ID OBSCN_HUMAN Reviewed; 7968 AA.
AC Q5VST9; Q2A664; Q5T7G8; Q5T7G9; Q5VSU2; Q86YC7; Q8NHN0; Q8NHN1;
AC Q8NHN2; Q8NHN3; Q8NHN4; Q8NHN5; Q8NHN6; Q8NHN7; Q8NHN8; Q8NHN9;
AC Q96AA2; Q9HCD3; Q9HCL6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 01-MAY-2013, entry version 111.
DE RecName: Full=Obscurin;
DE EC=2.7.11.1;
DE AltName: Full=Obscurin-RhoGEF;
DE AltName: Full=Obscurin-myosin light chain kinase;
DE Short=Obscurin-MLCK;
GN Name=OBSCN; Synonyms=KIAA1556, KIAA1639;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), VARIANTS THR-51;
RP ARG-502; ASP-1508 THR-3300; ARG-4381; ARG-4450 AND HIS-4534, FUNCTION,
RP AND INTERACTION WITH TTN AND CALMODULIN.
RC TISSUE=Heart;
RX PubMed=11448995; DOI=10.1083/jcb.200102110;
RA Young P.W., Ehler E., Gautel M.;
RT "Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor
RT protein involved in sarcomere assembly.";
RL J. Cell Biol. 154:123-136(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2734-4428 (ISOFORM 5), AND
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6009-7968 (ISOFORM 1).
RC TISSUE=Cardiac myocyte;
RX PubMed=16625316; DOI=10.1007/s10974-005-9025-6;
RA Fukuzawa A., Idowu S., Gautel M.;
RT "Complete human gene structure of obscurin: implications for isoform
RT generation by differential splicing.";
RL J. Muscle Res. Cell Motil. 26:427-434(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5386-7968 (ISOFORM 2),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2726-7968 (ISOFORM 4), AND
RP VARIANT VAL-7172.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes.
RT XVIII. The complete sequences of 100 new cDNA clones from brain which
RT code for large proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [5]
RP INTERACTION WITH TTN.
RX PubMed=11717165;
RA Bang M.-L., Centner T., Fornoff F., Geach A.J., Gotthardt M.,
RA McNabb M., Witt C.C., Labeit D., Gregorio C.C., Granzier H.,
RA Labeit S.;
RT "The complete gene sequence of titin, expression of an unusual ~700
RT kDa titin isoform and its interaction with obscurin identify a novel
RT Z-line to I-band linking system.";
RL Circ. Res. 89:1065-1072(2001).
RN [6]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=11814696; DOI=10.1016/S0378-1119(01)00795-8;
RA Russell M.W., Raeker M.O., Korytkowski K.A., Sonneman K.J.;
RT "Identification, tissue expression and chromosomal localization of
RT human obscurin-MLCK, a member of the titin and Dbl families of myosin
RT light chain kinases.";
RL Gene 282:237-246(2002).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ANK1.
RX PubMed=12527750; DOI=10.1083/jcb.200208109;
RA Bagnato P., Barone V., Giacomello E., Rossi D., Sorrentino V.;
RT "Binding of an ankyrin-1 isoform to obscurin suggests a molecular link
RT between the sarcoplasmic reticulum and myofibrils in striated
RT muscles.";
RL J. Cell Biol. 160:245-253(2003).
RN [8]
RP CHROMOSOMAL TRANSLOCATION WITH PTHB1.
RX PubMed=12618763; DOI=10.1038/sj.onc.1206332;
RA Vernon E.G., Malik K., Reynolds P., Powlesland R., Dallosso A.R.,
RA Jackson S., Henthorn K., Green E.D., Brown K.W.;
RT "The parathyroid hormone-responsive B1 gene is interrupted by a
RT t(1;7)(q42;p15) breakpoint associated with Wilms' tumour.";
RL Oncogene 22:1371-1380(2003).
RN [9]
RP FUNCTION.
RX PubMed=16205939; DOI=10.1007/s00418-005-0069-x;
RA Borisov A.B., Sutter S.B., Kontrogianni-Konstantopoulos A.,
RA Bloch R.J., Westfall M.V., Russell M.W.;
RT "Essential role of obscurin in cardiac myofibrillogenesis and
RT hypertrophic response: evidence from small interfering RNA-mediated
RT gene silencing.";
RL Histochem. Cell Biol. 125:227-238(2006).
RN [10]
RP STRUCTURE BY NMR OF 2826-3806.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the Ig domains of human obscurin.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [11]
RP STRUCTURE BY NMR OF 5601-5668.
RA Pfuhl M., Gautel M.;
RT "Solution structure of the SH3 domain of obscurin.";
RL Submitted (APR-2005) to the PDB data bank.
RN [12]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-1136; HIS-1792; MET-1930;
RP LYS-2090; PHE-2314; GLN-3983; HIS-4558; GLN-4810 AND THR-5071.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
RN [13]
RP VARIANTS [LARGE SCALE ANALYSIS] ARG-502; SER-804; ARG-1027; SER-1086;
RP THR-1090; THR-1091; PRO-1101; ARG-1121; VAL-1133; VAL-1136; GLN-1156;
RP HIS-1248; VAL-1532; MET-1566; THR-1601; VAL-3389; GLU-3426; GLY-3834;
RP SER-4823; GLN-5598 AND GLN-6473.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Involved in myofibrillogenesis. Seems to be involved in
CC assembly of myosin into sarcomeric A bands in striated muscle.
CC Isoform 3 together with ANK1 isoform Mu17/Ank1.5 may provide a
CC molecular link between the sarcoplasmic reticulum and myofibrils.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- SUBUNIT: Isoform 3 interacts with TTN/titin, ANK1 isoform
CC Mu17/ank1.5, and with calmodulin in a Ca(2+)-independent manner.
CC Associates with fast skeletal muscle myosin (By similarity).
CC -!- INTERACTION:
CC P16157:ANK1; NbExp=3; IntAct=EBI-941921, EBI-941686;
CC P16157-17:ANK1; NbExp=8; IntAct=EBI-941921, EBI-941819;
CC Q8WZ42:TTN; NbExp=4; IntAct=EBI-941850, EBI-681210;
CC -!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, myofibril, sarcomere,
CC M line. Cytoplasm, myofibril, sarcomere, Z line. Note=In
CC differentiating skeletal muscle cells, isoform 3 primarily
CC localizes to the sarcomeric M-line and less frequently to the Z-
CC disk. Isoform 3 colocalizes with ANK1 isoform Mu17/ank1.5 at the
CC M-line in differentiated skeletal muscle cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist;
CC Name=1; Synonyms=B, obscurin-MLCK giant kinase;
CC IsoId=Q5VST9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VST9-2; Sequence=VSP_018436;
CC Name=3; Synonyms=unc-89-like;
CC IsoId=Q5VST9-3; Sequence=VSP_018437, VSP_018438;
CC Note=Lacks the kinase domain. Initially described as obscurin;
CC Name=4;
CC IsoId=Q5VST9-5; Sequence=VSP_020086, VSP_020087;
CC Note=No experimental confirmation available. Ref.4 (BAB13382)
CC sequence differs from that shown due to frameshifts in positions
CC 3891, 5061, 5093, 5268, 6352 and 6919;
CC Name=5;
CC IsoId=Q5VST9-6; Sequence=VSP_026970;
CC -!- DISEASE: Note=A chromosomal aberration involving OBSCN has been
CC found in Wilms tumor. Translocation t(1;7)(q42;p15) with PTHB1.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC Ser/Thr protein kinase family.
