicationsCorresponds to variant rs377735262dbSNPEnsembl.1
Natural variantiVAR_057851618G → R in MMD1 and LGMD2B. 2 PublicationsCorresponds to variant rs201049092dbSNPEnsembl.1
Natural variantiVAR_057852621G → R in LGMD2B. 1 Publication1
Natural variantiVAR_057853625D → Y in LGMD2B. 1 PublicationCorresponds to variant rs121908960dbSNPEnsembl.1
Natural variantiVAR_057854731P → R in LGMD2B. 1 Publication1
Natural variantiVAR_012308791P → R in MMD1 and LGMD2B. 2 PublicationsCorresponds to variant rs121908956dbSNPEnsembl.1
Natural variantiVAR_057856930W → C in LGMD2B; unknown pathological significance. 2 PublicationsCorresponds to variant rs727503910dbSNPEnsembl.1
Natural variantiVAR_024860959R → W in MMD1 and LGMD2B. 2 PublicationsCorresponds to variant rs202218890dbSNPEnsembl.1
Natural variantiVAR_0248611022R → Q in LGMD2B; unknown pathological significance. 3 PublicationsCorresponds to variant rs34211915dbSNPEnsembl.1
Natural variantiVAR_0248621038R → Q in LGMD2B; unknown pathological significance. 3 PublicationsCorresponds to variant rs150877497dbSNPEnsembl.1
Natural variantiVAR_0248651208I → M in LGMD2B. 1 PublicationCorresponds to variant rs148858485dbSNPEnsembl.1
Natural variantiVAR_0578601228L → P in LGMD2B. 1 Publication1
Natural variantiVAR_0123091298I → V in MMD1 and LGMD2B. 1 PublicationCorresponds to variant rs121908954dbSNPEnsembl.1
Natural variantiVAR_0248681335E → K in MMD1 and LGMD2B. 3 PublicationsCorresponds to variant rs758993965dbSNPEnsembl.1
Natural variantiVAR_0578621341L → P in LGMD2B. 1 PublicationCorresponds to variant rs757917335dbSNPEnsembl.1
Natural variantiVAR_0578641505Y → C in LGMD2B. 1 PublicationCorresponds to variant rs757820496dbSNPEnsembl.1
Natural variantiVAR_0578651526K → T in LGMD2B. 1 PublicationCorresponds to variant rs76086153dbSNPEnsembl.1
Natural variantiVAR_0578661543G → D in LGMD2B. 1 Publication1
Natural variantiVAR_0578721734E → G in LGMD2B. 1 PublicationCorresponds to variant rs121908961dbSNPEnsembl.1
Natural variantiVAR_0578731768R → W in LGMD2B and proximodistal myopathy; unknown pathological significance. 2 PublicationsCorresponds to variant rs746243052dbSNPEnsembl.1
Natural variantiVAR_0578801970P → S in LGMD2B. 1 Publication1
Natural variantiVAR_0123112042R → C in MMD1, LGMD2B and proximodistal myopathy. 4 PublicationsCorresponds to variant rs121908955dbSNPEnsembl.1
Miyoshi muscular dystrophy 1 (MMD1)15 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA late-onset muscular dystrophy involving the distal lower limb musculature. It is characterized by weakness that initially affects the gastrocnemius muscle during early adulthood.
See also OMIM:254130
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05783567V → D in MMD1 and LGMD2B; Reduces calcium-sensitive phospholipid binding and interaction with AHNAK and AHNAK2. 2 PublicationsCorresponds to variant rs121908957dbSNPEnsembl.1
Natural variantiVAR_024853170A → E in MMD1 and LGMD2B; also found in patients with isolated hyperCKemia. 3 PublicationsCorresponds to variant rs34999029dbSNPEnsembl.1
Natural variantiVAR_024857299G → E in MMD1. 2 Publications1
Natural variantiVAR_057841299G → W in MMD1. 1 PublicationCorresponds to variant rs121908963dbSNPEnsembl.1
