OBSCN_DROME
ID OBSCN_DROME Reviewed; 4218 AA.
AC A8DYP0; A0A0B4LGC9; A0A0B4LGE3; A0A0B4LGI5; A0A0B4LHF2; Q1ZYJ8; Q59E65;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Obscurin {ECO:0000250|UniProtKB:A2AAJ9};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:A2AAJ9};
DE AltName: Full=Muscle M-line assembly protein Unc-89 {ECO:0000250|UniProtKB:O01761};
GN Name=Unc-89 {ECO:0000303|PubMed:15185077, ECO:0000312|FlyBase:FBgn0053519};
GN ORFNames=CG33519 {ECO:0000312|FlyBase:FBgn0053519};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:ABD83643.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-452.
RX PubMed=15185077; DOI=10.1007/s00427-004-0413-5;
RA Sutter S.B., Raeker M.O., Borisov A.B., Russell M.W.;
RT "Orthologous relationship of obscurin and Unc-89: phylogeny of a novel
RT family of tandem myosin light chain kinases.";
RL Dev. Genes Evol. 214:352-359(2004).
RN [4] {ECO:0000305}
RP INDUCTION.
RX PubMed=18515368; DOI=10.1529/biophysj.108.130005;
RA Miller M.S., Lekkas P., Braddock J.M., Farman G.P., Ballif B.A.,
RA Irving T.C., Maughan D.W., Vigoreaux J.O.;
RT "Aging enhances indirect flight muscle fiber performance yet decreases
RT flight ability in Drosophila.";
RL Biophys. J. 95:2391-2401(2008).
RN [5] {ECO:0000305}
RP ALTERNATIVE SPLICING, FUNCTION, INTERACTION WITH MYOSIN, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22467859; DOI=10.1242/jcs.097345;
RA Katzemich A., Kreiskoether N., Alexandrovich A., Elliott C., Schoeck F.,
RA Leonard K., Sparrow J., Bullard B.;
RT "The function of the M-line protein obscurin in controlling the symmetry of
RT the sarcomere in the flight muscle of Drosophila.";
RL J. Cell Sci. 125:3367-3379(2012).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH BALL; MASK AND TM1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26251439; DOI=10.1242/jcs.170639;
RA Katzemich A., West R.J., Fukuzawa A., Sweeney S.T., Gautel M., Sparrow J.,
RA Bullard B.;
RT "Binding partners of the kinase domains in Drosophila obscurin and their
RT effect on the structure of the flight muscle.";
RL J. Cell Sci. 128:3386-3397(2015).
CC -!- FUNCTION: Structural component of the muscle M line which is involved
CC in assembly and organization of sarcomere (PubMed:22467859,
CC PubMed:26251439). Required for the development and organization of
CC indirect flight muscle sarcomeres by regulating the formation of M line
CC and H zone and the correct assembly of thick and thin filaments in the
CC sarcomere (PubMed:22467859, PubMed:26251439). Likely to have
CC serine/threonine-protein kinase activity as one of the two protein
CC kinase domains appears to be functional (Probable).
CC {ECO:0000269|PubMed:22467859, ECO:0000269|PubMed:26251439,
CC ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:A2AAJ9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A2AAJ9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A2AAJ9};
CC -!- SUBUNIT: Interacts with myosin (PubMed:22467859). May interact (via
CC protein kinase domain 1) with ball (PubMed:26251439). May interact (via
CC protein kinase domain 1 or 2) with mask (PubMed:26251439). May interact
CC (via protein kinase domain 2) with Tm1/tropomyosin-1 (PubMed:26251439).
CC {ECO:0000269|PubMed:22467859, ECO:0000269|PubMed:26251439}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:22467859, ECO:0000269|PubMed:26251439}. Note=In the
CC embryo, localizes across the muscles in a striped pattern and is
CC positioned laterally to the sites at which muscles are attached to the
CC epidermis. In the larval body wall muscles, localizes to the M line and
CC moves away from the attachment sites. During pupal development,
CC progressively forms broad striations at the M line which become more
CC defined after pupal eclosion. Colocalizes with myosin thick filaments
CC at the M line. {ECO:0000269|PubMed:22467859}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=A number of isoforms are produced.
