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O97592

- DMD_CANFA

UniProt

O97592 - DMD_CANFA

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Protein

Dystrophin

Gene

DMD

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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

Regions

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

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding, Zinc

Names & Taxonomyi

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

Subcellular locationi

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

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. postsynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO97592.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000020300.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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

Zinc finger

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

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5069.
HOVERGENiHBG005495.
InParanoidiO97592.
KOiK10366.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

O97592-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL
60 70 80 90 100
LDLLEGLTGQ KLPKEKGSTR VHALNNVNKA LRVLQKNNVD LVNIGSTDIV
110 120 130 140 150
DGNHKLTLGL IWNIILHWQV KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN
160 170 180 190 200
YPQVNVINFT TSWSDGLALN ALIHSHRPDL FDWNSVVCQQ SATQRLEHAF
210 220 230 240 250
NIAKYQLGIE KLLDPEDVAT TYPDKKSILM YITSLFQVLP QQVSIEAIQE
260 270 280 290 300
VEMLPRPSQV TREEHFQIHH QMHYSQQITV SLAQGYERAP SFPKPRFKSY
310 320 330 340 350
AYTQAAYVTT SDPTRSPLPS QHLETPEDKS FGRSLTETEA NLDSYQTALE
360 370 380 390 400
EVLSWLLSAE DALQAQGEIS NDVEEVKEQF HTHEGYMMDL TSHQGRVGNV
410 420 430 440 450
LQLGSQLIGT GKLSEDEETE VQEQMNLLNS RWECLRVASM EKQSNLHKVL
460 470 480 490 500
MDLQNQQLKE LNDWLTKTEE RTRKMEKEPL GPDIEDLKRQ VQQHKVLQED
510 520 530 540 550
LEQEQVRVNS LTHMVVVVDE SSGDHATAAL EEQLKVLGDR WANICRWTED
560 570 580 590 600
RWVLLQDILL KWQRFTEEQC LFSAWLSEKE DAVNKIHTTG FKDQSEVLSN
610 620 630 640 650
LQKLAVLKTD LEKKKQTMDK LCSLNQDLLS ALKNTVVAHK MEAWLDNFAQ
660 670 680 690 700
RWDNLVQKLE KSSAQISQAV TTTQPSLTQT TVMETVTMVT TREHILVKHA
710 720 730 740 750
QEELPPPPPQ KKRQIIVDSE IRKRLDVDIT ELHSWITRSE AVLQSPEFAI
760 770 780 790 800
YRKEGNFSDL KEKVNAIERE KAEKFRKLQD ASRSAQALVE QMVNEGVNAD
810 820 830 840 850
SIKQASEQLN SRWIEFCQLL SERLNWLEYQ NNIITFYNQL QQLEQMTTTA
860 870 880 890 900
ENWLKTQPTT TSEPTAIKSQ LKICKDEINR LSALQPQIER LKIQSIALKE
910 920 930 940 950
KGQGPMFLDA DFVAFTNHFN QVFADVQARE KELQTIFDSL PPMRYQETMS
960 970 980 990 1000
TILTWIQQSE TKLSIPQVTV TEYDIMEQRL GELQALQSSL QEQQNGLNYL
1010 1020 1030 1040 1050
STTVKEMSKK APLSDISRKY QSEFEEIEGR WKKLSSQLVE HCQKLEEQMA
1060 1070 1080 1090 1100
