RMND1_HUMAN
ID RMND1_HUMAN Reviewed; 449 AA.
AC Q9NWS8; A8K8H4; Q0VDG6; Q5SZ48; Q5SZ83; Q6NSC5; Q96EN7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Required for meiotic nuclear division protein 1 homolog;
DE Flags: Precursor;
GN Name=RMND1; Synonyms=C6orf96;
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] (ISOFORM 1), AND VARIANT MET-132.
RC TISSUE=Signet-ring cell carcinoma, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP MET-132.
RC TISSUE=Kidney, and Skin;
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 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 [6]
RP INVOLVEMENT IN COXPD11, AND SUBCELLULAR LOCATION.
RX PubMed=23022099; DOI=10.1016/j.ajhg.2012.08.019;
RA Garcia-Diaz B., Barros M.H., Sanna-Cherchi S., Emmanuele V., Akman H.O.,
RA Ferreiro-Barros C.C., Horvath R., Tadesse S., El Gharaby N., DiMauro S.,
RA De Vivo D.C., Shokr A., Hirano M., Quinzii C.M.;
RT "Infantile encephaloneuromyopathy and defective mitochondrial translation
RT are due to a homozygous RMND1 mutation.";
RL Am. J. Hum. Genet. 91:729-736(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT
RP COXPD11 GLN-417.
RX PubMed=25604853; DOI=10.1038/ejhg.2014.293;
RA Janer A., van Karnebeek C.D., Sasarman F., Antonicka H., Al Ghamdi M.,
RA Shyr C., Dunbar M., Stockler-Ispiroglu S., Ross C.J., Vallance H.,
RA Dionne J., Wasserman W.W., Shoubridge E.A.;
RT "RMND1 deficiency associated with neonatal lactic acidosis, infantile onset
RT renal failure, deafness, and multiorgan involvement.";
RL Eur. J. Hum. Genet. 23:1301-1307(2015).
RN [9]
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 [10]
RP VARIANT COXPD11 GLN-417, FUNCTION, HOMOPOLYMERIZATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23022098; DOI=10.1016/j.ajhg.2012.08.020;
RA Janer A., Antonicka H., Lalonde E., Nishimura T., Sasarman F., Brown G.K.,
RA Brown R.M., Majewski J., Shoubridge E.A.;
RT "An RMND1 Mutation causes encephalopathy associated with multiple oxidative
RT phosphorylation complex deficiencies and a mitochondrial translation
RT defect.";
RL Am. J. Hum. Genet. 91:737-743(2012).
RN [11]
RP VARIANT COXPD11 GLN-417.
RX PubMed=26238252; DOI=10.1007/8904_2015_479;
RA Casey J.P., Crushell E., Thompson K., Twomey E., He L., Ennis S.,
RA Philip R.K., Taylor R.W., King M.D., Lynch S.A.;
RT "Periventricular Calcification, Abnormal Pterins and Dry Thickened Skin:
RT expanding the clinical spectrum of RMND1?";
RL JIMD Rep. 26:13-19(2016).
CC -!- FUNCTION: Required for mitochondrial translation, possibly by
CC coordinating the assembly or maintenance of the mitochondrial ribosome
CC (PubMed:23022098, PubMed:25604853). {ECO:0000269|PubMed:23022098,
CC ECO:0000269|PubMed:25604853}.
CC -!- SUBUNIT: Homooligomer (PubMed:23022098, PubMed:25604853).
CC {ECO:0000269|PubMed:23022098, ECO:0000269|PubMed:25604853}.
CC -!- INTERACTION:
CC Q9NWS8; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-4401316, EBI-10175124;
CC Q9NWS8-3; Q92993: KAT5; NbExp=3; IntAct=EBI-25884400, EBI-399080;
CC Q9NWS8-3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-25884400, EBI-11742507;
CC Q9NWS8-3; P23284: PPIB; NbExp=3; IntAct=EBI-25884400, EBI-359252;
CC Q9NWS8-3; P17252: PRKCA; NbExp=3; IntAct=EBI-25884400, EBI-1383528;
CC Q9NWS8-3; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-25884400, EBI-9090795;
CC Q9NWS8-3; P61981: YWHAG; NbExp=3; IntAct=EBI-25884400, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23022098,
CC ECO:0000269|PubMed:23022099, ECO:0000269|PubMed:25604853}. Note=May be
CC localized in mitochondrial RNA granules (PubMed:25604853).