CC {ECO:0000269|PubMed:22467859};
CC Name=C {ECO:0000312|FlyBase:FBgn0053519};
CC IsoId=A8DYP0-1; Sequence=Displayed;
CC Name=D {ECO:0000312|FlyBase:FBgn0053519};
CC IsoId=A8DYP0-2; Sequence=VSP_058765, VSP_058767;
CC Name=E {ECO:0000312|FlyBase:FBgn0053519};
CC IsoId=A8DYP0-3; Sequence=VSP_058767;
CC Name=F {ECO:0000312|FlyBase:FBgn0053519};
CC IsoId=A8DYP0-4; Sequence=VSP_058764;
CC Name=H {ECO:0000312|FlyBase:FBgn0053519};
CC IsoId=A8DYP0-5; Sequence=VSP_058763;
CC Name=G {ECO:0000312|FlyBase:FBgn0053519};
CC IsoId=A8DYP0-6; Sequence=VSP_058766, VSP_058767;
CC -!- TISSUE SPECIFICITY: Expressed in the thoracic muscles including the
CC indirect flight muscles (IFM) (at protein level).
CC {ECO:0000269|PubMed:22467859, ECO:0000269|PubMed:26251439}.
CC -!- DEVELOPMENTAL STAGE: Expression starts in embryos at stage 16 and is
CC found in the M line of somatic muscle during late larval stage 17, pupa
CC and in pharate adult. The various isoforms are expressed differentially
CC during development. {ECO:0000269|PubMed:22467859}.
CC -!- INDUCTION: Expression decreases with age.
CC {ECO:0000269|PubMed:18515368}.
CC -!- DOMAIN: The protein kinase domain 2 is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown either in the indirect
CC flight muscles (IFM) or in all muscles prevents flies from flying
CC without affecting jumping and slightly reduces larval crawling
CC (PubMed:22467859). Causes severe defects in IFM sarcomere development
CC and organization resulting in narrower myofibrils (PubMed:22467859).
CC During sarcomere development at the pupal stage, myosin is mislocalized
CC and no regular sarcomeres are formed (PubMed:22467859). In the adult,
CC abnormal localization of myosin in the mid-region of the sarcomere, H
CC zone shifts from the middle of the sarcomere and M lines are less
CC defined (PubMed:22467859). Thick filaments are asymmetric with the bare
CC zone often shifted towards the end of the filament (PubMed:22467859).
CC Thick filament length is mostly normal although some are longer and by-
CC pass the Z line (PubMed:22467859). Thin filaments are abnormally
CC shorter or longer and sometimes extend into the H zone
CC (PubMed:22467859). Several Z and M lines associated proteins are
CC mislocalized (PubMed:22467859, PubMed:26251439). zormin is more
CC diffused in both Z and M lines and tropomodulin is confined to the core
CC of the myofibril in the H zone (PubMed:22467859). ball is still
CC partially localized to the Z line but appears more diffuse across the
CC sarcomere compare to wild type (PubMed:26251439). mask localization to
CC Z lines is not affected but is absent or in a punctate form in the M
CC line (PubMed:26251439). kettin localization to the Z line is not
CC affected (PubMed:22467859). {ECO:0000269|PubMed:22467859,
CC ECO:0000269|PubMed:26251439}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AE013599; AAX52680.3; -; Genomic_DNA.
DR EMBL; AE013599; ABV53900.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56598.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56599.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56600.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56601.1; -; Genomic_DNA.
DR EMBL; DQ431841; ABD83643.1; -; mRNA.
DR RefSeq; NP_001014545.3; NM_001014545.3. [A8DYP0-2]
DR RefSeq; NP_001097440.1; NM_001103970.2. [A8DYP0-1]
DR RefSeq; NP_001286803.1; NM_001299874.1. [A8DYP0-3]
DR RefSeq; NP_001286804.1; NM_001299875.1. [A8DYP0-4]
DR RefSeq; NP_001286805.1; NM_001299876.1. [A8DYP0-5]
DR RefSeq; NP_001286806.1; NM_001299877.1. [A8DYP0-6]
DR IntAct; A8DYP0; 13.
DR STRING; 7227.FBpp0112375; -.
DR PaxDb; A8DYP0; -.
DR PRIDE; A8DYP0; -.
DR EnsemblMetazoa; FBtr0113464; FBpp0112375; FBgn0053519. [A8DYP0-1]
DR EnsemblMetazoa; FBtr0343283; FBpp0309948; FBgn0053519. [A8DYP0-2]
DR EnsemblMetazoa; FBtr0343284; FBpp0309949; FBgn0053519. [A8DYP0-3]
DR EnsemblMetazoa; FBtr0343285; FBpp0309950; FBgn0053519. [A8DYP0-4]
DR EnsemblMetazoa; FBtr0343286; FBpp0309951; FBgn0053519. [A8DYP0-5]
DR EnsemblMetazoa; FBtr0343287; FBpp0309952; FBgn0053519. [A8DYP0-6]
DR GeneID; 3346201; -.
DR KEGG; dme:Dmel_CG33519; -.