Natural variantiVAR_057844374V → L in MMD1; unknown pathological significance. 2 PublicationsCorresponds to variant rs150724610dbSNPEnsembl.1
Natural variantiVAR_057845386 – 390FRAED → Y in MMD1. 1 Publication5
Natural variantiVAR_057846389E → Q in MMD1. 1 Publication1
Natural variantiVAR_057848426G → R in MMD1. 1 Publication1
Natural variantiVAR_057849426G → V in MMD1. 1 Publication1
Natural variantiVAR_024858456C → W in MMD1. 2 Publications1
Natural variantiVAR_057850519G → R in MMD1. 1 PublicationCorresponds to variant rs121908962dbSNPEnsembl.1
Natural variantiVAR_024859555R → W in LGMD2B and MMD1; also found in patients with isolated hyperCKemia. 2 PublicationsCorresponds to variant rs377735262dbSNPEnsembl.1
Natural variantiVAR_057851618G → R in MMD1 and LGMD2B. 2 PublicationsCorresponds to variant rs201049092dbSNPEnsembl.1
Natural variantiVAR_012308791P → R in MMD1 and LGMD2B. 2 PublicationsCorresponds to variant rs121908956dbSNPEnsembl.1
Natural variantiVAR_024860959R → W in MMD1 and LGMD2B. 2 PublicationsCorresponds to variant rs202218890dbSNPEnsembl.1
Natural variantiVAR_057857999W → C in MMD1. 2 PublicationsCorresponds to variant rs28937581dbSNPEnsembl.1
Natural variantiVAR_0578581029P → L in MMD1. 1 Publication1
Natural variantiVAR_0578591041R → C in MMD1. 1 PublicationCorresponds to variant rs144598063dbSNPEnsembl.1
Natural variantiVAR_0248631046R → H in MMD1; dbNP:28939700. 3 PublicationsCorresponds to variant rs28939700dbSNPEnsembl.1
Natural variantiVAR_0123091298I → V in MMD1 and LGMD2B. 1 PublicationCorresponds to variant rs121908954dbSNPEnsembl.1
Natural variantiVAR_0248681335E → K in MMD1 and LGMD2B. 3 PublicationsCorresponds to variant rs758993965dbSNPEnsembl.1
Natural variantiVAR_0578631361C → R in MMD1. 1 PublicationCorresponds to variant rs776472879dbSNPEnsembl.1
Natural variantiVAR_0578681662T → R in MMD1. 1 Publication1
Natural variantiVAR_0578701679G → E in MMD1. 1 Publication1
Natural variantiVAR_0248701693R → Q in MMD1. 2 PublicationsCorresponds to variant rs779987458dbSNPEnsembl.1
Natural variantiVAR_0578711693R → W in MMD1. 1 Publication1
Natural variantiVAR_0578741837D → N in MMD1. 2 PublicationsCorresponds to variant rs398123794dbSNPEnsembl.1
Natural variantiVAR_0578751842G → D in MMD1. 1 Publication1
Natural variantiVAR_0123101857H → R in MMD1. 1 PublicationCorresponds to variant rs199601326dbSNPEnsembl.1
Natural variantiVAR_0578761922L → P in MMD1. 1 Publication1
Natural variantiVAR_0578771938 – 1939Missing in MMD1. 1 Publication2
Natural variantiVAR_0578781942C → G in MMD1. 1 Publication1
Natural variantiVAR_0248722000R → Q in MMD1. 1 PublicationCorresponds to variant rs115407852dbSNPEnsembl.1
Natural variantiVAR_0123112042R → C in MMD1, LGMD2B and proximodistal myopathy. 4 PublicationsCorresponds to variant rs121908955dbSNPEnsembl.1
Natural variantiVAR_0578812068P → L in MMD1. 1 PublicationCorresponds to variant rs149732545dbSNPEnsembl.1
Distal myopathy with anterior tibial onset (DMAT)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionOnset of the disorder is between 14 and 28 years of age and the anterior tibial muscles are the first muscle group to be involved. Inheritance is autosomal recessive.
See also OMIM:606768

