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Protein

Dystrophin

Gene

DMD

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri3296 – 3343ZZ-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Dystrophin
Gene namesi
Name:DMDImported
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Cell membranesarcolemma By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • 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 adult muscle, NMJ localization depends upon ANK2 presence, but not in newborn animals.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002275221 – 3674DystrophinCuratedAdd BLAST3674

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3472PhosphoserineBy similarity1
Modified residuei3479PhosphoserineBy similarity1
Modified residuei3489PhosphoserineBy similarity1
Modified residuei3601PhosphoserineBy similarity1
Modified residuei3602PhosphoserineBy similarity1
Modified residuei3606PhosphoserineBy similarity1
Modified residuei3612PhosphoserineBy similarity1
Modified residuei3613PhosphoserineBy similarity1
Modified residuei3655PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5GN48.
PeptideAtlasiQ5GN48.
PRIDEiQ5GN48.

Expressioni

Tissue specificityi

In the retina, expressed in the outer plexiform layer (OPL) and around the blood vessels. Also observed at the vitreal border of the retina corresponding to the inner limiting membrane (ILM). Presynaptically localized in cone pedicles and postsynaptically in bipolar cells (at protein level).1 Publication

Interactioni

Subunit structurei

Interacts with SYNM (By similarity). Interacts with the syntrophins 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 (By similarity). Interacts with SYNM; SNTA1 and SNTB1. 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. Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000030238.

Structurei

3D structure databases

ProteinModelPortaliQ5GN48.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 236Actin-bindingAdd BLAST236
Domaini11 – 115CH 1PROSITE-ProRule annotationAdd BLAST105
Domaini130 – 233CH 2PROSITE-ProRule annotationAdd BLAST104
Repeati335 – 443Spectrin 1Sequence analysisAdd BLAST109
Repeati444 – 552Spectrin 2Sequence analysisAdd BLAST109
Repeati555 – 663Spectrin 3Sequence analysisAdd BLAST109
Repeati715 – 824Spectrin 4Sequence analysisAdd BLAST110
Repeati826 – 930Spectrin 5Sequence analysisAdd BLAST105
Repeati939 – 1041Spectrin 6Sequence analysisAdd BLAST103
Repeati1044 – 1150Spectrin 7Sequence analysisAdd BLAST107
Repeati1153 – 1259Spectrin 8Sequence analysisAdd BLAST107
Repeati1262 – 1363Spectrin 9Sequence analysisAdd BLAST102
Repeati1364 – 1459Spectrin 10Add BLAST96
Repeati1464 – 1564Spectrin 11Add BLAST101
Repeati1567 – 1672Spectrin 12Add BLAST106
Repeati1675 – 1774Spectrin 13Add BLAST100
Repeati1775 – 1870Spectrin 14Add BLAST96
Repeati1873 – 1975Spectrin 15Add BLAST103
Repeati1988 – 2097Spectrin 16Add BLAST110
Repeati2100 – 2204Spectrin 17Add BLAST105
Repeati2207 – 2314Spectrin 18Add BLAST108
Repeati2315 – 2412Spectrin 19Add BLAST98
Repeati2464 – 2566Spectrin 20Add BLAST103
Repeati2569 – 2675Spectrin 21Add BLAST107
Repeati2678 – 2791Spectrin 22Add BLAST114
Repeati2797 – 2919Spectrin 23Add BLAST123
Repeati2924 – 3029Spectrin 24Add BLAST106
Domaini3044 – 3077WWPROSITE-ProRule annotationAdd BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni59 – 68ANK2- and ANK-3 bindingBy similarity10
Regioni1411 – 1909Interaction with SYNMBy similarityAdd BLAST499
Regioni3047 – 3397Interaction with SYNMBy similarityAdd BLAST351
Regioni3455 – 3507Binds to SNTB1By similarityAdd BLAST53

