ID RCC1L_HUMAN Reviewed; 464 AA. AC Q96I51; D3DXK0; F5GX55; F5H6C7; Q548B1; Q8IW88; Q8N572; Q9H0G7; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 22-APR-2020, entry version 153. DE RecName: Full=RCC1-like G exchanging factor-like protein; DE Short=RCC1-like {ECO:0000303|PubMed:28608466}; DE AltName: Full=Williams-Beuren syndrome chromosomal region 16 protein {ECO:0000303|PubMed:28608466}; DE Flags: Precursor; GN Name=RCC1L {ECO:0000312|HGNC:HGNC:14948}; GN Synonyms=WBSCR16 {ECO:0000303|PubMed:27667664, ECO:0000303|PubMed:28608466, GN ECO:0000303|PubMed:28746876}; 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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT RP GLY-30. RX PubMed=12073013; DOI=10.1007/s00439-002-0710-x; RA Merla G., Ucla C., Guipponi M., Reymond A.; RT "Identification of additional transcripts in the Williams-Beuren syndrome RT critical region."; RL Hum. Genet. 110:429-438(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS RP GLY-30 AND GLY-30. RC TISSUE=Lymph, and Uterus; 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 [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [8] RP FUNCTION, AND SUBUNIT. RX PubMed=27667664; DOI=10.1016/j.cmet.2016.08.017; RA Arroyo J.D., Jourdain A.A., Calvo S.E., Ballarano C.A., Doench J.G., RA Root D.E., Mootha V.K.; RT "A Genome-wide CRISPR Death Screen Identifies Genes Essential for Oxidative RT Phosphorylation."; RL Cell Metab. 24:875-885(2016). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=28746876; DOI=10.1016/j.celrep.2017.06.090; RA Huang G., Massoudi D., Muir A.M., Joshi D.C., Zhang C.L., Chiu S.Y., RA Greenspan D.S.; RT "WBSCR16 Is a Guanine Nucleotide Exchange Factor Important for RT Mitochondrial Fusion."; RL Cell Rep. 20:923-934(2017). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 32-464, DOMAIN, AND SUBCELLULAR RP LOCATION. RX PubMed=28608466; DOI=10.1002/pro.3210; RA Koyama M., Sasaki T., Sasaki N., Matsuura Y.; RT "Crystal structure of human WBSCR16, an RCC1-like protein in RT mitochondria."; RL Protein Sci. 26:1870-1877(2017). CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for mitochondrial CC dynamin-related GTPase OPA1. Activates OPA1, by exchanging bound GDP CC for free GTP, and drives OPA1 and MFN1-dependent mitochondrial fusion CC (PubMed:28746876). Plays an essential role in mitochondrial ribosome CC biogenesis. As a component of a functional protein-RNA module, CC consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S CC mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA CC abundance and is required for intra-mitochondrial translation of core CC subunits of the oxidative phosphorylation system (PubMed:27667664). CC {ECO:0000269|PubMed:27667664, ECO:0000269|PubMed:28746876}. CC -!- SUBUNIT: Forms a regulatory protein-RNA complex, consisting of RCC1L, CC NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA. Interacts with CC 16S mt-rRNA; this interaction is direct (PubMed:27667664). Interacts CC with OPA1; this interaction is direct (PubMed:28746876). CC {ECO:0000269|PubMed:27667664, ECO:0000269|PubMed:28746876}. CC -!- INTERACTION: CC Q96I51; O75414: NME6; NbExp=5; IntAct=EBI-2117080, EBI-3941531; CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane CC {ECO:0000269|PubMed:28608466, ECO:0000269|PubMed:28746876}. CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9CYF5}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96I51-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96I51-2; Sequence=VSP_055617, VSP_055618; CC Name=3; CC IsoId=Q96I51-3; Sequence=VSP_055619; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12073013}. CC -!- DOMAIN: The RCC1-like repeats assemble into a circular seven-bladed CC beta propeller structure. Each blade is composed of four antiparallel CC beta-strands with loops between each strand. CC {ECO:0000269|PubMed:28608466}. CC -!