ID DMD_RAT Reviewed; 3677 AA.
AC P11530; F1M705;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=Dystrophin;
GN Name=Dmd;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 766-794, AND TISSUE SPECIFICITY.
RX PubMed=3340214; DOI=10.1038/331635a0;
RA Nudel U., Robzyk K., Yaffe D.;
RT "Expression of the putative Duchenne muscular dystrophy gene in
RT differentiated myogenic cell cultures and in the brain.";
RL Nature 331:635-638(1988).
RN [3]
RP INTERACTION WITH DTNB.
RX PubMed=10545507; DOI=10.1083/jcb.147.3.645;
RA Blake D.J., Hawkes R., Benson M.A., Beesley P.W.;
RT "Different dystrophin-like complexes are expressed in neurons and glia.";
RL J. Cell Biol. 147:645-658(1999).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3615 AND SER-3616, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000250|UniProtKB:P11531}.
CC -!- SUBUNIT: Interacts with SYNM (By similarity). Interacts with the
CC syntrophins SNTG1 and SNTG2. Interacts with KRT19. Component of the
CC dystrophin-associated glycoprotein complex which is composed of three
CC subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA
CC and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the
CC transmembrane dystroglycan complex, and the sarcoglycan-sarcospan
CC complex. Interacts with DAG1 (betaDAG1) with DMD; the interaction is
CC inhibited by phosphorylation on the PPXY motif of DAG1 (By similarity).
CC Interacts with SYNM; SNTA1 and SNTB1. Interacts with CMYA5. Directly
CC interacts with ANK2 and ANK3; these interactions do not interfere with
CC betaDAG1-binding and are necessary for proper localization in muscle
CC cells. Identified in a dystroglycan complex that contains at least PRX,
CC DRP2, UTRN, DMD and DAG1 (By similarity). Interacts with DTNB
CC (PubMed:10545507). Interacts with PGM5; the interaction is direct (By
CC similarity). Interacts with NOS1; localizes NOS1 to sarcolemma in
CC muscle cells (By similarity). {ECO:0000250|UniProtKB:P11531,
CC ECO:0000250|UniProtKB:P11532, ECO:0000269|PubMed:10545507}.
CC -!- INTERACTION:
CC P11530; Q63279: Krt19; NbExp=3; IntAct=EBI-706166, EBI-876985;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P11531}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P11531}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P11531}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P11531}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P11531}. Note=In muscle cells, sarcolemma
CC localization requires the presence of ANK2, while localization to
CC costameres requires the presence of ANK3. Localizes to neuromuscular
CC junctions (NMJs). In adult muscle, NMJ localization depends upon ANK2
CC presence, but not in newborn animals. {ECO:0000250|UniProtKB:P11531}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in skeletal muscle and weak
CC expression observed in newborn brain which increases in adult brain.
CC {ECO:0000269|PubMed:3340214}.
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DR EMBL; AABR07073532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC097383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC111223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X07000; CAA30057.1; -; Genomic_DNA.
DR PIR; S01614; S01614.
DR RefSeq; XP_017457399.1; XM_017601910.1.
DR SMR; P11530; -.
DR CORUM; P11530; -.
DR IntAct; P11530; 11.
DR STRING; 10116.ENSRNOP00000029969; -.
DR GlyGen; P11530; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P11530; -.
DR PhosphoSitePlus; P11530; -.
DR jPOST; P11530; -.
DR PaxDb; 10116-ENSRNOP00000029969; -.
DR Ensembl; ENSRNOT00000035692.7; ENSRNOP00000029969.6; ENSRNOG00000046366.3.
DR AGR; RGD:2507; -.
DR RGD; 2507; Dmd.
DR eggNOG; KOG4286; Eukaryota.
DR GeneTree; ENSGT00940000154342; -.
DR InParanoid; P11530; -.
DR OMA; XVATTYP; -.
DR OrthoDB; 2880153at2759; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR PRO; PR:P11530; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000046366; Expressed in quadriceps femoris and 18 other cell types or tissues.
DR ExpressionAtlas; P11530; baseline and differential.
DR GO; GO:0097449; C:astrocyte projection; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0030054; C:cell junction; ISO:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0030055; C:cell-substrate junction; ISO:RGD.
DR GO; GO:0043034; C:costamere; ISO:RGD.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:RGD.