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16D → A: Fails to bind calcium. 1 Publication1
Mutagenesisi21D → A: Fails to bind calcium. 1 Publication1
Mutagenesisi71D → A: Fails to bind calcium. 1 Publication1
Mutagenesisi79R → D: Moderately increased calcium affinity. 1 Publication1
Mutagenesisi80F → A: Reduced calcium affinity. 1 Publication1

Keywords - Diseasei

Disease mutation, Limb-girdle muscular dystrophy

Organism-specific databases

DisGeNETi8291.
MalaCardsiDYSF.
MIMi253601. phenotype.
254130. phenotype.
606768. phenotype.
OpenTargetsiENSG00000135636.
Orphaneti268. Autosomal recessive limb-girdle muscular dystrophy type 2B.
199329. Congenital myopathy, Paradas type.
178400. Distal myopathy with anterior tibial onset.
45448. Miyoshi myopathy.
PharmGKBiPA27554.

Polymorphism and mutation databases

BioMutaiDYSF.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000578791 – 2080DysferlinAdd BLAST2080

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei166PhosphothreonineCombined sources1
Isoform 2 (identifier: O75923-2)
Modified residuei166PhosphoserineCombined sources1
Modified residuei197PhosphothreonineCombined sources1
Isoform 5 (identifier: O75923-5)
Modified residuei166PhosphoserineCombined sources1
Modified residuei197PhosphothreonineCombined sources1
Isoform 7 (identifier: O75923-7)
Modified residuei166PhosphoserineCombined sources1
Modified residuei197PhosphothreonineCombined sources1
Isoform 8 (identifier: O75923-8)
Modified residuei167PhosphoserineCombined sources1
Modified residuei198PhosphothreonineCombined sources1
Isoform 11 (identifier: O75923-11)
Modified residuei167PhosphoserineCombined sources1
Modified residuei198PhosphothreonineCombined sources1
Isoform 13 (identifier: O75923-13)
Modified residuei167PhosphoserineCombined sources1
Modified residuei198PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO75923.
MaxQBiO75923.
PaxDbiO75923.
PeptideAtlasiO75923.
PRIDEiO75923.

PTM databases

iPTMnetiO75923.
PhosphoSitePlusiO75923.

Expressioni

Tissue specificityi

Expressed in skeletal muscle, myoblast, myotube and in the syncytiotrophoblast (STB) of the placenta (at protein level). Ubiquitous. Highly expressed in skeletal muscle. Also found in heart, brain, spleen, intestine, placenta and at lower levels in liver, lung, kidney and pancreas.9 Publications

Developmental stagei

Expression in limb tissue from 5-6 weeks embryos; persists throughout development.1 Publication

Gene expression databases

BgeeiENSG00000135636.
GenevisibleiO75923. HS.

Organism-specific databases

HPAiCAB002510.
HPA017071.
HPA021945.

Interactioni

Subunit structurei

Interacts with CACNA1S. 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 similarity). Interacts with CAV3 and PARVB. Interacts with AHNAK; the interaction is direct and Ca2+-independent. Interacts with AHNAK2; the interaction is direct and Ca2+-independent.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTN2P356092EBI-2799016,EBI-77797
ALMS1Q8TCU43EBI-2799016,EBI-308651
APPL1Q9UKG12EBI-2799016,EBI-741243
CMYA5Q8N3K93EBI-2799016,EBI-2323272
DESP176613EBI-2799016,EBI-1055572
DGKDQ167603EBI-2799016,EBI-719333
DNAJB6O751902EBI-2799016,EBI-1053164
FLNCQ143153EBI-2799016,EBI-489954
MYBPC1Q008724EBI-2799016,EBI-5652924
MYOM1P521793EBI-2799016,EBI-5353249
MYOM2P542963EBI-2799016,EBI-5357134
NEBP209296EBI-2799016,EBI-1049657
OPTNQ96CV93EBI-2799016,EBI-748974
SAMHD1Q9Y3Z32EBI-2799016,EBI-1054601
SGCGQ133263EBI-2799016,EBI-5357343
SNAPINO952953EBI-2799016,EBI-296723
TTNQ8WZ4217EBI-2799016,EBI-681210

Protein-protein interaction databases

BioGridi113896. 10 interactors.
IntActiO75923. 50 interactors.
STRINGi9606.ENSP00000386881.