CC -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC -!- SIMILARITY: Contains 4 fibronectin type-III domains.
CC -!- SIMILARITY: Contains 55 Ig-like (immunoglobulin-like) domains.
CC -!- SIMILARITY: Contains 1 IQ domain.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 2 protein kinase domains.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- CAUTION: Initially the name obscurin was used to describe isoform
CC 3 which lacks the kinase domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC85746.1; Type=Erroneous gene model prediction;
CC Sequence=CAC85749.1; Type=Erroneous gene model prediction;
CC Sequence=CAC85750.1; Type=Erroneous gene model prediction;
CC Sequence=CAH71670.2; Type=Erroneous gene model prediction;
CC Sequence=CAI19283.1; Type=Erroneous gene model prediction;
CC Sequence=CAI19284.1; Type=Erroneous gene model prediction;
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DR EMBL; AJ002535; CAC44768.1; -; mRNA.
DR EMBL; AJ314896; CAC85745.1; -; Genomic_DNA.
DR EMBL; AJ314898; CAC85746.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ314900; CAC85747.1; -; Genomic_DNA.
DR EMBL; AJ314901; CAC85749.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ314903; CAC85750.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ314904; CAC85751.1; -; Genomic_DNA.
DR EMBL; AJ314905; CAC85752.1; -; Genomic_DNA.
DR EMBL; AJ314906; CAC85753.1; -; Genomic_DNA.
DR EMBL; AJ314907; CAC85754.1; -; Genomic_DNA.
DR EMBL; AJ314908; CAC85755.1; -; Genomic_DNA.
DR EMBL; AL670729; CAH71673.1; -; Genomic_DNA.
DR EMBL; AL353593; CAH71673.1; JOINED; Genomic_DNA.
DR EMBL; AL359510; CAH71673.1; JOINED; Genomic_DNA.
DR EMBL; AL359510; CAI15072.1; -; Genomic_DNA.
DR EMBL; AL670729; CAI15072.1; JOINED; Genomic_DNA.
DR EMBL; AL353593; CAI15072.1; JOINED; Genomic_DNA.
DR EMBL; AL353593; CAI19283.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL353593; CAI19284.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL353593; CAI19285.1; -; Genomic_DNA.
DR EMBL; AL670729; CAI19285.1; JOINED; Genomic_DNA.
DR EMBL; AL359510; CAI19285.1; JOINED; Genomic_DNA.
DR EMBL; AL670729; CAH71670.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AM231061; CAJ76912.1; -; mRNA.
DR EMBL; AB046776; BAB13382.1; ALT_FRAME; mRNA.
DR EMBL; AB046859; BAB13465.2; -; mRNA.
DR IPI; IPI00288940; -.
DR IPI; IPI00479915; -.
DR IPI; IPI00742748; -.
DR IPI; IPI00744119; -.
DR IPI; IPI00854629; -.
DR RefSeq; NP_001092093.2; NM_001098623.2.
DR RefSeq; NP_443075.3; NM_052843.3.
DR UniGene; Hs.650039; -.
DR UniGene; Hs.656999; -.
DR PDB; 1V1C; NMR; -; A=5601-5668.
DR PDB; 2CR6; NMR; -; A=2999-3100.
DR PDB; 2DKU; NMR; -; A=2915-3004.
DR PDB; 2DM7; NMR; -; A=3801-3887.
DR PDB; 2E7B; NMR; -; A=3184-3273.
DR PDB; 2EDF; NMR; -; A=2826-2915.
DR PDB; 2EDH; NMR; -; A=3614-3714.
DR PDB; 2EDL; NMR; -; A=3801-3887.
DR PDB; 2EDQ; NMR; -; A=3713-3806.
DR PDB; 2EDR; NMR; -; A=3361-3449.
DR PDB; 2EDT; NMR; -; A=3449-3537.
DR PDB; 2EDW; NMR; -; A=3537-3630.
DR PDB; 2ENY; NMR; -; A=2735-2825.
DR PDB; 2EO1; NMR; -; A=1623-1712.
DR PDB; 2GQH; NMR; -; A=3718-3807.
DR PDB; 2YZ8; X-ray; 2.00 A; A=3184-3273.
DR PDBsum; 1V1C; -.
DR PDBsum; 2CR6; -.
DR PDBsum; 2DKU; -.
DR PDBsum; 2DM7; -.
DR PDBsum; 2E7B; -.
DR PDBsum; 2EDF; -.
DR PDBsum; 2EDH; -.
DR PDBsum; 2EDL; -.
DR PDBsum; 2EDQ; -.
DR PDBsum; 2EDR; -.
DR PDBsum; 2EDT; -.
DR PDBsum; 2EDW; -.
DR PDBsum; 2ENY; -.
DR PDBsum; 2EO1; -.
DR PDBsum; 2GQH; -.
DR PDBsum; 2YZ8; -.
DR ProteinModelPortal; Q5VST9; -.
DR DIP; DIP-35727N; -.
DR IntAct; Q5VST9; 7.
DR MINT; MINT-254901; -.
DR PhosphoSite; Q5VST9; -.
DR DMDM; 215274225; -.
DR PaxDb; Q5VST9; -.
DR PRIDE; Q5VST9; -.
DR Ensembl; ENST00000284548; ENSP00000284548; ENSG00000154358.
DR Ensembl; ENST00000422127; ENSP00000409493; ENSG00000154358.
DR GeneID; 84033; -.
DR KEGG; hsa:84033; -.
DR UCSC; uc001hsn.3; human.
DR UCSC; uc009xez.1; human.
DR CTD; 84033; -.
DR GeneCards; GC01P228395; -.
DR H-InvDB; HIX0001664; -.
DR H-InvDB; HIX0159663; -.
DR H-InvDB; HIX0159975; -.
DR H-InvDB; HIX0160154; -.
DR HGNC; HGNC:15719; OBSCN.
DR HPA; HPA019497; -.
DR HPA; HPA021186; -.
DR MIM; 608616; gene.
DR neXtProt; NX_Q5VST9; -.
DR PharmGKB; PA31888; -.
DR eggNOG; COG0515; -.
DR HOVERGEN; HBG108206; -.
DR InParanoid; Q5VST9; -.
DR OMA; CEVGQEK; -.
DR Reactome; REACT_111102; Signal Transduction.
DR EvolutionaryTrace; Q5VST9; -.
DR GenomeRNAi; 84033; -.
DR NextBio; 73174; -.
DR ArrayExpress; Q5VST9; -.
DR Bgee; Q5VST9; -.
DR Genevestigator; Q5VST9; -.
DR GermOnline; ENSG00000154358; Homo sapiens.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031430; C:M band; ISS:BHF-UCL.
DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0008307; F:structural constituent of muscle; NAS:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0034613; P:cellular protein localization; ISS:BHF-UCL.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR GO; GO:0048011; P:nerve growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0045214; P:sarcomere organization; TAS:BHF-UCL.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.10; -; 60.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR020675; Myosin_light_ch_kinase-rel.
DR InterPro; IPR020682; Obscurin-myosin_light-ch_kin.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR000719; Prot_kinase_cat_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR22964; PTHR22964; 1.
DR PANTHER; PTHR22964:SF11; PTHR22964:SF11; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 48.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 33.
DR SMART; SM00408; IGc2; 20.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; DH-domain; 1.
DR SUPFAM; SSF49265; FN_III-like; 3.
DR SUPFAM; SSF56112; Kinase_like; 2.
DR SUPFAM; SSF50044; SH3; 1.