Sequence similaritiesi

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)DescriptionActionsGraphical viewLength
Zinc fingeri3296 – 3343ZZ-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4286. Eukaryota.
COG5069. LUCA.
HOGENOMiHOG000231175.
HOVERGENiHBG005495.
InParanoidiQ5GN48.
KOiK10366.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR016344. Dystrophin.
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. 17 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]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF47576. 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]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q5GN48-1) [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
MSEVSSDERE DVQKKTFTKW INAQFSKFGK QHIENLFNDL QDGRRLLDLL
60 70 80 90 100
EGLTGQKLPK EKGSTRVHAL NNVNKALQVL QKNNVDLVNI GSTDIVDGNH
110 120 130 140 150
KLTLGLIWNI ILHWQVKNVM KNIMAGLQQT NSEKILLSWV RQSTRNYPQV
160 170 180 190 200
NVINFTTSWS DGLALNALIH SHRPDLFDWN SVVCQQSATQ RLEHAFNIAK
210 220 230 240 250
YQLGIEKLLD PEDVATTYPD KKSILMYVTS LFQVLPQQVS IEAIQEVEML
260 270 280 290 300
PRPSKVTREE HFQLHHQMHY SQQITVCLAQ GYERTPSPKP RFKSYAYTQA
310 320 330 340 350
AYVTTSDPTR SPFPSQRLES PEDKSFGSSL LETEVNLDSY QTALEEVLSW
360 370 380 390 400
LLSAEDTLQA QGEISNDVEE VKEQFHTHEG YMMDLTSHQG RIGSVLQLGS
410 420 430 440 450
QLIGKGKLSE DEETEVQEQM NLLNSRWECL RVASVEKQSN LHKVLMDLQN
460 470 480 490 500
QQLKELNDWL TKTEEKTRKM EKEPLGPDLE DLKHQIQQHK VLQEDLEQEQ
510 520 530 540 550
VRVNSLTHMV VVVDESSGDH ATAALEEQLK VLGDRWANIC RWTEDRWVLL
560 570 580 590 600
QDILLKWQRF TEEQCLFSTW LSEKEDALNK IHTTGFKDQG EMLSSLQKLA
610 620 630 640 650
VLKTDLEKKK QTMDKLSSLN QDLLSTLKNT LVAQKMEAWL DNFAQRWDNL
660 670 680 690 700
VQKLEKSSTQ ISQAVTTTQP SLTQTTVMET VTMVTTREQI LVKHAQEELP
710 720 730 740 750
PPPPQKKRQI IVDSEIRKRL DVDITELHSW ITRSEAVLQS PEFAIYRKEG
760 770 780 790 800
NFSDLKEKVN AIEREKAEKF RKLQDASRSA QALVEQMVNE GVNADSIKQA
810 820 830 840 850
AEQLNSRWIE FCQLLSERLN WLEYQNRIIT FYNQLQQLEQ ITTAAENWLK
860 870 880 890 900
TQPITTSEPT AVKSQLKICK DEVNRLSALQ PQIERLKIES IALKEKGQGP
910 920 930 940 950
MFLDADSVAF TNHFNQVFAD MQAKEKELQI IFDTLPPMRY QETMSTILTW
960 970 980 990 1000
IQHSEAKLSI PQATVTEYEI MEQRLGELQA LQSSLQEQQN GLNYLSTTVK
1010 1020 1030 1040 1050
EMSKKAPSNI SRKYQSEFEE IEGRWKKLSA QLMEHCQKLE EQIAKLRKLQ
1060 1070 1080 1090 1100
NHIKTLKNWM AEVDIFLKEE WPALGDSEIL RKQLKQCRLL VSDIQTIQPS
1110 1120 1130 1140 1150
LNSVNEGGQK IKKEAEPEFA SRLETELREL NTQWDYICRQ VYARKEALKG
1160 1170 1180 1190 1200
GLDKTISLQK DLSEMHEWMT QAEEEYLERD FEYKTPDELQ TAVEEMKRAK
1210 1220 1230 1240 1250
EEAQQKEAKV KLLTESVNSV IAQAPPAAQE ALKKELDTLT TNYQWLCTRL
1260 1270 1280 1290 1300
NGKCKTLEEV WACWHELLSY LEKANKWLSE VEFKLKTTEN IPGGAEEISE
1310 1320 1330 1340 1350
VLESLENLMQ HSEDNPNQIR ILAQTLTDGG VMDELINEEL ETFNSRWREL
1360 1370 1380 1390 1400
HEEAVRRQKL LEQSIQSAQE IEKSLHLIQD SLSSIDHQLA VYIADKVDAA
1410 1420 1430 1440 1450
QMPQEAQKIQ SDLTSHEISL EEMKKHYQGK EAAPRVLSQI ELAQKKLQDV
1460 1470 1480 1490 1500
SMKFRLFQKP ANFEQRLQES KMILDEVKMH LPALEIKSVE QEVVQSQLNH
1510 1520 1530 1540 1550
CVNLYKSLSE VKSEVEMVIK TGRQIVQKKQ TENPKELDER VTALKLHYNE
1560 1570 1580 1590 1600
LGAKVTERKQ QLEKCLKLSR KMRKEMNVLT EWLAATDTEL TKRSAVEGMP
1610 1620 1630 1640 1650
SNLDSEVVWG KATQKEIEKQ KFHLKSISEI GEALKMVLGK KETLVEDKLS
1660 1670 1680 1690 1700
LLNSNWIAVT SRAEEWLNLL LEYQKHMENF DQNVDHITKW IIQADTLLDE
1710 1720 1730 1740 1750
SEKKKPQQKE DVLKRLKAEM NDMRPKVDST RDQAANLMAN RGDHCRKVIE
