RCC1L_MOUSE
ID RCC1L_MOUSE Reviewed; 461 AA.
AC Q9CYF5;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=RCC1-like G exchanging factor-like protein;
DE Short=RCC1-like;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 16 protein homolog;
DE Flags: Precursor;
GN Name=Rcc1l {ECO:0000312|MGI:MGI:2137600};
GN Synonyms=Wbscr16 {ECO:0000303|PubMed:28746876};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Liver;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
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).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q96I51, 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 (By similarity). Interacts with
CC OPA1; this interaction is direct (PubMed:28746876).
CC {ECO:0000250|UniProtKB:Q96I51, ECO:0000269|PubMed:28746876}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:28746876}.
CC -!- TISSUE SPECIFICITY: At E8.5, broadly expressed in yolk sac placenta,
CC decidua, and embryo, with highest levels found in the trophoblast giant
CC cells (TGCs) and ectoplacental cone (at protein level).
CC {ECO:0000269|PubMed:28746876}.
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:0000250|UniProtKB:Q96I51}.
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DR EMBL; AK017733; BAB30902.1; -; mRNA.
DR EMBL; BC024714; AAH24714.1; -; mRNA.
DR EMBL; BC055335; AAH55335.1; -; mRNA.
DR CCDS; CCDS19718.1; -.
DR RefSeq; NP_291050.1; NM_033572.2.
DR AlphaFoldDB; Q9CYF5; -.
DR SMR; Q9CYF5; -.
DR STRING; 10090.ENSMUSP00000075581; -.
DR iPTMnet; Q9CYF5; -.
DR PhosphoSitePlus; Q9CYF5; -.
DR EPD; Q9CYF5; -.
DR MaxQB; Q9CYF5; -.
DR PaxDb; Q9CYF5; -.
DR PRIDE; Q9CYF5; -.
DR ProteomicsDB; 255170; -.
DR Antibodypedia; 73171; 105 antibodies from 19 providers.
DR DNASU; 94254; -.
DR Ensembl; ENSMUST00000076228; ENSMUSP00000075581; ENSMUSG00000061979.
DR GeneID; 94254; -.
DR KEGG; mmu:94254; -.
DR UCSC; uc008zvc.2; mouse.
DR CTD; 81554; -.
DR MGI; MGI:2137600; Rcc1l.
DR VEuPathDB; HostDB:ENSMUSG00000061979; -.
DR eggNOG; KOG1426; Eukaryota.
DR GeneTree; ENSGT00940000157317; -.
DR HOGENOM; CLU_037900_0_0_1; -.
DR InParanoid; Q9CYF5; -.
DR OMA; GSFCMAL; -.
DR OrthoDB; 1062377at2759; -.
DR PhylomeDB; Q9CYF5; -.
DR TreeFam; TF317425; -.
DR BioGRID-ORCS; 94254; 24 hits in 70 CRISPR screens.
DR PRO; PR:Q9CYF5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CYF5; protein.
DR Bgee; ENSMUSG00000061979; Expressed in ectoplacental cone and 241 other tissues.
DR ExpressionAtlas; Q9CYF5; baseline and differential.
DR Genevisible; Q9CYF5; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS: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; PS50012; RCC1_3; 6.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..461
FT /note="RCC1-like G exchanging factor-like protein"
FT /id="PRO_0000206657"
FT REPEAT 55..121
FT /note="RCC1 1"
FT /evidence="ECO:0000255"
FT REPEAT 125..188
FT /note="RCC1 2"
FT /evidence="ECO:0000255"
FT REPEAT 190..244
FT /note="RCC1 3"
FT /evidence="ECO:0000255"
FT REPEAT 245..297
FT /note="RCC1 4"
FT /evidence="ECO:0000255"
FT REPEAT 298..350
FT /note="RCC1 5"
FT /evidence="ECO:0000255"
FT REPEAT 352..408
FT /note="RCC1 6"
FT /evidence="ECO:0000255"
FT REPEAT 409..458
FT /note="RCC1 7"
FT /evidence="ECO:0000255"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 49995 MW; 52B31CF2D31C2221 CRC64;
MLAAARALRG PRPRWPTPAR EHWTPAGRSR SRREAAEAEA DVPVFQYVGE RAARADRVFV
WGFSFSGALG VPSFVVPSSG PGPRAGLRPR RRIQPVPYRL ELDHKISSAA CGYGFTLLSS
KTKDVTKVWG MGLNKDSQLG FHRSRKDKTR GYEYVLEPSP VPLPLDRPQE TKVLQVSCGR
AHSLVLTDRE GVFSMGNNSH GQCGRKVVED EVYSESHKVH RMQDFDGQVV QVVCGQDHSL
FLTDKGEVYS CGWGADGQTG LGHYNITSTP SKLGGDLAGV TVVQVATYGD CCLALSADGG
VFGWGNSEYL QLASVTDSTQ VNVPRCLPFS GVGKVKQVAC GGTGCAVLNA EGHVFVWGYG
ILGKGPKLLE TAIPEMIPPT LFGLTEFNPE VQVSQIRCGL SHFAALTNKG ELFVWGKNIR
GCLGIGRLED QYFPWRVTMP GEPVDVACGV DHMVTLAKSF I