CC {ECO:0000269|PubMed:25604853}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NWS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NWS8-2; Sequence=VSP_017735;
CC Name=3;
CC IsoId=Q9NWS8-3; Sequence=VSP_017738, VSP_017739;
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 11 (COXPD11)
CC [MIM:614922]: A severe, multisystemic, autosomal recessive, disorder
CC characterized by deficiencies of multiple mitochondrial respiratory
CC enzymes leading to neonatal hypotonia and lactic acidosis. Affected
CC individuals may have respiratory insufficiency, foot deformities, or
CC seizures. {ECO:0000269|PubMed:23022098, ECO:0000269|PubMed:23022099,
CC ECO:0000269|PubMed:25604853, ECO:0000269|PubMed:26238252}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the RMD1/sif2 family. {ECO:0000305}.
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DR EMBL; AK000634; BAA91299.1; -; mRNA.
DR EMBL; AK292339; BAF85028.1; -; mRNA.
DR EMBL; AL590413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47747.1; -; Genomic_DNA.
DR EMBL; BC012081; AAH12081.1; -; mRNA.
DR EMBL; BC106065; AAI06066.1; -; mRNA.
DR EMBL; BC119683; AAI19684.1; -; mRNA.
DR CCDS; CCDS5232.1; -. [Q9NWS8-1]
DR RefSeq; NP_001258866.1; NM_001271937.1.
DR RefSeq; NP_060379.2; NM_017909.3. [Q9NWS8-1]
DR RefSeq; XP_005267097.1; XM_005267040.3. [Q9NWS8-2]
DR RefSeq; XP_016866477.1; XM_017010988.1. [Q9NWS8-2]
DR AlphaFoldDB; Q9NWS8; -.
DR BioGRID; 120337; 198.
DR IntAct; Q9NWS8; 38.
DR STRING; 9606.ENSP00000356272; -.
DR iPTMnet; Q9NWS8; -.
DR PhosphoSitePlus; Q9NWS8; -.
DR BioMuta; RMND1; -.
DR DMDM; 91208248; -.
DR EPD; Q9NWS8; -.
DR jPOST; Q9NWS8; -.
DR MassIVE; Q9NWS8; -.
DR MaxQB; Q9NWS8; -.
DR PaxDb; Q9NWS8; -.
DR PeptideAtlas; Q9NWS8; -.
DR PRIDE; Q9NWS8; -.
DR ProteomicsDB; 82973; -. [Q9NWS8-1]
DR ProteomicsDB; 82974; -. [Q9NWS8-2]
DR ProteomicsDB; 82975; -. [Q9NWS8-3]
DR Antibodypedia; 33335; 97 antibodies from 18 providers.
DR DNASU; 55005; -.
DR Ensembl; ENST00000444024.3; ENSP00000412708.2; ENSG00000155906.20. [Q9NWS8-1]
DR Ensembl; ENST00000491268.2; ENSP00000494948.1; ENSG00000155906.20. [Q9NWS8-3]
DR Ensembl; ENST00000683724.1; ENSP00000507984.1; ENSG00000155906.20. [Q9NWS8-1]
DR Ensembl; ENST00000684301.1; ENSP00000507824.1; ENSG00000155906.20. [Q9NWS8-3]
DR GeneID; 55005; -.
DR KEGG; hsa:55005; -.
DR MANE-Select; ENST00000444024.3; ENSP00000412708.2; NM_017909.4; NP_060379.2.
DR UCSC; uc003qoi.4; human. [Q9NWS8-1]
DR CTD; 55005; -.
DR DisGeNET; 55005; -.
