RCC1L_HUMAN
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 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 163.
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), AND TISSUE SPECIFICITY.
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), AND VARIANT ARG-30.
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], AND VARIANT ARG-30.
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).
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; Q92993: KAT5; NbExp=3; IntAct=EBI-2117080, EBI-399080;
CC Q96I51; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2117080, EBI-11742507;
CC Q96I51; O75414: NME6; NbExp=5; IntAct=EBI-2117080, EBI-3941531;
CC Q96I51; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-2117080, EBI-9090795;
CC Q96I51; P61981: YWHAG; NbExp=3; IntAct=EBI-2117080, EBI-359832;
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}.
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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 AlphaFoldDB; Q96I51; -.
DR BioGRID; 123518; 111.
DR IntAct; Q96I51; 22.
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; 105 antibodies from 19 providers.
DR DNASU; 81554; -.
DR Ensembl; ENST00000610322.5; ENSP00000480364.1; ENSG00000274523.5. [Q96I51-1]
DR Ensembl; ENST00000614461.4; ENSP00000477659.1; ENSG00000274523.5. [Q96I51-3]
DR Ensembl; ENST00000618035.4; ENSP00000480781.1; ENSG00000274523.5. [Q96I51-2]
DR GeneID; 81554; -.
DR KEGG; hsa:81554; -.
DR MANE-Select; ENST00000610322.5; ENSP00000480364.1; NM_030798.5; NP_110425.2.
DR UCSC; uc003ubr.5; human. [Q96I51-1]
DR CTD; 81554; -.
DR DisGeNET; 81554; -.
DR GeneCards; RCC1L; -.
DR HGNC; HGNC:14948; RCC1L.
DR HPA; ENSG00000274523; Low tissue specificity.
DR MIM; 194050; phenotype.
DR neXtProt; NX_Q96I51; -.
DR OpenTargets; ENSG00000274523; -.
DR PharmGKB; PA37941; -.
DR VEuPathDB; HostDB:ENSG00000274523; -.
DR eggNOG; KOG1426; Eukaryota.
DR GeneTree; ENSGT00940000157317; -.
DR HOGENOM; CLU_037900_0_0_1; -.
DR InParanoid; Q96I51; -.
DR OrthoDB; 1062377at2759; -.
DR PhylomeDB; Q96I51; -.
DR TreeFam; TF317425; -.
DR PathwayCommons; Q96I51; -.
DR SignaLink; Q96I51; -.
DR BioGRID-ORCS; 81554; 355 hits in 1078 CRISPR screens.
DR ChiTaRS; RCC1L; human.
DR GenomeRNAi; 81554; -.
DR Pharos; Q96I51; Tbio.
DR PRO; PR:Q96I51; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96I51; protein.
DR Bgee; ENSG00000274523; Expressed in gastrocnemius and 179 other tissues.
DR ExpressionAtlas; Q96I51; baseline and differential.
DR Genevisible; Q96I51; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
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:0008053; P:mitochondrial 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; Reference proteome;
KW 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="G -> R (in dbSNP:rs6955671)"
FT /evidence="ECO:0000269|PubMed:11230166, ECO:0000269|Ref.4"
FT /id="VAR_027972"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:5XGS"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:5XGS"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 183..193
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:5XGS"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 285..299
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:5XGS"
FT TURN 314..318
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:5XGS"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:5XGS"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:5XGS"
FT TURN 423..426
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 443..451
FT /evidence="ECO:0007829|PDB:5XGS"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:5XGS"
SQ SEQUENCE 464 AA; 49898 MW; 24070C01557E6A4D CRC64;
MALVALVAGA RLGRRLSGPG LGRGHWTAAG 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
