ID OBSL1_HUMAN Reviewed; 1896 AA. AC O75147; A4KVA5; Q96IW3; DT 22-AUG-2006, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 4. DT 25-JAN-2012, entry version 91. DE RecName: Full=Obscurin-like protein 1; DE Flags: Precursor; GN Name=OBSL1; Synonyms=KIAA0657; 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 [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE RP SPECIFICITY. 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [3] 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-1896 (ISOFORM 3). RC TISSUE=Brain; RX MEDLINE=98403880; 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. RT The complete sequences of 100 new cDNA clones from brain which can RT code for large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [5] RP SEQUENCE REVISION. RX MEDLINE=22158633; 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 [6] 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., RA Superti-Furga A., Holder S.E., Urquhart J., Hilton E., Manson F.D.C., RA Scambler P., Black G.C.M., Clayton P.E.; RT "The primordial growth disorder 3-M syndrome connects ubiquitination RT to the cytoskeletal adaptor OBSL1."; RL Am. J. Hum. Genet. 84:801-806(2009). RN [7] 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., RA Bhaskar S.S., Biesecker L.G., Skae M., Smith C., Cole T., Kirk J., RA Chandler K., Kingston H., Donnai D., Clayton P.E., Black G.C.; RT "Exome sequencing identifies CCDC8 mutations in 3-M syndrome, RT Suggesting that CCDC8 Contributes in a Pathway with CUL7 and OBSL1 to RT Control Human Growth."; RL Am. J. Hum. Genet. 89:148-153(2011). RN [8] RP STRUCTURE BY NMR OF 615-992. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of Ig-like domains from human obscurin-like RT protein 1."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- SUBUNIT: Interacts with CCDC8 and CUL7. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; 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 -!- TISSUE SPECIFICITY: Widely expressed, with predominant levels CC found in the heart. CC -!- DISEASE: Defects in OBSL1 are the cause of 3M syndrome type 2 CC (3M2) [MIM:612921]. An autosomal recessive disorder characterized CC by severe pre- and postnatal growth retardation, facial CC dysmorphism, large head circumference, and normal intelligence and CC endocrine function. Skeletal changes include long slender tubular CC bones and tall vertebral bodies. CC -!- SIMILARITY: Contains 1 fibronectin type-III domain. CC -!- SIMILARITY: Contains 11 Ig-like (immunoglobulin-like) domains. CC -!- SEQUENCE CAUTION: CC Sequence=AAH07201.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; 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; EF063638; ABO42328.1; -; mRNA. DR EMBL; AC009955; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007201; AAH07201.1; ALT_INIT; mRNA. DR EMBL; AB014557; BAA31632.2; -; mRNA. DR IPI; IPI00306305; -. DR IPI; IPI00883737; -. DR IPI; IPI00893234; -. DR RefSeq; NP_001166879.1; NM_001173408.1. DR RefSeq; NP_056126.1; NM_015311.2. DR UniGene; Hs.526594; -. DR PDB; 2CPC; NMR; -; A=893-992. DR PDB; 2E6P; NMR; -; A=714-804. DR PDB; 2E6Q; NMR; -; A=615-713. 