DR PROSITE; PS00741; DH_1; FALSE_NEG.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 47.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50002; SH3; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Chromosomal rearrangement; Complete proteome; Cytoplasm;
KW Developmental protein; Differentiation; Disulfide bond;
KW Immunoglobulin domain; Kinase; Magnesium; Metal-binding;
KW Muscle protein; Nucleotide-binding; Polymorphism; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; SH3 domain; Transferase.
FT CHAIN 1 7968 Obscurin.
FT /FTId=PRO_0000235298.
FT DOMAIN 10 100 Ig-like 1.
FT DOMAIN 110 202 Ig-like 2.
FT DOMAIN 236 322 Ig-like 3.
FT DOMAIN 331 414 Ig-like 4.
FT DOMAIN 420 508 Ig-like 5.
FT DOMAIN 512 607 Fibronectin type-III 1.
FT DOMAIN 619 698 Ig-like 6.
FT DOMAIN 701 790 Ig-like 7.
FT DOMAIN 798 884 Ig-like 8.
FT DOMAIN 886 977 Ig-like 9.
FT DOMAIN 978 1066 Ig-like 10.
FT DOMAIN 1070 1161 Ig-like 11.
FT DOMAIN 1162 1252 Ig-like 12.
FT DOMAIN 1254 1345 Ig-like 13.
FT DOMAIN 1346 1432 Ig-like 14.
FT DOMAIN 1438 1524 Ig-like 15.
FT DOMAIN 1530 1621 Ig-like 16.
FT DOMAIN 1622 1719 Ig-like 17.
FT DOMAIN 1731 1808 Fibronectin type-III 2.
FT DOMAIN 1809 1894 Ig-like 18.
FT DOMAIN 1896 1982 Ig-like 19.
FT DOMAIN 1987 2071 Ig-like 20.
FT DOMAIN 2077 2162 Ig-like 21.
FT DOMAIN 2165 2249 Ig-like 22.
FT DOMAIN 2289 2380 Ig-like 23.
FT DOMAIN 2468 2559 Ig-like 24.
FT DOMAIN 2564 2643 Ig-like 25.
FT DOMAIN 2646 2730 Ig-like 26.
FT DOMAIN 2736 2823 Ig-like 27.
FT DOMAIN 2826 2908 Ig-like 28.
FT DOMAIN 2920 2999 Ig-like 29.
FT DOMAIN 3003 3092 Ig-like 30.
FT DOMAIN 3095 3183 Ig-like 31.
FT DOMAIN 3184 3268 Ig-like 32.
FT DOMAIN 3273 3356 Ig-like 33.
FT DOMAIN 3359 3444 Ig-like 34.
FT DOMAIN 3449 3532 Ig-like 35.
FT DOMAIN 3537 3620 Ig-like 36.
FT DOMAIN 3625 3708 Ig-like 37.
FT DOMAIN 3713 3796 Ig-like 38.
FT DOMAIN 3801 3884 Ig-like 39.
FT DOMAIN 3890 3973 Ig-like 40.
FT DOMAIN 3978 4062 Ig-like 41.
FT DOMAIN 4068 4160 Ig-like 42.
FT DOMAIN 4171 4239 Ig-like 43.
FT DOMAIN 4248 4337 Ig-like 44.
FT DOMAIN 4340 4427 Ig-like 45.
FT DOMAIN 4430 4518 Ig-like 46.
FT DOMAIN 4523 4614 Fibronectin type-III 3.
FT DOMAIN 4624 4714 Ig-like 47.
FT DOMAIN 4872 4901 IQ.
FT DOMAIN 4898 4989 Ig-like 48.
FT DOMAIN 5126 5215 Ig-like 49.
FT DOMAIN 5260 5349 Ig-like 50.
FT DOMAIN 5371 5467 Ig-like 51.
FT DOMAIN 5601 5668 SH3.
FT DOMAIN 5693 5877 DH.
FT DOMAIN 5895 6004 PH.
FT DOMAIN 6014 6097 Ig-like 52.
FT DOMAIN 6108 6200 Ig-like 53.
FT DOMAIN 6357 6445 Ig-like 54.
FT DOMAIN 6468 6721 Protein kinase 1.
FT DOMAIN 7463 7552 Ig-like 55.
FT DOMAIN 7557 7644 Fibronectin type-III 4.
FT DOMAIN 7672 7924 Protein kinase 2.
FT NP_BIND 6474 6482 ATP (By similarity).
FT NP_BIND 7678 7686 ATP (By similarity).
FT COMPBIAS 192 198 Poly-Ala.
FT COMPBIAS 710 713 Poly-Ala.
FT COMPBIAS 931 934 Poly-Ser.
FT COMPBIAS 1115 1118 Poly-Ser.
FT COMPBIAS 1207 1210 Poly-Ser.
FT COMPBIAS 1299 1302 Poly-Ser.
FT COMPBIAS 1391 1394 Poly-Ser.
FT COMPBIAS 1575 1578 Poly-Ser.
FT COMPBIAS 1667 1670 Poly-Ser.
FT COMPBIAS 4398 4401 Poly-Leu.
FT COMPBIAS 4846 4849 Poly-Gln.
FT COMPBIAS 6789 6796 Poly-Ser.
FT COMPBIAS 6969 7117 Pro-rich.
FT ACT_SITE 6587 6587 Proton acceptor (By similarity).
FT ACT_SITE 7791 7791 Proton acceptor (By similarity).
FT BINDING 6497 6497 ATP (By similarity).
FT BINDING 7701 7701 ATP (By similarity).
FT DISULFID 31 82 By similarity.
FT DISULFID 259 311 By similarity.
FT DISULFID 354 404 By similarity.
FT DISULFID 819 870 By similarity.
FT DISULFID 912 962 By similarity.
FT DISULFID 1004 1054 By similarity.
FT DISULFID 1096 1146 By similarity.
FT DISULFID 1188 1238 By similarity.
FT DISULFID 1280 1330 By similarity.
FT DISULFID 1372 1422 By similarity.
FT DISULFID 1464 1514 By similarity.
FT DISULFID 1556 1606 By similarity.
FT DISULFID 1648 1698 By similarity.
FT DISULFID 1723 1791 By similarity.
FT DISULFID 1830 1880 By similarity.
FT DISULFID 2187 2237 By similarity.
FT DISULFID 2311 2361 By similarity.
FT DISULFID 2490 2540 By similarity.
FT DISULFID 2668 2718 By similarity.
FT DISULFID 2848 2898 By similarity.
FT DISULFID 2937 2987 By similarity.
FT DISULFID 3117 3167 By similarity.
FT DISULFID 3206 3256 By similarity.
FT DISULFID 3295 3344 By similarity.
FT DISULFID 3383 3432 By similarity.
FT DISULFID 3471 3520 By similarity.
FT DISULFID 3559 3608 By similarity.
FT DISULFID 3647 3696 By similarity.
FT DISULFID 3735 3784 By similarity.
FT DISULFID 3823 3872 By similarity.
FT DISULFID 3911 3961 By similarity.
FT DISULFID 4000 4050 By similarity.
FT DISULFID 4089 4141 By similarity.
FT DISULFID 4453 4508 By similarity.
FT DISULFID 4919 4971 By similarity.
FT DISULFID 5147 5199 By similarity.
FT DISULFID 6035 6087 By similarity.
FT DISULFID 6129 6182 By similarity.
FT DISULFID 7484 7536 By similarity.