Structurei

Secondary structure

12080
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 11Combined sources11
Beta strandi22 – 28Combined sources7
Beta strandi31 – 34Combined sources4
Beta strandi45 – 53Combined sources9
Beta strandi64 – 71Combined sources8
Beta strandi74 – 76Combined sources3
Beta strandi79 – 87Combined sources9
Helixi89 – 92Combined sources4
Beta strandi98 – 106Combined sources9
Beta strandi112 – 123Combined sources12
Beta strandi946 – 958Combined sources13
Beta strandi966 – 973Combined sources8
Helixi983 – 985Combined sources3
Beta strandi996 – 998Combined sources3
Beta strandi1000 – 1002Combined sources3
Beta strandi1011 – 1015Combined sources5
Beta strandi1021 – 1023Combined sources3
Beta strandi1028 – 1030Combined sources3
Beta strandi1037 – 1049Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CAHX-ray1.90B942-1052[»]
4CAIX-ray2.20A/B/C942-1052[»]
4IHBX-ray2.04A/B/C/D/E/F1-124[»]
4IQHX-ray1.76A/B/C28-124[»]
ProteinModelPortaliO75923.
SMRiO75923.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 85C2 1PROSITE-ProRule annotationAdd BLAST85
Domaini207 – 302C2 2PROSITE-ProRule annotationAdd BLAST96
Domaini366 – 479C2 3PROSITE-ProRule annotationAdd BLAST114
Domaini1139 – 1244C2 4PROSITE-ProRule annotationAdd BLAST106
Domaini1336 – 1423C2 5PROSITE-ProRule annotationAdd BLAST88
Domaini1565 – 1663C2 6PROSITE-ProRule annotationAdd BLAST99
Domaini1813 – 1926C2 7PROSITE-ProRule annotationAdd BLAST114

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1038 – 1097Arg-richAdd BLAST60

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. The C2 domain 1 from isoform 14 does not bind calcium in the absence of bound phospholipid (PubMed:24239457, PubMed:24461013).2 Publications

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

eggNOGiKOG1326. Eukaryota.
ENOG410XPT2. LUCA.
GeneTreeiENSGT00550000074414.
HOVERGENiHBG018972.
InParanoidiO75923.
KOiK18261.
OMAiPIFITVV.
OrthoDBiEOG091G00N6.
PhylomeDBiO75923.
TreeFamiTF316871.

Family and domain databases

Gene3Di2.60.40.150. 8 hits.
InterProiIPR000008. C2_dom.
IPR012968. FerIin_dom.
IPR012560. Ferlin_A-domain.
IPR012561. Ferlin_B-domain.
IPR032362. Ferlin_C.
IPR006614. Peroxin/Ferlin.
[Graphical view]
PfamiPF00168. C2. 7 hits.
PF08165. FerA. 1 hit.
PF08150. FerB. 1 hit.
PF08151. FerI. 1 hit.
PF16165. Ferlin_C. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 7 hits.
SM00694. DysFC. 2 hits.
SM00693. DysFN. 2 hits.
SM01200. FerA. 1 hit.
SM01201. FerB. 1 hit.
SM01202. FerI. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 8 hits.
PROSITEiPS50004. C2. 5 hits.
[Graphical view]

Sequences (15)i

Sequence statusi: Complete.

