ID I3LG08_PIG Unreviewed; 2334 AA.
AC I3LG08;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 5.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Dystrophin {ECO:0000256|ARBA:ARBA00040142};
GN Name=DMD {ECO:0000313|Ensembl:ENSSSCP00000023001.5};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000023001.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000023001.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000023001.5,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000023001.5}
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}. Cytoplasm, cytoskeleton
CC {ECO:0000256|PIRNR:PIRNR002341}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034100}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
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DR PeptideAtlas; I3LG08; -.
DR Ensembl; ENSSSCT00000026041.5; ENSSSCP00000023001.5; ENSSSCG00000028148.5.
DR GeneTree; ENSGT00940000154342; -.
DR HOGENOM; CLU_280408_0_0_1; -.
DR Proteomes; UP000008227; Chromosome X.
DR Bgee; ENSSSCG00000028148; Expressed in skeletal muscle tissue and 44 other cell types or tissues.
DR ExpressionAtlas; I3LG08; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16246; EFh_DMD; 1.
DR CDD; cd00176; SPEC; 5.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 10.
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; IPR035436; Dystrophin/utrophin.
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; 10.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR SMART; SM00150; SPEC; 13.
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; 10.
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 Actin-binding {ECO:0000256|PIRNR:PIRNR002341};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR002341}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR002341};
KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR002341};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002341};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Postsynaptic cell membrane {ECO:0000256|PIRNR:PIRNR002341};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|PIRNR:PIRNR002341};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 1704..1737
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1957..2013
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 2177..2203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2251..2334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 568..595
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 845..875
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1152..1196
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1571..1605
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2251..2322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2334 AA; 270083 MW; 6A080FC724B0F6EE CRC64;
MSGRKLRNLS YKKAVRRQKL LEQSIQSAQE IEKSLHLIQD SLSSIDHQLA VYIADKVDAA
QMPQEAQKIQ SDLTSHEISL EEMKKHYQGK EAAPRVLSQI ELAQKKLQDV SMKFRLFQKP
ANFEQRLQES KMILDEVKMH LPALEIKSVE QEVVQSQLNH CVNLYKSLSE VKSEVEMVIK
TGRQIVQKKQ TENPKELDER VTALKLHYNE LGAKVTERKQ QLEKCLKLSR KMRKEMNVLT
EWLAATDTEL TKRSAVEGMP SNLDSEVVWG KATQKEIEKQ KFHLKSISEI GEALKMVLGK
KETLVEDKLS LLNSNWIAVT SRAEEWLNLL LEYQKHMENF DQNVDHITKW IIQADTLLDE
SEKKKPQQKE DVLKRLKAEM NDMRPKVDST RDQAANLMAN RGDHCRKVIE PKISELNHRF
AAISHRIKTG KASIPLKELE QFNSDIQKLL EPLEAEIQQG VNLKEEDFNK DMSEDNEGTV
KELLQRGDNL QQRITDERKR EEIKIKQQLL QTKHNALKDL RSQRRKKALE ISHQWYQYKR
QADDLLKCLD DIEKKLASLP EPQDEKKIKE IDRELQKKKE ELDAVRRQAE GLSEDGAAMA
VEPTQIQLSK RWREIESKFA HFRRLNFAQI HTVHEESVMV MTEDMPLEIS YVPSAYLTEI
THVSQALSEV EQLLNAPDLC AKDFEDLFKQ EESLKNIKDS LQQISGRVDI IHNKKTAGLQ
SATPVERTRL QEALSQLDFQ WERVNKMYKD RQGKFDRSVE KWRRFHYDMK IFNQWLTEAE
HFLKKTQIPE NWEHAKYKWY LKELQDGIGQ RQTIVRVLNA TGEEVIQQSS KTDASILQEK
LGSLNLRWQE VCKQLAERKK RLEEQKNILS EFQRDLNEFV LWLEEADNIT SVALEPGNEQ
QLKEKLEEIK LLAEELPLRQ GILKQLNETG GTVLVSAPIS PEEQDKIENK LKQTNLQWIK
VSRILPEKQG EIEAHIKDLG QLEEQLNHLL VWLSPIKNQL EIYNQPNQTG PFDIKETEVA
VQAKQPDVEG ILSKGQHLYK EKPATQPVKR KLEDLSSEWK AVTHLLQELR AKWPGPTPGL
TTIEAPTSQT VTLVTQPTVT KETAISKPEM PSSLLLEVPA LADFNRAWTE LTDWLSLLDR
VIKSQRVMVG DLEDINEMII KQKATLQDLE QRRPQLEELI TAAQNLKNKT SNQEARTIIT
DRIERIQSQW DEVQEHLQNR RQQLNEMLKD STQWLEAKEE AEQVLGQARA KLESWKEGPY
TMDAIQRKIT ETKQLAKDLR QWQINVDVAN DLALKLLRDY SADDTRKVHM ITENINASWA
NIHKRLSERE TVLEETHRLL QQFPLDLEKF LAWLTEAETT ANVLQDATHK ERLLEDSKGV
RELMKQWQDL QGEIEAHTDI YHNLDENGQK ILRSLEGSDD AILLQRRLDN MNFKWSELRK
KSLNIRSHLE ASSDQWKRLH LSLQELLVWL QLKDDELSRQ APIGGDCPAV QKQNDVHRAF
KRELKTKEPV IMSTLETVRI FLTEQPLEGL EKLYQEPREL PPEERAQNVT RLLRKQAEEV
NTEWEKLNLH SADWQRKIDE ALERLQELQE ATDELDLKLR QAEVIKGSWQ PVGDLLIDSL
QDHLEKVKAL RGEMAPLKEN VSHVNDLARQ LTTLGIQLSP YNLSTLEDLN TRWKLLQVAV
EDRIRQLHEA HRDFGPASQH FLSTSVQGPW ERAISPNKVP YYINHETQTT CWDHPKMTEL
YQSLADLNNV RFSAYRTAMK LRRLQKALCL DLLSLSAACD ALDQHNLKQN DQPMDILQII
NCLTTVYDRL EQEHNNLVNV PLCVDMCLNW LLNVYDTGRT GRIRVLSFKT GIVSLCKAHL
EDKYRYLFKQ VASSTGFCDQ RRLGLLLHDS IQIPRQLGEV ASFGGSNIEP SVRSCFQFAN
NKPEIEAALF LDWMRLEPQS MVWLPVLHRV AAAETAKHQA KCNICKECPI IGFRYRSLKH
FNYDICQSCF FSGRVAKGHK MHYPMVEYCT PTTSGEDVRD FAKVLKNKFR TKRYFAKHPR
MGYLPVQTVL EGDNMETPVT LINFWPVDSA PASSPQLSHD DTHSRIEHYA SRLAEMENSN
GSYLNDSISP NESIDDEHLL IQHYCQSLNQ DSPLSQPRSP AQILISLESE ERGELERILA
DLEEENRNLQ AEYDRLKQQH EHKGLSPLPS PPEMMPTSPQ SPRDAELIAE AKLLRQHKGR
LEARMQILED HNKQLESQLH RLRQLLEQPQ AEAKVNGTTV SSPSTSLQRS DSSQPMLLRV
VGSQTSESMG EEDLLSPPQD TNTGLEEVME QLNNSFPSSR GRNTPGKPVR EDTM
//