1760 1770 1780 1790 1800
PKISELNHRF AAISHRIKTG KASIPLKELE QFNSDIQKLL EPLEAEIQQG
1810 1820 1830 1840 1850
VNLKEEDFNK DMSEDNEGTV KELLQRGDNL QQRITDERKR EEIKIKQQLL
1860 1870 1880 1890 1900
QTKHNALKDL RSQRRKKALE ISHQWYQYKR QADDLLKCLD DIEKKLASLP
1910 1920 1930 1940 1950
EPQDEKKIKE IDRELQKKKE ELDAVRRQAE GLSEDGAAMA VEPTQIQLSK
1960 1970 1980 1990 2000
RWREIESKFA HFRRLNFAQI HTVHEESVMV MTEDMPLEIS YVPSAYLTEI
2010 2020 2030 2040 2050
THVSQALSEV EQLLNAPDLC AKDFEDLFKQ EESLKNIKDS LQQISGRVDI
2060 2070 2080 2090 2100
IHNKKTAGLQ SATPVERTRL QEALSQLDFQ WERVNKMYKD RQGKFDRSVE
2110 2120 2130 2140 2150
KWRRFHYDMK IFNQWLTEAE HFLKKTQIPE NWEHAKYKWY LKELQDGIGQ
2160 2170 2180 2190 2200
RQTIVRVLNA TGEEVIQQSS KTDASILQEK LGSLNLRWQE VCKQLAERKK
2210 2220 2230 2240 2250
RLEEQKNILS EFQRDLNEFV LWLEEADNIT SVALEPGNEQ QLKEKLEEIK
2260 2270 2280 2290 2300
LLAEELPLRQ GTLKQLNETG GTVLVSAPIS PEEQDKIENK LKQTNLQWIK
2310 2320 2330 2340 2350
VSRILPEKQG EIEAHIKDLG QFEEQLNHLL VWLSPIKNQL EIYNQPNQTG
2360 2370 2380 2390 2400
PFDIKETEVA VQAKQLDVEG ILSKGQHLYK EKPATQPVKR KLEDLSSEWK
2410 2420 2430 2440 2450
AVTHLLQELR AKWPGPTPGL TTIEAPTSQT VTLVTQPTVT KETAISKPEM
2460 2470 2480 2490 2500
PSSLLLEVPA LADFNRAWTE LTDWLSLLDR VIKSQRVMVG DLEDINEMII
2510 2520 2530 2540 2550
KQKATLQDLE QRRPQLEELI TAAQNLKNKT SNQEARTIIT DRIERIQSQW
2560 2570 2580 2590 2600
DEVQEHLQNR RQQLNEMLKD STQWLEAKEE AEQVLGQARA KLESWKEGPY
2610 2620 2630 2640 2650
TMDAIQRKIT ETKQLAKDLR QWQINVDVAN DLALKLLRDY SADDTRKVHM
2660 2670 2680 2690 2700
ITENINASWA NIHKRLSERE TVLEETHRLL QQFPLDLEKF LAWLTEAETT
2710 2720 2730 2740 2750
ANVLQDATHK ERLLEDSKGV RELMKQWQDL QGEIEAHTDI YHNLDENGQK
2760 2770 2780 2790 2800
ILRSLEGSDD AILLQRRLDN MNFKWSELRK KSLNIRSHLE ASSDQWKRLH
2810 2820 2830 2840 2850
LSLQELLVWL QLKDDELSRQ APIGGDCPAV QKQNDVHRAF KRELKTKEPV
2860 2870 2880 2890 2900
IMSTLETVRI FLTEQPLEGL EKLYQEPREL PPEERAQNVT RLLRKQAEEV
2910 2920 2930 2940 2950
NTEWEKLNLH SADWQRKIDE ALERLQELQE ATDELDLKLR QAEVIKGSWQ
2960 2970 2980 2990 3000
PVGDLLIDSL QDHLEKVKAL RGEKAPLKEN VSHVNDLARQ LTTLGIQLSP
3010 3020 3030 3040 3050
YNLSTLEDLN TRWKLLQVAV EDRIRQLHEA HRDFGPASQH FLSTSVQGPW
3060 3070 3080 3090 3100
ERAISPNKVP YYINHETQTT CWDHPKMTEL YQSLADLNNV RFSAYRTAMK
3110 3120 3130 3140 3150
LRRLQKALCL DLLSLSAACD ALDQHNLKQN DQPMDILQII NCLTTVYDRL
3160 3170 3180 3190 3200
EQEHNNLVNV PLCVDMCLNW LLNVYDTGRT GRIRVLSFKT GIVSLCKAHL
3210 3220 3230 3240 3250
EDKYRYLFKQ VASSTGFCDQ RRLGLLLHDS IQIPRQLGEV ASFGGSNIEP
3260 3270 3280 3290 3300
SVRSCFQFAN NKPEIEAALF LDWMRLEPQS MVWLPVLHRV AAAETAKHQA
3310 3320 3330 3340 3350
KCNICKECPI IGFRYRSLKH FNYDICQSCF FSGRVAKGHK MHYPMVEYCT
3360 3370 3380 3390 3400
PTTSGEDVRD FAKVLKNKFR TKRYFAKHPR MGYLPVQTVL EGDNMETPVT
3410 3420 3430 3440 3450
LINFWPVDSA PASSPQLSHD DTHSRIEHYA SRLAEMENSN GSYLNDSISP
3460 3470 3480 3490 3500
NESIDDEHLL IQHYCQSLNQ DSPLSQPRSP AQILISLESE ERGELERILA
3510 3520 3530 3540 3550
DLEEENRNLQ AEYDRLKQQH EHKGLSPLPS PPEMMPTSPQ SPRDAELIAE
3560 3570 3580 3590 3600
AKLLRQHKGR LEARMQTLED HNKQLESQLH RLRQLLEQPQ AEAKVNGTTV
3610 3620 3630 3640 3650
SSPSTSLQRS DSSQPMLLRV VGSQTSESMG EEDLLSPPQD TSTGLEEVME
3660 3670
QLNNSFPSSR GRNTPGKPVR EDTM
Length:3,674
Mass (Da):424,858
Last modified:March 1, 2005 - v1
Checksum:i03C22FB8D805632C
GO
Isoform 31 Publication (identifier: Q5GN48-3) [UniParc]FASTAAdd to basket
Also known as: Dp711 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MREQLKG
     2-3064: Missing.
     3397-3410: Missing.