FT VAR_SEQ 3886 3886 R -> RALPARFTQDLKTKEASEGATATLQCELSKVAPVEW
FT KKGPETLRDGGRYSLKQDGTRCELQIHDLSVADAGEYSCMC
FT GQERTSATLTVRALPARFTEGLRNEEAMEGATATLQCELSK
FT AAPVEWRKGLEALRDGDKYSLRQDGAVCELQIHGLAMADNG
FT VYSCVCGQERTSATLTVRALPARFIEDMRNQKATEGATVTL
FT QCKLRKAAPVEWRKGPNTLKDGDRYSLKQDGTSCELQIRGL
FT VIADAGEYSCICEQERTSATLTVRALPARFIEDVRNHEATE
FT GATAVLQCELSKAAPVEWRKGSETLRDGDRYSLRQDGTRCE
FT LQIRGLAVEDTGEYLCVCGQERTSATLTVRALPARFIDNMT
FT NQEAREGATATLHCELSKVAPVEWRKGPETLRDGDRHSLRQ
FT DGTRCELQIRGLSVADAGEYSCVCGQERTSATLTIREATEG
FT ATAMLQCELSKVAPVEWRKGPETLRDGDRYNLRQDGTRCEL
FT QIHGLSVADTGEYSCVCGQEKTSATLTVK (in isoform
FT 5).
FT /FTId=VSP_026970.
FT VAR_SEQ 3888 3913 PQPVFREPLQSLQAEEGSTATLQCEL -> LPARIHSRSED
FT QGGLRRGHSYTAV (in isoform 4).
FT /FTId=VSP_020086.
FT VAR_SEQ 3914 7968 Missing (in isoform 4).
FT /FTId=VSP_020087.
FT VAR_SEQ 5753 5753 S -> SS (in isoform 2).
FT /FTId=VSP_018436.
FT VAR_SEQ 6221 6620 DTTLERADQEVTSVLKRLLGPKAPGPSTGDLTGPGPCPRGA
FT PALQETGSQPPVTGTSEAPAVPPRVPQPLLHEGPEQEPEAI
FT ARAQEWTVPIRMEGAAWPGAGTGELLWDVHSHVVRETTQRT
FT YTYQAIDTHTARPPSMQVTIEDVQAQTGGTAQFEAIIEGDP
FT QPSVTWYKDSVQLVDSTRLSQQQEGTTYSLVLRHVASKDAG
FT VYTCLAQNTGGQVLCKAELLVLGGDNEPDSEKQSHRRKLHS
FT FYEVKEEIGRGVFGFVKRVQHKGNKILCAAKFIPLRSRTRA
FT QAYRERDILAALSHPLVTGLLDQFETRKTLILILELCSSEE
FT LLDRLYRKGVVTEAEVKVYIQQLVEGLHYLHSHGVLHLDIK
FT PSNILMVHPAREDIKICDFGFAQNITPAELQ -> VTEQET
FT KVPKKTVIIEETITTVVKSPRGQRRSPSKSPSRSPSRCSAS
FT PLRPGLLAPDLLYLPGAGQPRRPEAEPGQKPVVPTLYVTEA
FT EAHSPALPGLSGPQPKWVEVEETIEVRVKKMGPQGVSPTTE
FT VPRSSSGHLFTLPGATPGGDPNSNNSNNKLLAQEAWAQGTA
FT MVGVREPLVFRVDARGSVDWAASGMGSLEEEGTMEEAGEEE
FT GEDGDAFVTEESQDTHSLGDRDPKILTHNGRMLTLADLEDY
FT VPGEGETFHCGGPGPGAPDDPPCEVSVIQREIGEPTVGQPV
FT LLSVGHALGPRGPLGLFRPEPRGASPPGPQVRSLEGTSFLL
FT REAPARPVGSAPWTQSFCTRIRRSADSGQSSFTTELSTQTV
FT NFGTVGETVTLHICPDRDGDEAAQP (in isoform 3).
FT /FTId=VSP_018437.
FT VAR_SEQ 6621 7968 Missing (in isoform 3).
FT /FTId=VSP_018438.
FT VARIANT 51 51 A -> T (in dbSNP:rs1771487).
FT /FTId=VAR_026409.
FT VARIANT 502 502 Q -> R (in dbSNP:rs1771487).
FT /FTId=VAR_034618.
FT VARIANT 804 804 G -> S (in dbSNP:rs55950009).
FT /FTId=VAR_042276.
FT VARIANT 908 908 A -> T (in dbSNP:rs1757153).
FT /FTId=VAR_047743.
FT VARIANT 1027 1027 K -> R (in dbSNP:rs55760713).
FT /FTId=VAR_042277.
FT VARIANT 1086 1086 A -> S.
FT /FTId=VAR_042278.
FT VARIANT 1090 1090 A -> T.
FT /FTId=VAR_042279.
FT VARIANT 1091 1091 S -> T.
FT /FTId=VAR_042280.
FT VARIANT 1101 1101 A -> P.
FT /FTId=VAR_042281.
FT VARIANT 1121 1121 G -> R.
FT /FTId=VAR_042282.
FT VARIANT 1133 1133 L -> V.
FT /FTId=VAR_042283.
FT VARIANT 1136 1136 A -> V (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035530.
FT VARIANT 1156 1156 H -> Q.
FT /FTId=VAR_042284.
FT VARIANT 1248 1248 Q -> H.
FT /FTId=VAR_042285.
FT VARIANT 1508 1508 V -> D (in dbSNP:rs7532342).
FT /FTId=VAR_034619.
FT VARIANT 1532 1532 A -> V (in dbSNP:rs453140).
FT /FTId=VAR_042286.
FT VARIANT 1566 1566 T -> M (in dbSNP:rs56217040).
FT /FTId=VAR_042287.
FT VARIANT 1601 1601 A -> T (in dbSNP:rs55706639).
FT /FTId=VAR_042288.
FT VARIANT 1792 1792 R -> H (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035531.
FT VARIANT 1930 1930 V -> M (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035532.
FT VARIANT 2090 2090 E -> K (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035533.
FT VARIANT 2106 2106 D -> E (in dbSNP:rs1188721).
FT /FTId=VAR_047744.
FT VARIANT 2116 2116 F -> L (in dbSNP:rs1188722).
FT /FTId=VAR_047745.
FT VARIANT 2314 2314 S -> F (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035534.
FT VARIANT 2529 2529 R -> Q (in dbSNP:rs3795783).
FT /FTId=VAR_047746.
FT VARIANT 2720 2720 V -> M (in dbSNP:rs1188697).
FT /FTId=VAR_047747.
FT VARIANT 2812 2812 R -> W (in dbSNP:rs3795785).
FT /FTId=VAR_047748.
FT VARIANT 3300 3300 A -> T (in dbSNP:rs437129).
FT /FTId=VAR_034620.
FT VARIANT 3372 3372 E -> D (in dbSNP:rs3795789).
FT /FTId=VAR_047749.
FT VARIANT 3373 3373 S -> C (in dbSNP:rs3795790).
FT /FTId=VAR_047750.
FT VARIANT 3389 3389 A -> V.
FT /FTId=VAR_042289.
FT VARIANT 3426 3426 D -> E.
FT /FTId=VAR_042290.
FT VARIANT 3834 3834 R -> G.
FT /FTId=VAR_042291.
FT VARIANT 3983 3983 R -> Q (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035535.
FT VARIANT 4039 4039 G -> R (in dbSNP:rs435776).
FT /FTId=VAR_047751.
FT VARIANT 4381 4381 H -> R (in dbSNP:rs1150912).
FT /FTId=VAR_034621.