DR GO; GO:0030175; C:filopodium; ISO:RGD.
DR GO; GO:0031527; C:filopodium membrane; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0099617; C:matrix side of mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0030016; C:myofibril; IDA:RGD.
DR GO; GO:0005883; C:neurofilament; IDA:RGD.
DR GO; GO:0044306; C:neuron projection terminus; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0099572; C:postsynaptic specialization; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005840; C:ribosome; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0002162; F:dystroglycan binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; IPI:RGD.
DR GO; GO:0005521; F:lamin binding; IPI:RGD.
DR GO; GO:0017022; F:myosin binding; ISO:RGD.
DR GO; GO:0050998; F:nitric-oxide synthase binding; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0008307; F:structural constituent of muscle; ISO:RGD.
DR GO; GO:0017166; F:vinculin binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0086001; P:cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEP:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0061448; P:connective tissue development; ISO:RGD.
DR GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR GO; GO:0008065; P:establishment of blood-nerve barrier; ISO:RGD.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0060173; P:limb development; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0032504; P:multicellular organism reproduction; ISO:RGD.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISO:RGD.
DR GO; GO:0055001; P:muscle cell development; ISO:RGD.
DR GO; GO:0042692; P:muscle cell differentiation; IEP:RGD.
DR GO; GO:0007517; P:muscle organ development; ISO:RGD.
DR GO; GO:0014904; P:myotube cell development; ISO:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
DR GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; ISO:RGD.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:RGD.
DR GO; GO:0051647; P:nucleus localization; ISO:RGD.
DR GO; GO:0021629; P:olfactory nerve structural organization; ISO:RGD.
DR GO; GO:0043043; P:peptide biosynthetic process; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
DR GO; GO:1903409; P:reactive oxygen species biosynthetic process; ISO:RGD.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISO:RGD.
DR GO; GO:0090287; P:regulation of cellular response to growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0090257; P:regulation of muscle system process; IBA:GO_Central.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0014819; P:regulation of skeletal muscle contraction; ISO:RGD.
DR GO; GO:0014809; P:regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; ISO:RGD.
DR GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IEP:RGD.
DR GO; GO:0035994; P:response to muscle stretch; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEP:RGD.
DR GO; GO:0055002; P:striated muscle cell development; ISO:RGD.
DR GO; GO:0006941; P:striated muscle contraction; ISO:RGD.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; ISO:RGD.
DR GO; GO:0090659; P:walking behavior; ISO:RGD.
DR CDD; cd21231; CH_DMD_rpt1; 1.
DR CDD; cd21233; CH_DMD_rpt2; 1.
DR CDD; cd16246; EFh_DMD; 1.
DR CDD; cd00176; SPEC; 11.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 16.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