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 PDBsum; 2CPC; -. DR PDBsum; 2E6P; -. DR PDBsum; 2E6Q; -. DR PDBsum; 2WP3; -. DR PDBsum; 2WWK; -. DR PDBsum; 2WWM; -. DR PDBsum; 3KNB; -. DR ProteinModelPortal; O75147; -. DR SMR; O75147; 8-103, 608-804, 893-992. DR IntAct; O75147; 4. DR STRING; O75147; -. DR PhosphoSite; O75147; -. DR PRIDE; O75147; -. DR Ensembl; ENST00000265318; ENSP00000265318; ENSG00000124006. DR Ensembl; ENST00000404537; ENSP00000385636; ENSG00000124006. DR GeneID; 23363; -. DR KEGG; hsa:23363; -. DR CTD; 23363; -. DR GeneCards; GC02M220415; -. DR H-InvDB; HIX0002869; -. DR HGNC; HGNC:29092; OBSL1. DR HPA; HPA036404; -. DR MIM; 610991; gene. DR MIM; 612921; phenotype. DR neXtProt; NX_O75147; -. DR Orphanet; 2616; 3M syndrome. DR eggNOG; prNOG07600; -. DR GeneTree; ENSGT00600000084278; -. DR HOGENOM; HBG714429; -. DR HOVERGEN; HBG082081; -. DR OMA; PTVLWEK; -. DR PhylomeDB; O75147; -. DR NextBio; 45409; -. DR ArrayExpress; O75147; -. DR Bgee; O75147; -. DR CleanEx; HS_OBSL1; -. DR Genevestigator; O75147; -. DR GermOnline; ENSG00000124006; Homo sapiens. 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; TAS:BHF-UCL. DR GO; GO:0030018; C:Z disc; TAS:BHF-UCL. DR GO; GO:0008093; F:cytoskeletal adaptor activity; NAS:BHF-UCL. DR GO; GO:0055003; P:cardiac myofibril assembly; IEP:BHF-UCL. DR InterPro; IPR003961; Fibronectin_type3. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 20. DR Pfam; PF07679; I-set; 15. DR SMART; SM00060; FN3; 1. DR SMART; SM00409; IG; 12. DR SMART; SM00408; IGc2; 6. DR SUPFAM; SSF49265; FN_III-like; 1. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS50835; IG_LIKE; 14. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Disulfide bond; KW Dwarfism; Immunoglobulin domain; Phosphoprotein; Reference proteome; KW Repeat; Signal. FT SIGNAL 1 29 Potential. FT CHAIN 30 1896 Obscurin-like protein 1. FT /FTId=PRO_0000247959. FT DOMAIN 30 100 Ig-like 1. FT DOMAIN 128 225 Ig-like 2. FT DOMAIN 243 330 Ig-like 3. FT DOMAIN 339 425 Ig-like 4. FT DOMAIN 517 610 Fibronectin type-III. FT DOMAIN 714 800 Ig-like 5. FT DOMAIN 804 893 Ig-like 6. FT DOMAIN 902 982 Ig-like 7. FT DOMAIN 986 1075 Ig-like 8. FT DOMAIN 1078 1172 Ig-like 9. FT DOMAIN 1174 1261 Ig-like 10. FT DOMAIN 1265 1357 Ig-like 11. FT DOMAIN 1357 1534 Ig-like 12. FT DOMAIN 1628 1720 Ig-like 13. FT DOMAIN 1794 1896 Ig-like 14. FT DISULFID 33 84 By similarity. FT DISULFID 149 209 By similarity. FT DISULFID 267 319 By similarity. FT DISULFID 362 412 By similarity. FT DISULFID 738 788 By similarity. FT DISULFID 829 879 By similarity. FT DISULFID 920 970 By similarity. FT DISULFID 1011 1061 By similarity. FT DISULFID 1103 1153 By similarity. FT DISULFID 1195 1245 By similarity. FT DISULFID 1381 1522 By similarity. FT DISULFID 1650 1700 By similarity. FT VAR_SEQ 986 1025 PPVRIIYPRDEVTLIAVTLECVVLMCELSREDAPVRWYKD FT -> SYQSQDSSNNNPELCVLLKKPKTRRLWSRFPPWRRTAG FT TE (in isoform 2). FT /FTId=VSP_040784. FT VAR_SEQ 1026 1896 Missing (in isoform 2). FT /FTId=VSP_040785. FT VAR_SEQ 1076 1167 Missing (in isoform 3). FT /FTId=VSP_040786. FT VAR_SEQ 1405 1493 VEMAQNGSSRILTLRGCQLGDAGTVTLRAGSTATSARLHVR FT ETELLFLRRLQDVRAEEGQDVCLEVETGRVGAAGAVRWVRG FT GQPLPHD -> RQSCCSYGGCRMCGQRKARTCVSKWRQAEW FT VQRGPCAGCEVGSPCPTTLACPWPRMGTSTASSSMVSYWPT FT RAPTAARATTIAPWPGSA (in isoform 3). FT /FTId=VSP_040787. FT VAR_SEQ 1494 1896 Missing (in isoform 3). FT /FTId=VSP_040788. FT CONFLICT 165 165 G -> R (in Ref. 4; BAA31632). FT CONFLICT 723 723 R -> K (in Ref. 3; AAH07201 and 4; FT BAA31632). FT CONFLICT 1365 1365 E -> D (in Ref. 4; BAA31632). FT STRAND 618 620 FT STRAND 625 628 FT STRAND 632 641 FT STRAND 646 651 FT STRAND 669 672 FT STRAND 678 685 FT STRAND 692 699 FT STRAND 702 711 FT STRAND 724 732 FT STRAND 748 751 FT STRAND 762 767 FT STRAND 770 777 FT TURN 780 782 FT STRAND 784 789 FT STRAND 797 802 FT STRAND 898 902 FT STRAND 906 911 FT STRAND 916 923 FT STRAND 930 933 FT STRAND 944 948 FT STRAND 950 959 FT TURN 962 964 FT STRAND 966 974 FT STRAND 976 984 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 //