FT VARIANT 4450 4450 C -> R (in dbSNP:rs1188732).
FT /FTId=VAR_034622.
FT VARIANT 4516 4516 R -> W (in dbSNP:rs11810627).
FT /FTId=VAR_059429.
FT VARIANT 4534 4534 R -> H (in dbSNP:rs4653942).
FT /FTId=VAR_026410.
FT VARIANT 4558 4558 R -> H (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035536.
FT VARIANT 4642 4642 S -> C (in dbSNP:rs1188729).
FT /FTId=VAR_056102.
FT VARIANT 4662 4662 R -> C (in dbSNP:rs3795800).
FT /FTId=VAR_056103.
FT VARIANT 4666 4666 G -> S (in dbSNP:rs3795801).
FT /FTId=VAR_056104.
FT VARIANT 4810 4810 R -> Q (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035537.
FT VARIANT 4823 4823 A -> S.
FT /FTId=VAR_042292.
FT VARIANT 4962 4962 D -> G (in dbSNP:rs373610).
FT /FTId=VAR_056105.
FT VARIANT 5071 5071 A -> T (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035538.
FT VARIANT 5269 5269 L -> V (in dbSNP:rs369909).
FT /FTId=VAR_056106.
FT VARIANT 5575 5575 R -> H (in dbSNP:rs3795809).
FT /FTId=VAR_056107.
FT VARIANT 5598 5598 R -> Q.
FT /FTId=VAR_042293.
FT VARIANT 5891 5891 Q -> E (in dbSNP:rs1188710).
FT /FTId=VAR_056108.
FT VARIANT 6473 6473 E -> Q.
FT /FTId=VAR_042294.
FT VARIANT 7172 7172 A -> V (in dbSNP:rs500049).
FT /FTId=VAR_056109.
FT CONFLICT 888 888 V -> A (in Ref. 1; CAC85746).
FT CONFLICT 895 895 L -> P (in Ref. 1; CAC85746).
FT CONFLICT 897 897 R -> C (in Ref. 1; CAC85746).
FT CONFLICT 899 900 KL -> EV (in Ref. 1; CAC85746).
FT CONFLICT 904 904 A -> V (in Ref. 1; CAC85746).
FT CONFLICT 917 917 A -> D (in Ref. 1; CAC85746).
FT CONFLICT 919 919 T -> M (in Ref. 1; CAC85746).
FT CONFLICT 937 938 CM -> HV (in Ref. 1; CAC85746).
FT CONFLICT 941 941 T -> V (in Ref. 1; CAC85746).
FT CONFLICT 944 944 T -> M (in Ref. 1; CAC85746).
FT CONFLICT 952 952 A -> V (in Ref. 1; CAC85746).
FT CONFLICT 957 957 A -> S (in Ref. 1; CAC85746).
FT CONFLICT 965 965 G -> R (in Ref. 1; CAC85746).
FT CONFLICT 969 969 L -> V (in Ref. 1; CAC85746).
FT CONFLICT 972 972 H -> R (in Ref. 1; CAC85746).
FT CONFLICT 999 999 S -> N (in Ref. 1; CAC44768).
FT CONFLICT 1011 1011 T -> A (in Ref. 1; CAC44768).
FT CONFLICT 1348 1348 A -> V (in Ref. 1; CAC85746).
FT CONFLICT 1355 1355 L -> P (in Ref. 1; CAC85749).
FT CONFLICT 1357 1357 H -> R (in Ref. 1; CAC85746).
FT CONFLICT 1359 1359 K -> E (in Ref. 1; CAC85749).
FT CONFLICT 1360 1360 V -> L (in Ref. 1; CAC85746).
FT CONFLICT 1367 1367 I -> S (in Ref. 1; CAC85746/CAC85749).
FT CONFLICT 1394 1394 S -> L (in Ref. 1; CAC85749).
FT CONFLICT 1397 1398 RM -> HV (in Ref. 1; CAC85749).
FT CONFLICT 1397 1397 R -> C (in Ref. 1; CAC85746).
FT CONFLICT 1401 1401 V -> A (in Ref. 1; CAC85749).
FT CONFLICT 1401 1401 V -> T (in Ref. 1; CAC85746).
FT CONFLICT 1413 1413 C -> G (in Ref. 1; CAC85746/CAC85749).
FT CONFLICT 1417 1417 T -> A (in Ref. 1; CAC85746).
FT CONFLICT 1428 1428 R -> Q (in Ref. 1; CAC85749).
FT CONFLICT 1432 1432 S -> H (in Ref. 1; CAC85746).
FT CONFLICT 1445 1445 E -> D (in Ref. 1; CAC85750).
FT CONFLICT 1455 1455 Q -> E (in Ref. 1; CAC85750).
FT CONFLICT 1458 1458 A -> T (in Ref. 1; CAC85750).
FT CONFLICT 1461 1461 T -> M (in Ref. 1; CAC85750).
FT CONFLICT 1524 1524 H -> R (in Ref. 1; CAC85749).
FT CONFLICT 1526 1526 H -> Q (in Ref. 1; CAC85749).
FT CONFLICT 1580 1582 VRM -> MRV (in Ref. 1; CAC85750).
FT CONFLICT 1607 1607 K -> E (in Ref. 1; CAC85750).
FT CONFLICT 1610 1610 D -> G (in Ref. 1; CAC85750).
FT CONFLICT 1633 1633 H -> C (in Ref. 1; CAC85750).
FT CONFLICT 1653 1655 AQT -> GQM (in Ref. 1; CAC85750).
FT CONFLICT 1673 1674 RV -> HM (in Ref. 1; CAC85750).
FT CONFLICT 1677 1679 VGC -> SGY (in Ref. 1; CAC85750).
FT CONFLICT 1692 1692 E -> D (in Ref. 1; CAC44768/CAC85750).
FT CONFLICT 1704 1704 Q -> R (in Ref. 1; CAC44768/CAC85750).
FT CONFLICT 1710 1710 Q -> H (in Ref. 1; CAC44768/CAC85750).
FT CONFLICT 1848 1848 L -> P (in Ref. 1; CAC44768).
FT CONFLICT 2014 2014 P -> A (in Ref. 1; CAC85750).
FT CONFLICT 3126 3126 V -> M (in Ref. 1; CAC44768).
FT CONFLICT 4155 4155 T -> TG (in Ref. 3; CAC85752).
FT CONFLICT 4489 4489 H -> Q (in Ref. 1; CAC44768).
FT CONFLICT 4959 4959 T -> A (in Ref. 1; CAC44768).
FT CONFLICT 5243 5243 S -> ST (in Ref. 1; CAC85753).
FT CONFLICT 5391 5391 S -> F (in Ref. 4; BAB13465).
FT CONFLICT 5499 5500 LE -> FQ (in Ref. 1; CAC44768).
FT CONFLICT 6115 6115 R -> L (in Ref. 1; CAC44768).
FT CONFLICT 6570 6570 Q -> E (in Ref. 3; CAJ76912).
FT CONFLICT 6710 6711 PS -> SG (in Ref. 3; CAJ76912).