This entry describes 15 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Note: Approximately 23% of the transcripts in skeletal muscle incorporate exon 1a from an alternative promoter and missing the calcium-binding sites of domain C2 1.
Isoform 1 (identifier: O75923-1) [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
MLRVFILYAE NVHTPDTDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF
60 70 80 90 100
EWDLKGIPLD QGSELHVVVK DHETMGRNRF LGEAKVPLRE VLATPSLSAS
110 120 130 140 150
FNAPLLDTKK QPTGASLVLQ VSYTPLPGAV PLFPPPTPLE PSPTLPDLDV
160 170 180 190 200
VADTGGEEDT EDQGLTGDEA EPFLDQSGGP GAPTTPRKLP SRPPPHYPGI
210 220 230 240 250
KRKRSAPTSR KLLSDKPQDF QIRVQVIEGR QLPGVNIKPV VKVTAAGQTK
260 270 280 290 300
RTRIHKGNSP LFNETLFFNL FDSPGELFDE PIFITVVDSR SLRTDALLGE
310 320 330 340 350
FRMDVGTIYR EPRHAYLRKW LLLSDPDDFS AGARGYLKTS LCVLGPGDEA
360 370 380 390 400
PLERKDPSED KEDIESNLLR PTGVALRGAH FCLKVFRAED LPQMDDAVMD
410 420 430 440 450
NVKQIFGFES NKKNLVDPFV EVSFAGKMLC SKILEKTANP QWNQNITLPA
460 470 480 490 500
MFPSMCEKMR IRIIDWDRLT HNDIVATTYL SMSKISAPGG EIEEEPAGAV
510 520 530 540 550
KPSKASDLDD YLGFLPTFGP CYINLYGSPR EFTGFPDPYT ELNTGKGEGV
560 570 580 590 600
AYRGRLLLSL ETKLVEHSEQ KVEDLPADDI LRVEKYLRRR KYSLFAAFYS
610 620 630 640 650
ATMLQDVDDA IQFEVSIGNY GNKFDMTCLP LASTTQYSRA VFDGCHYYYL
660 670 680 690 700
PWGNVKPVVV LSSYWEDISH RIETQNQLLG IADRLEAGLE QVHLALKAQC
710 720 730 740 750
STEDVDSLVA QLTDELIAGC SQPLGDIHET PSATHLDQYL YQLRTHHLSQ
760 770 780 790 800
ITEAALALKL GHSELPAALE QAEDWLLRLR ALAEEPQNSL PDIVIWMLQG
810 820 830 840 850
DKRVAYQRVP AHQVLFSRRG ANYCGKNCGK LQTIFLKYPM EKVPGARMPV
860 870 880 890 900
QIRVKLWFGL SVDEKEFNQF AEGKLSVFAE TYENETKLAL VGNWGTTGLT
910 920 930 940 950
YPKFSDVTGK IKLPKDSFRP SAGWTWAGDW FVCPEKTLLH DMDAGHLSFV
960 970 980 990 1000
EEVFENQTRL PGGQWIYMSD NYTDVNGEKV LPKDDIECPL GWKWEDEEWS
1010 1020 1030 1040 1050
TDLNRAVDEQ GWEYSITIPP ERKPKHWVPA EKMYYTHRRR RWVRLRRRDL
1060 1070 1080 1090 1100
SQMEALKRHR QAEAEGEGWE YASLFGWKFH LEYRKTDAFR RRRWRRRMEP
1110 1120 1130 1140 1150
LEKTGPAAVF ALEGALGGVM DDKSEDSMSV STLSFGVNRP TISCIFDYGN
1160 1170 1180 1190 1200
RYHLRCYMYQ ARDLAAMDKD SFSDPYAIVS FLHQSQKTVV VKNTLNPTWD
1210 1220 1230 1240 1250
QTLIFYEIEI FGEPATVAEQ PPSIVVELYD HDTYGADEFM GRCICQPSLE
1260 1270 1280 1290 1300
RMPRLAWFPL TRGSQPSGEL LASFELIQRE KPAIHHIPGF EVQETSRILD
1310 1320 1330 1340 1350
ESEDTDLPYP PPQREANIYM VPQNIKPALQ RTAIEILAWG LRNMKSYQLA
1360 1370 1380 1390 1400
NISSPSLVVE CGGQTVQSCV IRNLRKNPNF DICTLFMEVM LPREELYCPP
1410 1420 1430 1440 1450
ITVKVIDNRQ FGRRPVVGQC TIRSLESFLC DPYSAESPSP QGGPDDVSLL
1460 1470 1480 1490 1500
SPGEDVLIDI DDKEPLIPIQ EEEFIDWWSK FFASIGEREK CGSYLEKDFD
1510 1520 1530 1540 1550
TLKVYDTQLE NVEAFEGLSD FCNTFKLYRG KTQEETEDPS VIGEFKGLFK
1560 1570 1580 1590 1600
IYPLPEDPAI PMPPRQFHQL AAQGPQECLV RIYIVRAFGL QPKDPNGKCD
1610 1620 1630 1640 1650
PYIKISIGKK SVSDQDNYIP CTLEPVFGKM FELTCTLPLE KDLKITLYDY
1660 1670 1680 1690 1700
DLLSKDEKIG ETVVDLENRL LSKFGARCGL PQTYCVSGPN QWRDQLRPSQ
1710 1720 1730 1740 1750
LLHLFCQQHR VKAPVYRTDR VMFQDKEYSI EEIEAGRIPN PHLGPVEERL
1760 1770 1780 1790 1800
ALHVLQQQGL VPEHVESRPL YSPLQPDIEQ GKLQMWVDLF PKALGRPGPP
1810 1820 1830 1840 1850
FNITPRRARR FFLRCIIWNT RDVILDDLSL TGEKMSDIYV KGWMIGFEEH
1860 1870 1880 1890 1900
KQKTDVHYRS LGGEGNFNWR FIFPFDYLPA EQVCTIAKKD AFWRLDKTES
1910 1920 1930 1940 1950
KIPARVVFQI WDNDKFSFDD FLGSLQLDLN RMPKPAKTAK KCSLDQLDDA
1960 1970 1980 1990 2000
FHPEWFVSLF EQKTVKGWWP CVAEEGEKKI LAGKLEMTLE IVAESEHEER
2010 2020 2030 2040 2050
PAGQGRDEPN MNPKLEDPRR PDTSFLWFTS PYKTMKFILW RRFRWAIILF
2060 2070 2080
IILFILLLFL AIFIYAFPNY AAMKLVKPFS
Length:2,080
Mass (Da):237,295
Last modified:November 1, 1998 - v1
Checksum:i376E25A5AB9BE398
GO
Isoform 2 (identifier: O75923-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT

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Length:2,111
Mass (Da):240,649
Checksum:iAE2E2536294E3F8E
GO
Isoform 3 (identifier: O75923-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     494-508: EEPAGAVKPSKASDL → V

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Length:2,066
Mass (Da):235,913
Checksum:iBB177D29C6673190
GO
Isoform 4 (identifier: O75923-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1470-1470: Q → QLADGLSSLAPTNTASPPSSPH

Show »
Length:2,101
Mass (Da):239,297
Checksum:i26EEDCF011956BE1
GO
Isoform 5 (identifier: O75923-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT
     494-508: EEPAGAVKPSKASDL → V

Show »
Length:2,097
Mass (Da):239,267
Checksum:i5E5A7D7DC399343D
GO
Isoform 6 (identifier: O75923-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     494-508: EEPAGAVKPSKASDL → V
     1470-1470: Q → QLADGLSSLAPTNTASPPSSPH

Show »
Length:2,087
Mass (Da):237,916
Checksum:iE225F74E3A033173
GO
Isoform 7 (identifier: O75923-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT
     494-508: EEPAGAVKPSKASDL → V
     1470-1470: Q → QLADGLSSLAPTNTASPPSSPH

Show »
Length:2,118
Mass (Da):241,269
Checksum:i8E253645F2D76F4A
GO
Isoform 8 (identifier: O75923-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
     152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT

Show »
Length:2,112
Mass (Da):240,735
Checksum:i65D105E2EA06A54E
GO
Isoform 9 (identifier: O75923-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
     494-508: EEPAGAVKPSKASDL → V

Show »
Length:2,067
Mass (Da):236,000
Checksum:i5BE7B5C3285A6CBD
GO
Isoform 10 (identifier: O75923-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
     1470-1470: Q → QLADGLSSLAPTNTASPPSSPH

Show »
Length:2,102
Mass (Da):239,383
Checksum:iEBD1B370E34EF3E7
GO
Isoform 11 (identifier: O75923-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
     152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT
     494-508: EEPAGAVKPSKASDL → V

Show »
Length:2,098
Mass (Da):239,353
Checksum:i3C81E57B591C23C2
GO
Isoform 12 (identifier: O75923-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
     494-508: EEPAGAVKPSKASDL → V
     1470-1470: Q → QLADGLSSLAPTNTASPPSSPH

Show »
Length:2,088
Mass (Da):238,002
Checksum:iC068B3393FEBAEBA
GO
Isoform 13 (identifier: O75923-13) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
     152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT
     494-508: EEPAGAVKPSKASDL → V
     1470-1470: Q → QLADGLSSLAPTNTASPPSSPH

Show »
Length:2,119
Mass (Da):241,356
Checksum:i1E839F33439A3B81
GO
Isoform 14 (identifier: O75923-14) [UniParc]FASTAAdd to basket
Also known as: Dysferlin_v1, DYSF_v1

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR

Note: Produced by alternative promoter usage.
Show »
Length:2,081
Mass (Da):237,381
Checksum:iCE55314169D4B801
GO
Isoform 15 (identifier: O75923-15) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     494-508: EEPAGAVKPSKASDL → V
     1934-1968: KPAKTAKKCSLDQLDDAFHPEWFVSLFEQKTVKGW → SSASSSRPPRPDCPARVGRQTDGPAHTPRVANMEL
     1969-2080: Missing.