DR GeneCards; RMND1; -.
DR HGNC; HGNC:21176; RMND1.
DR HPA; ENSG00000155906; Low tissue specificity.
DR MalaCards; RMND1; -.
DR MIM; 614917; gene.
DR MIM; 614922; phenotype.
DR neXtProt; NX_Q9NWS8; -.
DR OpenTargets; ENSG00000155906; -.
DR Orphanet; 324535; Combined oxidative phosphorylation defect type 11.
DR PharmGKB; PA162401372; -.
DR VEuPathDB; HostDB:ENSG00000155906; -.
DR eggNOG; KOG2861; Eukaryota.
DR GeneTree; ENSGT00390000013337; -.
DR HOGENOM; CLU_011220_4_0_1; -.
DR InParanoid; Q9NWS8; -.
DR OMA; QVIHVQT; -.
DR OrthoDB; 954411at2759; -.
DR PhylomeDB; Q9NWS8; -.
DR TreeFam; TF105813; -.
DR PathwayCommons; Q9NWS8; -.
DR SignaLink; Q9NWS8; -.
DR BioGRID-ORCS; 55005; 84 hits in 1081 CRISPR screens.
DR ChiTaRS; RMND1; human.
DR GenomeRNAi; 55005; -.
DR Pharos; Q9NWS8; Tbio.
DR PRO; PR:Q9NWS8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NWS8; protein.
DR Bgee; ENSG00000155906; Expressed in ganglionic eminence and 194 other tissues.
DR ExpressionAtlas; Q9NWS8; baseline and differential.
DR Genevisible; Q9NWS8; HS.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR InterPro; IPR003734; DUF155.
DR Pfam; PF02582; DUF155; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Mitochondrion;
KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 13..449
FT /note="Required for meiotic nuclear division protein 1
FT homolog"
FT /id="PRO_0000229732"
FT VAR_SEQ 1..211
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_017735"
FT VAR_SEQ 205..208
FT /note="DAAN -> GTSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017738"
FT VAR_SEQ 209..449
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017739"
FT VARIANT 42
FT /note="S -> I (in dbSNP:rs11550103)"
FT /id="VAR_051864"
FT VARIANT 47
FT /note="R -> H (in dbSNP:rs6934360)"
FT /id="VAR_051865"
FT VARIANT 132
FT /note="T -> M (in dbSNP:rs3734800)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_025754"
FT VARIANT 417
FT /note="R -> Q (in COXPD11; alters homooligomeric formation
FT of the protein; decreases the levels of mitochondrial
FT protein synthesis; dbSNP:rs397515421)"
FT /evidence="ECO:0000269|PubMed:23022098,
FT ECO:0000269|PubMed:25604853, ECO:0000269|PubMed:26238252"
FT /id="VAR_069036"
FT CONFLICT 170
FT /note="L -> P (in Ref. 1; BAA91299)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 51604 MW; C4A7B8F6A397B385 CRC64;
MPATLLRAVA RSHHILSKAH QCRRIGHLML KPLKEFENTT CSTLTIRQSL DLFLPDKTAS
GLNKSQILEM NQKKSDTSML SPLNAARCQD EKAHLPTMKS FGTHRRVTHK PNLLGSKWFI
KILKRHFSSV STETFVPKQD FPQVKRPLKA SRTRQPSRTN LPVLSVNEDL MHCTAFATAD
EYHLGNLSQD LASHGYVEVT SLPRDAANIL VMGVENSAKE GDPGTIFFFR EGAAVFWNVK
DKTMKHVMKV LEKHEIQPYE IALVHWENEE LNYIKIEGQS KLHRGEIKLN SELDLDDAIL
EKFAFSNALC LSVKLAIWEA SLDKFIESIQ SIPEALKAGK KVKLSHEEVM QKIGELFALR
HRINLSSDFL ITPDFYWDRE NLEGLYDKTC QFLSIGRRVK VMNEKLQHCM ELTDLMRNHL
NEKRALRLEW MIVILITIEV MFELGRVFF