DR UCSC; CG33519-RC; d. melanogaster. [A8DYP0-1]
DR CTD; 3346201; -.
DR FlyBase; FBgn0053519; Unc-89.
DR VEuPathDB; VectorBase:FBgn0053519; -.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG4240; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR InParanoid; A8DYP0; -.
DR PhylomeDB; A8DYP0; -.
DR SignaLink; A8DYP0; -.
DR BioGRID-ORCS; 3346201; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Unc-89; fly.
DR GenomeRNAi; 3346201; -.
DR PRO; PR:A8DYP0; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0053519; Expressed in oviduct (Drosophila) and 16 other tissues.
DR ExpressionAtlas; A8DYP0; baseline and differential.
DR Genevisible; A8DYP0; DM.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0005523; F:tropomyosin binding; IPI:UniProtKB.
DR GO; GO:0007527; P:adult somatic muscle development; IMP:FlyBase.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0036309; P:protein localization to M-band; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0045214; P:sarcomere organization; IMP:UniProtKB.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.10; -; 23.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 21.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 21.
DR SMART; SM00408; IGc2; 18.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48726; SSF48726; 21.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 15.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW Disulfide bond; Immunoglobulin domain; Kinase; Magnesium; Metal-binding;
KW Muscle protein; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; SH3 domain; Transferase.
FT CHAIN 1..4218
FT /note="Obscurin"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438925"
FT DOMAIN 3..71
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 86..264
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1017..1103
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1152..1298
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1313..1400
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1504..1594
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1599..1689
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1694..1785
FT /note="Ig-like C2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1815..1906
FT /note="Ig-like C2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2018..2107
FT /note="Ig-like C2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2113..2214
FT /note="Ig-like C2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2220..2305
FT /note="Ig-like C2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2318..2409
FT /note="Ig-like C2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2415..2505
FT /note="Ig-like C2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2519..2609
FT /note="Ig-like C2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2614..2698
FT /note="Ig-like C2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2716..2792
FT /note="Ig-like C2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2832..2933
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3186..3440
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 3654..3738