FT STRAND 1634 1639
FT STRAND 1644 1646
FT STRAND 1653 1655
FT STRAND 1658 1661
FT STRAND 1670 1677
FT STRAND 1680 1685
FT TURN 1690 1692
FT STRAND 1696 1700
FT STRAND 1707 1712
FT STRAND 2745 2750
FT STRAND 2753 2758
FT STRAND 2771 2776
FT STRAND 2784 2788
FT STRAND 2791 2796
FT TURN 2801 2803
FT STRAND 2807 2811
FT STRAND 2814 2818
FT STRAND 2820 2823
FT STRAND 2829 2831
FT STRAND 2836 2838
FT STRAND 2844 2846
FT STRAND 2849 2854
FT STRAND 2859 2863
FT STRAND 2869 2877
FT STRAND 2880 2887
FT TURN 2890 2892
FT STRAND 2894 2899
FT STRAND 2904 2911
FT STRAND 2925 2928
FT STRAND 2931 2938
FT STRAND 2947 2952
FT STRAND 2957 2966
FT STRAND 2969 2976
FT TURN 2979 2981
FT STRAND 2983 2988
FT STRAND 2996 3001
FT STRAND 3006 3009
FT STRAND 3013 3017
FT STRAND 3027 3030
FT STRAND 3037 3042
FT STRAND 3048 3050
FT TURN 3057 3059
FT STRAND 3063 3065
FT TURN 3070 3072
FT STRAND 3074 3080
FT STRAND 3087 3092
FT STRAND 3187 3189
FT STRAND 3194 3197
FT STRAND 3202 3210
FT STRAND 3216 3219
FT STRAND 3227 3235
FT STRAND 3238 3243
FT HELIX 3248 3250
FT STRAND 3252 3258
FT STRAND 3261 3270
FT STRAND 3371 3374
FT STRAND 3386 3388
FT STRAND 3392 3397
FT STRAND 3402 3405
FT STRAND 3407 3410
FT STRAND 3412 3421
FT TURN 3424 3426
FT STRAND 3430 3433
FT STRAND 3438 3441
FT STRAND 3443 3446
FT STRAND 3452 3454
FT STRAND 3459 3462
FT STRAND 3467 3475
FT STRAND 3480 3483
FT STRAND 3490 3509
FT TURN 3512 3514
FT STRAND 3516 3522
FT STRAND 3525 3534
FT STRAND 3554 3560
FT STRAND 3562 3564
FT STRAND 3568 3570
FT STRAND 3579 3584
FT STRAND 3590 3597
FT TURN 3600 3602
FT STRAND 3604 3606
FT STRAND 3608 3612
FT STRAND 3617 3620
FT STRAND 3628 3630
FT STRAND 3643 3651
FT STRAND 3656 3663
FT STRAND 3667 3675
FT STRAND 3678 3683
FT STRAND 3692 3698
FT STRAND 3701 3709
FT STRAND 3716 3718
FT STRAND 3723 3726
FT STRAND 3731 3739
FT STRAND 3744 3751
FT STRAND 3754 3757
FT STRAND 3759 3763
FT STRAND 3766 3773
FT TURN 3776 3778
FT STRAND 3780 3788
FT STRAND 3790 3798
FT STRAND 3812 3814
FT STRAND 3819 3828
FT STRAND 3832 3839
FT STRAND 3842 3845
FT STRAND 3847 3851
FT STRAND 3854 3861
FT TURN 3864 3866
FT STRAND 3868 3874
FT STRAND 3877 3882
FT STRAND 3884 3886
FT STRAND 5604 5609
FT STRAND 5628 5636
FT STRAND 5639 5644
FT STRAND 5654 5657
FT HELIX 5659 5661
FT STRAND 5662 5665
SQ SEQUENCE 7968 AA; 868484 MW; 46550B34565CAC76 CRC64;
MDQPQFSGAP RFLTRPKAFV VSVGKDATLS CQIVGNPTPQ VSWEKDQQPV AAGARFRLAQ
DGDLYRLTIL DLALGDSGQY VCRARNAIGE AFAAVGLQVD AEAACAEQAP HFLLRPTSIR
VREGSEATFR CRVGGSPRPA VSWSKDGRRL GEPDGPRVRV EELGEASALR IRAARPRDGG
TYEVRAENPL GAASAAAALV VDSDAADTAS RPGTSTAALL AHLQRRREAM RAEGAPASPP
STGTRTCTVT EGKHARLSCY VTGEPKPETV WKKDGQLVTE GRRHVVYEDA QENFVLKILF
CKQSDRGLYT CTASNLVGQT YSSVLVVVRE PAVPFKKRLQ DLEVREKESA TFLCEVPQPS
TEAAWFKEET RLWASAKYGI EEEGTERRLT VRNVSADDDA VYICETPEGS RTVAELAVQG
NLLRKLPRKT AVRVGDTAMF CVELAVPVGP VHWLRNQEEV VAGGRVAISA EGTRHTLTIS
QCCLEDVGQV AFMAGDCQTS TQFCVSAPRK PPLQPPVDPV VKARMESSVI LSWSPPPHGE
RPVTIDGYLV EKKKLGTYTW IRCHEAEWVA TPELTVADVA EEGNFQFRVS ALNSFGQSPY
LEFPGTVHLA PKLAVRTPLK AVQAVEGGEV TFSVDLTVAS AGEWFLDGQA LKASSVYEIH
CDRTRHTLTI REVPASLHGA QLKFVANGIE SSIRMEVRAA PGLTANKPPA AAAREVLARL
HEEAQLLAEL SDQAAAVTWL KDGRTLSPGP KYEVQASAGR RVLLVRDVAR DDAGLYECVS
RGGRIAYQLS VQGLARFLHK DMAGSCVDAV AGGPAQFECE TSEAHVHVHW YKDGMELGHS
GERFLQEDVG TRHRLVAATV TRQDEGTYSC RVGEDSVDFR LRVSEPKVVF AKEQLARRKL
QAEAGASATL SCEVAQAQTE VTWYKDGKKL SSSSKVCMEA TGCTRRLVVQ QAGQADAGEY
SCEAGGQRLS FHLDVKEPKV VFAKDQVAHS EVQAEAGASA TLSCEVAQAQ TEVMWYKDGK
KLSSSLKVHV EAKGCRRRLV VQQAGKTDAG DYSCEARGQR VSFRLHITEP KMMFAKEQSV
HNEVQAEAGA SAMLSCEVAQ AQTEVTWYKD GKKLSSSSKV GMEVKGCTRR LVLPQAGKAD
AGEYSCEAGG QRVSFHLHIT EPKGVFAKEQ SVHNEVQAEA GTTAMLSCEV AQPQTEVTWY
KDGKKLSSSS KVRMEVKGCT RRLVVQQVGK ADAGEYSCEA GGQRVSFQLH ITEPKAVFAK
