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Q9ESD7 (DYSF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dysferlin
Alternative name(s):
Dystrophy-associated fer-1-like protein
Fer-1-like protein 1
Gene names
Name:Dysf
Synonyms:Fer1l1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2090 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.10

Subunit structure

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. Ref.6 Ref.8 Ref.9 Ref.12

Subcellular location

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. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11

Tissue specificity

Expressed in skeletal and cardiac muscles (at protein level). Expressed in skeletal muscle and heart. Also found in brain, liver and kidney. Ref.1 Ref.7

Domain

The C2 domain 1 associates with lipid membranes in a calcium-dependent manner. The C2 domain 1 seems to be largely unstructured in the absence of bound ligands. The C2 domain 1 contains one high-affinity calcium binding site; calcium binding leads to a more ordered conformation and increases protein stability By similarity.

Involvement in disease

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.

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.

Sequence similarities

Belongs to the ferlin family.

Contains 5 C2 domains.

Sequence caution

The sequence BAD21394.1 differs from that shown. Reason: Erroneous initiation.

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9ESD7-1)

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.
Isoform 2 (identifier: Q9ESD7-2)

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.
Isoform 3 (identifier: Q9ESD7-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20902090Dysferlin
PRO_0000057880

Regions

Topological domain1 – 20562056Cytoplasmic Potential
Transmembrane2057 – 207721Helical; Potential
Topological domain2078 – 209013Extracellular Potential
Domain1 – 8585C2 1
Domain209 – 30496C2 2
Domain368 – 486119C2 3
Domain1149 – 1254106C2 4
Domain1575 – 167399C2 5
Compositional bias1048 – 110760Arg-rich

Sites

Metal binding181Calcium By similarity
Metal binding191Calcium; via carbonyl oxygen By similarity
Metal binding211Calcium By similarity
Metal binding401Calcium By similarity

Natural variations

Alternative sequence1 – 2929MLRVF…SAVFA → MLCCLLARASNLPNVKKDRR SDPVASLIFR in isoform 2 and isoform 3.
VSP_035930
Alternative sequence1521P → PGGGQSRAETWSLLSDSTMD TRYSGKKWPVPT in isoform 2.
VSP_035931
Alternative sequence496 – 51015EEPAG…QATDL → V in isoform 2 and isoform 3.
VSP_035932
Alternative sequence647 – 6548Missing in isoform 2 and isoform 3.
VSP_035933

Experimental info

Sequence conflict4671D → G in CAB63111. Ref.4
Sequence conflict4761T → I in AAG17046. Ref.1
Sequence conflict5101L → V in CAB63111. Ref.4
Sequence conflict6841I → T in AAG17046. Ref.1
Sequence conflict690 – 6912RV → GI in AAG17046. Ref.1
Sequence conflict6981N → G in AAG17046. Ref.1
Sequence conflict7121S → T in AAG17046. Ref.1
Sequence conflict7171A → S in AAG17046. Ref.1
Sequence conflict7271L → I in AAG17046. Ref.1
Sequence conflict8851L → F in AAG17046. Ref.1
Sequence conflict909 – 9102LT → FS in AAG17046. Ref.1
Sequence conflict9311S → T in AAG17046. Ref.1
Sequence conflict9531D → A in AAG17046. Ref.1
Sequence conflict11751P → A in AAG17046. Ref.1
Sequence conflict11871A → S in CAB63111. Ref.4
Sequence conflict16941Y → C in AAG17046. Ref.1
Sequence conflict17011Q → K in AAG17046. Ref.1
Sequence conflict17051Q → K in AAG17046. Ref.1
Sequence conflict18061R → Q in AAG17046. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 16, 2008. Version 3.
Checksum: 0EBD1E2353946143

FASTA2,090237,911
        10         20         30         40         50         60 
MLRVFILFAE NVHTPDSDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF EWDLKGIPLD 

        70         80         90        100        110        120 
QSSELLVVVK DHETMGRNRF LGEAKIPLQE VLATPSLSAS FNAPLLDAKQ QPTGASLVLQ 

       130        140        150        160        170        180 
VSYTPPPGAV PLFPPPASLA PSPTLPDMDL VPDTGGEEDT EDQGLTGDEA EPFLDQSAAV 

       190        200        210        220        230        240 
GPGGPTTPRK PPSHPPPHYP GAKRKRSSAP PRKLLSDKPQ DFQIRVQVIE GRQLPGVNIK 

       250        260        270        280        290        300 
PVVKVTAAGQ TKRTRIQKGN SPLFNETLFF NVFDSPLELF DEPIFITVVD SRSLRTDALL 