KLRKIQNHIK TLKKWITEVD VFLKEEWPAL GDSEILKRQL KQCRLLVNDI
1110 1120 1130 1140 1150
QTIQPSLNSV NEGAQKMKNE AEPEFAGRLE TELRELNTQW DYMCRQVYAR
1160 1170 1180 1190 1200
KEALKGGLDK TVSLQKDLSE MHEWMTQAEE EYLERDFEYK TPDELQTAVE
1210 1220 1230 1240 1250
EMKRAKEEAQ QKEAKVKLLT ESVNSVIAQA PPAAQEALKK ELDTLTTNYQ
1260 1270 1280 1290 1300
WLCTRLNGKC KTLEEVWACW HELLSYLEKA NKWLSEVEVK LKTTENISGG
1310 1320 1330 1340 1350
AEEIAEVLDS LENLMQHSED NPNQIRILAQ TLTDGGVMDE LINEELETFN
1360 1370 1380 1390 1400
SRWRELHEEA VRRQKLLEQS IQSAQEIEKS LHLIQESLSS IDKQLAAYIA
1410 1420 1430 1440 1450
DKVDAAQMPQ EAQKIQSDLT SHEISLEEMK KHNQGKETAQ RVLSQIDVAQ
1460 1470 1480 1490 1500
KKLQDVSMKF RLFQKPANFE QRLQESKMIL DEVKMHLPAL ETKSVEQEVV
1510 1520 1530 1540 1550
QSQLNHCVNL YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL
1560 1570 1580 1590 1600
KLHYNELGAK VTERKQQLEK CLKLSRKMRK EMNALTEWLA ATDMELTKRS
1610 1620 1630 1640 1650
AVEGMPSNLD SEVAWGKATQ KEIEKQKVHL KSVTEVGEAL KTVLGKKEML
1660 1670 1680 1690 1700
VEDKLSLLNS NWIAVTSRAE EWLNLLLEYQ KHMETFDQNV DYITNWIIQA
1710 1720 1730 1740 1750
DALLDESEKK KPQQKEDILK RLKAEMNDIR PKVDSTRDQA ANLMANRGDH
1760 1770 1780 1790 1800
CRKVVEPKIS ELNHRFAAIS HRIKTGKASI PLKELEQFNS DIQKLLEPLE
1810 1820 1830 1840 1850
AEIQQGVNLK EEDFNKDMSE DNEGTVKELL QRGDNLQQRI TDERKREEIK
1860 1870 1880 1890 1900
IKQQLLQTKH NALKDLRSQR RKKALEISHQ WYQYKRQADD LLKCLDDIEK
1910 1920 1930 1940 1950
KLASLPEPRD ERKIKEIDRE LQKKKEELNA VRRQAEGLSE DGAAMAVEPT
1960 1970 1980 1990 2000
QIQLSKRWRE IESKFAQFRR LNFAQIHTVH EESVVAMTED MPLEISYVPS
2010 2020 2030 2040 2050
TYLTEITHVS QALSEVEELL NAPDLCAQDF EDLFKQEESL KNIKDSLQQI
2060 2070 2080 2090 2100
SGRIDIIHNK KTAALHSATP AERAKLQEAL SRLDFQWERV NNMYKDRQGR
2110 2120 2130 2140 2150
FDRSVEKWRR FHYDMKILNQ WLTEAEQFLK KTQIPENWEH AKYKWYLKEL
2160 2170 2180 2190 2200
QDGIGQRQSV VRVLNATGEE IIQQSSKTDA SILQEKLGSL NLRWQEVCKQ
2210 2220 2230 2240 2250
LAERKKRLEE QKNILSEFQR DVNEFVLWLE EADNVANIPL EPGNEQQLKE
2260 2270 2280 2290 2300
KLEQVKLLAE ELPLRQGILK QLNETGGTVL VSAPLSPEEQ DKLENKLKQT
2310 2320 2330 2340 2350
NLQWIKVSRN LPEKQEEIEA HVKDLGQLEE QLNHLLLWLS PIRNQLEIYN
2360 2370 2380 2390 2400
QPNQTGPFDI KEIEVAVQAK QPDVEGILSK GQHLYKEKPA TQPAKRKLED
2410 2420 2430 2440 2450
LSSDWKVVTQ LLQELRAKQP GPAPGLTTVR APPSQTVTLV TQPAVTKETA
2460 2470 2480 2490 2500
ISKLEMPSSL LLEVPALADF NRAWTELTDW LSLLDRVIKS QRVMVGDLED
2510 2520 2530 2540 2550
INEMIIKQKA TLQDLEQRRP QLEELITAAQ NLKNKTSNQE ARTIITDRIE
2560 2570 2580 2590 2600
RIQSQWDEVQ EHLQNRRLQL TEMLKDSTQW LEAKEEAEQV LGQARAKLES
2610 2620 2630 2640 2650
WKEAPYTVDA IQKKITETKQ LAKDLRQWQI NVDVANDLAL KLLRDYSADD
2660 2670 2680 2690 2700
TRKVHMITEN INASWASIHK RLSEREAALE ETHRLLQQFP LDLEKFLAWL
2710 2720 2730 2740 2750
TEAETTANVL QDATHKERLL EDSKGVRELM KQWQDLQGEI EAHTDIYHNL
2760 2770 2780 2790 2800