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; PF00307; CH; 2.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 17.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 23.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 15.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
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 1: Evidence at protein level;
KW Actin-binding; Calcium; Cell membrane; Cytoplasm; Cytoskeleton; Membrane;
KW Metal-binding; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..3677
FT /note="Dystrophin"
FT /id="PRO_0000076077"
FT DOMAIN 15..119
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 134..240
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 342..447
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 451..557
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 560..668
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 728..828
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 831..935
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 944..1046
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 1049..1154
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 1163..1264
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 1268..1464
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT REPEAT 1469..1569
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1573..1676
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1680..1777
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1779..1875
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1878..1980
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 2001..2098
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 2106..2209
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 2215..2316
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT REPEAT 2317..2415
FT /note="Spectrin 18"
FT /evidence="ECO:0000255"
FT REPEAT 2465..2569
FT /note="Spectrin 19"
FT /evidence="ECO:0000255"
FT REPEAT 2576..2678
FT /note="Spectrin 20"
FT /evidence="ECO:0000255"
FT REPEAT 2682..2786
FT /note="Spectrin 21"
FT /evidence="ECO:0000255"
FT REPEAT 2800..2922
FT /note="Spectrin 22"
FT /evidence="ECO:0000255"
FT REPEAT 2927..3032
FT /note="Spectrin 23"
FT /evidence="ECO:0000255"
FT DOMAIN 3047..3080
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 3300..3356
FT /note="ZZ-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..240
FT /note="Actin-binding"
FT REGION 63..72
FT /note="ANK2- and ANK-3 binding"
FT /evidence="ECO:0000250"
FT REGION 1416..1914
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000250"
FT REGION 3050..3400
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000250"
FT REGION 3458..3510
FT /note="Binds to SNTB1"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT REGION 3520..3546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3595..3677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3595..3664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 3475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
SQ SEQUENCE 3677 AA; 425828 MW; 50526FA367B87FAB CRC64;
MLWWEEVEDC YEREDVQKKT FTKWINAQFS KFGKQHIDNL FSDLQDGKRL LDLLEGLTGQ
KLPKEKGSTR VHALNNVNKA LQVLQKNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV
KNVMKTIMAG LQQTNSEKIL LSWVRESTRN YPQVNVLNFT SSWSDGLALN ALIHSHRPDL
FDWNSVVSQQ SATQRLEHAF NIAKCQLGIE KLLDPEDVAT TYPDKKSILM YITSLFQVLP
QQVSIEAIRE VEMLPRPSKV TREEHFQLHH QMHYSQQITV SLAQGYEQTS SSPKPRFKSY
AFTQAAYVAT SDSSQSPYPS QHLEAPGSKS FGSSLIETEV NLDSYQTALE EVLSWLLSAE