       310        320        330        340        350        360 
GEFRMDVGTV YREPRHAYLR KWLLLSDPDD FSAGARGYLK ASLCVLGPGD EAPLDKKDPS 

       370        380        390        400        410        420 
EDKEDIEGNL LRPTGVALRG AHFCLKLFRA EDLPQMDDAV MDNVKQIFGF DSNKKNLVDP 

       430        440        450        460        470        480 
FVEVSFAGKM LCSKILEKTA NPQWNQNITL PAMFPSMCEK MRIRVMDWDR LTHNDTVATT 

       490        500        510        520        530        540 
YLGMSKISAT GGEIEEEPAG VLKSPQATDL DDNLGFLPTF GPCYVNLYGS PREFTGFPDP 

       550        560        570        580        590        600 
YAELNTGKGE GVAYRGRVLL SLETKLVEHS EQKVEDLPAD DILRVEKYLR RRKYSLFAAF 

       610        620        630        640        650        660 
YSATMLQDVD DAIQFEVSIG NYGNKFDTTC LPLASTTQYS RAVFDGGSLP LPVGCHYYYL 

       670        680        690        700        710        720 
PWGNVKPVVV LSSYWEDISH RIEIQNQLLR VADRLEANLE QVHLALKAQC SSEDVDALVA 

       730        740        750        760        770        780 
QLTDELLADC SQPLCDIHEI PSATHLDQYL LRLRTRHLSQ IKEAALALKL GHSELSTALE 

       790        800        810        820        830        840 
QAEDWLLHLR ALAEEPQNSL PDIIIWMLQG DKRVAYQRVP AHEVLFSRRG PSYCGRNCGK 

       850        860        870        880        890        900 
LQTIFLKYPM EGMPGARMPV QIRIKLWFGL SVDEKEFNQF AEGKLSVFAE TYENQTKLAL 

       910        920        930        940        950        960 
VGNWGTTGLT YPKFSDVTGK IKLPKDSFRP SAGWAWAGDW FVCPEKTLLH DADAGHLSFV 

       970        980        990       1000       1010       1020 
EEVFENQTRL PGGQWIYMSD NYTDVNGEKV LPKDDIECPL GWKWEDEEWS TDLNRAVDEQ 

      1030       1040       1050       1060       1070       1080 
GWEYSITIPP DRKPKHWVPV EKMYYTHRRR RWVRLRRRDL SQMEALKRHR QAEAEGEGWE 

      1090       1100       1110       1120       1130       1140 
YASLFGWKFH LEYRKTDAFR RRRWRRRMEP LEKTGPAAVF ALEGALGGMV DDKSEDSMSV 

      1150       1160       1170       1180       1190       1200 
STLSFGVNRP TISCIFDYGN RYHLRCYLYQ ARDLPAMDKD SFSDPYAIVS FLHQSQKTVV 

      1210       1220       1230       1240       1250       1260 
EKNTLNPTWD QTLIFYEIEI FGEPASIAEH PPCIVVELYD HDTYGADEFM GRCICQPSLE 

      1270       1280       1290       1300       1310       1320 
RMPRLAWFPL TRGSQPAGEL LAAFELIQRE KPAIHHIPGF EMHETSRILD ETEDTDLPYP 

      1330       1340       1350       1360       1370       1380 
PPQREANIYM VPQNIKPALQ RTAIEILAWG LRNMKSYQMA SISSPSLVVE CGGQTVQSCV 

      1390       1400       1410       1420       1430       1440 
IRNLRKNPNF DVCTLFMEVM LPREDLYCPP IVVKVIDNRQ FGRRPVVGQC TIRSLENFLC 

      1450       1460       1470       1480       1490       1500 
DPYSAESPSP QGGPDDVSLL SPGEDVLIDI DDKEPLIPVQ EEEFIDWWSK FFASVGEREK 

      1510       1520       1530       1540       1550       1560 
CGSYLEKDFD TLKVYDTQLE NVEAFGGLSD FCNTFKLYRG RTQEETDDPS VIGEFKGLFK 

      1570       1580       1590       1600       1610       1620 
IYPLPEDPAI PMPPRQFHQL AAQGPQECLV RIYIVRAFGL QPKDPNGKCD PYIKISIGKK 

      1630       1640       1650       1660       1670       1680 
SVSDQDNYIP CTLEPVFGKM FELTCTLPLE KDLKITLYDY DLLSKDEKIG ETVIDLENRL 

      1690       1700       1710       1720       1730       1740 
LSKFGARCGL PQTYCVSGPN QWRDQLRPSQ LLHLFCQQHR IKAPVYRTDR VTFQDKDYTI 

