ID OBSL1_HUMAN Reviewed; 1896 AA. AC O75147; A0A024R468; A4KVA4; A4KVA5; Q96IW3; S4R3M6; DT 22-AUG-2006, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 4. DT 27-MAR-2024, entry version 184. DE RecName: Full=Obscurin-like protein 1 {ECO:0000303|PubMed:17289344}; GN Name=OBSL1 {ECO:0000312|HGNC:HGNC:29092}; Synonyms=KIAA0657; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND TISSUE RP SPECIFICITY. RC TISSUE=Heart; RX PubMed=17289344; DOI=10.1016/j.ygeno.2006.12.004; RA Geisler S.B., Robinson D., Hauringa M., Raeker M.O., Borisov A.B., RA Westfall M.V., Russell M.W.; RT "Obscurin-like 1, OBSL1, is a novel cytoskeletal protein related to RT obscurin."; RL Genomics 89:521-531(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-1896 (ISOFORM 3). RC TISSUE=Brain; RX PubMed=9734811; DOI=10.1093/dnares/5.3.169; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [6] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP INVOLVEMENT IN 3M2. RX PubMed=19481195; DOI=10.1016/j.ajhg.2009.04.021; RA Hanson D., Murray P.G., Sud A., Temtamy S.A., Aglan M., Superti-Furga A., RA Holder S.E., Urquhart J., Hilton E., Manson F.D.C., Scambler P., RA Black G.C.M., Clayton P.E.; RT "The primordial growth disorder 3-M syndrome connects ubiquitination to the RT cytoskeletal adaptor OBSL1."; RL Am. J. Hum. Genet. 84:801-806(2009). RN [9] RP INTERACTION WITH CCDC8 AND CUL7. RX PubMed=21737058; DOI=10.1016/j.ajhg.2011.05.028; RA Hanson D., Murray P.G., O'Sullivan J., Urquhart J., Daly S., Bhaskar S.S., RA Biesecker L.G., Skae M., Smith C., Cole T., Kirk J., Chandler K., RA Kingston H., Donnai D., Clayton P.E., Black G.C.; RT "Exome sequencing identifies CCDC8 mutations in 3-M syndrome, Suggesting RT that CCDC8 Contributes in a Pathway with CUL7 and OBSL1 to Control Human RT Growth."; RL Am. J. Hum. Genet. 89:148-153(2011). RN [10] RP FUNCTION, INTERACTION WITH FBXW8 AND CUL7, AND SUBCELLULAR LOCATION. RX PubMed=21572988; DOI=10.1371/journal.pbio.1001060; RA Litterman N., Ikeuchi Y., Gallardo G., O'Connell B.C., Sowa M.E., RA Gygi S.P., Harper J.W., Bonni A.; RT "An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi RT morphology and dendrite patterning."; RL PLoS Biol. 9:E1001060-E1001060(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP FUNCTION, IDENTIFICATION IN THE 3M COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=24793695; DOI=10.1016/j.molcel.2014.03.047; RA Yan J., Yan F., Li Z., Sinnott B., Cappell K.M., Yu Y., Mo J., Duncan J.A., RA Chen X., Cormier-Daire V., Whitehurst A.W., Xiong Y.; RT "The 3M complex maintains microtubule and genome integrity."; RL Mol. Cell 54:791-804(2014). RN [13] RP FUNCTION. RX PubMed=24793696; DOI=10.1016/j.molcel.2014.03.046; RA Li Z., Pei X.H., Yan J., Yan F., Cappell K.M., Whitehurst A.W., Xiong Y.; RT "CUL9 mediates the functions of the 3M complex and ubiquitylates survivin RT to maintain genome integrity."; RL Mol. Cell 54:805-819(2014). RN [14] RP INVOLVEMENT IN 3M2. RX PubMed=23018678; DOI=10.1530/jme-12-0034; RA Hanson D., Murray P.G., Coulson T., Sud A., Omokanye A., Stratta E., RA Sakhinia F., Bonshek C., Wilson L.C., Wakeling E., Temtamy S.A., Aglan M., RA Rosser E.M., Mansour S., Carcavilla A., Nampoothiri S., Khan W.I., RA Banerjee I., Chandler K.E., Black G.C., Clayton P.E.; RT "Mutations in CUL7, OBSL1 and CCDC8 in 3-M syndrome lead to disordered RT growth factor signalling."; RL J. Mol. Endocrinol. 