DTLRAQGEIS KDVEEVKEQF HAHEGFMMDL TSHQGLVGNV LQLGSRLVGK GKLTEDEETE
VQEQMNLLNS RWECLRVASM EKQSNLHKVL MDLQNQKLKE LDDWLTKTEE RTKKMEEEPL
GPDLEDLKCQ VQQHKVLQED LEQEQVRVNS LTHMVVVVDE SSGDHATAAL EEQLKVLGDR
WANICKWTED RWILLQDILL KWQRFTEEQC LFSKWLSEKE DAMKNIQTSG FEDQNEMVSS
LQNISALKID LEKKKQSMEK LSSLNQDLLS ALKNKSVTQK MEMWMENFAQ RWDNLTQKLE
KSSAQISQAV TTTQPSLTQT TVMETVTMVT TREQIMVKHA QEELPPPPPQ KKRQITVDSE
IRKRLDVDIT ELHSWITRSE AVLQSSEFAV YRKEGNISDL KEKVNAIARE KAEKFRKLQD
ASRSAQALVE QMVNEGVNAE SIRQASEQLN SRWTEFCQLL SERVNWLEYQ NNIITFYNQL
QQLEQMTTTA ENLLKTQPTT LSEPTAIKSQ LKICKDEVNR LSALQPQIER LKIQSLTLKE
KGQGPMFLDA DFVAFTNHFN YVFDGVRARE KELQTIFDTL PPMRYQETMS SIRTWIQQSE
NKLSIPHLSV TEYEIMEERL GKLQALQSSL KEQQNGFNYL NATVKEIAKK APSEISQKYQ
SEFEEVEGRW KKLSTQLVEH CQKLEEHMNK LRKFQNHKKT LQKWMAEVDV FLKEEWPALG
DAEILKKQLK QCRLLVGDIQ TIQPSLNSVN EGGQKIKSEA EFEFASRLEK ELKELNTQWD
HICRQVYTRK EALKAGLDKT VSLQKDLSEM HEWMTQAEEE YLERDFEYKT PDELQTAVEE
MKRAKEEALQ KEAKVKLLTE TVNSVISQAP PAAQEALKKE LETLTTNYQW LCTRLNGKCK
TLEEVWACWH ELLSYLEKAN KWLNEVELKL KATENVPAGA EEITEVLESL ENLMHHSEEN
PNQIRLLAQT LTDGGVMDEL INEELETFNS RWRELHEEAV RKQKLLEQSI QSAQEIEKSL
HLIQESLEFI DKQLAAYIAD KVDAAQMPQE AQKIQSDLTS HEISLEEMKK HNQGKDANQR
VLSQIDVAQK KLQDVSIKFR LFQKPANFEQ RLEESKMILD EVKMHLPALE TKSVEQEVVQ
SQLSHCVNLY KSLSEVKSEV EMVIKTGRQI VQKKQTENPK ELDERVTALK LHYNELGAKV
TERKQQLEKC LKLSRKMRKE MNVLTEWLAA TDTELTKRSA VEGMPSNLDS EVAWGKATQK
EIEKQKAHLK SVTELGDSLK TVLGKKETLV EDKLTLLNSN WIAVTSRVEE WLNLLLEYQK
HMESFDQNVE HITKWIIHTD ELLDESEKRK PQQKEDILKR LKAEMNDIRP KVDATRDQAA
KLMANRGDYC RKIVEPQISE LNRRFAAISH RIKTGKASIP LKELEQFNSD IQKLLEPLEA
EIQQGVNLKE EDFNKDMSED NEGTVNELLQ RGDNLQQRIT DERKREEIKL KQQLLQTKHN
ALKDLRSQRR KKALEISHQW YQYKSQADDL LKCLDEIEKK LASLPEPRDE RKIKEIDREL
QKKKEELNAV RRQAESLSEN GAAMAVEPTQ IQLSKRWREI ESNFAQFRRL NFAQIHTLHE
ETMVVTTEDM PLDVSYVPST YLTEISHILQ ALSEVEQLLN APELNAKDFE DLFKQEESLK
NIKENLQQIS GRIDVIHKKK TAALQSATPM ERVKLQEAVS QMDFHWEKLN RMYKERQGRF
DRSVEKWRHF HYDMKVFNQW LNDVEQFFKK TQNPENWEHA KYKWYLKELQ DGIGQRQAVV
RTLNATGEEI IQQSSKTDAN ILQEKLGSLS LRWHEVCKEL AERRKRVEEQ KNVFSEFQRD
LNEFVSWLEE ADNIATTPPG DEEQLKEKLE QVKLLTEELP LRQGILKQLN ETGGAVLVSA
PIRPEEQDKL EKKLKQTNLQ WIKVSRALPE KQGELEVHIK DFRQFEEQLD HLLLWLSPIR
NQLEIYNQPS QPGPFDLKET EVTVQAKQPD VERLLSKGQH LYKEKPSTQP VKRKLEDLRS
EWEAVNHLLW ELRTKQPDRA PGLSTTGASA SQTVTVVTQP VDTKETVISK LEMPSSLLLE
VPALADFNRA WTELTDWLSL LDRVIKSQRV MVGDLEDINE MIIKQKATLQ DLEQRRPQLE
ELITAAQNLK NKTSNQEART IITDRIERIQ IQWDEVQEQL QNRRQQLNEM LKDSTQWLEA
KEEAEQVIGQ ARGKLDSWKE GPHTMDAIQK KITETKQLAK DLRQRQINVD VANDLALKLL
RDYSADDTRK VHMITENINT SWGNILKRVS EREAALEETQ RLLQQFPLDL EKFLAWITEA
ETTANVLQDA SRKEKLLEDS RGVRELMKPW QDLQGEIEAH TDIYHNLDEN GQKILRSLEG
SDEAPLLQRR LDNMNFKWSE LRKKSLNIRS HLEVSSDQWK RLHLSLQELL VWLQLKDDEL
SRQAPIGGDF PAVQKQNDVH RAFKRELKTK EPVIMSTLET VRIFLTEQPL EGLEKLYQEP
RELPPEERAQ NVTRLLRKQA EEVNTEWDKL NLHSADWQRK IDEALERLQE LQEAADELDL
KLRQAEVIKG SWQPVGDLLI DSLQDHLEKV KALRGEIAPL KENVNHVNDL AHHLTTLGIQ
LSPYNLSILE DLNTRWRLLQ VAVEDRVRQL HEAHRDFGPA SQHFLSTSVQ GPWERAISPN
KVPYYINHET QTTCWDHPKM TELYQSLADL NNVRFSAYRT AMKLRRLQKA LCLDLLSLSA
ACDALDQHNL KQNDQPMDIL QIINCLTTIY DRLEQEHNNL VNVPLCVDMC LNWLLNVYDT
GRTGRIRVLS FKTGIISLCK AHLEDKYRYL FKQVASSTGF 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 LNQDSPLSQP
RSPAQILISL ESEERGELER ILADLEEENR NLQAEYDRLK QQHEHKGLSP LPSPPEMMPT
SPQSPRDAEL IAEAKLLRQH KGRLEARMQI LEDHNKQLES QLHRLRQLLE QPQAEAKVNG
TTVSSPSTSL QRSDSSQPML LRVVGSQTSE SMGEEDLLSP PQDTSTGLEE VMEQLNNSFP
SSRGRNAPGK PMREDTM
//