FT /note="Ig-like C2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3750..3843
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3897..4151
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 465..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..750
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3311
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 3192..3200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 3215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 3903..3911
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 3926
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DISULFID 1199..1282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2739..2790
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..908
FT /note="Missing (in isoform H)"
FT /evidence="ECO:0000305"
FT /id="VSP_058763"
FT VAR_SEQ 1..253
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_058764"
FT VAR_SEQ 1..3
FT /note="MDA -> MDAQ (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_058765"
FT VAR_SEQ 636..926
FT /note="GKQVVALEREPSPCSIPKIQVYRPVECENPVVTKHKPIELKDIVGYSESLRD
FT GDTAPAGGSPGRQQGYSANITDHASLTIWNNRLANIAGDRSGANQHLQQSGPPPPPIPP
FT NFTRMPGFFQPLPLIAYETTIEILIVKARPPSPPPPPPPTIKRVLVHTESLEQKTQNFF
FT EGIYDAASSDTSLRNAKQKIRSIKSTVLKSKDSTNYAQDTVQKAKARDFLHIFTPPVKK
FT RPIYEIVEEPVNIFELEGDYTESIADDFREPSADFEARGQSVGGMDDYYSGYSRASTRR
FT YET -> A (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_058766"
FT VAR_SEQ 1789..1813
FT /note="Missing (in isoform D, isoform E and isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_058767"
FT CONFLICT 145
FT /note="N -> S (in Ref. 3; ABD83643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4218 AA; 475655 MW; FAB9AA91F54A3E0A CRC64;
MDAVADIVFV SRDYQAQSLA TDEISVSRGD LVELISSKAS EKSRCFVRMF DSGDSPKEGW
VPIDILEFNP TMSSSNGKES GDAEFRKLTI LRELVETEEE FSRDLLHVVE KYIKGIDKPV
VPRSVRDNKD IIFCNFLQIA EFHNNVLKEG LKCYSNQPNM VAKTFLRLER DFDKHVVYCQ
NEPLAQDYLG SSPDAKKYFQ ELSKQLGDDK SLAEHLKLPI QRINDYQLLF KDFIKYSLSL
KENVKDLERA LELMLSVPSR AYDNRFLSSI EGCRGNIYKL GRLLLHAWCN VVDKEGKAHD
RYCFLFKSRI LVTKVRKISE NRSVFILQNI VKLPLCNIEL KADEKQIHLS LKAPEANSFL
PIDIKPHGPE AHLTWFNEIS SHINQDVTLQ EHNADDLKVD ASQIASESEL ILHLPQRAEA
HDPNLSVRPS DVAENYFLSK ETKERLQHEQ QELLKLEQEA IELYKKQQSS KSVSSKTESV
EITSSQVKSS SEVRKVVSPP PPPQAQVKEV TPVKVVSSPP PPKEITPAKV ATPPPQPQVV
TSPVKEVAPP PQPRAVASPA KEVTPSQSEP VKAPSPIKEV RKEVPPSASH SKEVEALVAT
EIRESLTETR STVVESGQSS EIREEIVVTE ESSLEGKQVV ALEREPSPCS IPKIQVYRPV
ECENPVVTKH KPIELKDIVG YSESLRDGDT APAGGSPGRQ QGYSANITDH ASLTIWNNRL
ANIAGDRSGA NQHLQQSGPP PPPIPPNFTR MPGFFQPLPL IAYETTIEIL IVKARPPSPP
PPPPPTIKRV LVHTESLEQK TQNFFEGIYD AASSDTSLRN AKQKIRSIKS TVLKSKDSTN
YAQDTVQKAK ARDFLHIFTP PVKKRPIYEI VEEPVNIFEL EGDYTESIAD DFREPSADFE
ARGQSVGGMD DYYSGYSRAS TRRYETKTRD YDRGTSYDST VERSQYGISS RRDRSSVDKV
EARSSLLATG RTESRAASRA ESRAESRASY SVAESRAGIR SSSRLQEDRP LRSVDKPVVV
KMLKSVQVEP GETAHFEIQF KDQPGLVTWL KDNKPLEDRL ADRITQTAAP MNSYRLDIKN
CSETDAGTYT IRAQSASETT TVSAQLAVGQ APGHDETKTN TEPAFLVSLK DAEMIENTLF
RFMVKIIGDP KPRVKFYKDE KEILETNDRI QIIRDKDYLG FYELVIADVQ KTDAGTYSCK
ATNKHGEANC EAIATTVEDK NPFGALSGQI LPAGEKPVFQ WKRNGEEFDP EERFKVLFGE
DEDSLALVFQ HVKPEDAGIY TCVAQTSTGN ISCSAELSVQ GAIQTLNREP EKPTLVIEHR