DENGQKVLRS LEGSDDAALL QRRLDNMNFK WSELRKKSLN IRSHLEASSD
2810 2820 2830 2840 2850
QWKRLHLSLQ ELLVWLQLKD DELSRQAPIG GDFPAVQKQN DVHRAFKREL
2860 2870 2880 2890 2900
KTKEPVIMST LETVRIFLTE QPLEGLEKLY QEPRELPPEE RAQNVTRLLR
2910 2920 2930 2940 2950
KQAEEVNTQW EKLNVHSADW QRKIDEALER LQELQEATDE LDLKLRQAEV
2960 2970 2980 2990 3000
IKGSWQPVGD LLIDSLQDHL EKVKALRGEI TPLKENVSYV NDLARQLTTL
3010 3020 3030 3040 3050
GIQLSPYNLN TLEDLNTRWK LLQVAIEDRI RQLHEAHRDF GPASQHFLST
3060 3070 3080 3090 3100
SVQGPWERAI SPNKVPYYIN HETQTTCWDH PKMTELYQSL ADLNNVRFSA
3110 3120 3130 3140 3150
YRTAMKLRRL QKALCLDLLS LSAACDALDQ HNLKQNDQPM DILQVINCLT
3160 3170 3180 3190 3200
TIYDRLEQEH NNLVNVPLCV DMCLNWLLNV YDTGRTGRIR VLSFKTGIIS
3210 3220 3230 3240 3250
LCKAHLEDKY RYLFKQVASS TGFCDQRRLG LLLHDSIQIP RQLGEVASFG
3260 3270 3280 3290 3300
GSNIEPSVRS CFQFANNKPE IEAALFLDWM RLEPQSMVWL PVLHRVAAAE
3310 3320 3330 3340 3350
TAKHQAKCNI CKECPIIGFR YRSLKHFNYD ICQSCFFSGR VAKGHKMHYP
3360 3370 3380 3390 3400
MVEYCTPTTS GEDVRDFAKV LKNKFRTKRY FAKHPRMGYL PVQTVLEGDN
3410 3420 3430 3440 3450
METPVTLINF WPVDSAPASS PQLSHDDTHS RIEHYASRLK KMENSNGSYL
3460 3470 3480 3490 3500
NDSISPNESI DDEHLLIQHY WRSLNQESPL SQPRSPAQIL ISLESEERGE
3510 3520 3530 3540 3550
LERILADLEG RNRNLQAEYD RLKQQHEHKG LSPLPSPPEM MPTSPQSPRD
3560 3570 3580 3590 3600
AELIAEAKLL RQHKGRLEAR MQILEDHNKQ LESQLHRLRQ LLEQPQAEAK
3610 3620 3630 3640 3650
VNGTTVSSPS TSLQRSDSSQ PMLLRVVGSQ TSESMGEEDL LSPPQDTSTG
3660 3670 3680
LEEVMEQLNH SFPSSRGRNT PGKPMREDTM
Length:3,680
Mass (Da):425,653
Last modified:May 1, 1999 - v1
Checksum:i539F1C9D72377872
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070485 mRNA. Translation: AAC83646.1.
RefSeqiNP_001003343.1. NM_001003343.1.
UniGeneiCfa.3738.

Genome annotation databases

GeneIDi606758.
KEGGicfa:606758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF070485 mRNA. Translation: AAC83646.1 .
RefSeqi NP_001003343.1. NM_001003343.1.
UniGenei Cfa.3738.

3D structure databases

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

Protein-protein interaction databases

STRINGi 9615.ENSCAFP00000020300.

Proteomic databases

PaxDbi O97592.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 606758.
KEGGi cfa:606758.

Organism-specific databases

CTDi 1756.

Phylogenomic databases

eggNOGi COG5069.
HOVERGENi HBG005495.
InParanoidi O97592.
KOi K10366.

Miscellaneous databases

NextBioi 20892530.

Family and domain databases

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

Publicationsi

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

Entry informationi

Entry nameiDMD_CANFA
AccessioniPrimary (citable) accession number: O97592
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 1999
Last modified: October 29, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3