EQLVHNEVRT EAGASATLSC EVAQAQTEVT WYKDGKKLSS SSKVRIEAAG CMRQLVVQQA
GQADAGEYTC EAGGQRLSFH LDVSEPKAVF AKEQLAHRKV QAEAGAIATL SCEVAQAQTE
VTWYKDGKKL SSSSKVRMEA VGCTRRLVVQ QACQADTGEY SCEAGGQRLS FSLDVAEPKV
VFAKEQPVHR EVQAQAGAST TLSCEVAQAQ TEVMWYKDGK KLSFSSKVRM EAVGCTRRLV
VQQAGQAVAG EYSCEAGSQR LSFHLHVAEP KAVFAKEQPA SREVQAEAGT SATLSCEVAQ
AQTEVTWYKD GKKLSSSSKV RMEAVGCTRR LVVQEAGQAD AGEYSCKAGD QRLSFHLHVA
EPKVVFAKEQ PAHREVQAEA GASATLSCEV AQAQTEVTWY KDGKKLSSSS KVRVEAVGCT
RRLVVQQAGQ AEAGEYSCEA GGQQLSFRLQ VAELEPQISE RPCRREPLVV KEHEDIILTA
TLATPSAATV TWLKDGVEIR RSKRHETASQ GDTHTLTVHG AQVLDSAIYS CRVGAEGQDF
PVQVEEVAAK FCRLLEPVCG ELGGTVTLAC ELSPACAEVV WRCGNTQLRV GKRFQMVAEG
PVRSLTVLGL RAEDAGEYVC ESRDDHTSAQ LTVSVPRVVK FMSGLSTVVA EEGGEATFQC
VVSPSDVAVV WFRDGALLQP SEKFAISQSG ASHSLTISDL VLEDAGQITV EAEGASSSAA
LRVREAPVLF KKKLEPQTVE ERSSVTLEVE LTRPWPELRW TRNATALAPG KNVEIHAEGA
RHRLVLHNVG FADRGFFGCE TPDDKTQAKL TVEMRQVRLV RGLQAVEARE QGTATMEVQL
SHADVDGSWT RDGLRFQQGP TCHLAVRGPM HTLTLSGLRP EDSGLMVFKA EGVHTSARLV
VTELPVSFSR PLQDVVTTEK EKVTLECELS RPNVDVRWLK DGVELRAGKT MAIAAQGACR
SLTIYRCEFA DQGVYVCDAH DAQSSASVKV QGRTYTLIYR RVLAEDAGEI QFVAENAESR
AQLRVKELPV TLVRPLRDKI AMEKHRGVLE CQVSRASAQV RWFKGSQELQ PGPKYELVSD
GLYRKLIISD VHAEDEDTYT CDAGDVKTSA QFFVEEQSIT IVRGLQDVTV MEPAPAWFEC
ETSIPSVRPP KWLLGKTVLQ AGGNVGLEQE GTVHRLMLRR TCSTMTGPVH FTVGKSRSSA
RLVVSDIPVV LTRPLEPKTG RELQSVVLSC DFRPAPKAVQ WYKDDTPLSP SEKFKMSLEG
QMAELRILRL MPADAGVYRC QAGSAHSSTE VTVEAREVTV TGPLQDAEAT EEGWASFSCE
LSHEDEEVEW SLNGMPLYND SFHEISHKGR RHTLVLKSIQ RADAGIVRAS SLKVSTSARL
EVRVKPVVFL KALDDLSAEE RGTLALQCEV SDPEAHVVWR KDGVQLGPSD KYDFLHTAGT
RGLVVHDVSP EDAGLYTCHV GSEETRARVR VHDLHVGITK RLKTMEVLEG ESCSFECVLS
HESASDPAMW TVGGKTVGSS SRFQATRQGR KYILVVREAA PSDAGEVVFS VRGLTSKASL
IVRERPAAII KPLEDQWVAP GEDVELRCEL SRAGTPVHWL KDRKAIRKSQ KYDVVCEGTM
AMLVIRGASL KDAGEYTCEV EASKSTASLH VEEKANCFTE ELTNLQVEEK GTAVFTCKTE
HPAATVTWRK GLLELRASGK HQPSQEGLTL RLTISALEKA DSDTYTCDIG QAQSRAQLLV
QGRRVHIIED LEDVDVQEGS SATFRCRISP ANYEPVHWFL DKTPLHANEL NEIDAQPGGY
HVLTLRQLAL KDSGTIYFEA GDQRASAALR VTEKPSVFSR ELTDATITEG EDLTLVCETS
TCDIPVCWTK DGKTLRGSAR CQLSHEGHRA QLLITGATLQ DSGRYKCEAG GACSSSIVRV
HARPVRFQEA LKDLEVLEGG AATLRCVLSS VAAPVKWCYG NNVLRPGDKY SLRQEGAMLE
LVVRNLRPQD SGRYSCSFGD QTTSATLTVT ALPAQFIGKL RNKEATEGAT ATLRCELSKA
APVEWRKGSE TLRDGDRYCL RQDGAMCELQ IRGLAMVDAA EYSCVCGEER TSASLTIRPM
PAHFIGRLRH QESIEGATAT LRCELSKAAP VEWRKGRESL RDGDRHSLRQ DGAVCELQIC
GLAVADAGEY SCVCGEERTS ATLTVKALPA KFTEGLRNEE AVEGATAMLW CELSKVAPVE
WRKGPENLRD GDRYILRQEG TRCELQICGL AMADAGEYLC VCGQERTSAT LTIRALPARF
IEDVKNQEAR EGATAVLQCE LNSAAPVEWR KGSETLRDGD RYSLRQDGTK CELQIRGLAM
ADTGEYSCVC GQERTSAMLT VRALPIKFTE GLRNEEATEG ATAVLRCELS KMAPVEWWKG
HETLRDGDRH SLRQDGARCE LQIRGLVAED AGEYLCMCGK ERTSAMLTVR AMPSKFIEGL
RNEEATEGDT ATLWCELSKA APVEWRKGHE TLRDGDRHSL RQDGSRCELQ IRGLAVVDAG
EYSCVCGQER TSATLTVRAL PARFIEDVKN QEAREGATAV LQCELSKAAP VEWRKGSETL
RGGDRYSLRQ DGTRCELQIH GLSVADTGEY SCVCGQERTS ATLTVRAPQP VFREPLQSLQ
AEEGSTATLQ CELSEPTATV VWSKGGLQLQ ANGRREPRLQ GCTAELVLQD LQREDTGEYT
CTCGSQATSA TLTVTAAPVR FLRELQHQEV DEGGTAHLCC ELSRAGASVE WRKGSLQLFP
CAKYQMVQDG AAAELLVRGV EQEDAGDYTC DTGHTQSMAS LSVRVPRPKF KTRLQSLEQE
TGDIARLCCQ LSDAESGAVV QWLKEGVELH AGPKYEMRSQ GATRELLIHQ LEAKDTGEYA
CVTGGQKTAA SLRVTEPEVT IVRGLVDAEV TADEDVEFSC EVSRAGATGV QWCLQGLPLQ
SNEVTEVAVR DGRIHTLRLK GVTPEDAGTV SFHLGNHASS AQLTVRAPEV TILEPLQDVQ
LSEGQDASFQ CRLSRASGQE ARWALGGVPL QANEMNDITV EQGTLHLLTL HKVTLEDAGT
VSFHVGTCSS EAQLKVTAKN TVVRGLENVE ALEGGEALFE CQLSQPEVAA HTWLLDDEPV
HTSENAEVVF FENGLRHLLL LKNLRPQDSC RVTFLAGDMV TSAFLTVRGW RLEILEPLKN
AAVRAGAQAC FTCTLSEAVP VGEASWYING AAVQPDDSDW TVTADGSHHA LLLRSAQPHH
AGEVTFACRD AVASARLTVL GLPDPPEDAE VVARSSHTVT LSWAAPMSDG GGGLCGYRVE
VKEGATGQWR LCHELVPGPE CVVDGLAPGE TYRFRVAAVG PVGAGEPVHL PQTVRLAEPP