EANASIGGSA ILELQCKGFP KPAVQWKHDG EVIQVDDRHK FMYEDEESMS LVIKNVDTVD
AGVYTIEAIN ELGQDESSIN LVVKAPPKIK KITDITCSAG ETIKMEIEVE GFPQPTVQVT
NNGKDVTAES NVKISSSSIG KSLEKVVVEV KEIKLSQAGN YSIKATNDLS QTSEYWSCTV
KSKPVIVKNF ESEYIHGEKE NVQMTVRIDA YPEAKLTWYH DETEIKITDS KYTVSSDGNA
YTLKITGATR VDAGKYTVKA TNEHGSATSS TQLLIKCAPE FTHKLKNITV AEGDSNVELV
VGVDAYPRPH AKWYIDGIEI DEKRNDFRHV EEGNDFKLIM NQVATNMQGN YTCKIMNDYG
KLEDNCVVTV NCKPKVKRGL KNVEVQEGKS FTLEVEVYSE PEAKIKWFKD GHEIYEDARI
KISRDTQRIE NYYLTLNLAR TEDAGTYEMK ATNFIGETTS TCKVAVLTSE ALSLEQTVTK
TLIATTEEPE EGAVPEIVHV DVFQQHSYES VPLKYEVIAT GIPKPEAIWY HDGKPITPDK
HTAITVDGDH YKLEVQSLDL VDAGEYKVVV QNKVGEKSHQ GELSLSGIAE YRKPILTQGP
GLKDIKVNKG DKVCEPVVFT ADPAPEIVLL KDGQPVVETN NVKLKVDKKD AENGLVQYTC
TLNILEAEIK DSGRYELKVK NKYGELVTSG WIDVLAKPEI SGLNDTKCLP GDTICFEALV
QANPKPKVSW TRGNENLCNH ENCEVIADVD ADKYRLVFQS VSPCEDGKYT ITATNSEGRA
AVDFNLAVLV EKPTFIVQPE SQSIHDYRPV STKVLVHGVP LPTIEWFKDD KPINYEAINK
PGKDKLYAKE DTKKGTDQIE SVLDIKSFRE NDVGAYTCVA TNEIGVTKAP FKLAMLSLAP
SFVKKLDNAL DVLQGEPLVL ECCVDGSPLP TVQWLKDGDE VKPSESIKIS TNPDGLVKLE
INSCQPNDSG AYKLIISNPH GEKVALCAVA VKPEEMQPKF LKPITSQTVV VGEPLKLEAQ
VTGFPAPEVK WYKDGMLLRP SPEINFINSP NGQIGLIIDA AQPLDAGVYK CLIANKGGEI
EGVSKVEIVP KESKPVFVAE LQDASSIEGF PVKMDIKVVG NPKPKLQWFH NGHEIKPDAS
HIAIVENPDN SSSLIIEKTA PGDSGLYEVI AQNPEGSTAS KAKLYVAPKA DETATEEAPQ
FVSALRDVNA DEGQELVLSA PFISNPMPEV IWSKDGVTLT PNERLLMTCD GKHIGLTIKP
AEAADSGNYT CLLANPLGED SSACNANVRK VYKPPVFTQK ISDQQQVFGN NAKIPVTVSG
VPYPDLEWYF QDKPIPKSEK YSIKNDGDHH MLIVNNCEKG DQGVYKCIAS NREGKDITQG
RLDIVNEIKK HSRSEPPVFL KKIGDCDIYE GMVAKFTACA TGYPEPEVEW FKNDQKLFPS
DRFLIDIEPN GLLRLTIKNV TEYDVGRYSC RIFNPYGDDI CHAELFYDSL DSQQKPLEDQ
YTDFKKYKKS GAPPPLSEGP IISRMTDRGL LLSWNPSVPL TPRYPITYQI EMMDLPEGDW
RTLRTGVRSC ACDIRNLEPF RDYRFRVRVE NKFGVSDPSP YTQTYRQKLV PDPPKTYTYL
PPGTDFRPET SPYFPKDFDI ERPPHDGLAQ APQFLLREQD ISYGVKDHNT ELMWFVYGYP
KPKMTYYFDD MLIESGGRFD QSYTRNGQAT LFINKMLDRD VGWYEAVATN EHGEARQRVR
LEIAEHPRFL KRPDETFIMA RKNGRIEAKL VGIPLPEVHW FKDWKPIVDS SRIKISSYDP
DIYVLSIHDS IIKDGGLYSI SARNIAGSIS TSVTVHIEEN EDQYIYKTYG RHPYVRSKQL
RYQDKYDIGD ELGRGTQGIT YHAVERSSGD NYAAKIMYGR PELRPFMLNE LEMMNTFNHK
NLIRPYDAYD TDRSVTLIME LAAGGELVRD NLLRRDYYTE RDIAHYIRQT LWGLEHMHEM
GVGHMGLTIK DLLISVVGGD IIKVSDFGLS RKINRHNLST LDYGMPEFVS PEVVNKEGVN
FSHDMWTVGL ITYVLLGGHN PFLGIDDRET LTKIREGRWD FKDEIWTHIS DDGRDFISRL
LLYSPEERMD VKTALKHPWF FMLDRPVYDH DYQIGTDRLR NYYDHFRDWY ANASCKNYFR
RRRLSGCFQH PSKMVYPPGH VYTPENTPEP LPEPRIRAKR EEVVSKYLHP DYELGLIQSE
SHYQYGPDTY LLQLRDVNFP VRLREYMKVA HRRSPSFALN DSVDWSLPVI RERRRFTDIM
DEEIDDERTR SRISMYAANE SYSIRRLRTE LGPRLDEYTE ADAMIETQRE GYPPFFREKP
QTIAITENQP SHIHCFAVGD PKPCVQWFKN DMVLTESKRI KISVDEDGRS ILRFEPALHF
DVGVYKVVAR NKVGQTVARC RIVVATLPDA PDSPEISANS GTEILLRWKQ PRDDGHSTVL
CYSLQYKLSN CDAWTTVADN IDHEFYLLHD LQPNTNYQFR LASKNRIGWS EMGIPVSAST
VGGDAPKIHI TKAMKHLQQL TENGHQVVPE EERVHTDYHC EREPPNWVTD SSVSDKYSFI
SEIARGEFST IVKGIQKSTD TVVVAKILEV TDENEDNVVA EFDNFKTLRH ERIPALFSAY
KPLNVPIAIF VMEKLQGADV LTYFSSRHEY SEQMVATVVT QLLDALQYLH WRGYCHLNIQ
PDNVVMASVR SIQVKLVDFG SAKKVNKLGM KVTPCGSLDF QPPEMINDEP IFPQSDIWSL
GALTYLLLSG CSPFRGADEY ETKQNISFVR YRFENLFKEV TPEATRFIML LFKRHPTKRP
YTEDCLEHRW LMSSDYMVRK RERAIFLGSR LKTFCDEYHD LKNASATSSK VLNTVAGGPT
PTQLLRSNSI QEELLTTF