49:267-275(2012). RN [15] RP STRUCTURE BY NMR OF 615-992. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of Ig-like domains from human obscurin-like protein RT 1."; RL Submitted (NOV-2005) to the PDB data bank. RN [16] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-105 IN COMPLEX WITH THE RP C-TERMINAL IG-LIKE DOMAIN OF TTN, AND INTERACTION WITH TTN. RX PubMed=20489725; DOI=10.1038/embor.2010.65; RA Sauer F., Vahokoski J., Song Y.H., Wilmanns M.; RT "Molecular basis of the head-to-tail assembly of giant muscle proteins RT obscurin-like 1 and titin."; RL EMBO Rep. 11:534-540(2010). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 1-106 OF WILD-TYPE AND MUTANT RP ARG-17 IN COMPLEX WITH THE C-TERMINAL IG-LIKE DOMAIN OF TTN, INTERACTION RP WITH TTN, AND MUTAGENESIS OF PHE-17. RX PubMed=20133654; DOI=10.1073/pnas.0913736107; RA Pernigo S., Fukuzawa A., Bertz M., Holt M., Rief M., Steiner R.A., RA Gautel M.; RT "Structural insight into M-band assembly and mechanics from the titin- RT obscurin-like-1 complex."; RL Proc. Natl. Acad. Sci. U.S.A. 107:2908-2913(2010). RN [18] RP STRUCTURE BY NMR OF 805-892. RG Northeast structural genomics consortium (NESG); RT "Solution NMR structure of Ig like domain (805-892) of obscurin-like RT protein 1 from Homo sapiens, Northeast Structural Genomics Consortium RT (NESG) Target HR8578K (CASP Target)."; RL Submitted (JUN-2012) to the PDB data bank. RN [19] RP STRUCTURE BY NMR OF 1277-1357. RG Northeast structural genomics consortium (NESG); RT "Solution NMR Structure of Ig like domain (1277-1357) of Obscurin-like RT protein 1 from Homo sapiens, Northeast Structural Genomics Consortium RT (NESG) Target HR8578D (CASP Target)."; RL Submitted (JUN-2012) to the PDB data bank. CC -!- FUNCTION: Core component of the 3M complex, a complex required to CC regulate microtubule dynamics and genome integrity. It is unclear how CC the 3M complex regulates microtubules, it could act by controlling the CC level of a microtubule stabilizer (PubMed:24793695, PubMed:24793696). CC Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, CC playing a critical role in the ubiquitin ligase pathway that regulates CC Golgi morphogenesis and dendrite patterning in brain. Required to CC localize CUL7 to the Golgi apparatus in neurons. CC {ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24793695, CC ECO:0000269|PubMed:24793696}. CC -!