Show »
Length:603
Mass (Da):68,775
Checksum:i47D2A48AA6DAB02F
GO
Isoform 41 Publication (identifier: Q5GN48-4) [UniParc]FASTAAdd to basket
Also known as: Dp741 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MREQLKG
     2-3064: Missing.
     3454-3507: IDDEHLLIQHYCQSLNQDSPLSQPRSPAQILISLESEERGELERILADLEEENR → M

Show »
Length:564
Mass (Da):64,194
Checksum:i16C18C3BD424AEFD
GO
Isoform 51 Publication (identifier: Q5GN48-5) [UniParc]FASTAAdd to basket
Also known as: Dp71-741 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MREQLKG
     2-3064: Missing.
     3398-3507: Missing.

Show »
Length:507
Mass (Da):57,895
Checksum:iFDAE7EB1BA70ECEC
GO
Isoform 21 Publication (identifier: Q5GN48-2)
Also known as: Dp2601 Publication
Sequence is not available
Length:
Mass (Da):

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0519671M → MREQLKG in isoform 3, isoform 4 and isoform 5. 1 Publication1
Alternative sequenceiVSP_0519682 – 3064Missing in isoform 3, isoform 4 and isoform 5. 1 PublicationAdd BLAST3063
Alternative sequenceiVSP_0519693397 – 3410Missing in isoform 3. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_0519703398 – 3507Missing in isoform 5. 1 PublicationAdd BLAST110
Alternative sequenceiVSP_0519713454 – 3507IDDEH…EEENR → M in isoform 4. 1 PublicationAdd BLAST54

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ865385 mRNA. Translation: CAI26302.1.
RefSeqiNP_001012408.1. NM_001012408.1. [Q5GN48-1]
UniGeneiSsc.42754.
Ssc.93582.

Genome annotation databases

GeneIDi497636.
KEGGissc:497636.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ865385 mRNA. Translation: CAI26302.1.
RefSeqiNP_001012408.1. NM_001012408.1. [Q5GN48-1]
UniGeneiSsc.42754.
Ssc.93582.

3D structure databases

ProteinModelPortaliQ5GN48.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000030238.

Proteomic databases

PaxDbiQ5GN48.
PeptideAtlasiQ5GN48.
PRIDEiQ5GN48.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi497636.
KEGGissc:497636.

Organism-specific databases

CTDi1756.

Phylogenomic databases

eggNOGiKOG4286. Eukaryota.
COG5069. LUCA.
HOGENOMiHOG000231175.
HOVERGENiHBG005495.
InParanoidiQ5GN48.
KOiK10366.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR016344. Dystrophin.
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. 17 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]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF47576. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiDMD_PIG
AccessioniPrimary (citable) accession number: Q5GN48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 1, 2005
Last modified: November 30, 2016
This is version 83 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.