Show »
Length:1,954
Mass (Da):222,315
Checksum:i99D137284A468A65
GO

Sequence cautioni

The sequence BAG51981 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA07603 differs from that shown. Reason: Frameshift at position 1972.Curated
The sequence CAA07603 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05783452W → R in LGMD2B. 1 Publication1
Natural variantiVAR_05783567V → D in MMD1 and LGMD2B; Reduces calcium-sensitive phospholipid binding and interaction with AHNAK and AHNAK2. 2 PublicationsCorresponds to variant rs121908957dbSNPEnsembl.1
Natural variantiVAR_05783684A → V.1 PublicationCorresponds to variant rs772008300dbSNPEnsembl.1
Natural variantiVAR_057837155G → R in LGMD2B. 1 PublicationCorresponds to variant rs200970855dbSNPEnsembl.1
Natural variantiVAR_024853170A → E in MMD1 and LGMD2B; also found in patients with isolated hyperCKemia. 3 PublicationsCorresponds to variant rs34999029dbSNPEnsembl.1
Natural variantiVAR_024854189L → V.2 PublicationsCorresponds to variant rs13407355dbSNPEnsembl.1
Natural variantiVAR_057838234G → E in LGMD2B. 1 PublicationCorresponds to variant rs141497053dbSNPEnsembl.1
Natural variantiVAR_024855253R → W Found in patients with isolated hyperCKemia. 2 PublicationsCorresponds to variant rs149827237dbSNPEnsembl.1
Natural variantiVAR_024856266L → P in pseudometabolic myopathy. 2 Publications1
Natural variantiVAR_057839284I → T in LGMD2B. 1 Publication1
Natural variantiVAR_024857299G → E in MMD1. 2 Publications1
Natural variantiVAR_057840299G → R in LGMD2B and proximodistal myopathy. 3 PublicationsCorresponds to variant rs121908963dbSNPEnsembl.1
Natural variantiVAR_057841299G → W in MMD1. 1 PublicationCorresponds to variant rs121908963dbSNPEnsembl.1
Natural variantiVAR_057842335G → A.1 Publication1
Natural variantiVAR_057843340S → R in proximodistal myopathy. 1 Publication1
Natural variantiVAR_057844374V → L in MMD1; unknown pathological significance. 2 PublicationsCorresponds to variant rs150724610dbSNPEnsembl.1
Natural variantiVAR_057845386 – 390FRAED → Y in MMD1. 1 Publication5
Natural variantiVAR_057846389E → Q in MMD1. 1 Publication1
Natural variantiVAR_057847390D → N.1 Publication1
Natural variantiVAR_057848426G → R in MMD1. 1 Publication1
Natural variantiVAR_057849426G → V in MMD1. 1 Publication1
Natural variantiVAR_024858456C → W in MMD1. 2 Publications1
Natural variantiVAR_057850519G → R in MMD1. 1 PublicationCorresponds to variant rs121908962dbSNPEnsembl.1
Natural variantiVAR_024859555R → W in LGMD2B and MMD1; also found in patients with isolated hyperCKemia. 2 PublicationsCorresponds to variant rs377735262dbSNPEnsembl.1
Natural variantiVAR_057851618G → R in MMD1 and LGMD2B. 2 PublicationsCorresponds to variant rs201049092dbSNPEnsembl.1
Natural variantiVAR_057852621G → R in LGMD2B. 1 Publication1
Natural variantiVAR_057853625D → Y in LGMD2B. 1 PublicationCorresponds to variant rs121908960dbSNPEnsembl.1
Natural variantiVAR_057854731P → R in LGMD2B. 1 Publication1
Natural variantiVAR_012308791P → R in MMD1 and LGMD2B. 2 PublicationsCorresponds to variant rs121908956dbSNPEnsembl.1
Natural variantiVAR_057855819R → Q.1 PublicationCorresponds to variant rs748636047dbSNPEnsembl.1
Natural variantiVAR_049055834I → V.Corresponds to variant rs34671418dbSNPEnsembl.1
Natural variantiVAR_057856930W → C in LGMD2B; unknown pathological significance. 2 PublicationsCorresponds to variant rs727503910dbSNPEnsembl.1
Natural variantiVAR_024860959R → W in MMD1 and LGMD2B. 2 PublicationsCorresponds to variant rs202218890dbSNPEnsembl.1
Natural variantiVAR_057857999W → C in MMD1. 2 PublicationsCorresponds to variant rs28937581dbSNPEnsembl.1
Natural variantiVAR_0248611022R → Q in LGMD2B; unknown pathological significance. 3 PublicationsCorresponds to variant rs34211915dbSNPEnsembl.1
Natural variantiVAR_0578581029P → L in MMD1. 1 Publication1
Natural variantiVAR_0248621038R → Q in LGMD2B; unknown pathological significance. 3 PublicationsCorresponds to variant rs150877497dbSNPEnsembl.1
Natural variantiVAR_0578591041R → C in MMD1. 1 Publication