- SUBUNIT: Component of the 3M complex, composed of core components CUL7, CC CCDC8 and OBSL1. Interacts with CCDC8. Interacts with CUL7; the CC interaction is direct. Interacts with FBXW8. Interacts (via N-terminal CC Ig-like domain) with TTN/titin (via C-terminal Ig-like domain); the CC interaction is direct. {ECO:0000269|PubMed:20133654, CC ECO:0000269|PubMed:20489725, ECO:0000269|PubMed:21572988, CC ECO:0000269|PubMed:21737058, ECO:0000269|PubMed:24793695}. CC -!- INTERACTION: CC O75147; Q8WZ42: TTN; NbExp=13; IntAct=EBI-1223896, EBI-681210; CC O75147-2; Q14999: CUL7; NbExp=4; IntAct=EBI-15927144, EBI-308606; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24793695}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:24793695}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:24793695}. Golgi apparatus CC {ECO:0000269|PubMed:21572988}. Note=Colocalizes with CUL7 at the Golgi CC apparatus in neurons (PubMed:21572988). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=O75147-3; Sequence=Displayed; CC Name=2; CC IsoId=O75147-2; Sequence=VSP_040784, VSP_040785; CC Name=3; CC IsoId=O75147-1; Sequence=VSP_040786, VSP_040787, VSP_040788; CC Name=4; CC IsoId=O75147-4; Sequence=VSP_054755, VSP_054756; CC -!- TISSUE SPECIFICITY: Widely expressed, with predominant levels found in CC the heart. {ECO:0000269|PubMed:17289344}. CC -!- DISEASE: 3M syndrome 2 (3M2) [MIM:612921]: An autosomal recessive CC disorder characterized by severe pre- and postnatal growth retardation, CC facial dysmorphism, large head circumference, and normal intelligence CC and endocrine function. Skeletal changes include long slender tubular CC bones and tall vertebral bodies. {ECO:0000269|PubMed:19481195, CC ECO:0000269|PubMed:23018678}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAH07201.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EF063637; ABO42327.1; -; mRNA. DR EMBL; EF063638; ABO42328.1; -; mRNA. DR EMBL; AC009955; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471063; EAW70770.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70767.1; -; Genomic_DNA. DR EMBL; BC007201; AAH07201.1; ALT_INIT; mRNA. DR EMBL; AB014557; BAA31632.2; -; mRNA. DR CCDS; CCDS46520.1; -. [O75147-3] DR CCDS; CCDS54433.1; -. [O75147-2] DR CCDS; CCDS63134.1; -. [O75147-4] DR RefSeq; NP_001166879.1; NM_001173408.1. [O75147-2] DR RefSeq; NP_001166902.1; NM_001173431.1. [O75147-4] DR RefSeq; NP_056126.1; NM_015311.2. [O75147-3] DR PDB; 2CPC; NMR; -; A=893-992. DR PDB; 2E6P; NMR; -; A=714-804. DR PDB; 2E6Q; NMR; -; A=615-713. DR PDB; 2LU7; NMR; -; A=1277-1357. DR PDB; 2LVC; NMR; -; A=805-892. DR PDB; 2WP3; X-ray; 1.48 A; O=1-106. DR PDB; 2WWK; X-ray; 1.70 A; O=1-106. DR PDB; 2WWM; X-ray; 2.30 A; C/O=1-106. DR PDB; 3KNB; X-ray; 1.40 A; B=1-105. DR PDB; 5FM5; X-ray; 3.10 A; O/P=251-339. DR PDBsum; 2CPC; -. DR PDBsum; 2E6P; -. DR PDBsum; 2E6Q; -. DR PDBsum; 2LU7; -. DR PDBsum; 2LVC; -. DR PDBsum; 2WP3; -. DR PDBsum; 2WWK; -. DR PDBsum; 2WWM; -. DR PDBsum; 3KNB; -. DR PDBsum; 5FM5; -. DR AlphaFoldDB; O75147; -. DR SMR; O75147; -. DR BioGRID; 116944; 901. DR ComplexPortal; CPX-2838; 3M complex. DR CORUM; O75147; -. DR DIP; DIP-38340N; -. DR IntAct; O75147; 55. DR MINT; O75147; -. DR STRING; 9606.ENSP00000385636; -. DR