      1750       1760       1770       1780       1790       1800 
EEIEAGRLPN PHLGPVEERL ALHVLQQQGL VPEHVESRPL YSPLQPDIEQ GKLQMWIDIF 

      1810       1820       1830       1840       1850       1860 
PKVLGRPGPP FNITPRKARR FFLRCIIWNT KDVILDDLSL TGEKMSDIYV KGWMVGFEEH 

      1870       1880       1890       1900       1910       1920 
KQKTDVHYRS LGGEGNFNWR FVFPFDYLPA EQVCAVAKKD AFWRLDKTES KIPARVVFQI 

      1930       1940       1950       1960       1970       1980 
WDNDKFSFDD FLGSLQLDLN RMPKPAKTAE KCSLDQLDDT FHPEWFVSLF EQKTVKGWWP 

      1990       2000       2010       2020       2030       2040 
CVTEEGEKKM LAGKLEMTLE IVAESEHEER PAGQGRDEPN MNPKLEDPRR PDTSFLWFTS 

      2050       2060       2070       2080       2090 
PYKTMKFILW RRFRCAIILF IILFILLLFL GVFVYAFPNY AAMKLVKPFR 

« Hide

Isoform 2 [UniParc].

Checksum: 3C8A7837C2F78273
Show »

FASTA2,100239,289
Isoform 3 [UniParc].

Checksum: BA9E838D870C6396
Show »

FASTA2,069235,908

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Dysferlin deletion in SJL mice (SJL-Dysf) defines a natural model for limb girdle muscular dystrophy 2B."
Bittner R.E., Anderson L.V.B., Burkhardt E., Bashir R., Vafiadaki E., Ivanova S., Raffelsberger T., Maerk I., Hoeger H., Jung M., Karbasiyan M., Storch M., Lassmann H., Moss J.A., Davison K., Harrison R., Bushby K.M.D., Reis A.
Nat. Genet. 23:141-142(1999) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001071162.1. NM_001077694.2.
NP_067444.2. NM_021469.3.
XP_006506243.1. XM_006506180.1.
UniGeneMm.220982.

3D structure databases

ProteinModelPortalQ9ESD7.
SMRQ9ESD7. Positions 1-128, 219-327, 381-491, 952-1062, 1163-1286, 1342-1433, 1552-1706, 1818-1943.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205052. 2 interactions.
IntActQ9ESD7. 4 interactions.
MINTMINT-4998243.

PTM databases

PhosphoSiteQ9ESD7.

Proteomic databases

PaxDbQ9ESD7.
PRIDEQ9ESD7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081904; ENSMUSP00000080579; ENSMUSG00000033788. [Q9ESD7-2]
ENSMUST00000113818; ENSMUSP00000109449; ENSMUSG00000033788. [Q9ESD7-3]
ENSMUST00000168387; ENSMUSP00000132297; ENSMUSG00000033788. [Q9ESD7-1]
GeneID26903.
KEGGmmu:26903.
UCSCuc009cos.2. mouse. [Q9ESD7-3]
uc009cot.1. mouse. [Q9ESD7-2]

Organism-specific databases

CTD8291.
MGIMGI:1349385. Dysf.

Phylogenomic databases

eggNOGNOG330124.
GeneTreeENSGT00550000074414.
HOGENOMHOG000006771.
HOVERGENHBG018972.
InParanoidQ6KAR3.
OMAQVHLALK.
TreeFamTF316871.

Gene expression databases

ArrayExpressQ9ESD7.
BgeeQ9ESD7.
CleanExMM_DYSF.
GenevestigatorQ9ESD7.

Family and domain databases

Gene3D2.60.40.150. 8 hits.
InterProIPR000008. C2_dom.
IPR012968. FerIin-domain.
IPR012560. Ferlin_A-domain.
IPR012561. Ferlin_B-domain.
IPR010482. Peroxin/Dysferlin.
IPR006614. Peroxin/Ferlin.
[Graphical view]
PfamPF00168. C2. 7 hits.
PF08165. FerA. 1 hit.
PF08150. FerB. 1 hit.
PF08151. FerI. 1 hit.
PF06398. Pex24p. 1 hit.
[Graphical view]
SMARTSM00239. C2. 7 hits.
SM00694. DysFC. 2 hits.
SM00693. DysFN. 2 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 7 hits.
PROSITEPS50004. C2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio304757.
PROQ9ESD7.
SOURCESearch...

Entry information

Entry nameDYSF_MOUSE
AccessionPrimary (citable) accession number: Q9ESD7
Secondary accession number(s): Q6KAR3, Q80VT0, Q9QXC0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: December 16, 2008
Last modified: April 16, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot