ID F7AQW9_MONDO Unreviewed; 1255 AA.
AC F7AQW9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Dystrophin {ECO:0000256|ARBA:ARBA00040142};
GN Name=DMD {ECO:0000313|Ensembl:ENSMODP00000037545.3};
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000037545.3, ECO:0000313|Proteomes:UP000002280};
RN [1] {ECO:0000313|Ensembl:ENSMODP00000037545.3, ECO:0000313|Proteomes:UP000002280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17495919; DOI=10.1038/nature05805;
RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT coding sequences.";
RL Nature 447:167-177(2007).
RN [2] {ECO:0000313|Ensembl:ENSMODP00000037545.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Anchors the extracellular matrix to the cytoskeleton via F-
CC actin. Ligand for dystroglycan. Component of the dystrophin-associated
CC glycoprotein complex which accumulates at the neuromuscular junction
CC (NMJ) and at a variety of synapses in the peripheral and central
CC nervous systems and has a structural function in stabilizing the
CC sarcolemma. Also implicated in signaling events and synaptic
CC transmission. {ECO:0000256|ARBA:ARBA00037032}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004278}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034100}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
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DR AlphaFoldDB; F7AQW9; -.
DR STRING; 13616.ENSMODP00000037545; -.
DR Ensembl; ENSMODT00000039143.3; ENSMODP00000037545.3; ENSMODG00000021126.4.
DR eggNOG; KOG4286; Eukaryota.
DR GeneTree; ENSGT00940000154342; -.
DR HOGENOM; CLU_001187_0_1_1; -.
DR InParanoid; F7AQW9; -.
DR OMA; HYEHNSN; -.
DR TreeFam; TF333986; -.
DR Proteomes; UP000002280; Chromosome 4.
DR Bgee; ENSMODG00000021126; Expressed in uterine wall and 19 other cell types or tissues.
DR ExpressionAtlas; F7AQW9; baseline.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0090257; P:regulation of muscle system process; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; IBA:GO_Central.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR CDD; cd16246; EFh_DMD; 1.
DR CDD; cd00176; SPEC; 3.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12268:SF25; DYSTROPHIN; 1.
DR PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 3.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00150; SPEC; 5.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 3.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 607..640
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 860..916
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 1082..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..99
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 474..543
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1048..1082
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1154..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1255 AA; 144701 MW; 2D90B0ECB68A5C63 CRC64;
MPSSLLLEVP ALADFNKAWT ELTDWLSLLD RVIKTQRVMV GDLEDINDMI IKQKLVESIM
NSDLQGATLQ DLEQRRPQLE ELITAAQNLK NKTGNQEART IITDRIEKIQ SQWDEVQEHL
QRRRQQLNEM LKDSAQWLEA KKEAEWTLEK AKTKLESWKE IPYTMEGIRK QSTETKQLAK
DLRQWQINVD VANDLARKLL RDYSTDDTRK VQMITDNINA TWADINKRVN EREAALEAAH
RLLQQFPLDL EKFLAWLTEA ETTANVLQDA THKERILEDT KGVRELMKQW QDLQGEIEAH
TDIFHNLDEN GQKILKSLEG SDDAVLLKRR LDNMNFKWSE LRKKSLNIRS HLEVSSDQWK
RLHLSLQELL VWLQLKDDEL SRQAPIGGDY PAVQQQNDIH RAFKRELKTK EPVITSTLET
VRIFLSEKPL EELEKHYQEP RELPPEERAH NVTRLLRKQA DEVNSEWEKL NLHSVDWQKK
IDEALGRLQD LQEAMDELDL KLRQAEVMRG SWQPVGDLLI DSLQEHLEKV KALRGEIAPL
EENINHVNGL ARQLTTSGIQ LSPYNLNSLE DLNTRWKLLL VAIDERIRQL HEAHRDFGPT
SQHFLSTSVQ GPWERAISPN KVPYYINHET QTTCWDHPKM TELYQSLADL NNVRFSAYRT
AMKLRRLQKA LCLDLLSLSA ACDALDQHNL KQNDQPMDIL QIINCLTTIY DRLEQEHNNL
VNVPLCVDMC LNWLLNVYDT GRTGRIRVLS FKTGVISLCK AHLEDKYRYL FKQVASSMGF
CDQRRLGLLL HDSIQIPRQL GEVASFGGSN IEPSVRSCFQ FANNKPEIEA ALFLDWMRLE
PQSMVWLPVL HRVAAAETAK HQAKCNICKE CPIIGFRYRS LKHFNYDICQ SCFFSGRVAK
GHKMHYPMVE YCTPTTSGED VRDFAKVLKN KFRTKRYFAK HPRMGYLPVQ TVLEGDNMET
PVTLINFWPV DSAPASSPQL SHDDTHSRIE HYASRLAEME NSNGSYLNDS ISPNESIDDE
HLLIQHYCQS LNQESPLSQP RSPAQILISL ESEERGELER ILADLEEENR NLQAEYDRLK
QQHEHKGLSP LPSPPEMMPI SPQSPRDAEL IAEAKLLRQH KGRLEARMQI LEDHNKQLES
QLHRLRQLLE QPQAEAKVNG TTVSSPSTSL QRSDSSQPML LRVVGSQTSE TMGEDDLLSP
PPQDTSTGLE EVMEQLNNSF PSTRGHNVGN LFHMADDLGR AMETLVTVMT DEGLE
//