GlyCosmos; O75147; 3 sites, 1 glycan. DR GlyGen; O75147; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; O75147; -. DR PhosphoSitePlus; O75147; -. DR BioMuta; OBSL1; -. DR EPD; O75147; -. DR jPOST; O75147; -. DR MassIVE; O75147; -. DR MaxQB; O75147; -. DR PaxDb; 9606-ENSP00000385636; -. DR PeptideAtlas; O75147; -. DR ProteomicsDB; 49811; -. [O75147-3] DR ProteomicsDB; 49812; -. [O75147-1] DR ProteomicsDB; 49813; -. [O75147-2] DR Pumba; O75147; -. DR Antibodypedia; 52509; 16 antibodies from 7 providers. DR DNASU; 23363; -. DR Ensembl; ENST00000373873.8; ENSP00000362980.4; ENSG00000124006.15. [O75147-2] DR Ensembl; ENST00000404537.6; ENSP00000385636.1; ENSG00000124006.15. [O75147-3] DR Ensembl; ENST00000603926.5; ENSP00000474519.1; ENSG00000124006.15. [O75147-4] DR GeneID; 23363; -. DR KEGG; hsa:23363; -. DR MANE-Select; ENST00000404537.6; ENSP00000385636.1; NM_015311.3; NP_056126.1. DR UCSC; uc002vmi.4; human. [O75147-3] DR AGR; HGNC:29092; -. DR CTD; 23363; -. DR DisGeNET; 23363; -. DR GeneCards; OBSL1; -. DR GeneReviews; OBSL1; -. DR HGNC; HGNC:29092; OBSL1. DR HPA; ENSG00000124006; Tissue enhanced (ovary). DR MalaCards; OBSL1; -. DR MIM; 610991; gene. DR MIM; 612921; phenotype. DR neXtProt; NX_O75147; -. DR OpenTargets; ENSG00000124006; -. DR Orphanet; 2616; 3M syndrome. DR PharmGKB; PA142671235; -. DR VEuPathDB; HostDB:ENSG00000124006; -. DR eggNOG; KOG0613; Eukaryota. DR GeneTree; ENSGT00940000156702; -. DR HOGENOM; CLU_000630_0_0_1; -. DR InParanoid; O75147; -. DR OMA; KAEVRWY; -. DR OrthoDB; 4633043at2759; -. DR PhylomeDB; O75147; -. DR PathwayCommons; O75147; -. DR Reactome; R-HSA-8951664; Neddylation. DR SignaLink; O75147; -. DR BioGRID-ORCS; 23363; 11 hits in 1153 CRISPR screens. DR ChiTaRS; CHPF; human. DR ChiTaRS; OBSL1; human. DR EvolutionaryTrace; O75147; -. DR GeneWiki; OBSL1; -. DR GenomeRNAi; 23363; -. DR Pharos; O75147; Tbio. DR PRO; PR:O75147; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; O75147; Protein. DR Bgee; ENSG00000124006; Expressed in right testis and 195 other cell types or tissues. DR ExpressionAtlas; O75147; baseline and differential. DR GO; GO:1990393; C:3M complex; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0014704; C:intercalated disc; TAS:BHF-UCL. DR GO; GO:0031430; C:M band; TAS:BHF-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0030018; C:Z disc; TAS:BHF-UCL. DR GO; GO:0008093; F:cytoskeletal anchor activity; NAS:BHF-UCL. DR GO; GO:0055003; P:cardiac myofibril assembly; NAS:BHF-UCL. DR GO; GO:0007010; P:cytoskeleton organization; NAS:BHF-UCL. DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB. DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB. DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:UniProtKB. DR CDD; cd00063; FN3; 1. DR CDD; cd00096; Ig; 3. DR CDD; cd04979; Ig_Semaphorin_C; 1. DR CDD; cd20967; IgI_C2_MyBP-C-like; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 20. 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 PANTHER; PTHR35971:SF6; OBSCURIN-LIKE PROTEIN 1; 1. DR PANTHER; PTHR35971; SI:DKEY-31G6.6; 1. DR Pfam; PF07679; I-set; 14. DR Pfam; PF13927; Ig_3; 1. DR SMART; SM00409; IG; 19. DR SMART; SM00408; IGc2; 14. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF48726; Immunoglobulin; 18. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS50835; IG_LIKE; 14. DR Genevisible; O75147; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; KW Disulfide bond; Dwarfism; Golgi apparatus; Immunoglobulin domain; KW Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..1896 FT /note="Obscurin-like protein 1" FT /id="PRO_0000247959" FT DOMAIN 12..100 FT /note="Ig-like 1" FT DOMAIN 128..225 FT /note="Ig-like 2" FT DOMAIN 243..330 FT /note="Ig-like 3" FT DOMAIN 339..425 FT /note="Ig-like 4" FT DOMAIN 517..615 FT /note="Fibronectin type-III" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 714..800 FT /note="Ig-like 5" FT DOMAIN 804..893 FT /note="Ig-like 6" FT DOMAIN 902..982 FT /note="Ig-like 7" FT DOMAIN 986..1075 FT /note="Ig-like 8" FT DOMAIN 1078..1172 FT /note="Ig-like 9" FT DOMAIN 1174..1261 FT /note="Ig-like 10" FT DOMAIN 1265..1357 FT /note="Ig-like 11" FT DOMAIN 1357..1534 FT /note="Ig-like 12" FT DOMAIN 1628..1720 FT /note="Ig-like 13" FT DOMAIN 1794..1896 FT /note="Ig-like 14" FT REGION 17..19 FT /note="Interaction with TTN" FT REGION 85..94 FT /note="Interaction with TTN" FT REGION 106..127 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT DISULFID 33..84 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 149..209 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 267..319 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 362..412 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 738..788 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 829..879 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 920..970 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1011..1061 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1103..1153 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1195..1245 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1381..1522 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1650..1700 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 986..1025 FT /note="PPVRIIYPRDEVTLIAVTLECVVLMCELSREDAPVRWYKD -> SYQSQDSS FT NNNPELCVLLKKPKTRRLWSRFPPWRRTAGTE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040784" FT VAR_SEQ 1026..1896 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040785" FT VAR_SEQ 1076..1167 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9734811" FT /id="VSP_040786" FT VAR_SEQ 1405..1493 FT /note="VEMAQNGSSRILTLRGCQLGDAGTVTLRAGSTATSARLHVRETELLFLRRLQ FT DVRAEEGQDVCLEVETGRVGAAGAVRWVRGGQPLPHD -> RQSCCSYGGCRMCGQRKA FT RTCVSKWRQAEWVQRGPCAGCEVGSPCPTTLACPWPRMGTSTASSSMVSYWPTRAPTAA FT RATTIAPWPGSA (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9734811" FT /id="VSP_040787" FT VAR_SEQ 1494..1896 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9734811" FT /id="VSP_040788" FT VAR_SEQ 1537..1543 FT /note="PRQLRVL -> RECPVLS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17289344" FT /id="VSP_054755" FT VAR_SEQ 1544..1896 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17289344" FT /id="VSP_054756" FT MUTAGEN 17 FT /note="F->R: Diminishes binding affinity for TTN." FT /evidence="ECO:0000269|PubMed:20133654" FT CONFLICT 165 FT /note="G -> R (in Ref. 5; BAA31632)" FT /evidence="ECO:0000305" FT CONFLICT 512 FT /note="C -> CG (in Ref. 1; ABO42327)" FT /evidence="ECO:0000305" FT CONFLICT 723 FT /note="R -> K (in Ref. 4; AAH07201, 5; BAA31632 and 3; FT EAW70767/EAW70770)" FT /evidence="ECO:0000305" FT CONFLICT 1365 FT /note="E -> D (in Ref. 5; BAA31632)" FT /evidence="ECO:0000305" FT STRAND 10..16 FT /evidence="ECO:0007829|PDB:3KNB" FT STRAND 21..24 FT /evidence="ECO:0007829|PDB:3KNB" FT STRAND 29..39 FT /evidence="ECO:0007829|PDB:3KNB" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:3KNB" FT STRAND 56..59 FT /evidence="ECO:0007829|PDB:3KNB" FT STRAND 66..73 FT /evidence="ECO:0007829|PDB:3KNB" FT HELIX 76..78 FT /evidence="ECO:0007829|PDB:3KNB" FT STRAND 80..88 FT /evidence="ECO:0007829|PDB:3KNB" FT STRAND 91..102 FT /evidence="ECO:0007829|PDB:3KNB" FT STRAND 254..258 FT /evidence="ECO:0007829|PDB:5FM5" FT STRAND 261..267 FT /evidence="ECO:0007829|PDB:5FM5" FT STRAND 269..273 FT /evidence="ECO:0007829|PDB:5FM5" FT STRAND 276..281 FT /evidence="ECO:0007829|PDB:5FM5" FT STRAND 290..296 FT /evidence="ECO:0007829|PDB:5FM5" FT STRAND 300..306 FT /evidence="ECO:0007829|PDB:5FM5" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:5FM5" FT STRAND 315..322 FT /evidence="ECO:0007829|PDB:5FM5" FT STRAND 327..337 FT /evidence="ECO:0007829|PDB:5FM5" FT STRAND 618..620 FT /evidence="ECO:0007829|PDB:2E6Q" FT STRAND 625..628 FT /evidence="ECO:0007829|PDB:2E6Q" FT STRAND 632..641 FT /evidence="ECO:0007829|PDB:2E6Q" FT STRAND 646..651 FT /evidence="ECO:0007829|PDB:2E6Q" FT STRAND 669..672 FT /evidence="ECO:0007829|PDB:2E6Q" FT STRAND 678..685 FT /evidence="ECO:0007829|PDB:2E6Q" FT STRAND 692..699 FT /evidence="ECO:0007829|PDB:2E6Q" FT STRAND 702..711 FT /evidence="ECO:0007829|PDB:2E6Q" FT STRAND 724..732 FT /evidence="ECO:0007829|PDB:2E6P" FT STRAND 748..751 FT /evidence="ECO:0007829|PDB:2E6P" FT STRAND 762..767 FT /evidence="ECO:0007829|PDB:2E6P" FT STRAND 770..777 FT /evidence="ECO:0007829|PDB:2E6P" FT TURN 780..782 FT /evidence="ECO:0007829|PDB:2E6P" FT STRAND 784..789 FT /evidence="ECO:0007829|PDB:2E6P" FT STRAND 797..802 FT /evidence="ECO:0007829|PDB:2E6P" FT STRAND 815..818 FT /evidence="ECO:0007829|PDB:2LVC" FT STRAND 825..830 FT /evidence="ECO:0007829|PDB:2LVC" FT STRAND 839..842 FT /evidence="ECO:0007829|PDB:2LVC" FT STRAND 854..858 FT /evidence="ECO:0007829|PDB:2LVC" FT STRAND 861..868 FT /evidence="ECO:0007829|PDB:2LVC" FT HELIX 871..873 FT /evidence="ECO:0007829|PDB:2LVC" FT STRAND 875..880 FT /evidence="ECO:0007829|PDB:2LVC" FT STRAND 885..891 FT /evidence="ECO:0007829|PDB:2LVC" FT STRAND 898..902 FT /evidence="ECO:0007829|PDB:2CPC" FT STRAND 906..911 FT /evidence="ECO:0007829|PDB:2CPC" FT STRAND 916..923 FT /evidence="ECO:0007829|PDB:2CPC" FT STRAND 930..933 FT /evidence="ECO:0007829|PDB:2CPC" FT STRAND 944..948 FT /evidence="ECO:0007829|PDB:2CPC" FT STRAND 950..959 FT /evidence="ECO:0007829|PDB:2CPC" FT TURN 962..964 FT /evidence="ECO:0007829|PDB:2CPC" FT STRAND 966..974 FT /evidence="ECO:0007829|PDB:2CPC" FT STRAND 976..984 FT /evidence="ECO:0007829|PDB:2CPC" FT STRAND 1279..1281 FT /evidence="ECO:0007829|PDB:2LU7" FT STRAND 1287..1290 FT /evidence="ECO:0007829|PDB:2LU7" FT STRAND 1301..1304 FT /evidence="ECO:0007829|PDB:2LU7" FT STRAND 1313..1319 FT /evidence="ECO:0007829|PDB:2LU7" FT STRAND 1324..1330 FT /evidence="ECO:0007829|PDB:2LU7" FT STRAND 1337..1342 FT /evidence="ECO:0007829|PDB:2LU7" FT TURN 1344..1346 FT /evidence="ECO:0007829|PDB:2LU7" FT STRAND 1348..1354 FT /evidence="ECO:0007829|PDB:2LU7" SQ SEQUENCE 1896 AA; 206947 MW; 6D592AC3E30E9ACA CRC64; MKASSGDQGS PPCFLRFPRP VRVVSGAEAE LKCVVLGEPP PVVVWEKGGQ QLAASERLSF PADGAEHGLL LTAALPTDAG VYVCRARNAA GEAYAAAAVT VLEPPASDPE LQPAERPLPS PGSGEGAPVF LTGPRSQWVL RGAEVVLTCR AGGLPEPTLY WEKDGMALDE VWDSSHFALQ PGRAEDGPGA SLALRILAAR LPDSGVYVCH ARNAHGHAQA GALLQVHQPP ESPPADPDEA PAPVVEPLKC APKTFWVNEG KHAKFRCYVM GKPEPEIEWH WEGRPLLPDR RRLMYRDRDG GFVLKVLYCQ AKDRGLYVCA ARNSAGQTLS AVQLHVKEPR LRFTRPLQDV EGREHGIAVL ECKVPNSRIP TAWFREDQRL LPCRKYEQIE EGTVRRLIIH RLKADDDGIY LCEMRGRVRT VANVTVKGPI LKRLPRKLDV LEGENAVLLV ETLEAGVEGR WSRDGEELPV ICQSSSGHMH ALVLPGVTRE DAGEVTFSLG NSRTTTLLRV KCVKHSPPGP PILAEMFKGH KNTVLLTWKP PEPAPETPFI YRLERQEVGS EDWIQCFSIE KAGAVEVPGD CVPSEGDYRF RICTVSGHGR SPHVVFHGSA HLVPTARLVA GLEDVQVYDG EDAVFSLDLS TIIQGTWFLN GEELKSNEPE GQVEPGALRY RIEQKGLQHR LILHAVKHQD SGALVGFSCP GVQDSAALTI QESPVHILSP QDRVSLTFTT SERVVLTCEL SRVDFPATWY KDGQKVEESE LLVVKMDGRK HRLILPEAKV QDSGEFECRT EGVSAFFGVT VQDPPVHIVD PREHVFVHAI TSECVMLACE VDREDAPVRW YKDGQEVEES DFVVLENEGP HRRLVLPATQ PSDGGEFQCV AGDECAYFTV TITDVSSWIV YPSGKVYVAA VRLERVVLTC ELCRPWAEVR WTKDGEEVVE SPALLLQKED TVRRLVLPAV QLEDSGEYLC EIDDESASFT VTVTEPPVRI IYPRDEVTLI AVTLECVVLM CELSREDAPV RWYKDGLEVE ESEALVLERD GPRCRLVLPA AQPEDGGEFV CDAGDDSAFF TVTVTAPPER IVHPAARSLD LHFGAPGRVE LRCEVAPAGS QVRWYKDGLE VEASDALQLG AEGPTRTLTL PHAQPEDAGE YVCETRHEAI TFNVILAEPP VQFLALETTP SPLCVAPGEP VVLSCELSRA GAPVVWSHNG RPVQEGEGLE LHAEGPRRVL CIQAAGPAHA GLYTCQSGAA PGAPSLSFTV QVAEPPVRVV APEAAQTRVR STPGGDLELV VHLSGPGGPV RWYKDGERLA SQGRVQLEQA GARQVLRVQG ARSGDAGEYL CDAPQDSRIF LVSVEEPLLV KLVSELTPLT VHEGDDATFR CEVSPPDADV TWLRNGAVVT PGPQVEMAQN GSSRILTLRG CQLGDAGTVT LRAGSTATSA RLHVRETELL FLRRLQDVRA EEGQDVCLEV ETGRVGAAGA VRWVRGGQPL PHDSRLSMAQ DGHIHRLFIH GVILADQGTY GCESHHDRTL ARLSVRPRQL RVLRPLEDVT ISEGGSATFQ LELSQEGVTG EWARGGVQLY PGPKCHIHSD GHRHRLVLNG LGLADSGCVS FTADSLRCAA RLIVREVPVT IVRGPHDLEV TEGDTATFEC ELSQALADVT WEKDGNALTP SPRLRLQALG TRRLLQLRRC GPSDAGTYSC AVGTARAGPV RLTVRERTVA VLSELRSVSA REGDGATFEC TVSEVETTGR WELGGRPLRP GARVRIRQEG KKHILVLSEL RAEDAGEVRF QAGPAQSLAL LEVEALPLQM CRHPPREKTV LVGRRAVLEV TVSRSGGHVC WLREGAELCP GDKYEMRSHG PTHSLVIHDV RPEDQGTYCC QAGQDSTHTR LLVEGN //