KPVPPQPSAP ESRQVAAGED VSLELEVVAE AGEVIWHKGM ERIQPGGRFE VVSQGRQQML
VIKGFTAEDQ GEYHCGLAQG SICPAAATFQ VALSPASVDE APQPSLPPEA AQEGDLHLLW
EALARKRRMS REPTLDSISE LPEEDGRSQR LPQEAEEVAP DLSEGYSTAD ELARTGDADL
SHTSSDDESR AGTPSLVTYL KKAGRPGTSP LASKVGAPAA PSVKPQQQQE PLAAVRPPLG
DLSTKDLGDP SMDKAAVKIQ AAFKGYKVRK EMKQQEGPMF SHTFGDTEAQ VGDALRLECV
VASKADVRAR WLKDGVELTD GRHHHIDQLG DGTCSLLITG LDRADAGCYT CQVSNKFGQV
THSACVVVSG SESEAESSSG GELDDAFRRA ARRLHRLFRT KSPAEVSDEE LFLSADEGPA
EPEEPADWQT YREDEHFICI RFEALTEARQ AVTRFQEMFA TLGIGVEIKL VEQGPRRVEM
CISKETPAPV VPPEPLPSLL TSDAAPVFLT ELQNQEVQDG YPVSFDCVVT GQPMPSVRWF
KDGKLLEEDD HYMINEDQQG GHQLIITAVV PADMGVYRCL AENSMGVSST KAELRVDLTS
TDYDTAADAT ESSSYFSAQG YLSSREQEGT ESTTDEGQLP QVVEELRDLQ VAPGTRLAKF
QLKVKGYPAP RLYWFKDGQP LTASAHIRMT DKKILHTLEI ISVTREDSGQ YAAYISNAMG
AAYSSARLLV RGPDEPEEKP ASDVHEQLVP PRMLERFTPK KVKKGSSITF SVKVEGRPVP
TVHWLREEAE RGVLWIGPDT PGYTVASSAQ QHSLVLLDVG RQHQGTYTCI ASNAAGQALC
SASLHVSGLP KVEEQEKVKE ALISTFLQGT TQAISAQGLE TASFADLGGQ RKEEPLAAKE
ALGHLSLAEV GTEEFLQKLT SQITEMVSAK ITQAKLQVPG GDSDEDSKTP SASPRHGRSR
PSSSIQESSS ESEDGDARGE IFDIYVVTAD YLPLGAEQDA ITLREGQYVE VLDAAHPLRW
LVRTKPTKSS PSRQGWVSPA YLDRRLKLSP EWGAAEAPEF PGEAVSEDEY KARLSSVIQE
LLSSEQAFVE ELQFLQSHHL QHLERCPHVP IAVAGQKAVI FRNVRDIGRF HSSFLQELQQ
CDTDDDVAMC FIKNQAAFEQ YLEFLVGRVQ AESVVVSTAI QEFYKKYAEE ALLAGDPSQP
PPPPLQHYLE QPVERVQRYQ ALLKELIRNK ARNRQNCALL EQAYAVVSAL PQRAENKLHV
SLMENYPGTL QALGEPIRQG HFIVWEGAPG ARMPWKGHNR HVFLFRNHLV ICKPRRDSRT
DTVSYVFRNM MKLSSIDLND QVEGDDRAFE VWQEREDSVR KYLLQARTAI IKSSWVKEIC
GIQQRLALPV WRPPDFEEEL ADCTAELGET VKLACRVTGT PKPVISWYKD GKAVQVDPHH
ILIEDPDGSC ALILDSLTGV DSGQYMCFAA SAAGNCSTLG KILVQVPPRF VNKVRASPFV
EGEDAQFTCT IEGAPYPQIR WYKDGALLTT GNKFQTLSEP RSGLLVLVIR AASKEDLGLY
ECELVNRLGS ARASAELRIQ SPMLQAQEQC HREQLVAAVE DTTLERADQE VTSVLKRLLG
PKAPGPSTGD LTGPGPCPRG APALQETGSQ PPVTGTSEAP AVPPRVPQPL LHEGPEQEPE
AIARAQEWTV PIRMEGAAWP GAGTGELLWD VHSHVVRETT QRTYTYQAID THTARPPSMQ
VTIEDVQAQT GGTAQFEAII EGDPQPSVTW YKDSVQLVDS TRLSQQQEGT TYSLVLRHVA
SKDAGVYTCL AQNTGGQVLC KAELLVLGGD NEPDSEKQSH RRKLHSFYEV KEEIGRGVFG
FVKRVQHKGN KILCAAKFIP LRSRTRAQAY RERDILAALS HPLVTGLLDQ FETRKTLILI
LELCSSEELL DRLYRKGVVT EAEVKVYIQQ LVEGLHYLHS HGVLHLDIKP SNILMVHPAR
EDIKICDFGF AQNITPAELQ FSQYGSPEFV SPEIIQQNPV SEASDIWAMG VISYLSLTCS
SPFAGESDRA TLLNVLEGRV SWSSPMAAHL SEDAKDFIKA TLQRAPQARP SAAQCLSHPW
FLKSMPAEEA HFINTKQLKF LLARSRWQRS LMSYKSILVM RSIPELLRGP PDSPSLGVAR
HLCRDTGGSS SSSSSSDNEL APFARAKSLP PSPVTHSPLL HPRGFLRPSA SLPEEAEASE
RSTEAPAPPA SPEGAGPPAA QGCVPRHSVI RSLFYHQAGE SPEHGALAPG SRRHPARRRH
LLKGGYIAGA LPGLREPLME HRVLEEEAAR EEQATLLAKA PSFETALRLP ASGTHLAPGH
SHSLEHDSPS TPRPSSEACG EAQRLPSAPS GGAPIRDMGH PQGSKQLPST GGHPGTAQPE
RPSPDSPWGQ PAPFCHPKQG SAPQEGCSPH PAVAPCPPGS FPPGSCKEAP LVPSSPFLGQ
PQAPPAPAKA SPPLDSKMGP GDISLPGRPK PGPCSSPGSA SQASSSQVSS LRVGSSQVGT
EPGPSLDAEG WTQEAEDLSD STPTLQRPQE QATMRKFSLG GRGGYAGVAG YGTFAFGGDA
GGMLGQGPMW ARIAWAVSQS EEEEQEEARA ESQSEEQQEA RAESPLPQVS ARPVPEVGRA
PTRSSPEPTP WEDIGQVSLV QIRDLSGDAE AADTISLDIS EVDPAYLNLS DLYDIKYLPF
EFMIFRKVPK SAQPEPPSPM AEEELAEFPE PTWPWPGELG PHAGLEITEE SEDVDALLAE
AAVGRKRKWS SPSRSLFHFP GRHLPLDEPA ELGLRERVKA SVEHISRILK GRPEGLEKEG
PPRKKPGLAS FRLSGLKSWD RAPTFLRELS DETVVLGQSV TLACQVSAQP AAQATWSKDG
APLESSSRVL ISATLKNFQL LTILVVVAED LGVYTCSVSN ALGTVTTTGV LRKAERPSSS
PCPDIGEVYA DGVLLVWKPV ESYGPVTYIV QCSLEGGSWT TLASDIFDCC YLTSKLSRGG
TYTFRTACVS KAGMGPYSSP SEQVLLGGPS HLASEEESQG RSAQPLPSTK TFAFQTQIQR
GRFSVVRQCW EKASGRALAA KIIPYHPKDK TAVLREYEAL KGLRHPHLAQ LHAAYLSPRH
LVLILELCSG PELLPCLAER ASYSESEVKD YLWQMLSATQ YLHNQHILHL DLRSENMIIT
EYNLLKVVDL GNAQSLSQEK VLPSDKFKDY LETMAPELLE GQGAVPQTDI WAIGVTAFIM
LSAEYPVSSE GARDLQRGLR KGLVRLSRCY AGLSGGAVAF LRSTLCAQPW GRPCASSCLQ
CPWLTEEGPA CSRPAPVTFP TARLRVFVRN REKRRALLYK RHNLAQVR
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