- DISEASE: Note=WBSCR16 is located in the Williams-Beuren syndrome (WBS) CC critical region. WBS results from a hemizygous deletion of several CC genes on chromosome 7q11.23, thought to arise as a consequence of CC unequal crossing over between highly homologous low-copy repeat CC sequences flanking the deleted region. Haploinsufficiency of WBSCR16 CC may be the cause of certain cardiovascular and musculo-skeletal CC abnormalities observed in the disease. {ECO:0000305|PubMed:12073013}. 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; AF410455; AAM62304.1; -; mRNA. DR EMBL; AL136804; CAB66738.1; -; mRNA. DR EMBL; AC124781; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471292; EAW52090.1; -; Genomic_DNA. DR EMBL; CH471292; EAW52091.1; -; Genomic_DNA. DR EMBL; BC007823; AAH07823.1; -; mRNA. DR EMBL; BC019008; AAH19008.1; -; mRNA. DR EMBL; BC032712; AAH32712.1; -; mRNA. DR EMBL; BC040695; AAH40695.1; -; mRNA. DR CCDS; CCDS5577.1; -. [Q96I51-1] DR CCDS; CCDS64683.1; -. [Q96I51-3] DR CCDS; CCDS64684.1; -. [Q96I51-2] DR RefSeq; NP_001268370.1; NM_001281441.1. DR RefSeq; NP_110425.2; NM_030798.4. DR RefSeq; NP_683682.1; NM_148842.2. DR PDB; 5XGS; X-ray; 2.00 A; A/B=32-464. DR PDBsum; 5XGS; -. DR SMR; Q96I51; -. DR BioGrid; 123518; 39. DR IntAct; Q96I51; 18. DR MINT; Q96I51; -. DR STRING; 9606.ENSP00000480364; -. DR iPTMnet; Q96I51; -. DR PhosphoSitePlus; Q96I51; -. DR BioMuta; RCC1L; -. DR DMDM; 116242843; -. DR EPD; Q96I51; -. DR jPOST; Q96I51; -. DR MassIVE; Q96I51; -. DR MaxQB; Q96I51; -. DR PaxDb; Q96I51; -. DR PeptideAtlas; Q96I51; -. DR PRIDE; Q96I51; -. DR ProteomicsDB; 24317; -. DR ProteomicsDB; 27147; -. DR ProteomicsDB; 76812; -. [Q96I51-1] DR Antibodypedia; 73171; 99 antibodies. DR DNASU; 81554; -. DR Ensembl; ENST00000610322; ENSP00000480364; ENSG00000274523. DR Ensembl; ENST00000614461; ENSP00000477659; ENSG00000274523. DR Ensembl; ENST00000618035; ENSP00000480781; ENSG00000274523. DR GeneID; 81554; -. DR KEGG; hsa:81554; -. DR UCSC; uc003ubr.5; human. [Q96I51-1] DR CTD; 81554; -. DR GeneCards; RCC1L; -. DR HGNC; HGNC:14948; RCC1L. DR HPA; ENSG00000274523; Tissue enhanced (skeletal). DR MIM; 194050; phenotype. DR neXtProt; NX_Q96I51; -. DR PharmGKB; PA37941; -. DR eggNOG; KOG1426; Eukaryota. DR eggNOG; COG5184; LUCA. DR HOGENOM; CLU_037900_0_0_1; -. DR InParanoid; Q96I51; -. DR KO; K23495; -. DR OrthoDB; 1062377at2759; -. DR PhylomeDB; Q96I51; -. DR TreeFam; TF317425; -. DR ChiTaRS; RCC1L; human. DR GenomeRNAi; 81554; -. DR Pharos; Q96I51; Tdark. DR PRO; PR:Q96I51; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q96I51; protein. DR Bgee; ENSG00000274523; Expressed in muscle of leg and 205 other tissues. DR ExpressionAtlas; Q96I51; baseline and differential. DR Genevisible; Q96I51; HS. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0019843; F:rRNA binding; IDA:UniProtKB. DR GO; GO:1990613; P:mitochondrial membrane fusion; IMP:UniProtKB. DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IMP:UniProtKB. DR Gene3D; 2.130.10.30; -; 2. DR InterPro; IPR009091; RCC1/BLIP-II. DR InterPro; IPR000408; Reg_chr_condens. DR Pfam; PF00415; RCC1; 3. DR PRINTS; PR00633; RCCNDNSATION. DR SUPFAM; SSF50985; SSF50985; 1. DR PROSITE; PS00626; RCC1_2; 1. DR PROSITE; PS50012; RCC1_3; 6. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; GTP-binding; KW Guanine-nucleotide releasing factor; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Nucleotide-binding; Polymorphism; KW Reference proteome; Repeat; RNA-binding; rRNA-binding; Transit peptide; KW Williams-Beuren syndrome. FT TRANSIT 1..31 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 32..464 FT /note="RCC1-like G exchanging factor-like protein" FT /id="PRO_0000206656" FT REPEAT 58..124 FT /note="RCC1 1" FT /evidence="ECO:0000255, ECO:0000305|PubMed:28608466" FT REPEAT 128..191 FT /note="RCC1 2" FT /evidence="ECO:0000255, ECO:0000305|PubMed:28608466" FT REPEAT 193..247 FT /note="RCC1 