OBSL1_HUMAN
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 03-AUG-2022, entry version 175.
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};
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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; 896.
DR CORUM; O75147; -.
DR DIP; DIP-38340N; -.
DR IntAct; O75147; 54.
DR MINT; O75147; -.
DR STRING; 9606.ENSP00000385636; -.
DR GlyGen; O75147; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; O75147; -.
DR PhosphoSitePlus; O75147; -.
DR BioMuta; OBSL1; -.
DR EPD; O75147; -.
DR jPOST; O75147; -.
DR MassIVE; O75147; -.
DR MaxQB; O75147; -.
DR PaxDb; O75147; -.
DR PeptideAtlas; O75147; -.
DR PRIDE; O75147; -.
DR ProteomicsDB; 49811; -. [O75147-3]
DR ProteomicsDB; 49812; -. [O75147-1]
DR ProteomicsDB; 49813; -. [O75147-2]
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 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; THRRCQA; -.
DR OrthoDB; 15947at2759; -.
DR PhylomeDB; O75147; -.
DR PathwayCommons; O75147; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; O75147; -.
DR BioGRID-ORCS; 23363; 10 hits in 1073 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 193 other tissues.
DR ExpressionAtlas; O75147; baseline and differential.
DR Genevisible; O75147; HS.
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:0045202; C:synapse; IBA:GO_Central.
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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
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 GO; GO:0010842; P:retina layer formation; IBA:GO_Central.
DR GO; GO:0007416; P:synapse assembly; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 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 Pfam; PF07679; I-set; 13.
DR SMART; SM00409; IG; 19.
DR SMART; SM00408; IGc2; 14.
DR SUPFAM; SSF48726; SSF48726; 18.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 14.
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
