ID   I3LPH8_PIG              Unreviewed;       930 AA.
AC   I3LPH8;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 4.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Dystrophin {ECO:0000313|Ensembl:ENSSSCP00000026005.4};
GN   Name=DMD {ECO:0000313|Ensembl:ENSSSCP00000026005.4};
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:ENSSSCP00000026005.4, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000026005.4, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000026005.4,
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:ENSSSCP00000026005.4}
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}.
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DR   AlphaFoldDB; I3LPH8; -.
DR   PeptideAtlas; I3LPH8; -.
DR   Ensembl; ENSSSCT00000029079.4; ENSSSCP00000026005.4; ENSSSCG00000028148.5.
DR   GeneTree; ENSGT00940000154342; -.
DR   HOGENOM; CLU_001187_1_2_1; -.
DR   Proteomes; UP000008227; Chromosome X.
DR   Bgee; ENSSSCG00000028148; Expressed in skeletal muscle tissue and 44 other cell types or tissues.
DR   ExpressionAtlas; I3LPH8; baseline and differential.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd16246; EFh_DMD; 1.
DR   CDD; cd00176; SPEC; 2.
DR   CDD; cd02334; ZZ_dystrophin; 1.
DR   Gene3D; 1.20.58.60; -; 3.
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; 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; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00150; SPEC; 3.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 2.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          588..644
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          773..799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          847..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          207..241
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        847..918
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   930 AA;  106952 MW;  623D6DC47771D579 CRC64;
     MQQDQCCSPR FKLKMLHRKT YHVKDLQGEI EAHTDIYHNL DENGQKILRS LEGSDDAILL
     QRRLDNMNFK WSELRKKSLN IRSHLEASSD QWKRLHLSLQ ELLVWLQLKD DELSRQAPIG
     GDCPAVQKQN DVHRAFKREL KTKEPVIMST LETVRIFLTE QPLEGLEKLY QEPRELPPEE
     RAQNVTRLLR KQAEEVNTEW EKLNLHSADW QRKIDEALER LQELQEATDE LDLKLRQAEV
     IKGSWQPVGD LLIDSLQDHL EKVKALRGEM APLKENVSHV NDLARQLTTL GIQLSPYNLS
     TLEDLNTRWK LLQVAVEDRI RQLHEAHRDF GPASQHFLST PDRGALAAMR EQLKGHETQT
     TCWDHPKMTE LYQSLADLNN VRFSAYRTAM KLRRLQKALC LDLLSLSAAC DALDQHNLKQ
     NDQPMDILQI INCLTTVYDR LEQEHNNLVN VPLCVDMCLN WLLNVYDTGR TGRIRVLSFK
     TGIVSLCKAH LEDKYRYLFK QVASSTGFCD QRRLGLLLHD SIQIPRQLGE VASFGGSNIE
     PSVRSCFQFA NNKPEIEAAL FLDWMRLEPQ SMVWLPVLHR VAAAETAKHQ AKCNICKECP
     IIGFRYRSLK HFNYDICQSC FFSGRVAKGH KMHYPMVEYC TPTTSGEDVR DFAKVLKNKF
     RTKRYFAKHP RMGYLPVQTV LEGDNMETLA EMENSNGSYL NDSISPNESI DDEHLLIQHY
     CQSLNQDSPL SQPRSPAQIL ISLESEERGE LERILADLEE ENRNLQAEYD RLKQQHEHKG
     LSPLPSPPEM MPTSPQSPRD AELIAEAKLL RQHKGRLEAR MQILEDHNKQ LESQLHRLRQ
     LLEQPQAEAK VNGTTVSSPS TSLQRSDSSQ PMLLRVVGSQ TSESMGEEDL LSPPQDTNTG
     LEEVMEQLNN SFPSSRGRNT PGKPVREDTM
//