3" FT /evidence="ECO:0000255, ECO:0000305|PubMed:28608466" FT REPEAT 248..300 FT /note="RCC1 4" FT /evidence="ECO:0000255, ECO:0000305|PubMed:28608466" FT REPEAT 302..353 FT /note="RCC1 5" FT /evidence="ECO:0000255, ECO:0000305|PubMed:28608466" FT REPEAT 354..411 FT /note="RCC1 6" FT /evidence="ECO:0000255, ECO:0000305|PubMed:28608466" FT REPEAT 412..461 FT /note="RCC1 7" FT /evidence="ECO:0000255, ECO:0000305|PubMed:28608466" FT VAR_SEQ 353..358 FT /note="GEGHVF -> DTWPQS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055617" FT VAR_SEQ 359..464 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055618" FT VAR_SEQ 440..464 FT /note="VTMPGEPVDVACGVDHMVTLAKSFI -> APAPSASAKTTGPLL (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055619" FT VARIANT 30 FT /note="R -> G (in dbSNP:rs6955671)" FT /evidence="ECO:0000269|PubMed:12073013, FT ECO:0000269|PubMed:15489334" FT /id="VAR_027972" FT STRAND 60..66 FT /evidence="ECO:0000244|PDB:5XGS" FT HELIX 75..78 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 79..81 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 95..102 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 109..114 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 116..123 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 126..128 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 131..136 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 156..163 FT /evidence="ECO:0000244|PDB:5XGS" FT TURN 171..173 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 176..181 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 183..193 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 195..199 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 223..225 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 228..230 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 232..237 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 239..246 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 251..255 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 264..268 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 270..275 FT /evidence="ECO:0000244|PDB:5XGS" FT HELIX 278..280 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 285..299 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 304..309 FT /evidence="ECO:0000244|PDB:5XGS" FT TURN 314..318 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 322..329 FT /evidence="ECO:0000244|PDB:5XGS" FT TURN 333..335 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 337..343 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 345..352 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 357..363 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 373..379 FT /evidence="ECO:0000244|PDB:5XGS" FT HELIX 382..385 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 389..391 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 396..401 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 403..410 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 415..419 FT /evidence="ECO:0000244|PDB:5XGS" FT TURN 423..426 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 428..430 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 434..440 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 443..451 FT /evidence="ECO:0000244|PDB:5XGS" FT STRAND 453..461 FT /evidence="ECO:0000244|PDB:5XGS" SQ SEQUENCE 464 AA; 49997 MW; 800F7AD456A9B4EF CRC64; MALVALVAGA RLGRRLSGPG LGRGHWTAAR RSRSRREAAE AEAEVPVVQY VGERAARADR VFVWGFSFSG ALGVPSFVVP SSGPGPRAGA RPRRRIQPVP YRLELDQKIS SAACGYGFTL LSSKTADVTK VWGMGLNKDS QLGFHRSRKD KTRGYEYVLE PSPVSLPLDR PQETRVLQVS CGRAHSLVLT DREGVFSMGN NSYGQCGRKV VENEIYSESH RVHRMQDFDG QVVQVACGQD HSLFLTDKGE VYSCGWGADG QTGLGHYNIT SSPTKLGGDL AGVNVIQVAT YGDCCLAVSA DGGLFGWGNS EYLQLASVTD STQVNVPRCL HFSGVGKVRQ AACGGTGCAV LNGEGHVFVW GYGILGKGPN LVESAVPEMI PPTLFGLTEF NPEIQVSRIR CGLSHFAALT NKGELFVWGK NIRGCLGIGR LEDQYFPWRV TMPGEPVDVA CGVDHMVTLA KSFI //